Full text data of SEC13
SEC13
(D3S1231E, SEC13L1, SEC13R)
[Confidence: low (only semi-automatic identification from reviews)]
Protein SEC13 homolog (SEC13-like protein 1; SEC13-related protein)
Protein SEC13 homolog (SEC13-like protein 1; SEC13-related protein)
UniProt
P55735
ID SEC13_HUMAN Reviewed; 322 AA.
AC P55735; A8MV37; Q5BJF0; Q9BRM6; Q9BUG7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 132.
DE RecName: Full=Protein SEC13 homolog;
DE AltName: Full=SEC13-like protein 1;
DE AltName: Full=SEC13-related protein;
GN Name=SEC13; Synonyms=D3S1231E, SEC13L1, SEC13R;
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).
RX PubMed=7987303; DOI=10.1093/hmg/3.8.1281;
RA Swaroop A., Yang-Feng T.L., Liu W., Gieser L., Barrow L.L., Chen K.C.,
RA Agarwal N., Meisler M.H., Smith D.I.;
RT "Molecular characterization of a novel human gene, SEC13R, related to
RT the yeast secretory pathway gene SEC13, and mapping to a conserved
RT linkage group on human chromosome 3p24-p25 and mouse chromosome 6.";
RL Hum. Mol. Genet. 3:1281-1286(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=9110174;
RA Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W.,
RA Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
RT "Large-scale concatenation cDNA sequencing.";
RL Genome Res. 7:353-358(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta, and Uterus;
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 2-27.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [6]
RP PROTEIN SEQUENCE OF 2-27; 44-54; 217-256 AND 291-322, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT VAL-2, AND MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [7]
RP PROTEIN SEQUENCE OF 182-192; 217-239 AND 291-322, AND MASS
RP SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8972206;
RA Tang B.L., Peter F., Krijnse-Locker J., Low S.H., Griffiths G.,
RA Hong W.;
RT "The mammalian homolog of yeast Sec13p is enriched in the intermediate
RT compartment and is essential for protein transport from the
RT endoplasmic reticulum to the Golgi apparatus.";
RL Mol. Cell. Biol. 17:256-266(1997).
RN [9]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH NUP96.
RX PubMed=14517296; DOI=10.1128/MCB.23.20.7271-7284.2003;
RA Enninga J., Levay A., Fontoura B.M.;
RT "Sec13 shuttles between the nucleus and the cytoplasm and stably
RT interacts with Nup96 at the nuclear pore complex.";
RL Mol. Cell. Biol. 23:7271-7284(2003).
RN [10]
RP INTERACTION WITH SEC31B.
RX PubMed=16495487; DOI=10.1242/jcs.02751;
RA Stankewich M.C., Stabach P.R., Morrow J.S.;
RT "Human Sec31B: a family of new mammalian orthologues of yeast Sec31p
RT that associate with the COPII coat.";
RL J. Cell Sci. 119:958-969(2006).
RN [11]
RP INTERACTION WITH SEC31A.
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309, 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 [14]
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 [15]
RP FUNCTION, IDENTIFICATION IN GATOR COMPLEX, AND INTERACTION WITH RRAG
RP PROTEINS.
RX PubMed=23723238; DOI=10.1126/science.1232044;
RA Bar-Peled L., Chantranupong L., Cherniack A.D., Chen W.W.,
RA Ottina K.A., Grabiner B.C., Spear E.D., Carter S.L., Meyerson M.,
RA Sabatini D.M.;
RT "A Tumor suppressor complex with GAP activity for the Rag GTPases that
RT signal amino acid sufficiency to mTORC1.";
RL Science 340:1100-1106(2013).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-316 IN COMPLEX WITH YEAST
RP NUP145C, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=18160040; DOI=10.1016/j.cell.2007.11.038;
RA Hsia K.C., Stavropoulos P., Blobel G., Hoelz A.;
RT "Architecture of a coat for the nuclear pore membrane.";
RL Cell 131:1313-1326(2007).
CC -!- FUNCTION: Functions as a component of the nuclear pore complex
CC (NPC) and the COPII coat. At the endoplasmic reticulum, SEC13 is
CC involved in the biogenesis of COPII-coated vesicles. As a
CC component of the GATOR2 complex, inhibits GATOR1 complex, an
CC inhibitor of the amino acid-sensing branch of the TORC1 pathway.
