Full text data of SEC31A
SEC31A
(KIAA0905, SEC31L1)
[Confidence: low (only semi-automatic identification from reviews)]
Protein transport protein Sec31A (ABP125; ABP130; SEC31-like protein 1; SEC31-related protein A; Web1-like protein)
Protein transport protein Sec31A (ABP125; ABP130; SEC31-like protein 1; SEC31-related protein A; Web1-like protein)
UniProt
O94979
ID SC31A_HUMAN Reviewed; 1220 AA.
AC O94979; B4DIW6; B7ZKZ7; H7C2W3; Q17RR5; Q5H9P6; Q5XG74; Q659G7;
read moreAC Q6ZU90; Q7LCX9; Q86TJ0; Q8IZH4; Q9P048; Q9P0A6; Q9UM05; Q9UM06;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 3.
DT 22-JAN-2014, entry version 110.
DE RecName: Full=Protein transport protein Sec31A;
DE AltName: Full=ABP125;
DE AltName: Full=ABP130;
DE AltName: Full=SEC31-like protein 1;
DE AltName: Full=SEC31-related protein A;
DE AltName: Full=Web1-like protein;
GN Name=SEC31A; Synonyms=KIAA0905, SEC31L1; ORFNames=HSPC275, HSPC334;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Pancreas;
RX PubMed=10788476; DOI=10.1074/jbc.275.18.13597;
RA Tang B.L., Zhang T., Low D.Y.H., Wong E.T., Horstmann H., Hong W.;
RT "Mammalian homologues of yeast sec31p. An ubiquitously expressed form
RT is localized to endoplasmic reticulum (ER) exit sites and is essential
RT for ER-Golgi transport.";
RL J. Biol. Chem. 275:13597-13604(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Spleen;
RA Noguchi J., Shibata M.;
RT "The yeast web1-like human protein that has WD repeat domain.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
RA Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [4]
RP SEQUENCE REVISION.
RA Ohara O., Suyama M., Kikuno R., Nagase T., Ishikawa K.;
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 7 AND 9).
RC TISSUE=Hippocampus, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC TISSUE=Uterine endothelium, and Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 5).
RC TISSUE=Brain, and PNS;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 599-1220 (ISOFORMS 3/6).
RC TISSUE=Placenta;
RA Yang Y., Trejo J.;
RT "SEC31 splicing variant.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 852-1220 (ISOFORM 8), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 899-1220 (ISOFORM 1).
RC TISSUE=Blood;
RA Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L.,
RA Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.;
RT "Human partial CDS from CD34+ stem cells.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP TISSUE SPECIFICITY.
RX PubMed=10574704;
RA Shugrue C.A., Kolen E.R., Peters H., Czernik A., Kaiser C.,
RA Matovcik L., Hubbard A.L., Gorelick F.;
RT "Identification of the putative mammalian orthologue of Sec31P, a
RT component of the COPII coat.";
RL J. Cell Sci. 112:4547-4556(1999).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527 AND SER-532, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH PDCD6 AND SEC13,
RP AND SUBCELLULAR LOCATION.
RX PubMed=16957052; DOI=10.1091/mbc.E06-05-0444;
RA Yamasaki A., Tani K., Yamamoto A., Kitamura N., Komada M.;
RT "The Ca2+-binding protein ALG-2 is recruited to endoplasmic reticulum
RT exit sites by Sec31A and stabilizes the localization of Sec31A.";
RL Mol. Biol. Cell 17:4876-4887(2006).
RN [15]
RP CHROMOSOMAL TRANSLOCATION WITH ALK.
RX PubMed=16161041; DOI=10.1002/ijc.21490;
RA Panagopoulos I., Nilsson T., Domanski H.A., Isaksson M., Lindblom P.,
RA Mertens F., Mandahl N.;
RT "Fusion of the SEC31L1 and ALK genes in an inflammatory
RT myofibroblastic tumor.";
RL Int. J. Cancer 118:1181-1186(2006).
RN [16]
RP INTERACTION WITH PDCD6.
RX PubMed=17196169; DOI=10.1016/j.bbrc.2006.12.101;
RA Shibata H., Suzuki H., Yoshida H., Maki M.;
RT "ALG-2 directly binds Sec31A and localizes at endoplasmic reticulum
RT exit sites in a Ca2+-dependent manner.";
RL Biochem. Biophys. Res. Commun. 353:756-763(2007).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-799 AND SER-1163, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-799 AND THR-1161, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527 AND SER-799, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [22]
RP SUBCELLULAR LOCATION, UBIQUITINATION AT LYS-647 AND LYS-1217,
RP MUTAGENESIS OF LYS-647 AND LYS-1217, AND INTERACTION WITH KLHL12.
RX PubMed=22358839; DOI=10.1038/nature10822;
RA Jin L., Pahuja K.B., Wickliffe K.E., Gorur A., Baumgartel C.,
RA Schekman R., Rape M.;
RT "Ubiquitin-dependent regulation of COPII coat size and function.";
RL Nature 482:495-500(2012).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Component of the coat protein complex II (COPII) which
CC promotes the formation of transport vesicles from the endoplasmic
CC reticulum (ER). The coat has two main functions, the physical
CC deformation of the endoplasmic reticulum membrane into vesicles
CC and the selection of cargo molecules (By similarity).
CC -!- SUBUNIT: COPII is composed of at least 5 proteins: the SEC23/24
CC complex, the SEC13/31 complex and SAR1. SEC13 and SEC31 make a 2:2
CC tetramer that forms the edge element of the COPII outer coat. The
CC tetramer self-assembles in multiple copies to form the complete
CC polyhedral cage. Interacts (via WD 8) with SEC13 (By similarity).
CC Interacts with PDCD6 in a calcium-dependent manner. Interacts with
CC KLHL12.
