COPG_YEAST
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 03-AUG-2022, entry version 193.
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;
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; 182.
DR ComplexPortal; CPX-1652; COPI vesicle coat complex.
DR DIP; DIP-1611N; -.
DR IntAct; P32074; 27.
DR MINT; P32074; -.
DR STRING; 4932.YNL287W; -.
DR iPTMnet; P32074; -.
DR MaxQB; P32074; -.
DR PaxDb; P32074; -.
DR PRIDE; P32074; -.
DR EnsemblFungi; YNL287W_mRNA; YNL287W; YNL287W.
DR GeneID; 855429; -.
DR KEGG; sce:YNL287W; -.
DR SGD; S000005231; SEC21.
DR VEuPathDB; FungiDB:YNL287W; -.
DR eggNOG; KOG1078; Eukaryota.
DR GeneTree; ENSGT00390000016313; -.
DR HOGENOM; CLU_010353_2_0_1; -.
DR InParanoid; P32074; -.
DR OMA; YMTQYHA; -.
DR BioCyc; YEAST:G3O-33277-MON; -.
DR Reactome; R-SCE-6807878; COPI-mediated anterograde transport.
DR Reactome; R-SCE-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
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: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 Gene3D; 1.25.10.10; -; 2.
DR Gene3D; 2.60.40.1480; -; 1.
DR Gene3D; 3.30.310.10; -; 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; PTHR10261; 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; SSF48371; 1.
DR SUPFAM; SSF49348; SSF49348; 1.
DR SUPFAM; SSF55711; SSF55711; 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
