Full text data of SEC22B
SEC22B
(SEC22L1)
[Confidence: high (present in two of the MS resources)]
Vesicle-trafficking protein SEC22b (ER-Golgi SNARE of 24 kDa; ERS-24; ERS24; SEC22 vesicle-trafficking protein homolog B; SEC22 vesicle-trafficking protein-like 1)
Vesicle-trafficking protein SEC22b (ER-Golgi SNARE of 24 kDa; ERS-24; ERS24; SEC22 vesicle-trafficking protein homolog B; SEC22 vesicle-trafficking protein-like 1)
hRBCD
IPI00006865
IPI00006865 Vesicle trafficking protein SEC22b Vesicle trafficking protein SEC22b membrane n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a 2 2 n/a n/a 2 1 n/a n/a n/a Type IV membrane protein n/a found at its expected molecular weight found at molecular weight
IPI00006865 Vesicle trafficking protein SEC22b Vesicle trafficking protein SEC22b membrane n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a 2 2 n/a n/a 2 1 n/a n/a n/a Type IV membrane protein n/a found at its expected molecular weight found at molecular weight
UniProt
O75396
ID SC22B_HUMAN Reviewed; 215 AA.
AC O75396; A8K1G0;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-JAN-2011, sequence version 4.
DT 22-JAN-2014, entry version 123.
DE RecName: Full=Vesicle-trafficking protein SEC22b;
DE AltName: Full=ER-Golgi SNARE of 24 kDa;
DE Short=ERS-24;
DE Short=ERS24;
DE AltName: Full=SEC22 vesicle-trafficking protein homolog B;
DE AltName: Full=SEC22 vesicle-trafficking protein-like 1;
GN Name=SEC22B; Synonyms=SEC22L1;
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 [LARGE SCALE MRNA], AND VARIANTS TYR-71; LYS-82;
RP ARG-130 AND ARG-190.
RC TISSUE=Umbilical cord blood;
RX PubMed=9653160; DOI=10.1073/pnas.95.14.8175;
RA Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H.,
RA He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H.,
RA Wang Y.-X., Chen S.-J., Chen Z.;
RT "Identification of genes expressed in human CD34(+) hematopoietic
RT stem/progenitor cells by expressed sequence tags and efficient full-
RT length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS TYR-71; LYS-82;
RP ARG-130 AND ARG-190.
RC TISSUE=Caudate nucleus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS TYR-71; LYS-82;
RP ARG-130 AND ARG-190.
RC TISSUE=Skin;
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 [5]
RP PROTEIN SEQUENCE OF 2-9; 29-38 AND 134-147, CLEAVAGE OF INITIATOR
RP METHIONINE, AND MASS SPECTROMETRY.
RC TISSUE=Platelet;
RA Bienvenut W.V., Claeys D.;
RL Submitted (NOV-2005) to UniProtKB.
RN [6]
RP FUNCTION, AND INTERACTION WITH BNIP1; STX18 AND USE1L.
RX PubMed=15272311; DOI=10.1038/sj.emboj.7600333;
RA Nakajima K., Hirose H., Taniguchi M., Kurashina H., Arasaki K.,
RA Nagahama M., Tani K., Yamamoto A., Tagaya M.;
RT "Involvement of BNIP1 in apoptosis and endoplasmic reticulum membrane
RT fusion.";
RL EMBO J. 23:3216-3226(2004).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
RA Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND MASS
RP 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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-38, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND MASS
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137; THR-140 AND
RP SER-177, AND 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 [13]
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).
RN [14]
RP VARIANT [LARGE SCALE ANALYSIS] ARG-130, AND MASS SPECTROMETRY.
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).
CC -!- FUNCTION: SNARE involved in targeting and fusion of ER-derived
CC transport vesicles with the Golgi complex as well as Golgi-derived
CC retrograde transport vesicles with the ER.
CC -!- SUBUNIT: Interacts with STX17 (By similarity). Component of two
CC distinct SNARE complexes consisting of STX5, GOSR2/BOS1, BET1 and
CC SEC22B or STX18, USE1L, BNIP1/SEC20L and SEC22B. YKT6 can probably
CC replace SEC22B in either complex.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC type IV membrane protein (By similarity). Endoplasmic reticulum-
CC Golgi intermediate compartment membrane (By similarity). Golgi
CC apparatus, cis-Golgi network membrane (By similarity). Golgi
CC apparatus, trans-Golgi network membrane (By similarity).
