ID SEC23_YEAST Reviewed; 768 AA. AC P15303; D6W4I1; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 11-DEC-2019, entry version 193. DE RecName: Full=Protein transport protein SEC23; GN Name=SEC23; OrderedLocusNames=YPR181C; ORFNames=P9705.14; 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], AND FUNCTION. RC STRAIN=MBY8-20C; RX PubMed=2670558; DOI=10.1002/j.1460-2075.1989.tb03559.x; RA Hicke L., Schekman R.W.; RT "Yeast Sec23p acts in the cytoplasm to promote protein transport from the RT endoplasmic reticulum to the Golgi complex in vivo and in vitro."; RL EMBO J. 8:1677-1684(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169875; RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., RA Vo D.H., Hani J.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."; RL Nature 387:103-105(1997). RN [3] RP GENOME REANNOTATION. 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 [4] RP FUNCTION. RX PubMed=6996832; DOI=10.1016/0092-8674(80)90128-2; RA Novick P., Field C., Schekman R.W.; RT "Identification of 23 complementation groups required for post- RT translational events in the yeast secretory pathway."; RL Cell 21:205-215(1980). RN [5] RP FUNCTION. RX PubMed=7026045; DOI=10.1016/0092-8674(81)90064-7; RA Novick P., Ferro S., Schekman R.W.; RT "Order of events in the yeast secretory pathway."; RL Cell 25:461-469(1981). RN [6] RP FUNCTION. RX PubMed=3293799; DOI=10.1016/0092-8674(88)90196-1; RA Baker D., Hicke L., Rexach M.F., Schleyer M., Schekman R.W.; RT "Reconstitution of SEC gene product-dependent intercompartmental protein RT transport."; RL Cell 54:335-344(1988). RN [7] RP FUNCTION. RX PubMed=3049622; DOI=10.1083/jcb.107.4.1465; RA Ruohola H., Kabcenell A.K., Ferro-Novick S.; RT "Reconstitution of protein transport from the endoplasmic reticulum to the RT Golgi complex in yeast: the acceptor Golgi compartment is defective in the RT sec23 mutant."; RL J. Cell Biol. 107:1465-1476(1988). RN [8] RP FUNCTION. RX PubMed=2188733; DOI=10.1016/0092-8674(90)90483-u; RA Kaiser C.A., Schekman R.W.; RT "Distinct sets of SEC genes govern transport vesicle formation and fusion RT early in the secretory pathway."; RL Cell 61:723-733(1990). RN [9] RP FUNCTION, AND SUBUNIT. RX PubMed=1498369; DOI=10.1091/mbc.3.6.667; RA Hicke L., Yoshihisa T., Schekman R.W.; RT "Sec23p and a novel 105-kDa protein function as a multimeric complex to RT promote vesicle budding and protein transport from the endoplasmic RT reticulum."; RL Mol. Biol. Cell 3:667-676(1992). RN [10] RP FUNCTION. RX PubMed=7925484; RA Liang S., Lacroute F., Kepes F.; RT "Multicopy STS1 restores both protein transport and ribosomal RNA stability RT in a new yeast sec23 mutant allele."; RL Eur. J. Cell Biol. 62:270-281(1993). RN [11] RP FUNCTION. RX PubMed=8451644; DOI=10.1126/science.8451644; RA Yoshihisa T., Barlowe C., Schekman R.W.; RT "Requirement for a GTPase-activating protein in vesicle budding from