SEC31_YEAST
ID SEC31_YEAST Reviewed; 1273 AA.
AC P38968; D6VRF8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Protein transport protein SEC31;
DE AltName: Full=Protein WEB1;
GN Name=SEC31; Synonyms=WEB1; OrderedLocusNames=YDL195W; ORFNames=D1229;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c / SNY243;
RX PubMed=7760818; DOI=10.1128/mcb.15.6.3227;
RA Zieler H.A., Walberg M., Berg P.;
RT "Suppression of mutations in two Saccharomyces cerevisiae genes by the
RT adenovirus E1A protein.";
RL Mol. Cell. Biol. 15:3227-3237(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8896272;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1065::aid-yea995>3.0.co;2-f;
RA Verhasselt P., Voet M., Mathys J., Volckaert G.;
RT "The sequence of 23 kb surrounding the SNF3 locus on the left arm of yeast
RT chromosome IV reveals the location of five known genes and characterizes at
RT least six new open reading frames including putative genes for ribosomal
RT protein L35 and a sugar transport protein.";
RL Yeast 12:1065-1070(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [4]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 367.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8548805; DOI=10.1016/0092-8674(95)90144-2;
RA Bednarek S.Y., Ravazzola M., Hosobuchi M., Amherdt M., Perrelet A.,
RA Schekman R.W., Orci L.;
RT "COPI- and COPII-coated vesicles bud directly from the endoplasmic
RT reticulum in yeast.";
RL Cell 83:1183-1196(1995).
RN [6]
RP FUNCTION.
RX PubMed=8852839; DOI=10.1093/genetics/142.2.393;
RA Wuestehube L.J., Duden R., Eun A., Hamamoto S., Korn P., Ram R.,
RA Schekman R.W.;
RT "New mutants of Saccharomyces cerevisiae affected in the transport of
RT proteins from the endoplasmic reticulum to the Golgi complex.";
RL Genetics 142:393-406(1996).
RN [7]
RP IDENTIFICATION IN THE COPII COAT, AND INTERACTION WITH SEC16.
RX PubMed=9325247; DOI=10.1074/jbc.272.41.25413;
RA Shaywitz D.A., Espenshade P.J., Gimeno R.E., Kaiser C.A.;
RT "COPII subunit interactions in the assembly of the vesicle coat.";
RL J. Biol. Chem. 272:25413-25416(1997).
RN [8]
RP FUNCTION, PHOSPHORYLATION, AND INTERACTION WITH SEC13.
RX PubMed=9190202; DOI=10.1091/mbc.8.2.205;
RA Salama N.R., Chuang J.S., Schekman R.W.;
RT "Sec31 encodes an essential component of the COPII coat required for
RT transport vesicle budding from the endoplasmic reticulum.";
RL Mol. Biol. Cell 8:205-217(1997).
RN [9]
RP FUNCTION.
RX PubMed=9023343; DOI=10.1073/pnas.94.3.837;
RA Campbell J.L., Schekman R.W.;
RT "Selective packaging of cargo molecules into endoplasmic reticulum-derived
RT COPII vesicles.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:837-842(1997).
RN [10]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=9568718; DOI=10.1016/s0092-8674(00)81577-9;
RA Matsuoka K., Orci L., Amherdt M., Bednarek S.Y., Hamamoto S.,
RA Schekman R.W., Yeung T.;
RT "COPII-coated vesicle formation reconstituted with purified coat proteins
RT and chemically defined liposomes.";
RL Cell 93:263-275(1998).
RN [11]
RP INTERACTION WITH SHR3.
RX PubMed=10564255; DOI=10.1091/mbc.10.11.3549;
RA Gilstring C.F., Melin-Larsson M., Ljungdahl P.O.;
RT "Shr3p mediates specific COPII coatomer-cargo interactions required for the
RT packaging of amino acid permeases into ER-derived transport vesicles.";
RL Mol. Biol. Cell 10:3549-3565(1999).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10720463; DOI=10.1006/meth.2000.0955;
RA Matsuoka K., Schekman R.W.;
RT "The use of liposomes to study COPII- and COPI-coated vesicle formation and
RT membrane protein sorting.";
RL Methods 20:417-428(2000).
RN [13]
RP INTERACTION WITH EMP24 AND ERV25.
RX PubMed=11560939; DOI=10.1074/jbc.m108113200;
RA Belden W.J., Barlowe C.;
RT "Distinct roles for the cytoplasmic tail sequences of Emp24p and Erv25p in
RT transport between the endoplasmic reticulum and Golgi complex.";
RL J. Biol. Chem. 276:43040-43048(2001).