CC -!- SUBUNIT: At the nuclear pore: component of the Y-shaped Nup107-160
CC subcomplex of the nuclear pore complex (NPC). The Nup107-160
CC subcomplex includes NUP160, NUP133, NUP107, NUP98, NUP85, NUP43,
CC NUP37, SEH1 and SEC13. At the COPII coat complex: interacts with
CC SEC31A and SEC31B. Within the GATOR complex, component of the
CC GATOR2 subcomplex, made of MIOS, SEC13, SEH1L, WDR24 and WDR59.
CC The GATOR complex strongly interacts with RRAGA/RRAGC and
CC RRAGB/RRAGC heterodimers.
CC -!- INTERACTION:
CC P49687:NUP145 (xeno); NbExp=9; IntAct=EBI-1046596, EBI-11730;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC membrane; Peripheral membrane protein; Cytoplasmic side.
CC Endoplasmic reticulum membrane; Peripheral membrane protein;
CC Cytoplasmic side. Nucleus, nuclear pore complex. Note=In
CC interphase, localizes at both sides of the NPC.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P55735-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P55735-2; Sequence=VSP_046191;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the WD repeat SEC13 family.
CC -!- SIMILARITY: Contains 6 WD repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH02634.2; Type=Erroneous initiation;
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DR EMBL; L09260; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AF052155; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC022384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002634; AAH02634.2; ALT_INIT; mRNA.
DR EMBL; BC006167; AAH06167.1; -; mRNA.
DR EMBL; BC091506; AAH91506.1; -; mRNA.
DR RefSeq; NP_001129498.1; NM_001136026.2.
DR RefSeq; NP_001129704.1; NM_001136232.2.
DR RefSeq; NP_109598.2; NM_030673.3.
DR RefSeq; NP_899195.1; NM_183352.2.
DR RefSeq; XP_005265436.1; XM_005265379.1.
DR UniGene; Hs.166924; -.
DR PDB; 3BG0; X-ray; 3.15 A; A/D/E/H=1-316.
DR PDB; 3BG1; X-ray; 3.00 A; A/D/E/H=1-316.
DR PDBsum; 3BG0; -.
DR PDBsum; 3BG1; -.
DR ProteinModelPortal; P55735; -.
DR SMR; P55735; 14-304.
DR DIP; DIP-39091N; -.
DR IntAct; P55735; 15.
DR MINT; MINT-1154053; -.
DR STRING; 9606.ENSP00000312122; -.
DR PhosphoSite; P55735; -.
DR DMDM; 50403748; -.
DR PaxDb; P55735; -.
DR PRIDE; P55735; -.
DR DNASU; 6396; -.
DR Ensembl; ENST00000337354; ENSP00000336566; ENSG00000157020.
DR Ensembl; ENST00000350697; ENSP00000312122; ENSG00000157020.
DR Ensembl; ENST00000397109; ENSP00000380298; ENSG00000157020.
DR GeneID; 6396; -.
DR KEGG; hsa:6396; -.
DR UCSC; uc003bvl.3; human.
DR CTD; 6396; -.
DR GeneCards; GC03M010337; -.
DR HGNC; HGNC:10697; SEC13.
DR HPA; HPA035292; -.
DR MIM; 600152; gene.
DR neXtProt; NX_P55735; -.
DR PharmGKB; PA35620; -.
DR eggNOG; COG2319; -.
DR HOGENOM; HOG000216895; -.
DR HOVERGEN; HBG057343; -.
DR InParanoid; P55735; -.
DR KO; K14004; -.
DR OrthoDB; EOG7966GP; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; P55735; -.
DR EvolutionaryTrace; P55735; -.
DR GeneWiki; SEC13; -.
DR GenomeRNAi; 6396; -.
DR NextBio; 24846; -.
DR PRO; PR:P55735; -.
DR ArrayExpress; P55735; -.
DR Bgee; P55735; -.
DR CleanEx; HS_SEC13; -.
DR Genevestigator; P55735; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
DR GO; GO:0031080; C:nuclear pore outer ring; IDA:UniProtKB.
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:0006886; P:intracellular protein transport; NAS:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; TAS:Reactome.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
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 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; 6.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasmic vesicle; Direct protein sequencing; Endoplasmic reticulum;
KW ER-Golgi transport; Membrane; mRNA transport; Nuclear pore complex;
KW Nucleus; Phosphoprotein; Polymorphism; Protein transport;
KW Reference proteome; Repeat; Translocation; Transport; WD repeat.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 322 Protein SEC13 homolog.
