true1990-04-012024-03-27213SEC23_YEASTYeast Sec23p acts in the cytoplasm to promote protein transport from the endoplasmic reticulum to the Golgi complex in vivo and in vitro.Hicke L.Schekman R.W.doi:10.1002/j.1460-2075.1989.tb03559.x1989EMBO J.81677-1684NUCLEOTIDE SEQUENCE [GENOMIC DNA]FUNCTIONMBY8-20CThe nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.Bussey H.Storms R.K.Ahmed A.Albermann K.Allen E.Ansorge W.Araujo R.Aparicio A.Barrell B.G.Badcock K.Benes V.Botstein D.Bowman S.Brueckner M.Carpenter J.Cherry J.M.Chung E.Churcher C.M.Coster F.Davis K.Davis R.W.Dietrich F.S.Delius H.DiPaolo T.Dubois E.Duesterhoeft A.Duncan M.Floeth M.Fortin N.Friesen J.D.Fritz C.Goffeau A.Hall J.Hebling U.Heumann K.Hilbert H.Hillier L.W.Hunicke-Smith S.Hyman R.W.Johnston M.Kalman S.Kleine K.Komp C.Kurdi O.Lashkari D.Lew H.Lin A.Lin D.Louis E.J.Marathe R.Messenguy F.Mewes H.-W.Mirtipati S.Moestl D.Mueller-Auer S.Namath A.Nentwich U.Oefner P.Pearson D.Petel F.X.Pohl T.M.Purnelle B.Rajandream M.A.Rechmann S.Rieger M.Riles L.Roberts D.Schaefer M.Scharfe M.Scherens B.Schramm S.Schroeder M.Sdicu A.-M.Tettelin H.Urrestarazu L.A.Ushinsky S.Vierendeels F.Vissers S.Voss H.Walsh S.V.Wambutt R.Wang Y.Wedler E.Wedler H.Winnett E.Zhong W.-W.Zollner A.Vo D.H.Hani J.1997Nature387103-105NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]ATCC 204508 / S288cThe reference genome sequence of Saccharomyces cerevisiae: Then and now.Engel S.R.Dietrich F.S.Fisk D.G.Binkley G.Balakrishnan R.Costanzo M.C.Dwight S.S.Hitz B.C.Karra K.Nash R.S.Weng S.Wong E.D.Lloyd P.Skrzypek M.S.Miyasato S.R.Simison M.Cherry J.M.doi:10.1534/g3.113.0089952014G3 (Bethesda)4389-398GENOME REANNOTATIONIdentification of 23 complementation groups required for post-translational events in the yeast secretory pathway.Novick P.Field C.Schekman R.W.doi:10.1016/0092-8674(80)90128-21980Cell21205-215FUNCTIONOrder of events in the yeast secretory pathway.Novick P.Ferro S.Schekman R.W.doi:10.1016/0092-8674(81)90064-71981Cell25461-469FUNCTIONReconstitution of SEC gene product-dependent intercompartmental protein transport.Baker D.Hicke L.Rexach M.F.Schleyer M.Schekman R.W.doi:10.1016/0092-8674(88)90196-11988Cell54335-344FUNCTIONReconstitution of protein transport from the endoplasmic reticulum to the Golgi complex in yeast: the acceptor Golgi compartment is defective in the sec23 mutant.Ruohola H.Kabcenell A.K.Ferro-Novick S.doi:10.1083/jcb.107.4.14651988J. Cell Biol.1071465-1476FUNCTIONDistinct sets of SEC genes govern transport vesicle formation and fusion early in the secretory pathway.Kaiser C.A.Schekman R.W.doi:10.1016/0092-8674(90)90483-u1990Cell61723-733FUNCTIONSec23p and a novel 105-kDa protein function as a multimeric complex to promote vesicle budding and protein transport from the endoplasmic reticulum.Hicke L.Yoshihisa T.Schekman R.W.doi:10.1091/mbc.3.6.6671992Mol. Biol. Cell3667-676FUNCTIONSUBUNITMulticopy STS1 restores both protein transport and ribosomal RNA stability in a new yeast sec23 mutant allele.Liang S.Lacroute F.Kepes F.1993Eur. J. Cell Biol.62270-281FUNCTIONRequirement for a GTPase-activating protein in vesicle budding from the endoplasmic reticulum.Yoshihisa T.Barlowe C.Schekman R.W.doi:10.1126/science.84516441993Science2591466-1468FUNCTIONCOPI- and COPII-coated vesicles bud directly from the endoplasmic reticulum in yeast.Bednarek S.Y.Ravazzola M.Hosobuchi M.Amherdt M.Perrelet A.Schekman R.W.Orci