RN [14]
RP IDENTIFICATION IN THE COPII COAT.
RX PubMed=11389436; DOI=10.1038/35078500;
RA Antonny B., Madden D.T., Hamamoto S., Orci L., Schekman R.W.;
RT "Dynamics of the COPII coat with GTP and stable analogues.";
RL Nat. Cell Biol. 3:531-537(2001).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1050, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-992; SER-999 AND THR-1050,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349; SER-836; SER-980;
RP SER-992; SER-999; THR-1050 AND SER-1053, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349; SER-974; SER-977;
RP SER-980; SER-988; SER-992; SER-999 AND THR-1050, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [19]
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., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [20]
RP ELECTRON MICROSCOPY OF THE SEC13/31 COMPLEX.
RX PubMed=11535824; DOI=10.1073/pnas.191359398;
RA Lederkremer G.Z., Cheng Y., Petre B.M., Vogan E., Springer S.,
RA Schekman R.W., Walz T., Kirchhausen T.;
RT "Structure of the Sec23p/24p and Sec13p/31p complexes of COPII.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:10704-10709(2001).
RN [21]
RP ELECTRON MICROSCOPY OF THE SEC13/31 COMPLEX.
RX PubMed=11717432; DOI=10.1073/pnas.241522198;
RA Matsuoka K., Schekman R.W., Orci L., Heuser J.E.;
RT "Surface structure of the COPII-coated vesicle.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:13705-13709(2001).
RN [22]
RP SUBCELLULAR LOCATION.
RX PubMed=12235121; DOI=10.1083/jcb.200207053;
RA Supek F., Madden D.T., Hamamoto S., Orci L., Schekman R.W.;
RT "Sec16p potentiates the action of COPII proteins to bud transport
RT vesicles.";
RL J. Cell Biol. 158:1029-1038(2002).
RN [23]
RP STRUCTURE OF THE COPII COMPLEX.
RX PubMed=12671686; DOI=10.1038/sj.embor.embor812;
RA Antonny B., Gounon P., Schekman R.W., Orci L.;
RT "Self-assembly of minimal COPII cages.";
RL EMBO Rep. 4:419-424(2003).
RN [24]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [25]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [26]
RP COPII COMPLEX ASSEMBLY, AND FUNCTION OF THE COPII COMPLEX.
RX PubMed=14627716; DOI=10.1074/jbc.c300457200;
RA Sato K., Nakano A.;
RT "Reconstitution of coat protein complex II (COPII) vesicle formation from
RT cargo-reconstituted proteoliposomes reveals the potential role of GTP
RT hydrolysis by Sar1p in protein sorting.";
RL J. Biol. Chem. 279:1330-1335(2004).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 1-763 IN COMPLEX WITH SEC13, AND
RP SUBUNIT.
RX PubMed=17604721; DOI=10.1016/j.cell.2007.05.036;
RA Fath S., Mancias J.D., Bi X., Goldberg J.;
RT "Structure and organization of coat proteins in the COPII cage.";
RL Cell 129:1325-1336(2007).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 899-947 IN COMPLEX WITH SEC23 AND
RP SAR1.
RX PubMed=17981133; DOI=10.1016/j.devcel.2007.10.006;
RA Bi X., Mancias J.D., Goldberg J.;
RT "Insights into COPII coat nucleation from the structure of Sec23.Sar1
RT complexed with the active fragment of Sec31.";
RL Dev. Cell 13:635-645(2007).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 370-746 IN COMPLEX WITH SEC13.
RX PubMed=20696705; DOI=10.1083/jcb.201003092;
RA Whittle J.R., Schwartz T.U.;
RT "Structure of the Sec13-Sec16 edge element, a template for assembly of the
RT COPII vesicle coat.";
RL J. Cell Biol. 190:347-361(2010).
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 and the
CC selection of cargo molecules. {ECO:0000269|PubMed:10720463,
CC ECO:0000269|PubMed:14627716, ECO:0000269|PubMed:8548805,
CC ECO:0000269|PubMed:8852839, ECO:0000269|PubMed:9023343,
CC ECO:0000269|PubMed:9190202}.
CC -!- SUBUNIT: The COPII coat is composed of at least 5 proteins: the
CC SEC23/24 complex, the SEC13/31 complex, and the protein SAR1. SEC13 and
CC SEC31 make a 2:2 tetramer that forms the edge element of the COPII
CC outer coat. The tetramer self-assembles in multiple copies to form the
CC complete polyhedral cage. Interacts (via WD 8) with SEC13. Interacts
CC with EMP24, ERV25, SEC16 and SHR3. {ECO:0000269|PubMed:10564255,
CC ECO:0000269|PubMed:11389436, ECO:0000269|PubMed:11560939,
CC ECO:0000269|PubMed:17604721, ECO:0000269|PubMed:17981133,
CC ECO:0000269|PubMed:20696705, ECO:0000269|PubMed:9190202,
CC ECO:0000269|PubMed:9325247, ECO:0000269|PubMed:9568718}.