FT /FTId=PRO_0000051203.
FT REPEAT 11 50 WD 1.
FT REPEAT 55 96 WD 2.
FT REPEAT 101 144 WD 3.
FT REPEAT 148 204 WD 4.
FT REPEAT 210 253 WD 5.
FT REPEAT 260 299 WD 6.
FT MOD_RES 2 2 N-acetylvaline.
FT MOD_RES 309 309 Phosphoserine.
FT VAR_SEQ 1 14 Missing (in isoform 2).
FT /FTId=VSP_046191.
FT VARIANT 172 172 S -> L (in dbSNP:rs34078590).
FT /FTId=VAR_053413.
FT CONFLICT 51 51 A -> V (in Ref. 1; L09260).
FT STRAND 16 21
FT HELIX 23 25
FT STRAND 27 32
FT STRAND 35 43
FT STRAND 46 54
FT STRAND 60 65
FT HELIX 68 70
FT STRAND 74 78
FT STRAND 83 86
FT STRAND 89 91
FT STRAND 95 99
FT STRAND 108 111
FT TURN 114 116
FT STRAND 120 123
FT STRAND 125 127
FT STRAND 129 134
FT STRAND 136 138
FT STRAND 140 142
FT STRAND 148 151
FT STRAND 181 183
FT STRAND 193 196
FT STRAND 202 206
FT STRAND 215 219
FT STRAND 230 235
FT STRAND 239 244
FT STRAND 246 249
FT STRAND 257 260
FT STRAND 265 270
FT TURN 272 274
FT STRAND 277 284
FT STRAND 286 291
FT STRAND 297 302
SQ SEQUENCE 322 AA; 35541 MW; 18E29627D87FB3DD CRC64;
MVSVINTVDT SHEDMIHDAQ MDYYGTRLAT CSSDRSVKIF DVRNGGQILI ADLRGHEGPV
WQVAWAHPMY GNILASCSYD RKVIIWREEN GTWEKSHEHA GHDSSVNSVC WAPHDYGLIL
ACGSSDGAIS LLTYTGEGQW EVKKINNAHT IGCNAVSWAP AVVPGSLIDH PSGQKPNYIK
RFASGGCDNL IKLWKEEEDG QWKEEQKLEA HSDWVRDVAW APSIGLPTST IASCSQDGRV
FIWTCDDASS NTWSPKLLHK FNDVVWHVSW SITANILAVS GGDNKVTLWK ESVDGQWVCI
SDVNKGQGSV SASVTEGQQN EQ
//
ID SEC13_HUMAN Reviewed; 322 AA.
AC P55735; A8MV37; Q5BJF0; Q9BRM6; Q9BUG7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 132.
DE RecName: Full=Protein SEC13 homolog;
DE AltName: Full=SEC13-like protein 1;
DE AltName: Full=SEC13-related protein;
GN Name=SEC13; Synonyms=D3S1231E, SEC13L1, SEC13R;
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).
RX PubMed=7987303; DOI=10.1093/hmg/3.8.1281;
RA Swaroop A., Yang-Feng T.L., Liu W., Gieser L., Barrow L.L., Chen K.C.,
RA Agarwal N., Meisler M.H., Smith D.I.;
RT "Molecular characterization of a novel human gene, SEC13R, related to
RT the yeast secretory pathway gene SEC13, and mapping to a conserved
RT linkage group on human chromosome 3p24-p25 and mouse chromosome 6.";
RL Hum. Mol. Genet. 3:1281-1286(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=9110174;
RA Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W.,
RA Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
RT "Large-scale concatenation cDNA sequencing.";
RL Genome Res. 7:353-358(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta, and Uterus;
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 2-27.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [6]
RP PROTEIN SEQUENCE OF 2-27; 44-54; 217-256 AND 291-322, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT VAL-2, AND MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [7]
RP PROTEIN SEQUENCE OF 182-192; 217-239 AND 291-322, AND MASS
RP SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8972206;
RA Tang B.L., Peter F., Krijnse-Locker J., Low S.H., Griffiths G.,
RA Hong W.;
RT "The mammalian homolog of yeast Sec13p is enriched in the intermediate
RT compartment and is essential for protein transport from the
RT endoplasmic reticulum to the Golgi apparatus.";
RL Mol. Cell. Biol. 17:256-266(1997).
