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 13-APR-2016, entry version 160. 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; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION. RC STRAIN=MBY8-20C; RX PubMed=2670558; RA Hicke L., Schekman R.W.; RT "Yeast Sec23p acts in the cytoplasm to promote protein transport from RT the 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., RA Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., RA Chung E., Churcher C.M., Coster F., Davis K., Davis R.W., RA Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., RA Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., RA Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., RA Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., RA Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., RA Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., RA 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., RA Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., RA Zollner A., 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., RA Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and RT 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 RT protein 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 RT the Golgi complex in yeast: the acceptor Golgi compartment is RT defective in the 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 RT fusion 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 RT to 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 RT stability 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 RT the 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 RT interacts 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 RT membrane protein Shr3p for packaging into transport vesicles in RT 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., RA 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- RT derived 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 RT Golgi 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 RT proteins 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 RT transport 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 RT to 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, RT could be involved in endocytosis of the Saccharomyces cerevisiae RT maltose 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 RT for the packaging of amino acid permeases into ER-derived transport RT 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., RA Schekman R.W.; RT "Lst1p and Sec24p cooperate in sorting of the plasma membrane ATPase RT into 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 RT formation and 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 RT formation from the endoplasmic reticulum in Saccharomyces RT 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 RT COPII 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 RT Erv25p in transport between the endoplasmic reticulum and Golgi RT 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 RT insights into evolution."; RL Science 325:1682-1686(2009). RN [32] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., RA Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N- RT terminal acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [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 RT COPII 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 RT from cargo-reconstituted proteoliposomes reveals the potential role of RT GTP 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., RA Weissman J.S., Krogan N.J.; RT "Exploration of the function and organization of the yeast early RT secretory 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 RT protein 