the RT endoplasmic reticulum."; RL Science 259:1466-1468(1993). RN [12] 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 [13] RP INTERACTION WITH SEC16. RX PubMed=7593161; DOI=10.1083/jcb.131.2.311; RA Espenshade P.J., Gimeno R.E., Holzmacher E., Teung P., Kaiser C.A.; RT "Yeast SEC16 gene encodes a multidomain vesicle coat protein that interacts RT with Sec23p."; RL J. Cell Biol. 131:311-324(1995). RN [14] RP FUNCTION. RX PubMed=8909535; DOI=10.1083/jcb.135.3.585; RA Kuehn M.J., Schekman R.W., Ljungdahl P.O.; RT "Amino acid permeases require COPII components and the ER resident membrane RT protein Shr3p for packaging into transport vesicles in vitro."; RL J. Cell Biol. 135:585-595(1996). RN [15] RP INTERACTION WITH SEC16. RX PubMed=8930902; DOI=10.1091/mbc.7.11.1815; RA Gimeno R.E., Espenshade P.J., Kaiser C.A.; RT "COPII coat subunit interactions: Sec24p and Sec23p bind to adjacent RT regions of Sec16p."; RL Mol. Biol. Cell 7:1815-1823(1996). RN [16] 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 [17] RP FUNCTION. RX PubMed=9427388; RA Suetterlin C., Doering T.L., Schimmoeller F., Schroeder S., Riezman H.; RT "Specific requirements for the ER to Golgi transport of GPI-anchored RT proteins in yeast."; RL J. Cell Sci. 110:2703-2714(1997). RN [18] 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 [19] RP FUNCTION. RX PubMed=9624457; RX DOI=10.1002/(sici)1097-0185(199806)251:2<256::aid-ar15>3.0.co;2-n; RA Morin-Ganet M.N., Rambourg A., Clermont Y., Kepes F.; RT "Role of endoplasmic reticulum-derived vesicles in the formation of Golgi RT elements in sec23 and sec18 Saccharomyces Cerevisiae mutants."; RL Anat. Rec. 251:256-264(1998). RN [20] 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 [21] RP FUNCTION OF THE SEC23/24 COMPLEX. RX PubMed=9428766; DOI=10.1038/34438; RA Kuehn M.J., Herrmann J.M., Schekman R.W.; RT "COPII-cargo interactions direct protein sorting into ER-derived transport RT vesicles."; RL Nature 391:187-190(1998). RN [22] RP INTERACTION WITH BET1; BOS1; SAR1 AND SEC24. RX PubMed=9685263; DOI=10.1126/science.281.5377.698; RA Springer S., Schekman R.W.; RT "Nucleation of COPII vesicular coat complex by endoplasmic reticulum to RT Golgi vesicle SNAREs."; RL Science 281:698-700(1998). RN [23] RP FUNCTION OF THE SEC23/24 COMPLEX. RX PubMed=10198022; RA Penalver E., Lucero P., Moreno E., Lagunas R.; RT "Clathrin and two components of the COPII complex, Sec23p and Sec24p, could RT be involved in endocytosis of the Saccharomyces cerevisiae maltose RT transporter."; RL J. Bacteriol. 