RN [9]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH NUP96.
RX PubMed=14517296; DOI=10.1128/MCB.23.20.7271-7284.2003;
RA Enninga J., Levay A., Fontoura B.M.;
RT "Sec13 shuttles between the nucleus and the cytoplasm and stably
RT interacts with Nup96 at the nuclear pore complex.";
RL Mol. Cell. Biol. 23:7271-7284(2003).
RN [10]
RP INTERACTION WITH SEC31B.
RX PubMed=16495487; DOI=10.1242/jcs.02751;
RA Stankewich M.C., Stabach P.R., Morrow J.S.;
RT "Human Sec31B: a family of new mammalian orthologues of yeast Sec31p
RT that associate with the COPII coat.";
RL J. Cell Sci. 119:958-969(2006).
RN [11]
RP INTERACTION WITH SEC31A.
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309, 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 [14]
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 [15]
RP FUNCTION, IDENTIFICATION IN GATOR COMPLEX, AND INTERACTION WITH RRAG
RP PROTEINS.
RX PubMed=23723238; DOI=10.1126/science.1232044;
RA Bar-Peled L., Chantranupong L., Cherniack A.D., Chen W.W.,
RA Ottina K.A., Grabiner B.C., Spear E.D., Carter S.L., Meyerson M.,
RA Sabatini D.M.;
RT "A Tumor suppressor complex with GAP activity for the Rag GTPases that
RT signal amino acid sufficiency to mTORC1.";
RL Science 340:1100-1106(2013).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-316 IN COMPLEX WITH YEAST
RP NUP145C, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=18160040; DOI=10.1016/j.cell.2007.11.038;
RA Hsia K.C., Stavropoulos P., Blobel G., Hoelz A.;
RT "Architecture of a coat for the nuclear pore membrane.";
RL Cell 131:1313-1326(2007).
CC -!- FUNCTION: Functions as a component of the nuclear pore complex
CC (NPC) and the COPII coat. At the endoplasmic reticulum, SEC13 is
CC involved in the biogenesis of COPII-coated vesicles. As a
CC component of the GATOR2 complex, inhibits GATOR1 complex, an
CC inhibitor of the amino acid-sensing branch of the TORC1 pathway.
CC -!- SUBUNIT: At the nuclear pore: component of the Y-shaped Nup107-160
CC subcomplex of the nuclear pore complex (NPC). The Nup107-160
CC subcomplex includes NUP160, NUP133, NUP107, NUP98, NUP85, NUP43,
CC NUP37, SEH1 and SEC13. At the COPII coat complex: interacts with
CC SEC31A and SEC31B. Within the GATOR complex, component of the
CC GATOR2 subcomplex, made of MIOS, SEC13, SEH1L, WDR24 and WDR59.
CC The GATOR complex strongly interacts with RRAGA/RRAGC and
CC RRAGB/RRAGC heterodimers.
CC -!- INTERACTION:
CC P49687:NUP145 (xeno); NbExp=9; IntAct=EBI-1046596, EBI-11730;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC membrane; Peripheral membrane protein; Cytoplasmic side.
CC Endoplasmic reticulum membrane; Peripheral membrane protein;
CC Cytoplasmic side. Nucleus, nuclear pore complex. Note=In
CC interphase, localizes at both sides of the NPC.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P55735-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P55735-2; Sequence=VSP_046191;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the WD repeat SEC13 family.
CC -!- SIMILARITY: Contains 6 WD repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH02634.2; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
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CC Distributed under the Creative Commons Attribution-NoDerivs License
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DR EMBL; L09260; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AF052155; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC022384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002634; AAH02634.2; ALT_INIT; mRNA.
DR EMBL; BC006167; AAH06167.1; -; mRNA.
DR EMBL; BC091506; AAH91506.1; -; mRNA.
DR RefSeq; NP_001129498.1; NM_001136026.2.
DR RefSeq; NP_001129704.1; NM_001136232.2.
DR RefSeq; NP_109598.2; NM_030673.3.
DR RefSeq; NP_899195.1; NM_183352.2.
DR RefSeq; XP_005265436.1; XM_005265379.1.
DR UniGene; Hs.166924; -.
