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COG1_YEAST
ID   COG1_YEAST              Reviewed;         417 AA.
AC   P53079; D6VVB2;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=Conserved oligomeric Golgi complex subunit 1;
DE            Short=COG complex subunit 1;
DE   AltName: Full=Complexed with DOR1 protein 3;
DE   AltName: Full=Component of oligomeric Golgi complex 1;
DE   AltName: Full=Protein SEC36;
GN   Name=COG1; Synonyms=COD3, SEC36, TFI1; OrderedLocusNames=YGL223C;
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].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9290212;
RX   DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA   Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT   "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT   chromosome VII.";
RL   Yeast 13:1077-1090(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(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   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   SUBUNIT.
RX   PubMed=11703943; DOI=10.1016/s1534-5807(01)00063-6;
RA   Whyte J.R., Munro S.;
RT   "The Sec34/35 Golgi transport complex is related to the exocyst, defining a
RT   family of complexes involved in multiple steps of membrane traffic.";
RL   Dev. Cell 1:527-537(2001).
RN   [6]
RP   IDENTIFICATION IN THE COG COMPLEX, AND FUNCTION OF THE COG COMPLEX.
RX   PubMed=12011112; DOI=10.1083/jcb.200111081;
RA   Suvorova E.S., Duden R., Lupashin V.V.;
RT   "The Sec34/Sec35p complex, a Ypt1p effector required for retrograde intra-
RT   Golgi trafficking, interacts with Golgi SNAREs and COPI vesicle coat
RT   proteins.";
RL   J. Cell Biol. 157:631-643(2002).
RN   [7]
RP   FUNCTION, AND IDENTIFICATION IN THE COG COMPLEX.
RX   PubMed=12006647; DOI=10.1091/mbc.01-10-0495;
RA   Ram R.J., Li B., Kaiser C.A.;
RT   "Identification of sec36p, sec37p, and sec38p: components of yeast complex
RT   that contains sec34p and sec35p.";
RL   Mol. Biol. Cell 13:1484-1500(2002).
RN   [8]
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   [9]
RP   COMPOSITION OF THE COG COMPLEX, AND INTERACTION WITH COG3 AND COG4.
RX   PubMed=15047703; DOI=10.1074/jbc.m400662200;
RA   Loh E., Hong W.;
RT   "The binary interacting network of the conserved oligomeric Golgi tethering
RT   complex.";
RL   J. Biol. Chem. 279:24640-24648(2004).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305, AND IDENTIFICATION BY
RP   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   [11]
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).
CC   -!- FUNCTION: Acts as essential component of the peripheral membrane COG
CC       complex that is involved in intra-Golgi protein trafficking. COG is
CC       located at the cis-Golgi, and regulates tethering of retrograde intra-
CC       Golgi vesicles and possibly a number of other membrane trafficking
CC       events. {ECO:0000269|PubMed:12006647, ECO:0000269|PubMed:12011112}.
CC   -!- SUBUNIT: Component of the conserved oligomeric Golgi (COG or
CC       Sec34/Sec35) complex which consists of eight different proteins COG1-
CC       COG8. {ECO:0000269|PubMed:11703943, ECO:0000269|PubMed:12006647,
CC       ECO:0000269|PubMed:12011112}.
CC   -!- INTERACTION:
CC       P53079; P53271: COG2; NbExp=16; IntAct=EBI-4835, EBI-16614;
CC       P53079; P40094: COG3; NbExp=12; IntAct=EBI-4835, EBI-16605;
CC       P53079; Q06096: COG4; NbExp=9; IntAct=EBI-4835, EBI-4823;
CC       P53079; P53951: COG5; NbExp=6; IntAct=EBI-4835, EBI-4841;
CC       P53079; P53959: COG6; NbExp=5; IntAct=EBI-4835, EBI-4829;
CC       P53079; Q04632: COG8; NbExp=8; IntAct=EBI-4835, EBI-6035;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC       {ECO:0000250}.
CC   -!- MISCELLANEOUS: Present with 2190 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the COG1 family. {ECO:0000305}.
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DR   EMBL; Z72745; CAA96939.1; -; Genomic_DNA.
DR   EMBL; AY692796; AAT92815.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA07896.1; -; Genomic_DNA.
DR   PIR; S64245; S64245.
DR   RefSeq; NP_011292.1; NM_001181088.1.
DR   AlphaFoldDB; P53079; -.
DR   SMR; P53079; -.
DR   BioGRID; 33036; 49.
DR   ComplexPortal; CPX-1840; COG Golgi transport complex.
DR   DIP; DIP-4374N; -.
DR   IntAct; P53079; 9.
DR   MINT; P53079; -.
DR   STRING; 4932.YGL223C; -.
DR   iPTMnet; P53079; -.
DR   MaxQB; P53079; -.
DR   PaxDb; P53079; -.
DR   PRIDE; P53079; -.
DR   EnsemblFungi; YGL223C_mRNA; YGL223C; YGL223C.
DR   GeneID; 852649; -.
DR   KEGG; sce:YGL223C; -.
DR   SGD; S000003191; COG1.
DR   VEuPathDB; FungiDB:YGL223C; -.
DR   eggNOG; ENOG502S2SK; Eukaryota.
DR   HOGENOM; CLU_657476_0_0_1; -.
DR   InParanoid; P53079; -.
DR   OMA; CFNDEKF; -.
DR   BioCyc; YEAST:G3O-30697-MON; -.
DR   PRO; PR:P53079; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P53079; protein.
DR   GO; GO:0000139; C:Golgi membrane; IC:ComplexPortal.
DR   GO; GO:0017119; C:Golgi transport complex; IMP:SGD.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; IMP:SGD.
DR   GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IMP:SGD.
DR   GO; GO:0007030; P:Golgi organization; IMP:SGD.
DR   GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IMP:SGD.
DR   GO; GO:0000301; P:retrograde transport, vesicle recycling within Golgi; IMP:SGD.
PE   1: Evidence at protein level;
KW   Acetylation; Golgi apparatus; Membrane; Phosphoprotein; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..417
FT                   /note="Conserved oligomeric Golgi complex subunit 1"
FT                   /id="PRO_0000213494"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         305
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   417 AA;  48337 MW;  65F7EF5B5194D9AB CRC64;
     MDEVLPLFRD SHIPQIKDYQ LELQNDLTKT NEAFQKNLLK NYNKILSLTD SVNDLSLNLK
     NVDQDFKSLC FNDEKFQLNK LTPLPYQTTT HISPPRDEEK VSIPSQNILV ISNWTISINN
     FCNRIVTSTT PSRIFDELLL NFHELSLIPV PSKFEALVKD KCCRLQKFLV DSMKTLNLTL
     LQWVKLYNLL NTEFSSKWDD DLLSIFNESL FETLFNDNVQ ALLISSANSK DHQYHSNQQY
     KDAIVVDFVN SSTFRDHLIR RTVKEINTHL DTLSTLRAKL KEPETLHKLD IFHDNDTNLN
     DGTVSPLDDD ALKQYIDTAV FYSKGLTNDT TLQIYQTVQP TIEILQNLEL YKCPQETLTD
     LRNKLITQLQ EFKTQISSRL PSPLENSTSV VDDFITSYNN HNLLQLVIDQ ITQLRQQ
 
 
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