181:2555-2563(1999). RN [24] 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 [25] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SFB3. RX PubMed=11086000; DOI=10.1083/jcb.151.5.973; RA Shimoni Y., Kurihara T., Ravazzola M., Amherdt M., Orci L., Schekman R.W.; RT "Lst1p and Sec24p cooperate in sorting of the plasma membrane ATPase into RT COPII vesicles in Saccharomyces cerevisiae."; RL J. Cell Biol. 151:973-984(2000). RN [26] 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 [27] RP INTERACTION WITH PDR17. RX PubMed=10712514; DOI=10.1091/mbc.11.3.983; RA Kurihara T., Hamamoto S., Gimeno R.E., Kaiser C.A., Schekman R.W., RA Yoshihisa T.; RT "Sec24p and Iss1p function interchangeably in transport vesicle formation RT from the endoplasmic reticulum in Saccharomyces cerevisiae."; RL Mol. Biol. Cell 11:983-998(2000). RN [28] RP INTERACTION WITH SYS1. RX PubMed=11726510; DOI=10.1093/emboj/20.23.6742; RA Votsmeier C., Gallwitz D.; RT "An acidic sequence of a putative yeast Golgi membrane protein binds COPII RT and facilitates ER export."; RL EMBO J. 20:6742-6750(2001). RN [29] 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 [30] 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 [31] RP IDENTIFICATION BY MASS 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 [32] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP 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 [33] RP ELECTRON MICROSCOPY OF THE SEC23/24 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 [34] RP ELECTRON MICROSCOPY OF THE SEC23/24 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 [35] 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 [36] RP FUNCTION OF THE SEC23/24 COMPLEX, AND INTERACTION WITH BET1; SEC22 AND RP SED5. RX PubMed=12941276; DOI=10.1016/s0092-8674(03)00608-1; RA Mossessova E., Bickford L.C., Goldberg J.; RT "SNARE selectivity of the COPII coat."; RL Cell 114:483-495(2003). RN [37] 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 [38] RP UBIQUITINATION, AND INTERACTION WITH SEC24. RX PubMed=12778054; DOI=10.1038/ncb1003; RA Cohen M., Stutz F., Belgareh N., Haguenauer-Tsapis R., Dargemont C.; RT "Ubp3 requires a cofactor, Bre5, to specifically de-ubiquitinate the COPII RT protein, Sec23."; RL Nat. Cell Biol. 5:661-667(2003). RN [39] 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 [40] RP FUNCTION, AND INTERACTION WITH GRH1. RX PubMed=16269340; DOI=10.1016/j.cell.2005.08.031; RA Schuldiner M., Collins S.R., Thompson N.J., Denic V., Bhamidipati A., RA Punna T., Ihmels J., Andrews B., Boone C., Greenblatt J.F., Weissman J.S., RA Krogan N.J.; RT "Exploration of the function and organization of the yeast early secretory RT pathway through an epistatic miniarray profile."; RL Cell 123:507-519(2005). RN [41] RP INTERACTION WITH GHR1. RX PubMed=17261844; DOI=10.1083/jcb.200607151; RA Behnia R., Barr F.A., Flanagan J.J., Barlowe C., Munro S.; RT "The yeast orthologue of GRASP65 forms a complex with a coiled-coil protein RT that contributes to ER to Golgi traffic."; RL J. Cell Biol. 176:255-261(2007). RN [42] RP FUNCTION, AND INTERACTION WITH BET3. RX PubMed=17287728; DOI=10.1038/nature05527; RA Cai H., Yu S., Menon S., Cai Y., Lazarova D., Fu C., Reinisch K., Hay J.C., RA Ferro-Novick S.; RT "TRAPPI tethers COPII vesicles by binding the coat subunit Sec23."; RL Nature 445:941-944(2007). RN [43] RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH SAR1 AND ZINC. RX PubMed=12239560; DOI=10.1038/nature01040; RA Bi X., Corpina R.A., Goldberg J.; RT "Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle RT coat."; RL Nature 419:271-277(2002). 