DR PDB; 3BG0; X-ray; 3.15 A; A/D/E/H=1-316.
DR PDB; 3BG1; X-ray; 3.00 A; A/D/E/H=1-316.
DR PDBsum; 3BG0; -.
DR PDBsum; 3BG1; -.
DR ProteinModelPortal; P55735; -.
DR SMR; P55735; 14-304.
DR DIP; DIP-39091N; -.
DR IntAct; P55735; 15.
DR MINT; MINT-1154053; -.
DR STRING; 9606.ENSP00000312122; -.
DR PhosphoSite; P55735; -.
DR DMDM; 50403748; -.
DR PaxDb; P55735; -.
DR PRIDE; P55735; -.
DR DNASU; 6396; -.
DR Ensembl; ENST00000337354; ENSP00000336566; ENSG00000157020.
DR Ensembl; ENST00000350697; ENSP00000312122; ENSG00000157020.
DR Ensembl; ENST00000397109; ENSP00000380298; ENSG00000157020.
DR GeneID; 6396; -.
DR KEGG; hsa:6396; -.
DR UCSC; uc003bvl.3; human.
DR CTD; 6396; -.
DR GeneCards; GC03M010337; -.
DR HGNC; HGNC:10697; SEC13.
DR HPA; HPA035292; -.
DR MIM; 600152; gene.
DR neXtProt; NX_P55735; -.
DR PharmGKB; PA35620; -.
DR eggNOG; COG2319; -.
DR HOGENOM; HOG000216895; -.
DR HOVERGEN; HBG057343; -.
DR InParanoid; P55735; -.
DR KO; K14004; -.
DR OrthoDB; EOG7966GP; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; P55735; -.
DR EvolutionaryTrace; P55735; -.
DR GeneWiki; SEC13; -.
DR GenomeRNAi; 6396; -.
DR NextBio; 24846; -.
DR PRO; PR:P55735; -.
DR ArrayExpress; P55735; -.
DR Bgee; P55735; -.
DR CleanEx; HS_SEC13; -.
DR Genevestigator; P55735; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
DR GO; GO:0031080; C:nuclear pore outer ring; IDA:UniProtKB.
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:0006886; P:intracellular protein transport; NAS:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; TAS:Reactome.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
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 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; 6.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasmic vesicle; Direct protein sequencing; Endoplasmic reticulum;
KW ER-Golgi transport; Membrane; mRNA transport; Nuclear pore complex;
KW Nucleus; Phosphoprotein; Polymorphism; Protein transport;
KW Reference proteome; Repeat; Translocation; Transport; WD repeat.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 322 Protein SEC13 homolog.
FT /FTId=PRO_0000051203.
FT REPEAT 11 50 WD 1.
FT REPEAT 55 96 WD 2.
FT REPEAT 101 144 WD 3.
FT REPEAT 148 204 WD 4.
FT REPEAT 210 253 WD 5.
FT REPEAT 260 299 WD 6.
FT MOD_RES 2 2 N-acetylvaline.
FT MOD_RES 309 309 Phosphoserine.
FT VAR_SEQ 1 14 Missing (in isoform 2).
FT /FTId=VSP_046191.
FT VARIANT 172 172 S -> L (in dbSNP:rs34078590).
FT /FTId=VAR_053413.
FT CONFLICT 51 51 A -> V (in Ref. 1; L09260).