CC -!- INTERACTION:
CC O75340:PDCD6; NbExp=6; IntAct=EBI-1767898, EBI-352915;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasmic
CC vesicle, COPII-coated vesicle membrane; Peripheral membrane
CC protein; Cytoplasmic side. Endoplasmic reticulum membrane;
CC Peripheral membrane protein (By similarity). Note=Associates with
CC membranes in a GTP-dependent manner (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Name=1;
CC IsoId=O94979-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O94979-2; Sequence=VSP_026750;
CC Name=3;
CC IsoId=O94979-3; Sequence=VSP_026748, VSP_026749;
CC Name=4;
CC IsoId=O94979-4; Sequence=VSP_026744;
CC Name=5;
CC IsoId=O94979-5; Sequence=VSP_026745, VSP_026746;
CC Note=No experimental confirmation available;
CC Name=6;
CC IsoId=O94979-6; Sequence=VSP_026744, VSP_026748, VSP_026749;
CC Name=7;
CC IsoId=O94979-7; Sequence=VSP_026742, VSP_026743, VSP_026744,
CC VSP_026747, VSP_026750;
CC Note=No experimental confirmation available;
CC Name=8;
CC IsoId=O94979-8; Sequence=VSP_026751;
CC Name=9;
CC IsoId=O94979-9; Sequence=VSP_044602, VSP_026750;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Abundantly and ubiquitously expressed.
CC -!- PTM: Monoubiquitinated by the BCR(KLHL12) E3 ubiquitin ligase
CC complex, leading to regulate the size of COPII coats.
CC -!- DISEASE: Note=A chromosomal aberration involving SEC31A is
CC associated with inflammatory myofibroblastic tumors (IMTs).
CC Translocation t(2;4)(p23;q21) with ALK.
CC -!- SIMILARITY: Belongs to the WD repeat SEC31 family.
CC -!- SIMILARITY: Contains 8 WD repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF28953.1; Type=Frameshift; Positions=857, 1079;
CC Sequence=AAF29012.1; Type=Frameshift; Positions=922, 946, 1029, 1080;
CC Sequence=CAI45995.1; Type=Erroneous termination; Positions=221; Note=Translated as Trp;
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DR EMBL; AF139184; AAF67836.1; -; mRNA.
DR EMBL; AB018358; BAA84923.1; -; mRNA.
DR EMBL; AB018359; BAA84924.1; -; mRNA.
DR EMBL; AB020712; BAA74928.2; -; mRNA.
DR EMBL; AK125897; BAC86336.1; -; mRNA.
DR EMBL; AK295810; BAG58628.1; -; mRNA.
DR EMBL; AL049463; CAH56418.1; -; mRNA.
DR EMBL; CR933696; CAI45995.1; ALT_SEQ; mRNA.
DR EMBL; AC021105; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC108469; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471057; EAX05908.1; -; Genomic_DNA.
DR EMBL; BC047883; AAH47883.1; -; mRNA.
DR EMBL; BC084583; AAH84583.1; -; mRNA.
DR EMBL; BC117221; AAI17222.1; -; mRNA.
DR EMBL; BC143489; AAI43490.1; -; mRNA.
DR EMBL; BC143491; AAI43492.1; -; mRNA.
DR EMBL; AY137583; AAN15221.1; -; mRNA.
DR EMBL; AF161393; AAF28953.1; ALT_FRAME; mRNA.
DR EMBL; AF161452; AAF29012.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001070674.1; NM_001077206.2.
DR RefSeq; NP_001070675.1; NM_001077207.2.
DR RefSeq; NP_001070676.1; NM_001077208.2.
DR RefSeq; NP_001177978.1; NM_001191049.1.
DR RefSeq; NP_055748.2; NM_014933.3.
DR RefSeq; NP_057295.2; NM_016211.3.
DR RefSeq; XP_005262904.1; XM_005262847.1.
DR RefSeq; XP_005262907.1; XM_005262850.1.
DR RefSeq; XP_005262911.1; XM_005262854.1.
DR UniGene; Hs.370024; -.
DR ProteinModelPortal; O94979; -.
DR SMR; O94979; 5-366, 537-770.
DR DIP; DIP-40438N; -.
DR IntAct; O94979; 32.
DR MINT; MINT-3002555; -.
DR PhosphoSite; O94979; -.
DR PaxDb; O94979; -.
DR PRIDE; O94979; -.
DR Ensembl; ENST00000311785; ENSP00000309070; ENSG00000138674.
DR Ensembl; ENST00000326950; ENSP00000325087; ENSG00000138674.
DR Ensembl; ENST00000348405; ENSP00000337602; ENSG00000138674.
DR Ensembl; ENST00000355196; ENSP00000347329; ENSG00000138674.
DR Ensembl; ENST00000395310; ENSP00000378721; ENSG00000138674.
DR Ensembl; ENST00000432794; ENSP00000407944; ENSG00000138674.
DR Ensembl; ENST00000443462; ENSP00000408027; ENSG00000138674.
DR Ensembl; ENST00000448323; ENSP00000400926; ENSG00000138674.
DR Ensembl; ENST00000500777; ENSP00000421464; ENSG00000138674.
DR Ensembl; ENST00000508502; ENSP00000424635; ENSG00000138674.
DR Ensembl; ENST00000509142; ENSP00000426569; ENSG00000138674.
DR Ensembl; ENST00000513858; ENSP00000426886; ENSG00000138674.
DR GeneID; 22872; -.
DR KEGG; hsa:22872; -.
DR UCSC; uc011ccm.2; human.
DR CTD; 22872; -.
DR GeneCards; GC04M083739; -.
DR HGNC; HGNC:17052; SEC31A.
DR HPA; HPA005457; -.
DR MIM; 610257; gene.
DR neXtProt; NX_O94979; -.
DR PharmGKB; PA162402737; -.
DR eggNOG; NOG248389; -.
DR HOVERGEN; HBG055626; -.
DR InParanoid; O94979; -.
DR KO; K14005; -.
DR OrthoDB; EOG7B31M1; -.
DR PhylomeDB; O94979; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; O94979; -.
DR ChiTaRS; SEC31A; human.
DR GeneWiki; SEC31A; -.
DR GenomeRNAi; 22872; -.
DR NextBio; 43407; -.
DR PRO; PR:O94979; -.
