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 27-MAR-2024, entry version 203. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 EMDB; EMD-11193; -. DR EMDB; EMD-11194; -. DR EMDB; EMD-11197; -. DR EMDB; EMD-11198; -. DR EMDB; EMD-11264; -. DR SMR; P38968; -. DR BioGRID; 31850; 259. DR ComplexPortal; CPX-2523; COPII vesicle coat complex. DR DIP; DIP-4792N; -. DR IntAct; P38968; 52. DR MINT; P38968; -. DR STRING; 4932.YDL195W; -. DR GlyGen; P38968; 15 sites, 1 O-linked glycan (15 sites). DR iPTMnet; P38968; -. DR MaxQB; P38968; -. DR PaxDb; 4932-YDL195W; -. DR PeptideAtlas; P38968; -. DR EnsemblFungi; YDL195W_mRNA; YDL195W; YDL195W. DR GeneID; 851332; -. DR KEGG; sce:YDL195W; -. DR AGR; SGD:S000002354; -. 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 OrthoDB; 149677at2759; -. DR BioCyc; YEAST:G3O-29580-MONOMER; -. DR Reactome; R-SCE-204005; COPII-mediated vesicle transport. DR BioGRID-ORCS; 851332; 4 hits in 10 CRISPR screens. 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; 1.25.40.980; -; 1. DR Gene3D; 2.20.25.400; -; 1. DR Gene3D; 6.10.140.1600; -; 1. DR Gene3D; 1.20.940.10; Functional domain of the splicing factor Prp18; 1. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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; IPR019775; WD40_repeat_CS. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR13923; SEC31-RELATED PROTEIN; 1. DR PANTHER; PTHR13923:SF11; SECRETORY 31, ISOFORM D; 1. 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; WD40 repeat-like; 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 //