FT STRAND 16 21
FT HELIX 23 25
FT STRAND 27 32
FT STRAND 35 43
FT STRAND 46 54
FT STRAND 60 65
FT HELIX 68 70
FT STRAND 74 78
FT STRAND 83 86
FT STRAND 89 91
FT STRAND 95 99
FT STRAND 108 111
FT TURN 114 116
FT STRAND 120 123
FT STRAND 125 127
FT STRAND 129 134
FT STRAND 136 138
FT STRAND 140 142
FT STRAND 148 151
FT STRAND 181 183
FT STRAND 193 196
FT STRAND 202 206
FT STRAND 215 219
FT STRAND 230 235
FT STRAND 239 244
FT STRAND 246 249
FT STRAND 257 260
FT STRAND 265 270
FT TURN 272 274
FT STRAND 277 284
FT STRAND 286 291
FT STRAND 297 302
SQ SEQUENCE 322 AA; 35541 MW; 18E29627D87FB3DD CRC64;
MVSVINTVDT SHEDMIHDAQ MDYYGTRLAT CSSDRSVKIF DVRNGGQILI ADLRGHEGPV
WQVAWAHPMY GNILASCSYD RKVIIWREEN GTWEKSHEHA GHDSSVNSVC WAPHDYGLIL
ACGSSDGAIS LLTYTGEGQW EVKKINNAHT IGCNAVSWAP AVVPGSLIDH PSGQKPNYIK
RFASGGCDNL IKLWKEEEDG QWKEEQKLEA HSDWVRDVAW APSIGLPTST IASCSQDGRV
FIWTCDDASS NTWSPKLLHK FNDVVWHVSW SITANILAVS GGDNKVTLWK ESVDGQWVCI
SDVNKGQGSV SASVTEGQQN EQ
//
MIM
600152
*RECORD*
*FIELD* NO
600152
*FIELD* TI
*600152 SEC13-LIKE PROTEIN 1; SEC13L1
;;SEC13, YEAST, HOMOLOG OF; SEC13;;
SEC13-RELATED PROTEIN; SEC13R;;
read moreD3S1231E
*FIELD* TX
DESCRIPTION
Bidirectional transport of macromolecules between the cytoplasm and
nucleus occurs through nuclear pore complexes (NPCs) embedded in the
nuclear envelope. NPCs are composed of subcomplexes, and SEC13L1 is part
of one such subcomplex, Nup107-160 (Loiodice et al., 2004).
CLONING
Gieser and Swaroop (1992) described sequence tagged sites (STSs) from 58
novel directionally cloned human cDNAs from an enriched retinal pigment
epithelial cell line library. The nucleotide sequence of one of the cDNA
clones, AA35 (D3S1231E), showed strong homology to the yeast SEC13 gene,
which is required for vesicle biogenesis from endoplasmic reticulum
during the transport of proteins. Swaroop et al. (1994) designated the
human gene SEC13R. The predicted amino acid sequence of the SEC13R gene
product shows 70% similarity to the yeast protein. The deduced
polypeptide sequence contains several beta-transducin-like WD40 repeats
and is rich in serine and threonine residues. A 1.4-kb transcript of
SEC13R was detected by Northern analysis of many human tissues. However,
RT-PCR analysis using 2 primer sets from different regions of the gene
suggested differential expression of alternatively spliced transcripts
in various tissues.
Using the N-terminal region of NUP96 (601021) as bait in a yeast
2-hybrid screen of B-cell, breast, and placenta cDNA libraries, Enninga
et al. (2003) cloned SEC13L1, which they called SEC13. The full-length
protein contains 322 amino acids. Western blot analysis detected
endogenous SEC13L1 at an apparent molecular mass of about 36 kD.
Immunoelectron microscopy detected SEC13L1 and NUP96 on both the
cytoplasmic and nucleoplasmic sides of the NPC, in addition to other
intracellular sites.
By proteomic analysis and mass spectrometry, Cronshaw et al. (2002)
identified 94 proteins associated with NPCs purified from rat liver
nuclei. Sec13r was relatively abundant, with 16 to 32 copies per NPC.
GENE FUNCTION
By mutation analysis, Enninga et al. (2003) determined that the
SEC13L1-NUP96 interaction required the WD repeat region of SEC13L1 and
residues 201 to 378 of NUP96. SEC13L1 did not bind NUP98 (601021). In
mitosis, SEC13L1 was dispersed throughout the cell, whereas a pool of
NUP96 colocalized with the spindle apparatus. Photobleaching experiments
showed that SEC13L1 shuttled between intranuclear sites and the
cytoplasm, and a fraction of SEC13L1 stably associated with NPCs.
Cotransfection of SEC13L1 and the SEC13L1-binding site of NUP96
decreased the mobile pool of SEC13L1. Targeting and mutation studies
showed that SEC13L1 is actively transported into the nucleus and
contains a C-terminal nuclear localization signal.
Loiodice et al. (2004) transfected HeLa cells with cDNAs encoding the
constituents of the Nup107-160 subcomplex. All proteins were properly
targeted at the nuclear envelope after 2 or 3 days, except for SEC13,
which gave an additional signal typical for endoplasmic reticulum (ER)
and ER exit sites. Coimmunoprecipitation of SEC13 with NUP37 (609264)
confirmed that SEC13 interacts with Nup107-160. The fraction of SEC13
associated with Nup107-160 was targeted to kinetochores from prophase to
anaphase during mitosis.
MAPPING
By a combination of study of somatic cell hybrids and isotopic in situ
hybridization, Swaroop et al. (1994) mapped the SEC13R gene to
chromosome 3p25-p24. They physically mapped SEC13R to a YAC clone
containing the von Hippel-Lindau disease locus (VHL; 608537). From the
diagram they provided, it appeared that SEC13R lies approximately 500 kb
centromeric to PMCA2 (108733) and 1,200 kb centromeric to VHL. In the
mouse, Swaroop et al. (1994) mapped the Sec13r gene to chromosome 6.
*FIELD* RF
1. Cronshaw, J. M.; Krutchinsky, A. N.; Zhang, W.; Chait, B. T.; Matunis,
M. J.: Proteomic analysis of the mammalian nuclear pore complex. J.
Cell Biol. 158: 915-927, 2002.
2. Enninga, J.; Levay, A.; Fontoura, B. M. A.: Sec13 shuttles between
the nucleus and the cytoplasm and stably interacts with Nup96 at the
nuclear pore complex. Molec. Cell. Biol. 23: 7271-7284, 2003.
3. Gieser, L.; Swaroop, A.: Expressed sequence tags and chromosomal
localization of cDNA clones from a subtracted retinal pigment epithelium
library. Genomics 13: 873-876, 1992.
4. Loiodice, I.; Alves, A.; Rabut, G.; van Overbeek, M.; Ellenberg,
J.; Sibarita, J.-B.; Doye, V.: The entire Nup107-160 complex, including
three new members, is targeted as one entity to kinetochores in mitosis. Molec.
Biol. Cell 15: 3333-3344, 2004.
5. Swaroop, A.; Yang-Feng, T. L.; Liu, W.; Gieser, L.; Barrow, L.
L.; Chen, K.-C.; Agarwal, N.; Meisler, M. H.; Smith, D. I.: Molecular
characterization of a novel human gene, SEC13R, related to the yeast
secretory pathway gene SEC13, and mapping to a conserved linkage group
on human chromosome 3p24-p25 and mouse chromosome 6. Hum. Molec.
Genet. 3: 1281-1286, 1994.
*FIELD* CN
Patricia A. Hartz - updated: 3/14/2005
*FIELD* CD
Victor A. McKusick: 10/18/1994
*FIELD* ED
mgross: 03/16/2005
mgross: 3/16/2005
terry: 3/14/2005
ckniffin: 3/23/2004
terry: 10/18/1994
*RECORD*
*FIELD* NO
600152
*FIELD* TI
*600152 SEC13-LIKE PROTEIN 1; SEC13L1
;;SEC13, YEAST, HOMOLOG OF; SEC13;;
SEC13-RELATED PROTEIN; SEC13R;;
read moreD3S1231E
*FIELD* TX
DESCRIPTION
Bidirectional transport of macromolecules between the cytoplasm and
nucleus occurs through nuclear pore complexes (NPCs) embedded in the
nuclear envelope. NPCs are composed of subcomplexes, and SEC13L1 is part
of one such subcomplex, Nup107-160 (Loiodice et al., 2004).
CLONING
Gieser and Swaroop (1992) described sequence tagged sites (STSs) from 58
novel directionally cloned human cDNAs from an enriched retinal pigment
epithelial cell line library. The nucleotide sequence of one of the cDNA
clones, AA35 (D3S1231E), showed strong homology to the yeast SEC13 gene,
which is required for vesicle biogenesis from endoplasmic reticulum
during the transport of proteins. Swaroop et al. (1994) designated the
human gene SEC13R. The predicted amino acid sequence of the SEC13R gene
product shows 70% similarity to the yeast protein. The deduced
polypeptide sequence contains several beta-transducin-like WD40 repeats
and is rich in serine and threonine residues. A 1.4-kb transcript of
SEC13R was detected by Northern analysis of many human tissues. However,
RT-PCR analysis using 2 primer sets from different regions of the gene
suggested differential expression of alternatively spliced transcripts
in various tissues.
Using the N-terminal region of NUP96 (601021) as bait in a yeast
2-hybrid screen of B-cell, breast, and placenta cDNA libraries, Enninga
et al. (2003) cloned SEC13L1, which they called SEC13. The full-length
protein contains 322 amino acids. Western blot analysis detected
endogenous SEC13L1 at an apparent molecular mass of about 36 kD.