L.doi:10.1016/0092-8674(95)90144-21995Cell831183-1196FUNCTIONSUBCELLULAR LOCATIONYeast SEC16 gene encodes a multidomain vesicle coat protein that interacts with Sec23p.Espenshade P.J.Gimeno R.E.Holzmacher E.Teung P.Kaiser C.A.doi:10.1083/jcb.131.2.3111995J. Cell Biol.131311-324INTERACTION WITH SEC16Amino acid permeases require COPII components and the ER resident membrane protein Shr3p for packaging into transport vesicles in vitro.Kuehn M.J.Schekman R.W.Ljungdahl P.O.doi:10.1083/jcb.135.3.5851996J. Cell Biol.135585-595FUNCTIONCOPII coat subunit interactions: Sec24p and Sec23p bind to adjacent regions of Sec16p.Gimeno R.E.Espenshade P.J.Kaiser C.A.doi:10.1091/mbc.7.11.18151996Mol. Biol. Cell71815-1823INTERACTION WITH SEC16COPII subunit interactions in the assembly of the vesicle coat.Shaywitz D.A.Espenshade P.J.Gimeno R.E.Kaiser C.A.doi:10.1074/jbc.272.41.254131997J. Biol. Chem.27225413-25416IDENTIFICATION IN THE COPII COATINTERACTION WITH SEC16Specific requirements for the ER to Golgi transport of GPI-anchored proteins in yeast.Suetterlin C.Doering T.L.Schimmoeller F.Schroeder S.Riezman H.doi:10.1242/jcs.110.21.27031997J. Cell Sci.1102703-2714FUNCTIONSelective packaging of cargo molecules into endoplasmic reticulum-derived COPII vesicles.Campbell J.L.Schekman R.W.doi:10.1073/pnas.94.3.8371997Proc. Natl. Acad. Sci. U.S.A.94837-842FUNCTIONRole of endoplasmic reticulum-derived vesicles in the formation of Golgi elements in sec23 and sec18 Saccharomyces Cerevisiae mutants.Morin-Ganet M.N.Rambourg A.Clermont Y.Kepes F.doi:10.1002/(sici)1097-0185(199806)251:2<256::aid-ar15>3.0.co;2-n1998Anat. Rec.251256-264FUNCTIONCOPII-coated vesicle formation reconstituted with purified coat proteins and chemically defined liposomes.Matsuoka K.Orci L.Amherdt M.Bednarek S.Y.Hamamoto S.Schekman R.W.Yeung T.doi:10.1016/s0092-8674(00)81577-91998Cell93263-275SUBUNITSUBCELLULAR LOCATIONCOPII-cargo interactions direct protein sorting into ER-derived transport vesicles.Kuehn M.J.Herrmann J.M.Schekman R.W.doi:10.1038/344381998Nature391187-190FUNCTION OF THE SEC23/24 COMPLEXNucleation of COPII vesicular coat complex by endoplasmic reticulum to Golgi vesicle SNAREs.Springer S.Schekman R.W.doi:10.1126/science.281.5377.6981998Science281698-700INTERACTION WITH BET1; BOS1; SAR1 AND SEC24Clathrin and two components of the COPII complex, Sec23p and Sec24p, could be involved in endocytosis of the Saccharomyces cerevisiae maltose transporter.Penalver E.Lucero P.Moreno E.Lagunas R.doi:10.1128/jb.181.8.2555-2563.19991999J. Bacteriol.1812555-2563FUNCTION OF THE SEC23/24 COMPLEXShr3p mediates specific COPII coatomer-cargo interactions required for the packaging of amino acid permeases into ER-derived transport vesicles.Gilstring C.F.Melin-Larsson M.Ljungdahl P.O.doi:10.1091/mbc.10.11.35491999Mol. Biol. Cell103549-3565INTERACTION WITH SHR3Lst1p and Sec24p cooperate in sorting of the plasma membrane ATPase into COPII vesicles in Saccharomyces cerevisiae.Shimoni Y.Kurihara T.Ravazzola M.Amherdt M.Orci L.Schekman R.W.doi:10.1083/jcb.151.5.9732000J. Cell Biol.151973-984FUNCTIONSUBCELLULAR LOCATIONINTERACTION WITH SFB3The use of liposomes to study COPII- and COPI-coated vesicle formation and membrane protein sorting.Matsuoka K.Schekman R.W.doi:10.1006/meth.2000.09552000Methods20417-428FUNCTIONSUBCELLULAR LOCATIONSec24p and Iss1p function interchangeably in transport vesicle formation from the endoplasmic reticulum in Saccharomyces cerevisiae.Kurihara