ID   COPG_YEAST              Reviewed;         935 AA.
AC   P32074; D6W0Q6;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   02-SEP-2026, entry version 210.
DE   RecName: Full=Coatomer subunit gamma;
DE   AltName: Full=Gamma-coat protein;
DE            Short=Gamma-COP;
GN   Name=SEC21; OrderedLocusNames=YNL287W; ORFNames=N0543;
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], FUNCTION, SUBUNIT, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=1461285; DOI=10.1038/360603a0;
RA   Hosobuchi M.M., Kreis T., Schekman R.;
RT   "SEC21 is a gene required for ER to Golgi protein transport that encodes a
RT   subunit of a yeast coatomer.";
RL   Nature 360:603-605(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873; DOI=10.1038/387s093;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(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=8001155; DOI=10.1016/0092-8674(94)90011-6;
RA   Letourneur F., Gaynor E.C., Hennecke S., Demolliere C., Durden R.,
RA   Emr S.D., Riezman H., Cosson P.;
RT   "Coatomer is essential for retrieval of dilysine-tagged proteins to the
RT   endoplasmic reticulum.";
RL   Cell 79:1199-1207(1994).
RN   [5]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [7]
RP   SUBCELLULAR LOCATION.
RX   PubMed=17101773; DOI=10.1128/mcb.00577-06;
RA   Gabriely G., Kama R., Gerst J.E.;
RT   "Involvement of specific COPI subunits in protein sorting from the late
RT   endosome to the vacuole in yeast.";
RL   Mol. Cell. Biol. 27:526-540(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-653, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [9]
RP   INTERACTION WITH GEA1.
RX   PubMed=19039328; DOI=10.1038/embor.2008.221;
RA   Deng Y., Golinelli-Cohen M.P., Smirnova E., Jackson C.L.;
RT   "A COPI coat subunit interacts directly with an early-Golgi localized Arf
RT   exchange factor.";
RL   EMBO Rep. 10:58-64(2009).
RN   [10]
RP   INTERACTION WITH KEI1.
RX   PubMed=19726565; DOI=10.1091/mbc.e09-03-0235;
RA   Sato K., Noda Y., Yoda K.;
RT   "Kei1: a novel subunit of inositolphosphorylceramide synthase, essential
RT   for its enzyme activity and Golgi localization.";
RL   Mol. Biol. Cell 20:4444-4457(2009).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-638; SER-643 AND SER-653, AND
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   [12]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-647, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22106047; DOI=10.1002/pmic.201100166;
RA   Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT   "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL   Proteomics 12:236-240(2012).
CC   -!- FUNCTION: The coatomer is a cytosolic protein complex that binds to
CC       dilysine motifs and reversibly associates with Golgi non-clathrin-
CC       coated vesicles, which further mediate biosynthetic protein transport
CC       from the ER, via the Golgi up to the trans Golgi network. Coatomer
CC       complex is required for budding from Golgi membranes, and is essential
CC       for the retrograde Golgi-to-ER transport of dilysine-tagged proteins.
CC       {ECO:0000269|PubMed:1461285, ECO:0000269|PubMed:8001155}.
CC   -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC       beta', gamma, delta, epsilon and zeta subunits. Interacts (via C-
CC       terminus) with GEA1 (via N-terminal region) and KEI1 (via C-terminal
CC       region). {ECO:0000269|PubMed:1461285, ECO:0000269|PubMed:19039328,
CC       ECO:0000269|PubMed:19726565}.
CC   -!- INTERACTION:
CC       P32074; P47102: GEA1; NbExp=6; IntAct=EBI-4891, EBI-7539;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus membrane; Peripheral
CC       membrane protein; Cytoplasmic side. Cytoplasmic vesicle, COPI-coated
CC       vesicle membrane; Peripheral membrane protein; Cytoplasmic side.
CC       Endosome. Note=The coatomer is cytoplasmic or polymerized on the
CC       cytoplasmic side of the Golgi, as well as on the vesicles/buds
CC       originating from it. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Present with 77900 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the COPG family. {ECO:0000305}.
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DR   EMBL; M59708; AAA34598.1; -; Genomic_DNA.
DR   EMBL; Z71563; CAA96204.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10272.1; -; Genomic_DNA.
DR   PIR; S63261; S63261.
DR   RefSeq; NP_014112.1; NM_001183125.1.
DR   AlphaFoldDB; P32074; -.
DR   SMR; P32074; -.
DR   BioGRID; 35550; 202.
DR   ComplexPortal; CPX-1652; COPI vesicle coat complex.
DR   DIP; DIP-1611N; -.
DR   FunCoup; P32074; 1503.
DR   IntAct; P32074; 29.
DR   MINT; P32074; -.
DR   STRING; 4932.YNL287W; -.
DR   iPTMnet; P32074; -.
DR   PaxDb; 4932-YNL287W; -.
DR   PeptideAtlas; P32074; -.
DR   EnsemblFungi; YNL287W_mRNA; YNL287W; YNL287W.
DR   GeneID; 855429; -.
DR   KEGG; sce:YNL287W; -.
DR   AGR; SGD:S000005231; -.
DR   SGD; S000005231; SEC21.
DR   VEuPathDB; FungiDB:YNL287W; -.
DR   eggNOG; KOG1078; Eukaryota.
DR   HOGENOM; CLU_010353_2_0_1; -.
DR   InParanoid; P32074; -.
DR   OMA; DFIEDCE; -.
DR   OrthoDB; 1074925at2759; -.
DR   BioCyc; YEAST:G3O-33277-MONOMER; -.
DR   Reactome; R-SCE-6807878; COPI-mediated anterograde transport.
DR   Reactome; R-SCE-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR   BioGRID-ORCS; 855429; 3 hits in 10 CRISPR screens.
DR   PRO; PR:P32074; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P32074; protein.
DR   GO; GO:0030126; C:COPI vesicle coat; IDA:SGD.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0070971; C:endoplasmic reticulum exit site; IDA:SGD.
DR   GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IBA:GO_Central.
DR   GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:SGD.
DR   GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0009306; P:protein secretion; IBA:GO_Central.
DR   GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IMP:SGD.
DR   FunFam; 1.25.10.10:FF:000368; Coatomer subunit gamma; 1.
DR   FunFam; 2.60.40.1480:FF:000001; Coatomer subunit gamma; 1.
DR   FunFam; 3.30.310.10:FF:000008; Coatomer subunit gamma; 1.
DR   Gene3D; 2.60.40.1480; Coatomer, gamma subunit, appendage domain; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR   Gene3D; 3.30.310.10; TATA-Binding Protein; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR   InterPro; IPR013041; Clathrin_app_Ig-like_sf.
DR   InterPro; IPR009028; Coatomer/calthrin_app_sub_C.
DR   InterPro; IPR032154; Coatomer_g_Cpla.
DR   InterPro; IPR017106; Coatomer_gsu.
DR   InterPro; IPR013040; Coatomer_gsu_app_Ig-like_dom.
DR   InterPro; IPR037067; Coatomer_gsu_app_sf.
DR   InterPro; IPR012295; TBP_dom_sf.
DR   PANTHER; PTHR10261; COATOMER SUBUNIT GAMMA; 1.
DR   PANTHER; PTHR10261:SF0; COATOMER SUBUNIT GAMMA-2; 1.
DR   Pfam; PF01602; Adaptin_N; 1.
DR   Pfam; PF16381; Coatomer_g_Cpla; 1.
DR   Pfam; PF08752; COP-gamma_platf; 1.
DR   PIRSF; PIRSF037093; Coatomer_gamma_subunit; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF49348; Clathrin adaptor appendage domain; 1.
DR   SUPFAM; SSF55711; Subdomain of clathrin and coatomer appendage domain; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoplasmic vesicle; Endosome; ER-Golgi transport;
KW   Golgi apparatus; Isopeptide bond; Membrane; Phosphoprotein;
KW   Protein transport; Reference proteome; Repeat; Transport; Ubl conjugation.
FT   CHAIN           1..935
FT                   /note="Coatomer subunit gamma"
FT                   /id="PRO_0000193861"
FT   REPEAT          258..296
FT                   /note="HEAT 1"
FT   REPEAT          337..372
FT                   /note="HEAT 2"
FT   REPEAT          373..410
FT                   /note="HEAT 3"
FT   REPEAT          412..449
FT                   /note="HEAT 4"
FT   REPEAT          524..562
FT                   /note="HEAT 5"
FT   REGION          630..656
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         638
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         643
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         653
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   CROSSLNK        647
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
FT   CONFLICT        353
FT                   /note="D -> N (in Ref. 1; AAA34598)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   935 AA;  104831 MW;  99DC7D737D4EF761 CRC64;
     MSAHTYKKFE NSTSGDLPDK MTIYQDCMNT FNESPVNSKR CRLLISRLLR LLAQGETFPQ
     NEATALFFSI SKLFQHQNDP LRQAVYLAIK ELSGISEDVL MATSSIMKDV QNGSDLIKPD
     AIRSLTYVLD ESTAFSAERL LKSAVVSRHP SISSAALCTS YHLLPISEVT IRRFTNETQE
     AVLDLKQFPN QHGNSEYYPN STYISQYHAL GLLYQLKKTD KMALLKLVRH FSENNSMKNQ
     LAKVELVKIV NDLIYRDPQL FSQFRPLLSD WLSNKFESVQ LETAKLITSF ATRNSRLVAP
     ELYAAAISAL QSLLTVPRVS SRFAALRILN RISMVSPEKI VVCNPELESL INDSNRNIST
     YAITTLLKTG TSKNISSLIS TITNFIHDVS DDFKIIIIDA VRTLSLNFPQ EWKSILNFLI
     DVLKNSEGGF KFKNSIVEAL IDIVSFVPQS KELALENLCD FIEDCEFNEI LVRILHLLGK
     EGPSAPNPSL YVRHIYNRVV LENSIIRSAA VVALSKFALT KNDPTLYESI ISLLKRIAND
     KDDEVRDRAT IALEFIDSAR NKDDVIAQNL IESKYFYDIP SLESKLSSYI SSNTDSFATA
     FDVNQVRKFT EDEMKAINLK RKQEQIFNQK SETTLDTTPE AESVPEKRAD ANSFAGPNLD
     DHQEDLLATK YADELLSIEQ IKPFGQLVNS SRAISLTEPE AEFVVRGVKH LFKDNVVLQF
     NITNTLTDIA LDNVSVVCTP EISDEAELEE LFTLQVDRLL PSEEAACYVA FKKLDEIVME
     GFLNNLTFTT KEINPDTNEP FDGDEGFQDE YEIDSIFLNA GDYVKSSFTG NFSATFDELP
     CEEVAVFNIQ EDLSIQEVVD KIILNSSCLP VESTQFAPSD SNSHTLKLFG KSALTGSKVA
     LQIKMIKSSK GLALKVHGKG EDSLLCSDLV NGLMQ
//