CC -!- INTERACTION:
CC P38968; Q04491: SEC13; NbExp=6; IntAct=EBI-20524, EBI-16529;
CC P38968; P48415: SEC16; NbExp=3; IntAct=EBI-20524, EBI-16551;
CC P38968; P15303: SEC23; NbExp=3; IntAct=EBI-20524, EBI-16584;
CC P38968; P40482: SEC24; NbExp=4; IntAct=EBI-20524, EBI-16592;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC membrane; Peripheral membrane protein; Cytoplasmic side. Endoplasmic
CC reticulum membrane; Peripheral membrane protein; Cytoplasmic side.
CC -!- MISCELLANEOUS: Present with 1840 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the WD repeat SEC31 family. {ECO:0000305}.
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DR EMBL; U15219; AAA50367.1; -; Genomic_DNA.
DR EMBL; X83276; CAA58252.1; -; Genomic_DNA.
DR EMBL; Z74243; CAA98772.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11668.2; -; Genomic_DNA.
DR PIR; S58782; S58782.
DR RefSeq; NP_010086.2; NM_001180255.2.
DR PDB; 2PM6; X-ray; 2.45 A; A/C=370-763.
DR PDB; 2PM7; X-ray; 2.35 A; A/C=370-763.
DR PDB; 2PM9; X-ray; 3.30 A; A=1-411.
DR PDB; 2QTV; X-ray; 2.50 A; D=899-947.
DR PDB; 3MZL; X-ray; 2.80 A; B/D/F/H=370-746.
DR PDB; 4BZJ; EM; 40.00 A; A/C=1-1273.
DR PDB; 4BZK; EM; 40.00 A; A/C=1-1273.
DR PDB; 6ZG5; EM; 40.00 A; A/C=1-1273.
DR PDB; 6ZG6; EM; 40.00 A; A/C/E/G=1-1273.
DR PDB; 6ZL0; EM; 40.00 A; A/C=1-1273.
DR PDBsum; 2PM6; -.
DR PDBsum; 2PM7; -.
DR PDBsum; 2PM9; -.
DR PDBsum; 2QTV; -.
DR PDBsum; 3MZL; -.
DR PDBsum; 4BZJ; -.
DR PDBsum; 4BZK; -.
DR PDBsum; 6ZG5; -.
DR PDBsum; 6ZG6; -.
DR PDBsum; 6ZL0; -.
DR AlphaFoldDB; P38968; -.
DR SMR; P38968; -.
DR BioGRID; 31850; 251.
DR ComplexPortal; CPX-2523; COPII vesicle coat complex.
DR DIP; DIP-4792N; -.
DR IntAct; P38968; 52.
DR MINT; P38968; -.
DR STRING; 4932.YDL195W; -.
DR iPTMnet; P38968; -.
DR MaxQB; P38968; -.
DR PaxDb; P38968; -.
DR PRIDE; P38968; -.
DR EnsemblFungi; YDL195W_mRNA; YDL195W; YDL195W.
DR GeneID; 851332; -.
DR KEGG; sce:YDL195W; -.
DR SGD; S000002354; SEC31.
DR VEuPathDB; FungiDB:YDL195W; -.
DR eggNOG; KOG0307; Eukaryota.
DR GeneTree; ENSGT00390000003175; -.
DR HOGENOM; CLU_003033_2_0_1; -.
DR InParanoid; P38968; -.
DR OMA; AQWAFGG; -.
DR BioCyc; YEAST:G3O-29580-MON; -.
DR Reactome; R-SCE-204005; COPII-mediated vesicle transport.
DR EvolutionaryTrace; P38968; -.
DR PRO; PR:P38968; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P38968; protein.
DR GO; GO:0030127; C:COPII vesicle coat; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:ComplexPortal.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043332; C:mating projection tip; HDA:SGD.
DR GO; GO:0005198; F:structural molecule activity; IDA:SGD.
DR GO; GO:0090114; P:COPII-coated vesicle budding; IDA:SGD.
DR GO; GO:0090110; P:COPII-coated vesicle cargo loading; IBA:GO_Central.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:1902953; P:positive regulation of ER to Golgi vesicle-mediated transport; IDA:ComplexPortal.