DR ArrayExpress; O94979; -.
DR Bgee; O94979; -.
DR Genevestigator; O94979; -.
DR GO; GO:0030127; C:COPII vesicle coat; NAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0006987; P:activation of signaling protein activity involved in unfolded protein response; TAS:Reactome.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
DR GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome.
DR GO; GO:0048208; P:COPII vesicle coating; TAS:Reactome.
DR GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; TAS:Reactome.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0051592; P:response to calcium ion; IDA:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR017986; WD40_repeat_dom.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromosomal rearrangement; Complete proteome;
KW Cytoplasm; Cytoplasmic vesicle; Endoplasmic reticulum;
KW ER-Golgi transport; Isopeptide bond; Membrane; Phosphoprotein;
KW Polymorphism; Protein transport; Proto-oncogene; Reference proteome;
KW Repeat; Transport; Ubl conjugation; WD repeat.
FT CHAIN 1 1220 Protein transport protein Sec31A.
FT /FTId=PRO_0000295147.
FT REPEAT 4 47 WD 1.
FT REPEAT 68 111 WD 2.
FT REPEAT 120 160 WD 3.
FT REPEAT 166 206 WD 4.
FT REPEAT 209 254 WD 5.
FT REPEAT 258 298 WD 6.
FT REPEAT 301 342 WD 7.
FT REPEAT 397 430 WD 8; interaction with SEC13 (By
FT similarity).
FT REGION 161 471 Interaction with SEC13.
FT REGION 800 1113 Interaction with PDCD6.
FT COMPBIAS 800 1091 Pro-rich.
FT MOD_RES 527 527 Phosphoserine.
FT MOD_RES 532 532 Phosphoserine.
FT MOD_RES 799 799 Phosphoserine.
FT MOD_RES 1161 1161 Phosphothreonine.
FT MOD_RES 1163 1163 Phosphoserine.
FT CROSSLNK 647 647 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CROSSLNK 1217 1217 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT VAR_SEQ 1 228 Missing (in isoform 7).
FT /FTId=VSP_026742.
FT VAR_SEQ 1 26 MKLKEVDRTAMQAWSPAQNHPIYLAT -> MLGESDERCTN
FT AGSGCRRSSP (in isoform 9).
FT /FTId=VSP_044602.
FT VAR_SEQ 229 260 MVLASEDDRLPVIQMWDLRFASSPLRVLENHA -> MVKLV
FT LLSIVLLKVTVPKLSNYLLQLDFMPIH (in isoform
FT 7).
FT /FTId=VSP_026743.
FT VAR_SEQ 504 542 Missing (in isoform 4, isoform 6 and
FT isoform 7).
FT /FTId=VSP_026744.
FT VAR_SEQ 504 509 IALALN -> VNFWES (in isoform 5).
FT /FTId=VSP_026745.
FT VAR_SEQ 510 1220 Missing (in isoform 5).
FT /FTId=VSP_026746.
FT VAR_SEQ 834 834 H -> HVRIAPTVTTWSNKTPTALPSHPPAASPSDTQ (in
FT isoform 7).
FT /FTId=VSP_026747.
FT VAR_SEQ 876 876 P -> R (in isoform 3 and isoform 6).
FT /FTId=VSP_026748.
FT VAR_SEQ 877 990 Missing (in isoform 3 and isoform 6).
FT /FTId=VSP_026749.
FT VAR_SEQ 974 988 Missing (in isoform 2, isoform 7 and
FT isoform 9).
FT /FTId=VSP_026750.
FT VAR_SEQ 989 989 T -> TENQSIQDQAPMLE (in isoform 8).
FT /FTId=VSP_026751.
FT VARIANT 263 263 I -> V (in dbSNP:rs34554214).
FT /FTId=VAR_033225.
FT VARIANT 456 456 N -> K (in dbSNP:rs3797036).
FT /FTId=VAR_053414.
FT VARIANT 841 841 P -> L (in dbSNP:rs35579207).
FT /FTId=VAR_033226.
FT VARIANT 1055 1055 P -> T (in dbSNP:rs35739017).
FT /FTId=VAR_033227.
FT MUTAGEN 647 647 K->R: Does not abolish monoubiquitination
FT by the BCR(KLHL12) E3 ubiquitin ligase
FT complex, revealing flexibility of
FT ubiquitination sites; when associated
FT with R-1217.
FT MUTAGEN 1217 1217 K->R: Does not abolish monoubiquitination
FT by the BCR(KLHL12) E3 ubiquitin ligase
FT complex, revealing flexibility of
FT ubiquitination sites; when associated
FT with R-647.
FT CONFLICT 200 200 K -> E (in Ref. 2; BAA84923).
FT CONFLICT 284 284 K -> R (in Ref. 5; BAC86336).
FT CONFLICT 854 854 A -> S (in Ref. 2; BAA84923/BAA84924).
FT CONFLICT 1007 1007 K -> R (in Ref. 5; BAG58628).