CC Melanosome. Note=Concentrated most in the intermediate
CC compartment/cis-Golgi network and the cis-Golgi cisternae 1 and 2.
CC Greatly reduced in concentration at the trans end of the Golgi
CC apparatus. Identified by mass spectrometry in melanosome fractions
CC from stage I to stage IV.
CC -!- SIMILARITY: Belongs to the synaptobrevin family.
CC -!- SIMILARITY: Contains 1 longin domain.
CC -!- SIMILARITY: Contains 1 v-SNARE coiled-coil homology domain.
CC -!- CAUTION: The reference genome displays a polymorphic premature
CC stop codon in position 39.
CC -!- SEQUENCE CAUTION:
CC Sequence=AL359758; Type=Erroneous termination; Positions=39; Note=Translated as Gln;
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DR EMBL; AF047442; AAC39893.1; -; mRNA.
DR EMBL; AK289875; BAF82564.1; -; mRNA.
DR EMBL; AL359758; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX537145; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001364; AAH01364.1; -; mRNA.
DR RefSeq; NP_004883.3; NM_004892.5.
DR UniGene; Hs.632438; -.
DR PDB; 2NUP; X-ray; 2.80 A; C=1-195.
DR PDB; 2NUT; X-ray; 2.30 A; C=1-195.
DR PDB; 3EGD; X-ray; 2.70 A; C=1-157.
DR PDB; 3EGX; X-ray; 3.30 A; C=1-157.
DR PDBsum; 2NUP; -.
DR PDBsum; 2NUT; -.
DR PDBsum; 3EGD; -.
DR PDBsum; 3EGX; -.
DR ProteinModelPortal; O75396; -.
DR SMR; O75396; 1-157.
DR IntAct; O75396; 10.
DR MINT; MINT-5000824; -.
DR STRING; 9606.ENSP00000420824; -.
DR PhosphoSite; O75396; -.
DR PaxDb; O75396; -.
DR PeptideAtlas; O75396; -.
DR PRIDE; O75396; -.
DR DNASU; 9554; -.
DR GeneID; 9554; -.
DR KEGG; hsa:9554; -.
DR UCSC; uc031poa.1; human.
DR CTD; 9554; -.
DR GeneCards; GC01P145096; -.
DR HGNC; HGNC:10700; SEC22B.
DR MIM; 604029; gene.
DR neXtProt; NX_O75396; -.
DR PharmGKB; PA35623; -.
DR eggNOG; COG5143; -.
DR HOVERGEN; HBG052748; -.
DR KO; K08517; -.
DR EvolutionaryTrace; O75396; -.
DR GeneWiki; SEC22B; -.
DR GenomeRNAi; 9554; -.
DR NextBio; 35831; -.
DR PRO; PR:O75396; -.
DR CleanEx; HS_SEC22B; -.
DR Genevestigator; O75396; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; TAS:ProtInc.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.30.450.50; -; 1.
DR InterPro; IPR011012; Longin-like_dom.
DR InterPro; IPR010908; Longin_dom.
DR InterPro; IPR001388; Synaptobrevin.
DR Pfam; PF13774; Longin; 1.
DR Pfam; PF00957; Synaptobrevin; 1.
DR PRINTS; PR00219; SYNAPTOBREVN.
DR SUPFAM; SSF64356; SSF64356; 1.
DR PROSITE; PS50859; LONGIN; 1.
DR PROSITE; PS50892; V_SNARE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Coiled coil; Complete proteome;
KW Direct protein sequencing; Endoplasmic reticulum; ER-Golgi transport;
KW Golgi apparatus; Membrane; Phosphoprotein; Polymorphism;
KW Protein transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 215 Vesicle-trafficking protein SEC22b.
FT /FTId=PRO_0000206770.
FT TOPO_DOM 2 194 Cytoplasmic (Potential).
FT TRANSMEM 195 215 Helical; Anchor for type IV membrane
FT protein; (Potential).
FT DOMAIN 6 119 Longin.
FT DOMAIN 134 194 v-SNARE coiled-coil homology.
FT MOD_RES 38 38 N6-acetyllysine.
FT MOD_RES 137 137 Phosphoserine.
FT MOD_RES 140 140 Phosphothreonine.
FT MOD_RES 177 177 Phosphoserine.
FT VARIANT 71 71 D -> Y (in dbSNP:rs2596331).
FT /FTId=VAR_060311.
FT VARIANT 82 82 T -> K (in dbSNP:rs2794053).
FT /FTId=VAR_060312.
FT VARIANT 108 108 R -> Q (in dbSNP:rs2655551).
FT /FTId=VAR_057343.
FT VARIANT 130 130 C -> R (in dbSNP:rs2590131).
FT /FTId=VAR_060313.
FT VARIANT 190 190 H -> R (in dbSNP:rs2655557).
FT /FTId=VAR_060314.
FT VARIANT 214 214 W -> C (in dbSNP:rs7534444).
FT /FTId=VAR_057344.
FT STRAND 5 9
FT TURN 10 12
FT STRAND 15 19
FT HELIX 30 43
FT STRAND 50 56
FT STRAND 59 66
FT STRAND 69 76
FT HELIX 81 99
FT TURN 100 105
FT TURN 109 112
FT HELIX 113 115
FT HELIX 116 123
FT TURN 124 126
FT TURN 129 131
FT STRAND 150 152
FT HELIX 153 156
SQ SEQUENCE 215 AA; 24593 MW; 9FA59C20F2D3F690 CRC64;
MVLLTMIARV ADGLPLAASM QEDEQSGRDL QQYQSQAKQL FRKLNEQSPT RCTLEAGAMT
FHYIIEQGVC DLVLCEAAFP KTLAFAYLED LHSEFDEQHG KKVPTVSRPY SFIEFDTFIQ
KTKKLYIDSC ARRNLGSINT ELQDVQRIMV ANIEEVLQRG EALSALDSKA NNLSSLSKKY
RQDAKYLNMH STYAKLAAVA VFFIMLIVYV RFWWL
//
ID SC22B_HUMAN Reviewed; 215 AA.
AC O75396; A8K1G0;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-JAN-2011, sequence version 4.
DT 22-JAN-2014, entry version 123.
DE RecName: Full=Vesicle-trafficking protein SEC22b;
DE AltName: Full=ER-Golgi SNARE of 24 kDa;
DE Short=ERS-24;
DE Short=ERS24;
DE AltName: Full=SEC22 vesicle-trafficking protein homolog B;
DE AltName: Full=SEC22 vesicle-trafficking protein-like 1;
GN Name=SEC22B; Synonyms=SEC22L1;
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 [LARGE SCALE MRNA], AND VARIANTS TYR-71; LYS-82;
RP ARG-130 AND ARG-190.
RC TISSUE=Umbilical cord blood;
RX PubMed=9653160; DOI=10.1073/pnas.95.14.8175;
RA Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H.,
RA He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H.,
RA Wang Y.-X., Chen S.-J., Chen Z.;
RT "Identification of genes expressed in human CD34(+) hematopoietic
RT stem/progenitor cells by expressed sequence tags and efficient full-
RT length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS TYR-71; LYS-82;
RP ARG-130 AND ARG-190.
RC TISSUE=Caudate nucleus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS TYR-71; LYS-82;
RP ARG-130 AND ARG-190.
RC TISSUE=Skin;
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 [5]
RP PROTEIN SEQUENCE OF 2-9; 29-38 AND 134-147, CLEAVAGE OF INITIATOR
RP METHIONINE, AND MASS SPECTROMETRY.
RC TISSUE=Platelet;
RA Bienvenut W.V., Claeys D.;
RL Submitted (NOV-2005) to UniProtKB.
RN [6]
RP FUNCTION, AND INTERACTION WITH BNIP1; STX18 AND USE1L.
RX PubMed=15272311; DOI=10.1038/sj.emboj.7600333;
RA Nakajima K., Hirose H., Taniguchi M., Kurashina H., Arasaki K.,
RA Nagahama M., Tani K., Yamamoto A., Tagaya M.;
RT "Involvement of BNIP1 in apoptosis and endoplasmic reticulum membrane
RT fusion.";
RL EMBO J. 23:3216-3226(2004).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
RA Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND MASS
RP 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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-38, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND MASS
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137; THR-140 AND
RP SER-177, AND 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 [13]
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).
RN [14]
RP VARIANT [LARGE SCALE ANALYSIS] ARG-130, AND MASS SPECTROMETRY.
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).
CC -!- FUNCTION: SNARE involved in targeting and fusion of ER-derived
CC transport vesicles with the Golgi complex as well as Golgi-derived
CC retrograde transport vesicles with the ER.
CC -!- SUBUNIT: Interacts with STX17 (By similarity). Component of two
CC distinct SNARE complexes consisting of STX5, GOSR2/BOS1, BET1 and
CC SEC22B or STX18, USE1L, BNIP1/SEC20L and SEC22B. YKT6 can probably
CC replace SEC22B in either complex.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC type IV membrane protein (By similarity). Endoplasmic reticulum-
CC Golgi intermediate compartment membrane (By similarity). Golgi
CC apparatus, cis-Golgi network membrane (By similarity). Golgi
CC apparatus, trans-Golgi network membrane (By similarity).
CC Melanosome. Note=Concentrated most in the intermediate
CC compartment/cis-Golgi network and the cis-Golgi cisternae 1 and 2.
CC Greatly reduced in concentration at the trans end of the Golgi
CC apparatus. Identified by mass spectrometry in melanosome fractions
CC from stage I to stage IV.
CC -!- SIMILARITY: Belongs to the synaptobrevin family.
CC -!- SIMILARITY: Contains 1 longin domain.
CC -!- SIMILARITY: Contains 1 v-SNARE coiled-coil homology domain.
CC -!- CAUTION: The reference genome displays a polymorphic premature
CC stop codon in position 39.
CC -!- SEQUENCE CAUTION:
CC Sequence=AL359758; Type=Erroneous termination; Positions=39; Note=Translated as Gln;
CC -----------------------------------------------------------------------
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DR EMBL; AF047442; AAC39893.1; -; mRNA.
DR EMBL; AK289875; BAF82564.1; -; mRNA.
DR EMBL; AL359758; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX537145; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001364; AAH01364.1; -; mRNA.
DR RefSeq; NP_004883.3; NM_004892.5.
DR UniGene; Hs.632438; -.
DR PDB; 2NUP; X-ray; 2.80 A; C=1-195.
DR PDB; 2NUT; X-ray; 2.30 A; C=1-195.
DR PDB; 3EGD; X-ray; 2.70 A; C=1-157.
DR PDB; 3EGX; X-ray; 3.30 A; C=1-157.
DR PDBsum; 2NUP; -.
DR PDBsum; 2NUT; -.
DR PDBsum; 3EGD; -.
DR PDBsum; 3EGX; -.
DR ProteinModelPortal; O75396; -.
DR SMR; O75396; 1-157.
DR IntAct; O75396; 10.
DR MINT; MINT-5000824; -.
DR STRING; 9606.ENSP00000420824; -.
DR PhosphoSite; O75396; -.
DR PaxDb; O75396; -.
DR PeptideAtlas; O75396; -.
DR PRIDE; O75396; -.
DR DNASU; 9554; -.
DR GeneID; 9554; -.
DR KEGG; hsa:9554; -.
DR UCSC; uc031poa.1; human.
DR CTD; 9554; -.
DR GeneCards; GC01P145096; -.
DR HGNC; HGNC:10700; SEC22B.
DR MIM; 604029; gene.
DR neXtProt; NX_O75396; -.
DR PharmGKB; PA35623; -.
DR eggNOG; COG5143; -.
DR HOVERGEN; HBG052748; -.
DR KO; K08517; -.
DR EvolutionaryTrace; O75396; -.
DR GeneWiki; SEC22B; -.
DR GenomeRNAi; 9554; -.
DR NextBio; 35831; -.
DR PRO; PR:O75396; -.
DR CleanEx; HS_SEC22B; -.
DR Genevestigator; O75396; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; TAS:ProtInc.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.30.450.50; -; 1.
DR InterPro; IPR011012; Longin-like_dom.
DR InterPro; IPR010908; Longin_dom.
DR InterPro; IPR001388; Synaptobrevin.
DR Pfam; PF13774; Longin; 1.
DR Pfam; PF00957; Synaptobrevin; 1.
DR PRINTS; PR00219; SYNAPTOBREVN.
DR SUPFAM; SSF64356; SSF64356; 1.
DR PROSITE; PS50859; LONGIN; 1.
DR PROSITE; PS50892; V_SNARE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Coiled coil; Complete proteome;
KW Direct protein sequencing; Endoplasmic reticulum; ER-Golgi transport;
KW Golgi apparatus; Membrane; Phosphoprotein; Polymorphism;
KW Protein transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 215 Vesicle-trafficking protein SEC22b.
FT /FTId=PRO_0000206770.
FT TOPO_DOM 2 194 Cytoplasmic (Potential).
FT TRANSMEM 195 215 Helical; Anchor for type IV membrane
FT protein; (Potential).
FT DOMAIN 6 119 Longin.
FT DOMAIN 134 194 v-SNARE coiled-coil homology.
FT MOD_RES 38 38 N6-acetyllysine.
FT MOD_RES 137 137 Phosphoserine.
FT MOD_RES 140 140 Phosphothreonine.
FT MOD_RES 177 177 Phosphoserine.
FT VARIANT 71 71 D -> Y (in dbSNP:rs2596331).
FT /FTId=VAR_060311.
FT VARIANT 82 82 T -> K (in dbSNP:rs2794053).
FT /FTId=VAR_060312.
FT VARIANT 108 108 R -> Q (in dbSNP:rs2655551).
FT /FTId=VAR_057343.
FT VARIANT 130 130 C -> R (in dbSNP:rs2590131).
FT /FTId=VAR_060313.
FT VARIANT 190 190 H -> R (in dbSNP:rs2655557).
FT /FTId=VAR_060314.
FT VARIANT 214 214 W -> C (in dbSNP:rs7534444).
FT /FTId=VAR_057344.
FT STRAND 5 9
FT TURN 10 12
FT STRAND 15 19
FT HELIX 30 43
FT STRAND 50 56
FT STRAND 59 66
FT STRAND 69 76
FT HELIX 81 99
FT TURN 100 105
FT TURN 109 112
FT HELIX 113 115
FT HELIX 116 123
FT TURN 124 126
FT TURN 129 131
FT STRAND 150 152
FT HELIX 153 156
SQ SEQUENCE 215 AA; 24593 MW; 9FA59C20F2D3F690 CRC64;
MVLLTMIARV ADGLPLAASM QEDEQSGRDL QQYQSQAKQL FRKLNEQSPT RCTLEAGAMT
FHYIIEQGVC DLVLCEAAFP KTLAFAYLED LHSEFDEQHG KKVPTVSRPY SFIEFDTFIQ
KTKKLYIDSC ARRNLGSINT ELQDVQRIMV ANIEEVLQRG EALSALDSKA NNLSSLSKKY
RQDAKYLNMH STYAKLAAVA VFFIMLIVYV RFWWL
//
MIM
604029
*RECORD*
*FIELD* NO
604029
*FIELD* TI
*604029 SECRETION DEFICIENT 22, S. CEREVISIAE, HOMOLOG-LIKE 1; SEC22L1
;;SEC22B
*FIELD* TX
read more
CLONING
Hay et al. (1997) isolated mouse Sec22b cDNAs and determined that the
Sec22b protein is distinct from the previously identified rat SEC22A
protein (612442). Sequence analysis revealed that mouse Sec22b is a
cytoplasmically oriented, C-terminally anchored integral membrane
protein.
Mao et al. (1998) identified an umbilical cord blood CD34-positive cell
cDNA encoding the human homolog of Sec22b. The predicted human protein
contains 215 amino acids.
MAPPING
By analysis of radiation hybrids, Mao et al. (1998) mapped the human
SEC22B gene to chromosome 1q21.2-q21.3.