T.Hamamoto S.Gimeno R.E.Kaiser C.A.Schekman R.W.Yoshihisa T.doi:10.1091/mbc.11.3.9832000Mol. Biol. Cell11983-998INTERACTION WITH PDR17An acidic sequence of a putative yeast Golgi membrane protein binds COPII and facilitates ER export.Votsmeier C.Gallwitz D.doi:10.1093/emboj/20.23.67422001EMBO J.206742-6750INTERACTION WITH SYS1Distinct roles for the cytoplasmic tail sequences of Emp24p and Erv25p in transport between the endoplasmic reticulum and Golgi complex.Belden W.J.Barlowe C.doi:10.1074/jbc.m1081132002001J. Biol. Chem.27643040-43048INTERACTION WITH EMP24 AND ERV25Dynamics of the COPII coat with GTP and stable analogues.Antonny B.Madden D.T.Hamamoto S.Orci L.Schekman R.W.doi:10.1038/350785002001Nat. Cell Biol.3531-537IDENTIFICATION IN THE COPII COATGlobal analysis of Cdk1 substrate phosphorylation sites provides insights into evolution.Holt L.J.Tuch B.B.Villen J.Johnson A.D.Gygi S.P.Morgan D.O.doi:10.1126/science.11728672009Science3251682-1686IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.Van Damme P.Lasa M.Polevoda B.Gazquez C.Elosegui-Artola A.Kim D.S.De Juan-Pardo E.Demeyer K.Hole K.Larrea E.Timmerman E.Prieto J.Arnesen T.Sherman F.Gevaert K.Aldabe R.doi:10.1073/pnas.12103031092012Proc. Natl. Acad. Sci. U.S.A.10912449-12454ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Structure of the Sec23p/24p and Sec13p/31p complexes of COPII.Lederkremer G.Z.Cheng Y.Petre B.M.Vogan E.Springer S.Schekman R.W.Walz T.Kirchhausen T.doi:10.1073/pnas.1913593982001Proc. Natl. Acad. Sci. U.S.A.9810704-10709ELECTRON MICROSCOPY OF THE SEC23/24 COMPLEXSurface structure of the COPII-coated vesicle.Matsuoka K.Schekman R.W.Orci L.Heuser J.E.doi:10.1073/pnas.2415221982001Proc. Natl. Acad. Sci. U.S.A.9813705-13709ELECTRON MICROSCOPY OF THE SEC23/24 COMPLEXSec16p potentiates the action of COPII proteins to bud transport vesicles.Supek F.Madden D.T.Hamamoto S.Orci L.Schekman R.W.doi:10.1083/jcb.2002070532002J. Cell Biol.1581029-1038SUBCELLULAR LOCATIONSNARE selectivity of the COPII coat.Mossessova E.Bickford L.C.Goldberg J.doi:10.1016/s0092-8674(03)00608-12003Cell114483-495FUNCTION OF THE SEC23/24 COMPLEXINTERACTION WITH BET1; SEC22 AND SED5Self-assembly of minimal COPII cages.Antonny B.Gounon P.Schekman R.W.Orci L.doi:10.1038/sj.embor.embor8122003EMBO Rep.4419-424STRUCTURE OF THE COPII COMPLEXUbp3 requires a cofactor, Bre5, to specifically de-ubiquitinate the COPII protein, Sec23.Cohen M.Stutz F.Belgareh N.Haguenauer-Tsapis R.Dargemont C.doi:10.1038/ncb10032003Nat. Cell Biol.5661-667UBIQUITINATIONINTERACTION WITH SEC24Reconstitution of coat protein complex II (COPII) vesicle formation from cargo-reconstituted proteoliposomes reveals the potential role of GTP hydrolysis by Sar1p in protein sorting.Sato K.Nakano A.doi:10.1074/jbc.c3004572002004J. Biol. Chem.2791330-1335COPII COMPLEX ASSEMBLYFUNCTION OF THE COPII COMPLEXExploration of the function and organization of the yeast early secretory pathway through an epistatic miniarray profile.Schuldiner M.Collins S.R.Thompson N.J.Denic V.Bhamidipati A.Punna T.Ihmels J.Andrews B.Boone C.Greenblatt J.F.Weissman J.S.Krogan N.J.doi:10.1016/j.cell.2005.08.0312005Cell123507-519FUNCTIONINTERACTION WITH GRH1The yeast orthologue of GRASP65 forms a complex with a coiled-coil protein that contributes to ER to Golgi traffic.Behnia R.Barr F.A.Flanagan J.J.Barlowe C.Munro S.doi:10.1083/jcb.2006071512007J. Cell Biol.176255-261INTERACTION WITH GHR1TRAPPI