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Coatomer subunit gamma (Gamma-coat protein) (Gamma-COP)

 COPG_YEAST              Reviewed;         935 AA.
P32074; D6W0Q6;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 2.
22-NOV-2017, entry version 160.
RecName: Full=Coatomer subunit gamma;
AltName: Full=Gamma-coat protein;
Short=Gamma-COP;
Name=SEC21; OrderedLocusNames=YNL287W; ORFNames=N0543;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, AND SUBCELLULAR
LOCATION.
PubMed=1461285; DOI=10.1038/360603a0;
Hosobuchi M.M., Kreis T., Schekman R.;
"SEC21 is a gene required for ER to Golgi protein transport that
encodes a subunit of a yeast coatomer.";
Nature 360:603-605(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169873;
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F.,
Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M.,
Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N.,
Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D.,
Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A.,
Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A.,
Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C.,
Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M.,
Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J.,
Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L.,
Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M.,
Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P.,
Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A.,
Wambutt R., Wedler H., Zollner A., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV
and its evolutionary implications.";
Nature 387:93-98(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
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.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
FUNCTION.
PubMed=8001155; DOI=10.1016/0092-8674(94)90011-6;
Letourneur F., Gaynor E.C., Hennecke S., Demolliere C., Durden R.,
Emr S.D., Riezman H., Cosson P.;
"Coatomer is essential for retrieval of dilysine-tagged proteins to
the endoplasmic reticulum.";
Cell 79:1199-1207(1994).
[5]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[6]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[7]
SUBCELLULAR LOCATION.
PubMed=17101773; DOI=10.1128/MCB.00577-06;
Gabriely G., Kama R., Gerst J.E.;
"Involvement of specific COPI subunits in protein sorting from the
late endosome to the vacuole in yeast.";
Mol. Cell. Biol. 27:526-540(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-653, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[9]
INTERACTION WITH GEA1.
PubMed=19039328; DOI=10.1038/embor.2008.221;
Deng Y., Golinelli-Cohen M.P., Smirnova E., Jackson C.L.;
"A COPI coat subunit interacts directly with an early-Golgi localized
Arf exchange factor.";
EMBO Rep. 10:58-64(2009).
[10]
INTERACTION WITH KEI1.
PubMed=19726565; DOI=10.1091/mbc.E09-03-0235;
Sato K., Noda Y., Yoda K.;
"Kei1: a novel subunit of inositolphosphorylceramide synthase,
essential for its enzyme activity and Golgi localization.";
Mol. Biol. Cell 20:4444-4457(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-638; SER-643 AND
SER-653, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[12]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-647, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22106047; DOI=10.1002/pmic.201100166;
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
"Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
Proteomics 12:236-240(2012).
-!- FUNCTION: The coatomer is a cytosolic protein complex that binds
to dilysine motifs and reversibly associates with Golgi non-
clathrin-coated vesicles, which further mediate biosynthetic
protein transport from the ER, via the Golgi up to the trans Golgi
network. Coatomer complex is required for budding from Golgi
membranes, and is essential for the retrograde Golgi-to-ER
transport of dilysine-tagged proteins.
{ECO:0000269|PubMed:1461285, ECO:0000269|PubMed:8001155}.
-!- SUBUNIT: Oligomeric complex that consists of at least the alpha,
beta, beta', gamma, delta, epsilon and zeta subunits. Interacts
(via C-terminus) with GEA1 (via N-terminal region) and KEI1 (via
C-terminal region). {ECO:0000269|PubMed:1461285,
ECO:0000269|PubMed:19039328, ECO:0000269|PubMed:19726565}.
-!- INTERACTION:
P47102:GEA1; NbExp=6; IntAct=EBI-4891, EBI-7539;
-!- SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus membrane;
Peripheral membrane protein; Cytoplasmic side. Cytoplasmic
vesicle, COPI-coated vesicle membrane; Peripheral membrane
protein; Cytoplasmic side. Endosome. Note=The coatomer is
cytoplasmic or polymerized on the cytoplasmic side of the Golgi,
as well as on the vesicles/buds originating from it.
{ECO:0000250}.
-!- MISCELLANEOUS: Present with 77900 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the COPG family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M59708; AAA34598.1; -; Genomic_DNA.
EMBL; Z71563; CAA96204.1; -; Genomic_DNA.
EMBL; BK006947; DAA10272.1; -; Genomic_DNA.
PIR; S63261; S63261.
RefSeq; NP_014112.1; NM_001183125.1.
ProteinModelPortal; P32074; -.
BioGrid; 35550; 148.
DIP; DIP-1611N; -.
IntAct; P32074; 27.
MINT; MINT-399140; -.
STRING; 4932.YNL287W; -.
iPTMnet; P32074; -.
MaxQB; P32074; -.
PRIDE; P32074; -.
EnsemblFungi; YNL287W; YNL287W; YNL287W.
GeneID; 855429; -.
KEGG; sce:YNL287W; -.
EuPathDB; FungiDB:YNL287W; -.
SGD; S000005231; SEC21.
GeneTree; ENSGT00390000016313; -.
HOGENOM; HOG000184434; -.
InParanoid; P32074; -.
KO; K17267; -.
OMA; SPYAVCM; -.
OrthoDB; EOG092C0K4D; -.
BioCyc; YEAST:G3O-33277-MONOMER; -.
Reactome; R-SCE-6807878; COPI-mediated anterograde transport.
Reactome; R-SCE-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
PRO; PR:P32074; -.
Proteomes; UP000002311; Chromosome XIV.
GO; GO:0030126; C:COPI vesicle coat; IDA:SGD.
GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; IMP:SGD.
GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; IMP:SGD.
Gene3D; 1.25.10.10; -; 1.
Gene3D; 2.60.40.1480; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
InterPro; IPR013041; Clathrin_app_Ig-like_sf.
InterPro; IPR009028; Coatomer/calthrin_app_sub_C.
InterPro; IPR032154; Coatomer_g_Cpla.
InterPro; IPR017106; Coatomer_gsu.
InterPro; IPR013040; Coatomer_gsu_app_Ig-like_dom.
InterPro; IPR037067; Coatomer_gsu_app_sf.
PANTHER; PTHR10261; PTHR10261; 1.
Pfam; PF01602; Adaptin_N; 1.
Pfam; PF16381; Coatomer_g_Cpla; 1.
Pfam; PF08752; COP-gamma_platf; 1.
PIRSF; PIRSF037093; Coatomer_gamma_subunit; 1.
SUPFAM; SSF48371; SSF48371; 1.
SUPFAM; SSF49348; SSF49348; 1.
SUPFAM; SSF55711; SSF55711; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Cytoplasmic vesicle; Endosome;
ER-Golgi transport; Golgi apparatus; Isopeptide bond; Membrane;
Phosphoprotein; Protein transport; Reference proteome; Repeat;
Transport; Ubl conjugation.
CHAIN 1 935 Coatomer subunit gamma.
/FTId=PRO_0000193861.
REPEAT 258 296 HEAT 1.
REPEAT 337 372 HEAT 2.
REPEAT 373 410 HEAT 3.
REPEAT 412 449 HEAT 4.
REPEAT 524 562 HEAT 5.
MOD_RES 638 638 Phosphothreonine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 643 643 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 653 653 Phosphoserine.
{ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
CROSSLNK 647 647 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
CONFLICT 353 353 D -> N (in Ref. 1; AAA34598).
{ECO:0000305}.
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


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