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. SEC23 interacts with BET3 in order to CC target TRAPPI complex to COPII involved in internalisation of plasma CC membrane proteins like the maltose transporter. CC {ECO:0000269|PubMed:10198022, ECO:0000269|PubMed:10720463, CC ECO:0000269|PubMed:11086000, ECO:0000269|PubMed:12941276, CC ECO:0000269|PubMed:14627716, ECO:0000269|PubMed:1498369, CC ECO:0000269|PubMed:16269340, ECO:0000269|PubMed:17287728, CC ECO:0000269|PubMed:2188733, ECO:0000269|PubMed:2670558, CC ECO:0000269|PubMed:3049622, ECO:0000269|PubMed:3293799, CC ECO:0000269|PubMed:6996832, ECO:0000269|PubMed:7026045, CC ECO:0000269|PubMed:7925484, ECO:0000269|PubMed:8451644, CC ECO:0000269|PubMed:8548805, ECO:0000269|PubMed:8909535, CC ECO:0000269|PubMed:9023343, ECO:0000269|PubMed:9427388, CC ECO:0000269|PubMed:9428766, ECO:0000269|PubMed:9624457}. CC -!- SUBUNIT: The COPII coat is composed of at least 7 proteins: the CC SEC23/24 complex, the SEC13/31 complex, SFB2, SFB3 and the protein CC SAR1. Forms two other heterodimeric complexes with SFB3 and PDR17. CC Interacts with BET1, BET3, BOS1, EMP24, GRH1, SEC16, SEC22 and SYS1. CC {ECO:0000269|PubMed:10564255, ECO:0000269|PubMed:10712514, CC ECO:0000269|PubMed:11086000, ECO:0000269|PubMed:11389436, CC ECO:0000269|PubMed:11560939, ECO:0000269|PubMed:11726510, CC ECO:0000269|PubMed:12239560, ECO:0000269|PubMed:12778054, CC ECO:0000269|PubMed:12941276, ECO:0000269|PubMed:1498369, CC ECO:0000269|PubMed:16269340, ECO:0000269|PubMed:17261844, CC ECO:0000269|PubMed:17287728, ECO:0000269|PubMed:7593161, CC ECO:0000269|PubMed:8930902, ECO:0000269|PubMed:9325247, CC ECO:0000269|PubMed:9568718, ECO:0000269|PubMed:9685263}. CC -!- INTERACTION: CC Q04410:GRH1; NbExp=4; IntAct=EBI-16584, EBI-32083; CC P29295:HRR25; NbExp=5; IntAct=EBI-16584, EBI-8536; CC P20606:SAR1; NbExp=3; IntAct=EBI-16584, EBI-16472; CC P48415:SEC16; NbExp=5; IntAct=EBI-16584, EBI-16551; CC P40482:SEC24; NbExp=5; IntAct=EBI-16584, EBI-16592; CC P38968:SEC31; NbExp=3; IntAct=EBI-16584, EBI-20524; CC P53953:SFB2; NbExp=4; IntAct=EBI-16584, EBI-17006; CC Q99394:TRS33; NbExp=3; IntAct=EBI-16584, EBI-19480; CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle CC membrane {ECO:0000269|PubMed:10720463, ECO:0000269|PubMed:11086000, CC ECO:0000269|PubMed:12235121, ECO:0000269|PubMed:8548805, CC ECO:0000269|PubMed:9568718}; Peripheral membrane protein CC {ECO:0000269|PubMed:11086000, ECO:0000269|PubMed:8548805}; Cytoplasmic CC side {ECO:0000269|PubMed:8548805}. Cytoplasm CC {ECO:0000269|PubMed:8548805}. Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:8548805}; Peripheral membrane protein; Cytoplasmic CC side. Golgi apparatus membrane {ECO:0000305}; Peripheral membrane CC protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. CC -!- PTM: Ubiquitinated. Ubiquitination is required for the formation of the CC SEC23/24 complex. Deubiquitinated by the UBP3/BRE5 complex. CC {ECO:0000269|PubMed:12778054}. CC -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC23 subfamily. CC {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; X15474; CAA33501.1; -; Genomic_DNA. DR EMBL; U25842; AAB68114.1; -; Genomic_DNA. DR EMBL; BK006949; DAA11597.1; -; Genomic_DNA. DR PIR; S05742; BVBY23. DR RefSeq; NP_015507.1; NM_001184278.1. DR PDB; 1M2O; X-ray; 2.50 A; A/C=1-768. DR PDB; 1M2V; X-ray; 2.75 A; A=1-768. DR PDB; 2QTV; X-ray; 2.50 A; A=2-768. DR PDB; 4BZI; EM; 23.00 A; A/D/G=1-768. DR PDB; 6GNI; EM; 4.90 A; A=2-768. DR PDBsum; 1M2O; -. DR PDBsum; 1M2V; -. DR PDBsum; 2QTV; -. DR PDBsum; 4BZI; -. DR PDBsum; 6GNI; -. DR SMR; P15303; -. DR BioGrid; 36353; 512. DR ComplexPortal; CPX-1341; SEC23-LST1 COPII cargo recruitment complex. DR ComplexPortal; CPX-2523; COPII vesicle coat complex. DR DIP; DIP-2232N; -. DR IntAct; P15303; 41. DR MINT; P15303; -. DR STRING; 4932.YPR181C; -. DR MoonDB; P15303; Predicted. DR iPTMnet; P15303; -. DR MaxQB; P15303; -. DR PaxDb; P15303; -. DR PRIDE; P15303; -. DR EnsemblFungi; YPR181C_mRNA; YPR181C; YPR181C. DR GeneID; 856311; -. DR KEGG; sce:YPR181C; -. DR EuPathDB; FungiDB:YPR181C; -. DR SGD; S000006385; SEC23. DR HOGENOM; HOG000231690; -. DR InParanoid; P15303; -. DR KO; K14006; -. DR OMA; SLKVFME; -. DR BioCyc; YEAST:G3O-34306-MONOMER; -. DR Reactome; R-SCE-204005; COPII-mediated vesicle transport. DR Reactome; R-SCE-5694530; Cargo concentration in the ER. DR Reactome; R-SCE-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC. DR EvolutionaryTrace; P15303; -. DR PRO; PR:P15303; -. DR Proteomes; UP000002311; Chromosome XVI. DR RNAct; P15303; protein. DR GO; GO:0030127; C:COPII vesicle coat; IDA:SGD. DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD. 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:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005096; F:GTPase activator activity; IDA:FlyBase. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0090110; P:COPII-coated vesicle cargo loading; IBA:GO_Central. DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro. DR GO; GO:0016236; P:macroautophagy; IMP:SGD. DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:FlyBase. DR GO; GO:0003400; P:regulation of COPII vesicle coating; IDA:SGD. DR GO; GO:0061709; P:reticulophagy; IMP:SGD. DR CDD; cd11287; Sec23_C; 1. DR Gene3D; 3.40.20.10; -; 1. DR Gene3D; 3.40.50.410; -; 1. DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf. DR InterPro; IPR007123; Gelsolin-like_dom. DR InterPro; IPR036180; Gelsolin-like_dom_sf. DR