tethers COPII vesicles by binding the coat subunit Sec23.Cai H.Yu S.Menon S.Cai Y.Lazarova D.Fu C.Reinisch K.Hay J.C.Ferro-Novick S.doi:10.1038/nature055272007Nature445941-944FUNCTIONINTERACTION WITH BET3Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coat.Bi X.Corpina R.A.Goldberg J.doi:10.1038/nature010402002Nature419271-277X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH SAR1 AND ZINCBVBY232.50A/C=1-7682.75A=1-7682.50A=2-76823.00A/D/G=1-7684.90A=2-7684.60A/E=2-7683.80A=1-768519SEC23-LST1 COPII cargo recruitment complexCOPII vesicle coat complex41PredictedSEC23EukaryotaCOPII-mediated vesicle transportCargo concentration in the ERAntigen Presentation: Folding, assembly and peptide loading of class I MHC9 hits in 10 CRISPR screensProteinSec23-likeSec23_Cbeta-sandwich domain of Sec23/24Sec23/Sec24 helical domainSeverinvon Willebrand factor, type A domainZn-finger domain of Sec23/24ADF-H/Gelsolin-like_dom_sfGelsolin-like_domGelsolin-like_dom_sfSec23Sec23/24_helical_domSec23/24_helical_dom_sfSec23/24_trunk_domSec23_24_beta_SSec23_CvWFA_dom_sfZnf_Sec23_Sec24Znf_Sec23_Sec24_sfPROTEIN TRANSPORT PROTEIN SEC23PROTEIN TRANSPORT PROTEIN SEC23GelsolinSec23_BSSec23_helicalSec23_trunkzf-Sec23_Sec24beta-sandwich domain of Sec23/24C-terminal, gelsolin-like domain of Sec23/24Helical domain of Sec23/24vWA-likeZn-finger domain of Sec23/24Protein transport protein SEC23SEC23YPR181CP9705.14Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. SEC23 interacts with BET3 in order to target TRAPPI complex to COPII involved in internalization of plasma membrane proteins like the maltose transporter.The COPII coat is composed of at least 7 proteins: the SEC23/24 complex, the SEC13/31 complex, SFB2, SFB3 and the protein SAR1. Forms two other heterodimeric complexes with SFB3 and PDR17. Interacts with BET1, BET3, BOS1, EMP24, GRH1, SEC16, SEC22 and SYS1.Ubiquitinated. Ubiquitination is required for the formation of the SEC23/24 complex. Deubiquitinated by the UBP3/BRE5 complex.Belongs to the SEC23/SEC24 family. SEC23 subfamily.Protein transport protein SEC2385385176856618083N-acetylmethionine310112223283337485159697273767779818688919398100103105108113123129134149156168172183190198221223224227228230231243262276283290294297311315322339342348355365369373378386394397399408412420437439443450456462484495496498499512517521525539545563564567571573578581582592594596603613618625628632634636645647653657659666668676678680682684685703710715719721722725740742752763false4false5false3false5false5false3false4false3GRH1HRR25SAR1SEC16SEC24SEC31SFB2TRS331990-04-01185385ac9c20f9b74ad92c0a4e834b8ade68a3MDFETNEDINGVRFTWNVFPSTRSDANSNVVPVGCLYTPLKEYDELNVAPYNPVVCSGPHCKSILNPYCVIDPRNSSWSCPICNSRNHLPPQYTNLSQENMPLELQSTTIEYITNKPVTVPPIFFFVVDLTSETENLDSLKESIITSLSLLPPNALIGLITYGNVVQLHDLSSETIDRCNVFRGDREYQLEALTEMLTGQKPTGPGGAASHLPNAMNKVTPFSLNRFFLPLEQVEFKLNQLLENLSPDQWSVPAGHRPLRATGSALNIASLLLQGCYKNIPARIILFASGPGTVAPGLIVNSELKDPLRSHHDIDSDHAQHYKKACKFYNQIAQRVAANGHTVDIFAGCYDQIGMSEMKQLTDSTGGVLLLTDAFSTAIFKQSYLRLFAKDEEGYLKMAFNGNMAVKTSKDLKVQGLIGHASAVKKTDANNISESEIGIGATSTWKMASLSPYHSYAIFFEIANTAANSNPMMSAPGSADRPHLAYTQFITTYQHSSGTNRIRVTTVANQLLPFGTPAIAASFDQEAAAVLMARIAVHKAETDDGADVIRWLDRTLIKLCQKYADYNKDDPQSFRLAPNFSLYPQFTYYLRRSQFLSVFNNSPDETAFYRHIFTREDTTNSLIMIQPTLTSFSMEDDPQPVLLDSISVKPNTILLLDTFFFILIYHGEQIAQWRKAGYQDDPQYADFKALLEEPKLEAAELLVDRFPLPRFIDTEAGGSQARFLLSKLNPSDNYQDMARGGSTIVLTDDVSLQNFMTHLQQVAVSGQAtruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetrue