SEC23_YEAST
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 03-AUG-2022, entry version 206.
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; DOI=10.1242/jcs.110.21.2703;
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; DOI=10.1128/jb.181.8.2555-2563.1999;
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 internalization 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 P15303; Q04410: GRH1; NbExp=4; IntAct=EBI-16584, EBI-32083;
CC P15303; P29295: HRR25; NbExp=5; IntAct=EBI-16584, EBI-8536;
CC P15303; P20606: SAR1; NbExp=3; IntAct=EBI-16584, EBI-16472;
CC P15303; P48415: SEC16; NbExp=5; IntAct=EBI-16584, EBI-16551;
CC P15303; P40482: SEC24; NbExp=5; IntAct=EBI-16584, EBI-16592;
CC P15303; P38968: SEC31; NbExp=3; IntAct=EBI-16584, EBI-20524;
CC P15303; P53953: SFB2; NbExp=4; IntAct=EBI-16584, EBI-17006;
CC P15303; 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}.
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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 PDB; 6ZGA; EM; 4.60 A; A/E=2-768.
DR PDBsum; 1M2O; -.
DR PDBsum; 1M2V; -.
DR PDBsum; 2QTV; -.
DR PDBsum; 4BZI; -.
DR PDBsum; 6GNI; -.
DR PDBsum; 6ZGA; -.
DR AlphaFoldDB; P15303; -.
DR SMR; P15303; -.
DR BioGRID; 36353; 516.
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 SGD; S000006385; SEC23.
DR VEuPathDB; FungiDB:YPR181C; -.
DR eggNOG; KOG1986; Eukaryota.
DR GeneTree; ENSGT00390000006916; -.
DR HOGENOM; CLU_008658_3_0_1; -.
DR InParanoid; P15303; -.
DR OMA; FPPHYAE; -.
DR BioCyc; YEAST:G3O-34306-MON; -.
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; 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: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; IDA:ComplexPortal.
DR GO; GO:0006886; P:intracellular protein transport; IDA:ComplexPortal.
DR GO; GO:0016236; P:macroautophagy; IMP:SGD.
DR GO; GO:1902953; P:positive regulation of ER to Golgi vesicle-mediated transport; IDA:ComplexPortal.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:FlyBase.
DR GO; GO:0070863; P:positive regulation of protein exit from endoplasmic reticulum; IDA:ComplexPortal.
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 BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:12239560"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:12239560"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:12239560"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:12239560"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT HELIX 3..10
FT /evidence="ECO:0007829|PDB:1M2O"
FT STRAND 11..22
FT /evidence="ECO:0007829|PDB:1M2O"
FT HELIX 23..28
FT /evidence="ECO:0007829|PDB:1M2O"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:1M2O"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:2QTV"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:1M2O"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:1M2V"
FT TURN 73..76
FT /evidence="ECO:0007829|PDB:1M2O"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:2QTV"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:1M2O"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:2QTV"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:1M2O"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:1M2V"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:1M2O"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:1M2O"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:1M2O"
FT HELIX 134..149
FT /evidence="ECO:0007829|PDB:1M2O"
FT STRAND 156..168
FT /evidence="ECO:0007829|PDB:1M2O"
FT STRAND 172..183
FT /evidence="ECO:0007829|PDB:1M2O"
FT HELIX 190..198
FT /evidence="ECO:0007829|PDB:1M2O"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:1M2O"
FT HELIX 224..227
FT /evidence="ECO:0007829|PDB:1M2O"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:1M2O"
FT HELIX 231..243
FT /evidence="ECO:0007829|PDB:1M2O"
FT HELIX 262..276
FT /evidence="ECO:0007829|PDB:1M2O"
FT STRAND 283..290
FT /evidence="ECO:0007829|PDB:1M2O"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:1M2O"
FT HELIX 311..315
FT /evidence="ECO:0007829|PDB:1M2O"
FT HELIX 322..339
FT /evidence="ECO:0007829|PDB:1M2O"
FT STRAND 342..348
FT /evidence="ECO:0007829|PDB:1M2O"
FT HELIX 355..365
FT /evidence="ECO:0007829|PDB:1M2O"
FT STRAND 369..373
FT /evidence="ECO:0007829|PDB:1M2O"
FT HELIX 378..386
FT /evidence="ECO:0007829|PDB:1M2O"
FT STRAND 394..397
FT /evidence="ECO:0007829|PDB:1M2O"
FT STRAND 399..408
FT /evidence="ECO:0007829|PDB:1M2O"
FT STRAND 412..420
FT /evidence="ECO:0007829|PDB:1M2O"
FT STRAND 437..439
FT /evidence="ECO:0007829|PDB:1M2O"
FT STRAND 443..450
FT /evidence="ECO:0007829|PDB:1M2O"
FT STRAND 456..462
FT /evidence="ECO:0007829|PDB:1M2O"
FT STRAND 484..495
FT /evidence="ECO:0007829|PDB:1M2O"
FT TURN 496..498
FT /evidence="ECO:0007829|PDB:1M2O"
FT STRAND 499..512
FT /evidence="ECO:0007829|PDB:1M2O"
FT HELIX 517..521
FT /evidence="ECO:0007829|PDB:1M2O"
FT HELIX 525..539
FT /evidence="ECO:0007829|PDB:1M2O"
FT HELIX 545..563
FT /evidence="ECO:0007829|PDB:1M2O"
FT STRAND 564..567
FT /evidence="ECO:0007829|PDB:2QTV"
FT HELIX 571..573
FT /evidence="ECO:0007829|PDB:1M2O"
FT TURN 578..581
FT /evidence="ECO:0007829|PDB:1M2O"
FT HELIX 582..592
FT /evidence="ECO:0007829|PDB:1M2O"
FT TURN 594..596
FT /evidence="ECO:0007829|PDB:1M2O"
FT HELIX 603..613
FT /evidence="ECO:0007829|PDB:1M2O"
FT HELIX 618..625
FT /evidence="ECO:0007829|PDB:1M2O"
FT STRAND 628..632
FT /evidence="ECO:0007829|PDB:1M2O"
FT STRAND 634..636
FT /evidence="ECO:0007829|PDB:1M2O"
FT HELIX 645..647
FT /evidence="ECO:0007829|PDB:1M2O"
FT STRAND 653..657
FT /evidence="ECO:0007829|PDB:1M2O"
FT STRAND 659..666
FT /evidence="ECO:0007829|PDB:1M2O"
FT HELIX 668..676
FT /evidence="ECO:0007829|PDB:1M2O"
FT HELIX 678..680
FT /evidence="ECO:0007829|PDB:1M2O"
FT HELIX 682..684
FT /evidence="ECO:0007829|PDB:1M2V"
FT HELIX 685..703
FT /evidence="ECO:0007829|PDB:1M2O"
FT STRAND 710..715
FT /evidence="ECO:0007829|PDB:1M2O"
FT HELIX 719..721
FT /evidence="ECO:0007829|PDB:1M2O"
FT HELIX 722..725
FT /evidence="ECO:0007829|PDB:1M2O"
FT STRAND 740..742
FT /evidence="ECO:0007829|PDB:2QTV"
FT HELIX 752..763
FT /evidence="ECO:0007829|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