InterPro; IPR037364; Sec23. DR InterPro; IPR006900; Sec23/24_helical_dom. DR InterPro; IPR036175; Sec23/24_helical_dom_sf. DR InterPro; IPR006896; Sec23/24_trunk_dom. DR InterPro; IPR012990; Sec23_24_beta_S. DR InterPro; IPR037550; Sec23_C. DR InterPro; IPR036465; vWFA_dom_sf. DR InterPro; IPR006895; Znf_Sec23_Sec24. DR InterPro; IPR036174; Znf_Sec23_Sec24_sf. DR PANTHER; PTHR11141; PTHR11141; 1. DR Pfam; PF00626; Gelsolin; 1. DR Pfam; PF08033; Sec23_BS; 1. DR Pfam; PF04815; Sec23_helical; 1. DR Pfam; PF04811; Sec23_trunk; 1. DR Pfam; PF04810; zf-Sec23_Sec24; 1. DR SUPFAM; SSF53300; SSF53300; 1. DR SUPFAM; SSF81811; SSF81811; 1. DR SUPFAM; SSF82754; SSF82754; 1. DR SUPFAM; SSF82919; SSF82919; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Cytoplasmic vesicle; KW Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus; Membrane; KW Metal-binding; Protein transport; Reference proteome; Transport; KW Ubl conjugation; Zinc. FT CHAIN 1..768 FT /note="Protein transport protein SEC23" FT /id="PRO_0000205145" FT METAL 56 FT /note="Zinc" FT /evidence="ECO:0000269|PubMed:12239560" FT METAL 61 FT /note="Zinc" FT /evidence="ECO:0000269|PubMed:12239560" FT METAL 80 FT /note="Zinc" FT /evidence="ECO:0000269|PubMed:12239560" FT METAL 83 FT /note="Zinc" FT /evidence="ECO:0000269|PubMed:12239560" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000244|PubMed:22814378" FT HELIX 3..10 FT /evidence="ECO:0000244|PDB:1M2O" FT STRAND 11..22 FT /evidence="ECO:0000244|PDB:1M2O" FT HELIX 23..28 FT /evidence="ECO:0000244|PDB:1M2O" FT STRAND 33..37 FT /evidence="ECO:0000244|PDB:1M2O" FT STRAND 48..51 FT /evidence="ECO:0000244|PDB:2QTV" FT TURN 59..61 FT /evidence="ECO:0000244|PDB:1M2O" FT STRAND 69..72 FT /evidence="ECO:0000244|PDB:1M2V" FT TURN 73..76 FT /evidence="ECO:0000244|PDB:1M2O" FT STRAND 77..79 FT /evidence="ECO:0000244|PDB:2QTV" FT TURN 81..83 FT /evidence="ECO:0000244|PDB:1M2O" FT STRAND 86..88 FT /evidence="ECO:0000244|PDB:2QTV" FT HELIX 91..93 FT /evidence="ECO:0000244|PDB:1M2O" FT STRAND 98..100 FT /evidence="ECO:0000244|PDB:1M2V" FT HELIX 103..105 FT /evidence="ECO:0000244|PDB:1M2O" FT STRAND 108..113 FT /evidence="ECO:0000244|PDB:1M2O" FT STRAND 123..129 FT /evidence="ECO:0000244|PDB:1M2O" FT HELIX 134..149 FT /evidence="ECO:0000244|PDB:1M2O" FT STRAND 156..168 FT /evidence="ECO:0000244|PDB:1M2O" FT STRAND 172..183 FT /evidence="ECO:0000244|PDB:1M2O" FT HELIX 190..198 FT /evidence="ECO:0000244|PDB:1M2O" FT STRAND 221..223 FT /evidence="ECO:0000244|PDB:1M2O" FT HELIX 224..227 FT /evidence="ECO:0000244|PDB:1M2O" FT STRAND 228..230 FT /evidence="ECO:0000244|PDB:1M2O" FT HELIX 231..243 FT /evidence="ECO:0000244|PDB:1M2O" FT HELIX 262..276 FT /evidence="ECO:0000244|PDB:1M2O" FT STRAND 283..290 FT /evidence="ECO:0000244|PDB:1M2O" FT STRAND 294..297 FT /evidence="ECO:0000244|PDB:1M2O" FT HELIX 311..315 FT /evidence="ECO:0000244|PDB:1M2O" FT HELIX 322..339 FT /evidence="ECO:0000244|PDB:1M2O" FT