GENE FUNCTION
In S. cerevisiae, the vesicle trafficking protein complexes directing
transport between the endoplasmic reticulum (ER) and Golgi appear to
include Sed5 (see syntaxin-5; 603189), proposed to be a cis-Golgi
receptor protein, and Sec22 and Bet1 (605456), potential Sed5 docking
partners localized on ER-derived vesicles. The Sly1 protein may bind to
and regulate the activity of Sed5 for docking with ER-derived vesicle
proteins. See membrin (GOSR2; 604027). Hay et al. (1997) isolated a rat
liver protein complex representing an intermediate in ER-to-Golgi
transfer reactions. The complex contained syntaxin-5, GOS28 (604026),
the rat homologs of Bet1 and Sly1, and 2 novel proteins, rat SEC22B and
membrin. By immunofluorescence of mammalian cells expressing
epitope-tagged mouse Sec22b, Hay et al. (1997) found that Sec22b and
membrin accumulated primarily at the ER. Other members of the complex
localized to Golgi membranes, indicating that the complex recapitulates
vesicle docking between distinct organelles in the ER/Golgi transport
cycle. Expression of recombinant membrin and Sec22b disrupted normal
trafficking, demonstrating that these proteins regulate ER-to-Golgi
trafficking.
To fuse transport vesicles with target membranes, proteins of the SNARE
complex must be located on both the vesicle and the target membrane. In
yeast, 4 integral membrane proteins, Sed5, Bos1, Sec22, and Bet1 each
are believed to contribute a single helix to form the SNARE complex that
is needed for transport from endoplasmic reticulum to Golgi. This
generates a 4-helix bundle, which ultimately mediates the actual fusion
event. Parlati et al. (2000) explored how the anchoring arrangement of
the 4 helices affects their ability to mediate fusion. Parlati et al.
(2000) reconstituted 2 populations of phospholipid bilayer vesicles,
with the individual SNARE proteins distributed in all possible
combinations between them. Of the 8 nonredundant permutations of 4
subunits distributed over 2 vesicle populations, only 1 resulted in
membrane fusion. Fusion occurred only when the v-SNARE Bet1 is on 1
membrane and the syntaxin heavy chain Sed5 and its 2 light chains, Bos1
and Sec22, are on the other membrane, where they form a functional
t-SNARE. Thus, each SNARE protein is topologically restricted by design
to function either as a v-SNARE or as part of a t-SNARE complex.
*FIELD* RF
1. Hay, J. C.; Chao, D. S.; Kuo, C. S.; Scheller, R. H.: Protein
interactions regulating vesicle transport between the endoplasmic
reticulum and Golgi apparatus in mammalian cells. Cell 89: 149-158,
1997.
2. Mao, M.; Fu, G.; Wu, J.-S.; Zhang, Q.-H.; Zhou, J.; Kan, L.-X.;
Huang, Q.-H.; He, K.-L.; Gu, B.-W.; Han, Z.-G.; Shen, Y.; Gu, J.;
Yu, Y.-P.; Xu, S.-H.; Wang, Y.-X.; Chen, S.-J.; Chen, Z.: Identification
of genes expressed in human CD34+ hematopoietic stem/progenitor cells
by expressed sequence tags and efficient full-length cDNA cloning. Proc.
Nat. Acad. Sci. 95: 8175-8180, 1998.
3. Parlati, F.; McNew, J. A.; Fukuda, R.; Miller, R.; Sollner, T.
H.; Rothman, J. E.: Topological restriction of SNARE-dependent membrane
fusion. Nature 407: 194-198, 2000.
*FIELD* CN
Ada Hamosh - updated: 9/13/2000
*FIELD* CD
Rebekah S. Rasooly: 7/19/1999
*FIELD* ED
carol: 11/25/2008
mgross: 12/6/2000
alopez: 9/13/2000
alopez: 7/19/1999
*RECORD*
*FIELD* NO
604029
*FIELD* TI
*604029 SECRETION DEFICIENT 22, S. CEREVISIAE, HOMOLOG-LIKE 1; SEC22L1
;;SEC22B
*FIELD* TX
read more
CLONING
Hay et al. (1997) isolated mouse Sec22b cDNAs and determined that the
Sec22b protein is distinct from the previously identified rat SEC22A
protein (612442). Sequence analysis revealed that mouse Sec22b is a
cytoplasmically oriented, C-terminally anchored integral membrane
protein.