SQ SEQUENCE 1220 AA; 133015 MW; 2A633B4436DB7482 CRC64;
MKLKEVDRTA MQAWSPAQNH PIYLATGTSA QQLDATFSTN ASLEIFELDL SDPSLDMKSC
ATFSSSHRYH KLIWGPYKMD SKGDVSGVLI AGGENGNIIL YDPSKIIAGD KEVVIAQNDK
HTGPVRALDV NIFQTNLVAS GANESEIYIW DLNNFATPMT PGAKTQPPED ISCIAWNRQV
QHILASASPS GRATVWDLRK NEPIIKVSDH SNRMHCSGLA WHPDVATQMV LASEDDRLPV
IQMWDLRFAS SPLRVLENHA RGILAIAWSM ADPELLLSCG KDAKILCSNP NTGEVLYELP
TNTQWCFDIQ WCPRNPAVLS AASFDGRISV YSIMGGSTDG LRQKQVDKLS SSFGNLDPFG
TGQPLPPLQI PQQTAQHSIV LPLKKPPKWI RRPVGASFSF GGKLVTFENV RMPSHQGAEQ
QQQQHHVFIS QVVTEKEFLS RSDQLQQAVQ SQGFINYCQK KIDASQTEFE KNVWSFLKVN
FEDDSRGKYL ELLGYRKEDL GKKIALALNK VDGANVALKD SDQVAQSDGE ESPAAEEQLL
GEHIKEEKEE SEFLPSSGGT FNISVSGDID GLITQALLTG NFESAVDLCL HDNRMADAII
LAIAGGQELL ARTQKKYFAK SQSKITRLIT AVVMKNWKEI VESCDLKNWR EALAAVLTYA
KPDEFSALCD LLGTRLENEG DSLLQTQACL CYICAGNVEK LVACWTKAQD GSHPLSLQDL
IEKVVILRKA VQLTQAMDTS TVGVLLAAKM SQYANLLAAQ GSIAAALAFL PDNTNQPNIM
QLRDRLCRAQ GEPVAGHESP KIPYEKQQLP KGRPGPVAGH HQMPRVQTQQ YYPHGENPPP
PGFIMHGNVN PNAAGQLPTS PGHMHTQVPP YPQPQPYQPA QPYPFGTGGS AMYRPQQPVA
PPTSNAYPNT PYISSASSYT GQSQLYAAQH QASSPTSSPA TSFPPPPSSG ASFQHGGPGA
PPSSSAYALP PGTTGTLPAA SELPASQRTG PQNGWNDPPA LNRVPKKKKM PENFMPPVPI
TSPIMNPLGD PQSQMLQQQP SAPVPLSSQS SFPQPHLPGG QPFHGVQQPL GQTGMPPSFS
KPNIEGAPGA PIGNTFQHVQ SLPTKKITKK PIPDEHLILK TTFEDLIQRC LSSATDPQTK
RKLDDASKRL EFLYDKLREQ TLSPTITSGL HNIARSIETR NYSEGLTMHT HIVSTSNFSE
TSAFMPVLKV VLTQANKLGV
//
ID SC31A_HUMAN Reviewed; 1220 AA.
AC O94979; B4DIW6; B7ZKZ7; H7C2W3; Q17RR5; Q5H9P6; Q5XG74; Q659G7;
read moreAC Q6ZU90; Q7LCX9; Q86TJ0; Q8IZH4; Q9P048; Q9P0A6; Q9UM05; Q9UM06;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 3.
DT 22-JAN-2014, entry version 110.
DE RecName: Full=Protein transport protein Sec31A;
DE AltName: Full=ABP125;
DE AltName: Full=ABP130;
DE AltName: Full=SEC31-like protein 1;
DE AltName: Full=SEC31-related protein A;
DE AltName: Full=Web1-like protein;
GN Name=SEC31A; Synonyms=KIAA0905, SEC31L1; ORFNames=HSPC275, HSPC334;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Pancreas;
RX PubMed=10788476; DOI=10.1074/jbc.275.18.13597;
RA Tang B.L., Zhang T., Low D.Y.H., Wong E.T., Horstmann H., Hong W.;
RT "Mammalian homologues of yeast sec31p. An ubiquitously expressed form
RT is localized to endoplasmic reticulum (ER) exit sites and is essential
RT for ER-Golgi transport.";
RL J. Biol. Chem. 275:13597-13604(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Spleen;
RA Noguchi J., Shibata M.;
RT "The yeast web1-like human protein that has WD repeat domain.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
RA Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [4]
RP SEQUENCE REVISION.
RA Ohara O., Suyama M., Kikuno R., Nagase T., Ishikawa K.;
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 7 AND 9).
RC TISSUE=Hippocampus, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC TISSUE=Uterine endothelium, and Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 5).
RC TISSUE=Brain, and PNS;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 599-1220 (ISOFORMS 3/6).
RC TISSUE=Placenta;
RA Yang Y., Trejo J.;
RT "SEC31 splicing variant.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 852-1220 (ISOFORM 8), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 899-1220 (ISOFORM 1).
RC TISSUE=Blood;
RA Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L.,
RA Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.;
RT "Human partial CDS from CD34+ stem cells.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP TISSUE SPECIFICITY.
RX PubMed=10574704;
RA Shugrue C.A., Kolen E.R., Peters H., Czernik A., Kaiser C.,
RA Matovcik L., Hubbard A.L., Gorelick F.;
RT "Identification of the putative mammalian orthologue of Sec31P, a
RT component of the COPII coat.";
RL J. Cell Sci. 112:4547-4556(1999).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527 AND SER-532, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH PDCD6 AND SEC13,
RP AND SUBCELLULAR LOCATION.
RX PubMed=16957052; DOI=10.1091/mbc.E06-05-0444;
RA Yamasaki A., Tani K., Yamamoto A., Kitamura N., Komada M.;
RT "The Ca2+-binding protein ALG-2 is recruited to endoplasmic reticulum
RT exit sites by Sec31A and stabilizes the localization of Sec31A.";
RL Mol. Biol. Cell 17:4876-4887(2006).
RN [15]
RP CHROMOSOMAL TRANSLOCATION WITH ALK.
RX PubMed=16161041; DOI=10.1002/ijc.21490;
RA Panagopoulos I., Nilsson T., Domanski H.A., Isaksson M., Lindblom P.,
RA Mertens F., Mandahl N.;
RT "Fusion of the SEC31L1 and ALK genes in an inflammatory
RT myofibroblastic tumor.";
RL Int. J. Cancer 118:1181-1186(2006).
RN [16]
RP INTERACTION WITH PDCD6.
RX PubMed=17196169; DOI=10.1016/j.bbrc.2006.12.101;
RA Shibata H., Suzuki H., Yoshida H., Maki M.;
RT "ALG-2 directly binds Sec31A and localizes at endoplasmic reticulum
RT exit sites in a Ca2+-dependent manner.";
RL Biochem. Biophys. Res. Commun. 353:756-763(2007).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-799 AND SER-1163, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-799 AND THR-1161, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527 AND SER-799, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [22]
RP SUBCELLULAR LOCATION, UBIQUITINATION AT LYS-647 AND LYS-1217,
RP MUTAGENESIS OF LYS-647 AND LYS-1217, AND INTERACTION WITH KLHL12.
RX PubMed=22358839; DOI=10.1038/nature10822;
RA Jin L., Pahuja K.B., Wickliffe K.E., Gorur A., Baumgartel C.,
RA Schekman R., Rape M.;
RT "Ubiquitin-dependent regulation of COPII coat size and function.";
RL Nature 482:495-500(2012).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Component of the coat protein complex II (COPII) which
CC promotes the formation of transport vesicles from the endoplasmic
CC reticulum (ER). The coat has two main functions, the physical
CC deformation of the endoplasmic reticulum membrane into vesicles
CC and the selection of cargo molecules (By similarity).
CC -!- SUBUNIT: COPII is composed of at least 5 proteins: the SEC23/24
CC complex, the SEC13/31 complex and SAR1. SEC13 and SEC31 make a 2:2
CC tetramer that forms the edge element of the COPII outer coat. The
CC tetramer self-assembles in multiple copies to form the complete
CC polyhedral cage. Interacts (via WD 8) with SEC13 (By similarity).
CC Interacts with PDCD6 in a calcium-dependent manner. Interacts with
CC KLHL12.
CC -!- INTERACTION:
CC O75340:PDCD6; NbExp=6; IntAct=EBI-1767898, EBI-352915;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasmic
CC vesicle, COPII-coated vesicle membrane; Peripheral membrane
CC protein; Cytoplasmic side. Endoplasmic reticulum membrane;
CC Peripheral membrane protein (By similarity). Note=Associates with
CC membranes in a GTP-dependent manner (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Name=1;
CC IsoId=O94979-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O94979-2; Sequence=VSP_026750;
CC Name=3;
CC IsoId=O94979-3; Sequence=VSP_026748, VSP_026749;
CC Name=4;
CC IsoId=O94979-4; Sequence=VSP_026744;
CC Name=5;
CC IsoId=O94979-5; Sequence=VSP_026745, VSP_026746;
CC Note=No experimental confirmation available;
CC Name=6;
CC IsoId=O94979-6; Sequence=VSP_026744, VSP_026748, VSP_026749;
CC Name=7;
CC IsoId=O94979-7; Sequence=VSP_026742, VSP_026743, VSP_026744,
CC VSP_026747, VSP_026750;
CC Note=No experimental confirmation available;
CC Name=8;
CC IsoId=O94979-8; Sequence=VSP_026751;
CC Name=9;
CC IsoId=O94979-9; Sequence=VSP_044602, VSP_026750;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Abundantly and ubiquitously expressed.
CC -!- PTM: Monoubiquitinated by the BCR(KLHL12) E3 ubiquitin ligase
CC complex, leading to regulate the size of COPII coats.
CC -!- DISEASE: Note=A chromosomal aberration involving SEC31A is
CC associated with inflammatory myofibroblastic tumors (IMTs).
CC Translocation t(2;4)(p23;q21) with ALK.
CC -!- SIMILARITY: Belongs to the WD repeat SEC31 family.
CC -!- SIMILARITY: Contains 8 WD repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF28953.1; Type=Frameshift; Positions=857, 1079;
CC Sequence=AAF29012.1; Type=Frameshift; Positions=922, 946, 1029, 1080;
CC Sequence=CAI45995.1; Type=Erroneous termination; Positions=221; Note=Translated as Trp;
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DR EMBL; AF139184; AAF67836.1; -; mRNA.
DR EMBL; AB018358; BAA84923.1; -; mRNA.
DR EMBL; AB018359; BAA84924.1; -; mRNA.
DR EMBL; AB020712; BAA74928.2; -; mRNA.
DR EMBL; AK125897; BAC86336.1; -; mRNA.
DR EMBL; AK295810; BAG58628.1; -; mRNA.
DR EMBL; AL049463; CAH56418.1; -; mRNA.
DR EMBL; CR933696; CAI45995.1; ALT_SEQ; mRNA.
DR EMBL; AC021105; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC108469; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471057; EAX05908.1; -; Genomic_DNA.
DR EMBL; BC047883; AAH47883.1; -; mRNA.
DR EMBL; BC084583; AAH84583.1; -; mRNA.
DR EMBL; BC117221; AAI17222.1; -; mRNA.
DR EMBL; BC143489; AAI43490.1; -; mRNA.
DR EMBL; BC143491; AAI43492.1; -; mRNA.
DR EMBL; AY137583; AAN15221.1; -; mRNA.
DR EMBL; AF161393; AAF28953.1; ALT_FRAME; mRNA.
DR EMBL; AF161452; AAF29012.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001070674.1; NM_001077206.2.
DR RefSeq; NP_001070675.1; NM_001077207.2.
DR RefSeq; NP_001070676.1; NM_001077208.2.
DR RefSeq; NP_001177978.1; NM_001191049.1.
DR RefSeq; NP_055748.2; NM_014933.3.
DR RefSeq; NP_057295.2; NM_016211.3.
DR RefSeq; XP_005262904.1; XM_005262847.1.
DR RefSeq; XP_005262907.1; XM_005262850.1.
DR RefSeq; XP_005262911.1; XM_005262854.1.
DR UniGene; Hs.370024; -.
DR ProteinModelPortal; O94979; -.
DR SMR; O94979; 5-366, 537-770.
DR DIP; DIP-40438N; -.
DR IntAct; O94979; 32.
DR MINT; MINT-3002555; -.
DR PhosphoSite; O94979; -.
DR PaxDb; O94979; -.
DR PRIDE; O94979; -.
DR Ensembl; ENST00000311785; ENSP00000309070; ENSG00000138674.
DR Ensembl; ENST00000326950; ENSP00000325087; ENSG00000138674.
DR Ensembl; ENST00000348405; ENSP00000337602; ENSG00000138674.
DR Ensembl; ENST00000355196; ENSP00000347329; ENSG00000138674.
DR Ensembl; ENST00000395310; ENSP00000378721; ENSG00000138674.
DR Ensembl; ENST00000432794; ENSP00000407944; ENSG00000138674.
DR Ensembl; ENST00000443462; ENSP00000408027; ENSG00000138674.
DR Ensembl; ENST00000448323; ENSP00000400926; ENSG00000138674.
DR Ensembl; ENST00000500777; ENSP00000421464; ENSG00000138674.
DR Ensembl; ENST00000508502; ENSP00000424635; ENSG00000138674.
DR Ensembl; ENST00000509142; ENSP00000426569; ENSG00000138674.
DR Ensembl; ENST00000513858; ENSP00000426886; ENSG00000138674.
DR GeneID; 22872; -.
DR KEGG; hsa:22872; -.
DR UCSC; uc011ccm.2; human.
DR CTD; 22872; -.
DR GeneCards; GC04M083739; -.
DR HGNC; HGNC:17052; SEC31A.
DR HPA; HPA005457; -.
DR MIM; 610257; gene.
DR neXtProt; NX_O94979; -.
DR PharmGKB; PA162402737; -.
DR eggNOG; NOG248389; -.
DR HOVERGEN; HBG055626; -.
DR InParanoid; O94979; -.
DR KO; K14005; -.
DR OrthoDB; EOG7B31M1; -.
DR PhylomeDB; O94979; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; O94979; -.
DR ChiTaRS; SEC31A; human.
DR GeneWiki; SEC31A; -.
DR GenomeRNAi; 22872; -.
DR NextBio; 43407; -.
DR PRO; PR:O94979; -.
DR ArrayExpress; O94979; -.
DR Bgee; O94979; -.
DR Genevestigator; O94979; -.
DR GO; GO:0030127; C:COPII vesicle coat; NAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0006987; P:activation of signaling protein activity involved in unfolded protein response; TAS:Reactome.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
DR GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome.
DR GO; GO:0048208; P:COPII vesicle coating; TAS:Reactome.
DR GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; TAS:Reactome.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0051592; P:response to calcium ion; IDA:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR017986; WD40_repeat_dom.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromosomal rearrangement; Complete proteome;
KW Cytoplasm; Cytoplasmic vesicle; Endoplasmic reticulum;
KW ER-Golgi transport; Isopeptide bond; Membrane; Phosphoprotein;
KW Polymorphism; Protein transport; Proto-oncogene; Reference proteome;
KW Repeat; Transport; Ubl conjugation; WD repeat.
FT CHAIN 1 1220 Protein transport protein Sec31A.
FT /FTId=PRO_0000295147.
FT REPEAT 4 47 WD 1.
FT REPEAT 68 111 WD 2.
FT REPEAT 120 160 WD 3.
FT REPEAT 166 206 WD 4.
FT REPEAT 209 254 WD 5.
FT REPEAT 258 298 WD 6.
FT REPEAT 301 342 WD 7.
FT REPEAT 397 430 WD 8; interaction with SEC13 (By
FT similarity).
FT REGION 161 471 Interaction with SEC13.
FT REGION 800 1113 Interaction with PDCD6.
FT COMPBIAS 800 1091 Pro-rich.
FT MOD_RES 527 527 Phosphoserine.
FT MOD_RES 532 532 Phosphoserine.
FT MOD_RES 799 799 Phosphoserine.
FT MOD_RES 1161 1161 Phosphothreonine.
FT MOD_RES 1163 1163 Phosphoserine.
FT CROSSLNK 647 647 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CROSSLNK 1217 1217 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT VAR_SEQ 1 228 Missing (in isoform 7).
FT /FTId=VSP_026742.
FT VAR_SEQ 1 26 MKLKEVDRTAMQAWSPAQNHPIYLAT -> MLGESDERCTN
FT AGSGCRRSSP (in isoform 9).
FT /FTId=VSP_044602.
FT VAR_SEQ 229 260 MVLASEDDRLPVIQMWDLRFASSPLRVLENHA -> MVKLV
FT LLSIVLLKVTVPKLSNYLLQLDFMPIH (in isoform
FT 7).
FT /FTId=VSP_026743.
FT VAR_SEQ 504 542 Missing (in isoform 4, isoform 6 and
FT isoform 7).
FT /FTId=VSP_026744.
FT VAR_SEQ 504 509 IALALN -> VNFWES (in isoform 5).
FT /FTId=VSP_026745.
FT VAR_SEQ 510 1220 Missing (in isoform 5).
FT /FTId=VSP_026746.
FT VAR_SEQ 834 834 H -> HVRIAPTVTTWSNKTPTALPSHPPAASPSDTQ (in
FT isoform 7).
FT /FTId=VSP_026747.
FT VAR_SEQ 876 876 P -> R (in isoform 3 and isoform 6).
FT /FTId=VSP_026748.
FT VAR_SEQ 877 990 Missing (in isoform 3 and isoform 6).
FT /FTId=VSP_026749.
FT VAR_SEQ 974 988 Missing (in isoform 2, isoform 7 and
FT isoform 9).
FT /FTId=VSP_026750.
FT VAR_SEQ 989 989 T -> TENQSIQDQAPMLE (in isoform 8).
FT /FTId=VSP_026751.
FT VARIANT 263 263 I -> V (in dbSNP:rs34554214).
FT /FTId=VAR_033225.
FT VARIANT 456 456 N -> K (in dbSNP:rs3797036).
FT /FTId=VAR_053414.
FT VARIANT 841 841 P -> L (in dbSNP:rs35579207).
FT /FTId=VAR_033226.
FT VARIANT 1055 1055 P -> T (in dbSNP:rs35739017).
FT /FTId=VAR_033227.
FT MUTAGEN 647 647 K->R: Does not abolish monoubiquitination
FT by the BCR(KLHL12) E3 ubiquitin ligase
FT complex, revealing flexibility of
FT ubiquitination sites; when associated
FT with R-1217.
FT MUTAGEN 1217 1217 K->R: Does not abolish monoubiquitination
FT by the BCR(KLHL12) E3 ubiquitin ligase
FT complex, revealing flexibility of
FT ubiquitination sites; when associated
FT with R-647.
FT CONFLICT 200 200 K -> E (in Ref. 2; BAA84923).
FT CONFLICT 284 284 K -> R (in Ref. 5; BAC86336).
FT CONFLICT 854 854 A -> S (in Ref. 2; BAA84923/BAA84924).
FT CONFLICT 1007 1007 K -> R (in Ref. 5; BAG58628).
SQ SEQUENCE 1220 AA; 133015 MW; 2A633B4436DB7482 CRC64;
MKLKEVDRTA MQAWSPAQNH PIYLATGTSA QQLDATFSTN ASLEIFELDL SDPSLDMKSC
ATFSSSHRYH KLIWGPYKMD SKGDVSGVLI AGGENGNIIL YDPSKIIAGD KEVVIAQNDK
HTGPVRALDV NIFQTNLVAS GANESEIYIW DLNNFATPMT PGAKTQPPED ISCIAWNRQV
QHILASASPS GRATVWDLRK NEPIIKVSDH SNRMHCSGLA WHPDVATQMV LASEDDRLPV
IQMWDLRFAS SPLRVLENHA RGILAIAWSM ADPELLLSCG KDAKILCSNP NTGEVLYELP
TNTQWCFDIQ WCPRNPAVLS AASFDGRISV YSIMGGSTDG LRQKQVDKLS SSFGNLDPFG
TGQPLPPLQI PQQTAQHSIV LPLKKPPKWI RRPVGASFSF GGKLVTFENV RMPSHQGAEQ
QQQQHHVFIS QVVTEKEFLS RSDQLQQAVQ SQGFINYCQK KIDASQTEFE KNVWSFLKVN
FEDDSRGKYL ELLGYRKEDL GKKIALALNK VDGANVALKD SDQVAQSDGE ESPAAEEQLL
GEHIKEEKEE SEFLPSSGGT FNISVSGDID GLITQALLTG NFESAVDLCL HDNRMADAII
LAIAGGQELL ARTQKKYFAK SQSKITRLIT AVVMKNWKEI VESCDLKNWR EALAAVLTYA
KPDEFSALCD LLGTRLENEG DSLLQTQACL CYICAGNVEK LVACWTKAQD GSHPLSLQDL
IEKVVILRKA VQLTQAMDTS TVGVLLAAKM SQYANLLAAQ GSIAAALAFL PDNTNQPNIM
QLRDRLCRAQ GEPVAGHESP KIPYEKQQLP KGRPGPVAGH HQMPRVQTQQ YYPHGENPPP
PGFIMHGNVN PNAAGQLPTS PGHMHTQVPP YPQPQPYQPA QPYPFGTGGS AMYRPQQPVA
PPTSNAYPNT PYISSASSYT GQSQLYAAQH QASSPTSSPA TSFPPPPSSG ASFQHGGPGA
PPSSSAYALP PGTTGTLPAA SELPASQRTG PQNGWNDPPA LNRVPKKKKM PENFMPPVPI
TSPIMNPLGD PQSQMLQQQP SAPVPLSSQS SFPQPHLPGG QPFHGVQQPL GQTGMPPSFS
KPNIEGAPGA PIGNTFQHVQ SLPTKKITKK PIPDEHLILK TTFEDLIQRC LSSATDPQTK
RKLDDASKRL EFLYDKLREQ TLSPTITSGL HNIARSIETR NYSEGLTMHT HIVSTSNFSE
TSAFMPVLKV VLTQANKLGV
//
MIM
610257
*RECORD*
*FIELD* NO
610257
*FIELD* TI
*610257 SEC31, YEAST, HOMOLOG OF, A; SEC31A
;;SEC31-LIKE 1; SEC31L1;;
KIAA0905
*FIELD* TX
read more
DESCRIPTION
SEC31A is a subunit of coat protein complex II (COPII)-coated vesicles,
which are essential for secretion (Jin et al., 2012).
CLONING
By sequencing clones obtained from a size-fractionated adult brain cDNA
library, Nagase et al. (1998) cloned SEC31L1, which they designated
KIAA0905. The deduced protein contains 1,220 amino acids. RT-PCR
detected moderate expression in all adult and fetal tissues and specific
brain regions examined.
By searching EST databases for sequences similar to yeast Sec31,
followed by screening a pancreas cDNA library, Tang et al. (2000) cloned
SEC31L1, which they called SEC31A. The deduced 1,218-amino acid protein
shares 25.8% identity with yeast Sec31. It contains 5 WD40 or WD40-like
repeats at its N terminus and a proline-rich region in its C-terminal
half. Northern blot analysis detected a 4-kb transcript that was
abundantly and ubiquitously expressed. In rat kidney cells, Sec31a
colocalized with Sec13 (SEC13L1; 600152) in vesicular-tubular structures
characteristic of endoplasmic reticulum (ER) exit sites.
GENE FUNCTION
By immunostaining for Sec31a in intact and permeabilized rat kidney
cells, Tang et al. (2000) found that Sec31a was not tightly associated
with the membrane. Binding of Sec31a to specific membrane structures was
restored by incubating washed cells with cytosol, indicating that Sec31a
was recruited to membranes. The membrane association of Sec31a was
greatly enhanced in the presence of a nonhydrolyzable GTP analog. Tang
et al. (2000) demonstrated that Sec31A and Sec13 coimmunoprecipitated
and that the proteins existed in a 600- to 700-kD complex.
Immunodepletion studies showed that rat Sec31a was required for
ER-to-Golgi vesicular transport.
Jin et al. (2012) found that monoubiquitination of Sec31 in mouse
embryonic stem cells by Klhl12 (614522) and the Cul3 (603136) E3
ubiquitin ligase complex was required for COPII vesicle expansion to
accommodate large cargo proteins, such as procollagens (see 120150). A
Sec31-binding mutant of Klhl12 neither colocalized with Sec31 at
intracellular vesicles nor induced formation of large vesicles.