DR GO; GO:0070863; P:positive regulation of protein exit from endoplasmic reticulum; IDA:ComplexPortal.
DR DisProt; DP01840; -.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR024298; ACE1_Sec16_Sec31.
DR InterPro; IPR021614; Sec31.
DR InterPro; IPR040251; SEC31-like.
DR InterPro; IPR009917; SRA1/Sec31.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR13923; PTHR13923; 2.
DR Pfam; PF12931; Sec16_C; 1.
DR Pfam; PF11549; Sec31; 1.
DR Pfam; PF07304; SRA1; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasmic vesicle; Endoplasmic reticulum;
KW ER-Golgi transport; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Transport; WD repeat.
FT CHAIN 1..1273
FT /note="Protein transport protein SEC31"
FT /id="PRO_0000051436"
FT REPEAT 6..46
FT /note="WD 1"
FT REPEAT 60..99
FT /note="WD 2"
FT REPEAT 106..146
FT /note="WD 3"
FT REPEAT 158..198
FT /note="WD 4"
FT REPEAT 207..250
FT /note="WD 5"
FT REPEAT 255..295
FT /note="WD 6"
FT REPEAT 298..338
FT /note="WD 7"
FT REPEAT 385..405
FT /note="WD 8; interaction with SEC13"
FT REGION 815..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 933..1162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 944..958
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 990..1043
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1067..1096
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1117..1162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 836
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 974
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 977
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 980
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 988
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 992
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 999
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 1050
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1053
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 317
FT /note="A -> T (in Ref. 1; AAA50367)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="T -> S (in Ref. 2; CAA58252 and 3; CAA98772)"
FT /evidence="ECO:0000305"
FT CONFLICT 691
FT /note="S -> N (in Ref. 1; AAA50367)"
FT /evidence="ECO:0000305"
FT CONFLICT 754
FT /note="A -> V (in Ref. 1; AAA50367)"
FT /evidence="ECO:0000305"
FT CONFLICT 877
FT /note="T -> A (in Ref. 1; AAA50367)"
FT /evidence="ECO:0000305"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:2PM9"
FT STRAND 17..20
FT /evidence="ECO:0007829|PDB:2PM9"
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:2PM9"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:2PM9"
FT STRAND 43..49
FT /evidence="ECO:0007829|PDB:2PM9"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:2PM9"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:2PM9"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:2PM9"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:2PM9"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:2PM9"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:2PM9"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:2PM9"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:2PM9"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:2PM9"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:2PM9"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:2PM9"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:2PM9"
FT TURN 138..141
FT /evidence="ECO:0007829|PDB:2PM9"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:2PM9"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:2PM9"
FT STRAND 175..183
FT /evidence="ECO:0007829|PDB:2PM9"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:2PM9"
FT TURN 190..193