STRAND 342..348 FT /evidence="ECO:0000244|PDB:1M2O" FT HELIX 355..365 FT /evidence="ECO:0000244|PDB:1M2O" FT STRAND 369..373 FT /evidence="ECO:0000244|PDB:1M2O" FT HELIX 378..386 FT /evidence="ECO:0000244|PDB:1M2O" FT STRAND 394..397 FT /evidence="ECO:0000244|PDB:1M2O" FT STRAND 399..408 FT /evidence="ECO:0000244|PDB:1M2O" FT STRAND 412..420 FT /evidence="ECO:0000244|PDB:1M2O" FT STRAND 437..439 FT /evidence="ECO:0000244|PDB:1M2O" FT STRAND 443..450 FT /evidence="ECO:0000244|PDB:1M2O" FT STRAND 456..462 FT /evidence="ECO:0000244|PDB:1M2O" FT STRAND 484..495 FT /evidence="ECO:0000244|PDB:1M2O" FT TURN 496..498 FT /evidence="ECO:0000244|PDB:1M2O" FT STRAND 499..512 FT /evidence="ECO:0000244|PDB:1M2O" FT HELIX 517..521 FT /evidence="ECO:0000244|PDB:1M2O" FT HELIX 525..539 FT /evidence="ECO:0000244|PDB:1M2O" FT HELIX 545..563 FT /evidence="ECO:0000244|PDB:1M2O" FT STRAND 564..567 FT /evidence="ECO:0000244|PDB:2QTV" FT HELIX 571..573 FT /evidence="ECO:0000244|PDB:1M2O" FT TURN 578..581 FT /evidence="ECO:0000244|PDB:1M2O" FT HELIX 582..592 FT /evidence="ECO:0000244|PDB:1M2O" FT TURN 594..596 FT /evidence="ECO:0000244|PDB:1M2O" FT HELIX 603..613 FT /evidence="ECO:0000244|PDB:1M2O" FT HELIX 618..625 FT /evidence="ECO:0000244|PDB:1M2O" FT STRAND 628..632 FT /evidence="ECO:0000244|PDB:1M2O" FT STRAND 634..636 FT /evidence="ECO:0000244|PDB:1M2O" FT HELIX 645..647 FT /evidence="ECO:0000244|PDB:1M2O" FT STRAND 653..657 FT /evidence="ECO:0000244|PDB:1M2O" FT STRAND 659..666 FT /evidence="ECO:0000244|PDB:1M2O" FT HELIX 668..676 FT /evidence="ECO:0000244|PDB:1M2O" FT HELIX 678..680 FT /evidence="ECO:0000244|PDB:1M2O" FT HELIX 682..684 FT /evidence="ECO:0000244|PDB:1M2V" FT HELIX 685..703 FT /evidence="ECO:0000244|PDB:1M2O" FT STRAND 710..715 FT /evidence="ECO:0000244|PDB:1M2O" FT HELIX 719..721 FT /evidence="ECO:0000244|PDB:1M2O" FT HELIX 722..725 FT /evidence="ECO:0000244|PDB:1M2O" FT STRAND 740..742 FT /evidence="ECO:0000244|PDB:2QTV" FT HELIX 752..763 FT /evidence="ECO:0000244|PDB:1M2O" SQ SEQUENCE 768 AA; 85385 MW; 69811913848265FB CRC64; MDFETNEDIN GVRFTWNVFP STRSDANSNV VPVGCLYTPL KEYDELNVAP YNPVVCSGPH CKSILNPYCV IDPRNSSWSC PICNSRNHLP PQYTNLSQEN MPLELQSTTI EYITNKPVTV PPIFFFVVDL TSETENLDSL KESIITSLSL LPPNALIGLI TYGNVVQLHD LSSETIDRCN VFRGDREYQL EALTEMLTGQ KPTGPGGAAS HLPNAMNKVT PFSLNRFFLP LEQVEFKLNQ LLENLSPDQW SVPAGHRPLR ATGSALNIAS LLLQGCYKNI PARIILFASG PGTVAPGLIV NSELKDPLRS HHDIDSDHAQ HYKKACKFYN QIAQRVAANG HTVDIFAGCY DQIGMSEMKQ LTDSTGGVLL LTDAFSTAIF KQSYLRLFAK DEEGYLKMAF NGNMAVKTSK DLKVQGLIGH ASAVKKTDAN NISESEIGIG ATSTWKMASL SPYHSYAIFF EIANTAANSN PMMSAPGSAD RPHLAYTQFI TTYQHSSGTN RIRVTTVANQ LLPFGTPAIA ASFDQEAAAV LMARIAVHKA ETDDGADVIR WLDRTLIKLC QKYADYNKDD PQSFRLAPNF SLYPQFTYYL RRSQFLSVFN NSPDETAFYR HIFTREDTTN SLIMIQPTLT SFSMEDDPQP VLLDSISVKP NTILLLDTFF FILIYHGEQI AQWRKAGYQD DPQYADFKAL LEEPKLEAAE LLVDRFPLPR FIDTEAGGSQ ARFLLSKLNP SDNYQDMARG GSTIVLTDDV SLQNFMTHLQ QVAVSGQA //