Immunoelectron microscopy detected SEC13L1 and NUP96 on both the
cytoplasmic and nucleoplasmic sides of the NPC, in addition to other
intracellular sites.
By proteomic analysis and mass spectrometry, Cronshaw et al. (2002)
identified 94 proteins associated with NPCs purified from rat liver
nuclei. Sec13r was relatively abundant, with 16 to 32 copies per NPC.
GENE FUNCTION
By mutation analysis, Enninga et al. (2003) determined that the
SEC13L1-NUP96 interaction required the WD repeat region of SEC13L1 and
residues 201 to 378 of NUP96. SEC13L1 did not bind NUP98 (601021). In
mitosis, SEC13L1 was dispersed throughout the cell, whereas a pool of
NUP96 colocalized with the spindle apparatus. Photobleaching experiments
showed that SEC13L1 shuttled between intranuclear sites and the
cytoplasm, and a fraction of SEC13L1 stably associated with NPCs.
Cotransfection of SEC13L1 and the SEC13L1-binding site of NUP96
decreased the mobile pool of SEC13L1. Targeting and mutation studies
showed that SEC13L1 is actively transported into the nucleus and
contains a C-terminal nuclear localization signal.
Loiodice et al. (2004) transfected HeLa cells with cDNAs encoding the
constituents of the Nup107-160 subcomplex. All proteins were properly
targeted at the nuclear envelope after 2 or 3 days, except for SEC13,
which gave an additional signal typical for endoplasmic reticulum (ER)
and ER exit sites. Coimmunoprecipitation of SEC13 with NUP37 (609264)
confirmed that SEC13 interacts with Nup107-160. The fraction of SEC13
associated with Nup107-160 was targeted to kinetochores from prophase to
anaphase during mitosis.
MAPPING
By a combination of study of somatic cell hybrids and isotopic in situ
hybridization, Swaroop et al. (1994) mapped the SEC13R gene to
chromosome 3p25-p24. They physically mapped SEC13R to a YAC clone
containing the von Hippel-Lindau disease locus (VHL; 608537). From the
diagram they provided, it appeared that SEC13R lies approximately 500 kb
centromeric to PMCA2 (108733) and 1,200 kb centromeric to VHL. In the
mouse, Swaroop et al. (1994) mapped the Sec13r gene to chromosome 6.
*FIELD* RF
1. Cronshaw, J. M.; Krutchinsky, A. N.; Zhang, W.; Chait, B. T.; Matunis,
M. J.: Proteomic analysis of the mammalian nuclear pore complex. J.
Cell Biol. 158: 915-927, 2002.
2. Enninga, J.; Levay, A.; Fontoura, B. M. A.: Sec13 shuttles between
the nucleus and the cytoplasm and stably interacts with Nup96 at the
nuclear pore complex. Molec. Cell. Biol. 23: 7271-7284, 2003.
3. Gieser, L.; Swaroop, A.: Expressed sequence tags and chromosomal
localization of cDNA clones from a subtracted retinal pigment epithelium
library. Genomics 13: 873-876, 1992.
4. Loiodice, I.; Alves, A.; Rabut, G.; van Overbeek, M.; Ellenberg,
J.; Sibarita, J.-B.; Doye, V.: The entire Nup107-160 complex, including
three new members, is targeted as one entity to kinetochores in mitosis. Molec.
Biol. Cell 15: 3333-3344, 2004.
5. Swaroop, A.; Yang-Feng, T. L.; Liu, W.; Gieser, L.; Barrow, L.
L.; Chen, K.-C.; Agarwal, N.; Meisler, M. H.; Smith, D. I.: Molecular
characterization of a novel human gene, SEC13R, related to the yeast
secretory pathway gene SEC13, and mapping to a conserved linkage group
on human chromosome 3p24-p25 and mouse chromosome 6. Hum. Molec.
Genet. 3: 1281-1286, 1994.
*FIELD* CN
Patricia A. Hartz - updated: 3/14/2005
*FIELD* CD
Victor A. McKusick: 10/18/1994
*FIELD* ED
mgross: 03/16/2005
mgross: 3/16/2005
terry: 3/14/2005
ckniffin: 3/23/2004
terry: 10/18/1994