FT /evidence="ECO:0007829|PDB:2PM9"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:2PM9"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:2PM9"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:2PM9"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:2PM9"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:2PM9"
FT STRAND 260..265
FT /evidence="ECO:0007829|PDB:2PM9"
FT STRAND 273..285
FT /evidence="ECO:0007829|PDB:2PM9"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:2PM9"
FT STRAND 292..297
FT /evidence="ECO:0007829|PDB:2PM9"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:2PM9"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:2PM9"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:2PM9"
FT STRAND 321..330
FT /evidence="ECO:0007829|PDB:2PM9"
FT STRAND 385..387
FT /evidence="ECO:0007829|PDB:2PM7"
FT TURN 388..390
FT /evidence="ECO:0007829|PDB:2PM7"
FT STRAND 391..395
FT /evidence="ECO:0007829|PDB:2PM7"
FT STRAND 402..405
FT /evidence="ECO:0007829|PDB:2PM7"
FT HELIX 416..424
FT /evidence="ECO:0007829|PDB:2PM7"
FT HELIX 428..436
FT /evidence="ECO:0007829|PDB:2PM7"
FT HELIX 441..456
FT /evidence="ECO:0007829|PDB:2PM7"
FT HELIX 458..466
FT /evidence="ECO:0007829|PDB:2PM7"
FT HELIX 509..519
FT /evidence="ECO:0007829|PDB:2PM7"
FT HELIX 523..531
FT /evidence="ECO:0007829|PDB:2PM7"
FT TURN 532..534
FT /evidence="ECO:0007829|PDB:2PM7"
FT HELIX 536..543
FT /evidence="ECO:0007829|PDB:2PM7"
FT HELIX 549..563
FT /evidence="ECO:0007829|PDB:2PM7"
FT HELIX 568..577
FT /evidence="ECO:0007829|PDB:2PM7"
FT HELIX 582..587
FT /evidence="ECO:0007829|PDB:2PM7"
FT HELIX 590..592
FT /evidence="ECO:0007829|PDB:2PM7"
FT HELIX 593..603
FT /evidence="ECO:0007829|PDB:2PM7"
FT HELIX 608..623
FT /evidence="ECO:0007829|PDB:2PM7"
FT TURN 624..626
FT /evidence="ECO:0007829|PDB:2PM7"
FT HELIX 628..637
FT /evidence="ECO:0007829|PDB:2PM7"
FT HELIX 641..650
FT /evidence="ECO:0007829|PDB:2PM7"
FT HELIX 652..661
FT /evidence="ECO:0007829|PDB:2PM7"
FT HELIX 666..685
FT /evidence="ECO:0007829|PDB:2PM7"
FT HELIX 697..711
FT /evidence="ECO:0007829|PDB:2PM7"
FT TURN 712..714
FT /evidence="ECO:0007829|PDB:2PM7"
FT HELIX 716..725
FT /evidence="ECO:0007829|PDB:2PM7"
FT HELIX 731..744
FT /evidence="ECO:0007829|PDB:2PM7"
FT STRAND 909..911
FT /evidence="ECO:0007829|PDB:2QTV"
FT HELIX 916..919
FT /evidence="ECO:0007829|PDB:2QTV"
SQ SEQUENCE 1273 AA; 138717 MW; 87F192E4B10E7571 CRC64;
MVKLAEFSRT ATFAWSHDKI PLLVSGTVSG TVDANFSTDS SLELWSLLAA DSEKPIASLQ
VDSKFNDLDW SHNNKIIAGA LDNGSLELYS TNEANNAINS MARFSNHSSS VKTVKFNAKQ
DNVLASGGNN GEIFIWDMNK CTESPSNYTP LTPGQSMSSV DEVISLAWNQ SLAHVFASAG
SSNFASIWDL KAKKEVIHLS YTSPNSGIKQ QLSVVEWHPK NSTRVATATG SDNDPSILIW
DLRNANTPLQ TLNQGHQKGI LSLDWCHQDE HLLLSSGRDN TVLLWNPESA EQLSQFPARG
NWCFKTKFAP EAPDLFACAS FDNKIEVQTL QNLTNTLDEQ ETETKQQESE TDFWNNVSRE
ESKEKPTVFH LQAPTWYGEP SPAAHWAFGG KLVQITPDGK GVSITNPKIS GLESNTTLSE
ALKTKDFKPL INQRLVKVID DVNEEDWNLL EKLSMDGTEE FLKEALAFDN DESDAQDDAN
NEKEDDGEEF FQQIETNFQP EGDFSLSGNI EQTISKNLVS GNIKSAVKNS LENDLLMEAM
VIALDSNNER LKESVKNAYF AKYGSKSSLS RILYSISKRE VDDLVENLDV SQWKFISKAI
QNLYPNDIAQ RNEMLIKLGD RLKENGHRQD SLTLYLAAGS LDKVASIWLS EFPDLEDKLK
KDNKTIYEAH SECLTEFIER FTVFSNFING SSTINNEQLI AKFLEFINLT TSTGNFELAT
EFLNSLPSDN EEVKTEKARV LIASGKSLPA QNPATATTSK AKYTNAKTNK NVPVLPTPGM
PSTTSIPSMQ APFYGMTPGA SANALPPKPY VPATTTSAPV HTEGKYAPPS QPSMASPFVN
KTNSSTRLNS FAPPPNPYAT ATVPATNVST TSIPQNTFAP IQPGMPIMGD YNAQSSSIPS
QPPINAVSGQ TPHLNRKAND GWNDLPLKVK EKPSRAKAVS VAPPNILSTP TPLNGIPANA
ASTMPPPPLS RAPSSVSMVS PPPLHKNSRV PSLVATSESP RASISNPYAP PQSSQQFPIG
TISTANQTSN TAQVASSNPY APPPQQRVAT PLSGGVPPAP LPKASNPYAP TATTQPNGSS
YPPTGPYTNN HTMTSPPPVF NKPPTGPPPI SMKKRSNKLA SIEQNPSQGA TYPPTLSSSA
SPLQPSQPPT LASQVNTSAE NVSHEIPADQ QPIVDFLKEE LARVTPLTPK EYSKQLKDCD
KRLKILFYHL EKQDLLTQPT IDCLHDLVAL MKEKKYKEAM VIHANIATNH AQEGGNWLTG
VKRLIGIAEA TLN