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., RA Hay J.C., 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 RT vesicle 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 CC and the selection of cargo molecules. SEC23 interacts with BET3 in CC order to target TRAPPI complex to COPII involved in CC internalisation of plasma membrane proteins like the maltose CC transporter. {ECO:0000269|PubMed:10198022, CC ECO:0000269|PubMed:10720463, ECO:0000269|PubMed:11086000, CC ECO:0000269|PubMed:12941276, ECO:0000269|PubMed:14627716, CC ECO:0000269|PubMed:1498369, ECO:0000269|PubMed:16269340, CC ECO:0000269|PubMed:17287728, ECO:0000269|PubMed:2188733, CC ECO:0000269|PubMed:2670558, ECO:0000269|PubMed:3049622, CC ECO:0000269|PubMed:3293799, ECO:0000269|PubMed:6996832, CC ECO:0000269|PubMed:7026045, ECO:0000269|PubMed:7925484, CC ECO:0000269|PubMed:8451644, ECO:0000269|PubMed:8548805, CC ECO:0000269|PubMed:8909535, ECO:0000269|PubMed:9023343, CC ECO:0000269|PubMed:9427388, ECO:0000269|PubMed:9428766, CC 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 CC SYS1. {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 O75477:ERLIN1 (xeno); NbExp=3; IntAct=EBI-16584, EBI-359299; CC Q04410:GRH1; NbExp=4; IntAct=EBI-16584, EBI-32083; CC P15108:HSC82; NbExp=5; IntAct=EBI-16584, EBI-8666; CC Q8IYX7:SAXO1 (xeno); NbExp=3; IntAct=EBI-16584, EBI-3957636; CC P48415:SEC16; NbExp=5; IntAct=EBI-16584, EBI-16551; CC P40482:SEC24; NbExp=5; IntAct=EBI-16584, EBI-16592; CC P38968:SEC31; NbExp=4; IntAct=EBI-16584, EBI-20524; CC P53953:SFB2; NbExp=9; IntAct=EBI-16584, EBI-17006; CC P38810:SFB3; NbExp=3; IntAct=EBI-16584, EBI-17012; CC Q9BSE2:TMEM79 (xeno); NbExp=3; IntAct=EBI-16584, EBI-8649725; CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle CC membrane {ECO:0000269|PubMed:10720463, CC ECO:0000269|PubMed:11086000, ECO:0000269|PubMed:12235121, CC ECO:0000269|PubMed:8548805, ECO:0000269|PubMed:9568718}; CC Peripheral membrane protein {ECO:0000269|PubMed:11086000, CC ECO:0000269|PubMed:8548805}; Cytoplasmic side CC {ECO:0000269|PubMed:8548805}. Cytoplasm CC {ECO:0000269|PubMed:8548805}. Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:8548805}; Peripheral membrane protein; CC Cytoplasmic side. Golgi apparatus membrane {ECO:0000305}; CC Peripheral membrane protein {ECO:0000305}; Cytoplasmic side CC {ECO:0000305}. CC -!- PTM: Ubiquitinated. Ubiquitination is required for the formation CC of the 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 PDBsum; 1M2O; -. DR PDBsum; 1M2V; -. DR PDBsum; 2QTV; -. DR PDBsum; 4BZI; -. DR ProteinModelPortal; P15303; -. DR SMR; P15303; 2-768. DR BioGrid; 36353; 131. DR DIP; DIP-2232N; -. DR IntAct; P15303; 49. DR MINT; MINT-540233; -. DR iPTMnet; P15303; -. DR MaxQB; P15303; -. DR PeptideAtlas; P15303; -. DR EnsemblFungi; YPR181C; YPR181C; YPR181C. DR GeneID; 856311; -. DR KEGG; sce:YPR181C; -. DR EuPathDB; FungiDB:YPR181C; -. DR SGD; S000006385; SEC23. DR GeneTree; ENSGT00390000006916; -. DR HOGENOM; HOG000231690; -. DR InParanoid; P15303; -. DR KO; K14006; -. DR OMA; RMAFGAN; -. DR OrthoDB; EOG7MPRPC; -. DR BioCyc; YEAST:G3O-34306-MONOMER; -. DR Reactome; R-SCE-204005; COPII (Coat Protein 2) 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 NextBio; 981685; -. DR PRO; PR:P15303; -. DR Proteomes; UP000002311; Chromosome XVI. DR GO; GO:0030127; C:COPII vesicle coat; IDA:SGD. 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:0006888; P:ER to Golgi vesicle-mediated transport; IEA:InterPro. 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 Gene3D; 3.40.20.10; -; 1. DR Gene3D; 3.40.50.410; -; 1. DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom. DR InterPro; IPR007123; Gelsolin-like_dom. DR InterPro; IPR006900; Sec23/24_helical_dom. DR InterPro; IPR006896; Sec23/24_trunk_dom. DR InterPro; IPR012990; Sec23_24_beta_S. DR InterPro; IPR002035; VWF_A. DR InterPro; IPR006895; Znf_Sec23_Sec24. 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 SMART; SM00327; VWA; 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; Complete proteome; Cytoplasm; KW Cytoplasmic vesicle; Endoplasmic reticulum; ER-Golgi transport; KW Golgi apparatus; Membrane; Metal-binding; Protein transport; KW Reference proteome; Transport; Ubl conjugation; Zinc. FT CHAIN 1 768 Protein transport protein SEC23. FT /FTId=PRO_0000205145. FT METAL 56 56 Zinc. {ECO:0000269|PubMed:12239560}. FT METAL 61 61 Zinc. {ECO:0000269|PubMed:12239560}. FT METAL 80 80 Zinc. {ECO:0000269|PubMed:12239560}. FT METAL 83 83 Zinc. {ECO:0000269|PubMed:12239560}. FT MOD_RES 1 1 N-acetylmethionine. FT {ECO:0000244|PubMed:22814378}. FT HELIX 3 10 {ECO:0000244|PDB:1M2O}. FT STRAND 11 22 {ECO:0000244|PDB:1M2O}. FT HELIX 23 28 {ECO:0000244|PDB:1M2O}. FT STRAND 33 37 {ECO:0000244|PDB:1M2O}. FT STRAND 48 51 {ECO:0000244|PDB:2QTV}. FT TURN 59 61 {ECO:0000244|PDB:1M2O}. FT STRAND 69 72 {ECO:0000244|PDB:1M2V}. FT TURN 73 76 {ECO:0000244|PDB:1M2O}. FT STRAND 77 79 {ECO:0000244|PDB:2QTV}. FT TURN 81 83 {ECO:0000244|PDB:1M2O}. FT STRAND 86 88 {ECO:0000244|PDB:2QTV}. FT HELIX 91 93 {ECO:0000244|PDB:1M2O}. FT STRAND 98 100 {ECO:0000244|PDB:1M2V}. FT HELIX 103 105 {ECO:0000244|PDB:1M2O}. FT STRAND 108 113 {ECO:0000244|PDB:1M2O}. FT STRAND 123 129 {ECO:0000244|PDB:1M2O}. FT HELIX 134 149 {ECO:0000244|PDB:1M2O}. FT STRAND 156 168 {ECO:0000244|PDB:1M2O}. FT STRAND 172 183 {ECO:0000244|PDB:1M2O}. FT HELIX 190 198 {ECO:0000244|PDB:1M2O}. FT STRAND 221 223 {ECO:0000244|PDB:1M2O}. FT HELIX 224 227 {ECO:0000244|PDB:1M2O}. FT STRAND 228 230 {ECO:0000244|PDB:1M2O}. FT HELIX 231 243 {ECO:0000244|PDB:1M2O}. FT HELIX 262 276 {ECO:0000244|PDB:1M2O}. FT STRAND 283 290 {ECO:0000244|PDB:1M2O}. FT STRAND 294 297 {ECO:0000244|PDB:1M2O}. FT HELIX 311 315 {ECO:0000244|PDB:1M2O}. FT HELIX 322 339 {ECO:0000244|PDB:1M2O}. FT STRAND 342 348 {ECO:0000244|PDB:1M2O}. FT HELIX 355 365 {ECO:0000244|PDB:1M2O}. FT STRAND 369 373 {ECO:0000244|PDB:1M2O}. FT HELIX 378 386 {ECO:0000244|PDB:1M2O}. FT STRAND 394 397 {ECO:0000244|PDB:1M2O}. FT STRAND 399 408 {ECO:0000244|PDB:1M2O}. FT STRAND 412 420 {ECO:0000244|PDB:1M2O}. FT STRAND 437 439 {ECO:0000244|PDB:1M2O}. FT STRAND 443 450 {ECO:0000244|PDB:1M2O}. FT STRAND 456 462 {ECO:0000244|PDB:1M2O}. FT STRAND 484 495 {ECO:0000244|PDB:1M2O}. FT TURN 496 498 {ECO:0000244|PDB:1M2O}. FT STRAND 499 512 {ECO:0000244|PDB:1M2O}. FT HELIX 517 521 {ECO:0000244|PDB:1M2O}. FT HELIX 525 539 {ECO:0000244|PDB:1M2O}. FT HELIX 545 563 {ECO:0000244|PDB:1M2O}. FT STRAND 564 567 {ECO:0000244|PDB:2QTV}. FT HELIX 571 573 {ECO:0000244|PDB:1M2O}. FT TURN 578 581 {ECO:0000244|PDB:1M2O}. FT HELIX 582 592 {ECO:0000244|PDB:1M2O}. FT TURN 594 596 {ECO:0000244|PDB:1M2O}. FT HELIX 603 613 {ECO:0000244|PDB:1M2O}. FT HELIX 618 625 {ECO:0000244|PDB:1M2O}. FT STRAND 628 632 {ECO:0000244|PDB:1M2O}. FT STRAND 634 636 {ECO:0000244|PDB:1M2O}. FT HELIX 645 647 {ECO:0000244|PDB:1M2O}. FT STRAND 653 657 {ECO:0000244|PDB:1M2O}. FT STRAND 659 666 {ECO:0000244|PDB:1M2O}. FT HELIX 668 676 {ECO:0000244|PDB:1M2O}. FT HELIX 678 680 {ECO:0000244|PDB:1M2O}. FT HELIX 682 684 {ECO:0000244|PDB:1M2V}. FT HELIX 685 703 {ECO:0000244|PDB:1M2O}. FT STRAND 710 715 {ECO:0000244|PDB:1M2O}. FT HELIX 719 721 {ECO:0000244|PDB:1M2O}. FT HELIX 722 725 {ECO:0000244|PDB:1M2O}. FT STRAND 740 742 {ECO:0000244|PDB:2QTV}. FT HELIX 752 763 {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 //