Mao et al. (1998) identified an umbilical cord blood CD34-positive cell
cDNA encoding the human homolog of Sec22b. The predicted human protein
contains 215 amino acids.
MAPPING
By analysis of radiation hybrids, Mao et al. (1998) mapped the human
SEC22B gene to chromosome 1q21.2-q21.3.
GENE FUNCTION
In S. cerevisiae, the vesicle trafficking protein complexes directing
transport between the endoplasmic reticulum (ER) and Golgi appear to
include Sed5 (see syntaxin-5; 603189), proposed to be a cis-Golgi
receptor protein, and Sec22 and Bet1 (605456), potential Sed5 docking
partners localized on ER-derived vesicles. The Sly1 protein may bind to
and regulate the activity of Sed5 for docking with ER-derived vesicle
proteins. See membrin (GOSR2; 604027). Hay et al. (1997) isolated a rat
liver protein complex representing an intermediate in ER-to-Golgi
transfer reactions. The complex contained syntaxin-5, GOS28 (604026),
the rat homologs of Bet1 and Sly1, and 2 novel proteins, rat SEC22B and
membrin. By immunofluorescence of mammalian cells expressing
epitope-tagged mouse Sec22b, Hay et al. (1997) found that Sec22b and
membrin accumulated primarily at the ER. Other members of the complex
localized to Golgi membranes, indicating that the complex recapitulates
vesicle docking between distinct organelles in the ER/Golgi transport
cycle. Expression of recombinant membrin and Sec22b disrupted normal
trafficking, demonstrating that these proteins regulate ER-to-Golgi
trafficking.
To fuse transport vesicles with target membranes, proteins of the SNARE
complex must be located on both the vesicle and the target membrane. In
yeast, 4 integral membrane proteins, Sed5, Bos1, Sec22, and Bet1 each
are believed to contribute a single helix to form the SNARE complex that
is needed for transport from endoplasmic reticulum to Golgi. This
generates a 4-helix bundle, which ultimately mediates the actual fusion
event. Parlati et al. (2000) explored how the anchoring arrangement of
the 4 helices affects their ability to mediate fusion. Parlati et al.
(2000) reconstituted 2 populations of phospholipid bilayer vesicles,
with the individual SNARE proteins distributed in all possible
combinations between them. Of the 8 nonredundant permutations of 4
subunits distributed over 2 vesicle populations, only 1 resulted in
membrane fusion. Fusion occurred only when the v-SNARE Bet1 is on 1
membrane and the syntaxin heavy chain Sed5 and its 2 light chains, Bos1
and Sec22, are on the other membrane, where they form a functional
t-SNARE. Thus, each SNARE protein is topologically restricted by design
to function either as a v-SNARE or as part of a t-SNARE complex.
*FIELD* RF
1. Hay, J. C.; Chao, D. S.; Kuo, C. S.; Scheller, R. H.: Protein
interactions regulating vesicle transport between the endoplasmic
reticulum and Golgi apparatus in mammalian cells. Cell 89: 149-158,
1997.
2. Mao, M.; Fu, G.; Wu, J.-S.; Zhang, Q.-H.; Zhou, J.; Kan, L.-X.;
Huang, Q.-H.; He, K.-L.; Gu, B.-W.; Han, Z.-G.; Shen, Y.; Gu, J.;
Yu, Y.-P.; Xu, S.-H.; Wang, Y.-X.; Chen, S.-J.; Chen, Z.: Identification
of genes expressed in human CD34+ hematopoietic stem/progenitor cells
by expressed sequence tags and efficient full-length cDNA cloning. Proc.
Nat. Acad. Sci. 95: 8175-8180, 1998.
3. Parlati, F.; McNew, J. A.; Fukuda, R.; Miller, R.; Sollner, T.
H.; Rothman, J. E.: Topological restriction of SNARE-dependent membrane
fusion. Nature 407: 194-198, 2000.
*FIELD* CN
Ada Hamosh - updated: 9/13/2000
*FIELD* CD
Rebekah S. Rasooly: 7/19/1999
*FIELD* ED
carol: 11/25/2008
mgross: 12/6/2000
alopez: 9/13/2000
alopez: 7/19/1999