Disruption of KLHL12-CUL3 function in human HT1080 fibrosarcoma cells
impaired COPII vesicle expansion and collagen export, but it had no
effect on export of smaller cargo by small COPII vesicles. Jin et al.
(2012) concluded that KLHL12-CUL3 monoubiquitination of SEC31 is
required for COPII vesicle expansion to accommodate large or bulky cargo
molecules.
MAPPING
By radiation hybrid analysis, Nagase et al. (1998) mapped the SEC31L1
gene to chromosome 4.
*FIELD* RF
1. Jin, L.; Pahuja, K. B.; Wickliffe, K. E.; Gorur, A.; Baumgartel,
C.; Schekman, R.; Rape, M.: Ubiquitin-dependent regulation of COPII
coat size and function. Nature 482: 495-500, 2012.
2. Nagase, T.; Ishikawa, K.; Suyama, M.; Kikuno, R.; Hirosawa, M.;
Miyajima, N.; Tanaka, A.; Kotani, H.; Nomura, N.; Oharo, O.: Prediction
of the coding sequences of unidentified human genes. XII. The complete
sequences of 100 new cDNA clones from brain which code for large proteins
in vitro. DNA Res. 5: 355-364, 1998.
3. Tang, B. L.; Zhang, T.; Low, D. Y. H.; Wong, E. T.; Horstmann,
H.; Hong, W.: Mammalian homologues of yeast Sec31p: an ubiquitously
expressed form is localized to endoplasmic reticulum (ER) exit sites
and is essential for ER-Golgi transport. J. Biol. Chem. 275: 13597-13604,
2000.
*FIELD* CN
Patricia A. Hartz - updated: 3/8/2012
*FIELD* CD
Patricia A. Hartz: 7/14/2006
*FIELD* ED
mgross: 03/08/2012
terry: 3/8/2012
mgross: 7/14/2006
*RECORD*
*FIELD* NO
610257
*FIELD* TI
*610257 SEC31, YEAST, HOMOLOG OF, A; SEC31A
;;SEC31-LIKE 1; SEC31L1;;
KIAA0905
*FIELD* TX
read more
DESCRIPTION
SEC31A is a subunit of coat protein complex II (COPII)-coated vesicles,
which are essential for secretion (Jin et al., 2012).
CLONING
By sequencing clones obtained from a size-fractionated adult brain cDNA
library, Nagase et al. (1998) cloned SEC31L1, which they designated
KIAA0905. The deduced protein contains 1,220 amino acids. RT-PCR
detected moderate expression in all adult and fetal tissues and specific
brain regions examined.
By searching EST databases for sequences similar to yeast Sec31,
followed by screening a pancreas cDNA library, Tang et al. (2000) cloned
SEC31L1, which they called SEC31A. The deduced 1,218-amino acid protein
shares 25.8% identity with yeast Sec31. It contains 5 WD40 or WD40-like
repeats at its N terminus and a proline-rich region in its C-terminal
half. Northern blot analysis detected a 4-kb transcript that was
abundantly and ubiquitously expressed. In rat kidney cells, Sec31a
colocalized with Sec13 (SEC13L1; 600152) in vesicular-tubular structures
characteristic of endoplasmic reticulum (ER) exit sites.
GENE FUNCTION
By immunostaining for Sec31a in intact and permeabilized rat kidney
cells, Tang et al. (2000) found that Sec31a was not tightly associated
with the membrane. Binding of Sec31a to specific membrane structures was
restored by incubating washed cells with cytosol, indicating that Sec31a
was recruited to membranes. The membrane association of Sec31a was
greatly enhanced in the presence of a nonhydrolyzable GTP analog. Tang
et al. (2000) demonstrated that Sec31A and Sec13 coimmunoprecipitated
and that the proteins existed in a 600- to 700-kD complex.
Immunodepletion studies showed that rat Sec31a was required for
ER-to-Golgi vesicular transport.
Jin et al. (2012) found that monoubiquitination of Sec31 in mouse
embryonic stem cells by Klhl12 (614522) and the Cul3 (603136) E3
ubiquitin ligase complex was required for COPII vesicle expansion to
accommodate large cargo proteins, such as procollagens (see 120150). A
Sec31-binding mutant of Klhl12 neither colocalized with Sec31 at
intracellular vesicles nor induced formation of large vesicles.
Disruption of KLHL12-CUL3 function in human HT1080 fibrosarcoma cells
impaired COPII vesicle expansion and collagen export, but it had no
effect on export of smaller cargo by small COPII vesicles. Jin et al.
(2012) concluded that KLHL12-CUL3 monoubiquitination of SEC31 is
required for COPII vesicle expansion to accommodate large or bulky cargo
molecules.
MAPPING
By radiation hybrid analysis, Nagase et al. (1998) mapped the SEC31L1
gene to chromosome 4.
*FIELD* RF
1. Jin, L.; Pahuja, K. B.; Wickliffe, K. E.; Gorur, A.; Baumgartel,
C.; Schekman, R.; Rape, M.: Ubiquitin-dependent regulation of COPII
coat size and function. Nature 482: 495-500, 2012.
2. Nagase, T.; Ishikawa, K.; Suyama, M.; Kikuno, R.; Hirosawa, M.;
Miyajima, N.; Tanaka, A.; Kotani, H.; Nomura, N.; Oharo, O.: Prediction
of the coding sequences of unidentified human genes. XII. The complete
sequences of 100 new cDNA clones from brain which code for large proteins
in vitro. DNA Res. 5: 355-364, 1998.
3. Tang, B. L.; Zhang, T.; Low, D. Y. H.; Wong, E. T.; Horstmann,
H.; Hong, W.: Mammalian homologues of yeast Sec31p: an ubiquitously
expressed form is localized to endoplasmic reticulum (ER) exit sites
and is essential for ER-Golgi transport. J. Biol. Chem. 275: 13597-13604,
2000.
*FIELD* CN
Patricia A. Hartz - updated: 3/8/2012
*FIELD* CD
Patricia A. Hartz: 7/14/2006
*FIELD* ED
mgross: 03/08/2012
terry: 3/8/2012
mgross: 7/14/2006