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COG3_YEAST
ID   COG3_YEAST              Reviewed;         801 AA.
AC   P40094; D3DM64;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 174.
DE   RecName: Full=Conserved oligomeric Golgi complex subunit 3;
DE            Short=COG complex subunit 3;
DE   AltName: Full=Component of oligomeric Golgi complex 3;
DE   AltName: Full=Protein SEC34;
GN   Name=COG3; Synonyms=GRD20, SEC34; OrderedLocusNames=YER157W;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169868;
RA   Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA   Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA   Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA   Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA   Botstein D., Davis R.W.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL   Nature 387:78-81(1997).
RN   [2]
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   [3]
RP   FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=10562277; DOI=10.1083/jcb.147.4.729;
RA   VanRheenen S.M., Cao X., Sapperstein S.K., Chiang E.C., Lupashin V.V.,
RA   Barlowe C., Waters M.G.;
RT   "Sec34p, a protein required for vesicle tethering to the yeast Golgi
RT   apparatus, is in a complex with Sec35p.";
RL   J. Cell Biol. 147:729-742(1999).
RN   [4]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=10588657; DOI=10.1091/mbc.10.12.4263;
RA   Spelbrink R.G., Nothwehr S.F.;
RT   "The yeast GRD20 gene is required for protein sorting in the trans-Golgi
RT   network/endosomal system and for polarization of the actin cytoskeleton.";
RL   Mol. Biol. Cell 10:4263-4281(1999).
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   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   [7]
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   [8]
RP   COMPOSITION OF THE COG COMPLEX, AND INTERACTION WITH COG1 AND COG2.
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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507 AND SER-647, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [10]
RP   IDENTIFICATION BY 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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-647, 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).
CC   -!- FUNCTION: Acts as component of the peripheral membrane COG complex that
CC       is involved in intra-Golgi protein trafficking. COG is located at the
CC       cis- Golgi, and regulates tethering of retrograde intra-Golgi vesicles
CC       and possibly a number of other membrane trafficking events. COG3 is
CC       also involved in actin cytoskeleton organization.
CC       {ECO:0000269|PubMed:10562277, ECO:0000269|PubMed:10588657,
CC       ECO:0000269|PubMed:12006647}.
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:10562277, ECO:0000269|PubMed:11703943,
CC       ECO:0000269|PubMed:12006647}.
CC   -!- INTERACTION:
CC       P40094; P53079: COG1; NbExp=12; IntAct=EBI-16605, EBI-4835;
CC       P40094; P53271: COG2; NbExp=16; IntAct=EBI-16605, EBI-16614;
CC       P40094; Q06096: COG4; NbExp=4; IntAct=EBI-16605, EBI-4823;
CC       P40094; P53951: COG5; NbExp=3; IntAct=EBI-16605, EBI-4841;
CC       P40094; P53959: COG6; NbExp=3; IntAct=EBI-16605, EBI-4829;
CC       P40094; P53195: COG7; NbExp=2; IntAct=EBI-16605, EBI-4847;
CC       P40094; Q01590: SED5; NbExp=4; IntAct=EBI-16605, EBI-16930;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000269|PubMed:10562277, ECO:0000269|PubMed:10588657}; Peripheral
CC       membrane protein {ECO:0000269|PubMed:10562277,
CC       ECO:0000269|PubMed:10588657}; Cytoplasmic side
CC       {ECO:0000269|PubMed:10562277, ECO:0000269|PubMed:10588657}.
CC   -!- MISCELLANEOUS: Present with 4140 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the COG3 family. {ECO:0000305}.
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DR   EMBL; U18917; AAB64684.1; -; Genomic_DNA.
DR   EMBL; BK006939; DAA07818.1; -; Genomic_DNA.
DR   PIR; S50660; S50660.
DR   RefSeq; NP_011084.1; NM_001179047.1.
DR   AlphaFoldDB; P40094; -.
DR   SMR; P40094; -.
DR   BioGRID; 36907; 1029.
DR   ComplexPortal; CPX-1840; COG Golgi transport complex.
DR   DIP; DIP-4728N; -.
DR   IntAct; P40094; 24.
DR   MINT; P40094; -.
DR   STRING; 4932.YER157W; -.
DR   iPTMnet; P40094; -.
DR   MaxQB; P40094; -.
DR   PaxDb; P40094; -.
DR   PRIDE; P40094; -.
DR   EnsemblFungi; YER157W_mRNA; YER157W; YER157W.
DR   GeneID; 856901; -.
DR   KEGG; sce:YER157W; -.
DR   SGD; S000000959; COG3.
DR   VEuPathDB; FungiDB:YER157W; -.
DR   eggNOG; KOG2604; Eukaryota.
DR   GeneTree; ENSGT00390000015682; -.
DR   HOGENOM; CLU_011639_2_0_1; -.
DR   InParanoid; P40094; -.
DR   OMA; LDEFELW; -.
DR   BioCyc; YEAST:G3O-30318-MON; -.
DR   PRO; PR:P40094; -.
DR   Proteomes; UP000002311; Chromosome V.
DR   RNAct; P40094; protein.
DR   GO; GO:0005801; C:cis-Golgi network; IEA:InterPro.
DR   GO; GO:0000139; C:Golgi membrane; IC:ComplexPortal.
DR   GO; GO:0017119; C:Golgi transport complex; IMP:SGD.
DR   GO; GO:0140312; F:cargo adaptor activity; IMP:SGD.
DR   GO; GO:0006914; P:autophagy; IBA:GO_Central.
DR   GO; GO:0030242; P:autophagy of peroxisome; IMP:SGD.
DR   GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IMP:SGD.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IGI:SGD.
DR   GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR   GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IMP:SGD.
DR   GO; GO:0016236; P:macroautophagy; IMP:SGD.
DR   GO; GO:0000301; P:retrograde transport, vesicle recycling within Golgi; IMP:SGD.
DR   InterPro; IPR007265; COG_su3.
DR   PANTHER; PTHR13302; PTHR13302; 1.
DR   Pfam; PF04136; Sec34; 1.
PE   1: Evidence at protein level;
KW   Golgi apparatus; Membrane; Phosphoprotein; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..801
FT                   /note="Conserved oligomeric Golgi complex subunit 3"
FT                   /id="PRO_0000213503"
FT   REGION          470..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         507
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
FT   MOD_RES         647
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   801 AA;  92544 MW;  C7AFBE99010FE571 CRC64;
     MARSRKNSLV RDIASHPTIP ESQTIVGLLD DSYLFDKLKK LSLAVENSDS LQRTDVSEGC
     SEVNGSEATT SADVKKTNKY LYYTTYLDQL NIKIDEYKVV LDQTRQVNDQ LDSSIKKFRK
     ISQDTGAFIE ETKTIYEKQS KLSNLTESIP KALHYFEVLD PIMRRLNHAT SPAIVKKSSF
     TTMLATIDES LRFLDENSDL KDAAAYRIKF KQCLIRACEL ISHFLTNLLK QTNQEILDKT
     KNKNSLTGLP STTRDAFLYS KFYTIADTFK IQVSEIVKRS NEKAYNKYHD ELNSILYECF
     NHYFQTRLRL LTPVIWSHID EIVVKDKDQG LVKFIQDGKV YFQQLCADEY KLFVEFFPEK
     ECRFKINQWF LQLCEPLYDS IRVRVLKETD ICTLCDSVTL FAPYYEFEEG SEEYVKQFTD
     IQYDKLFEPI VQKVQARLIL RVQIYVQQNI LSYRPTRDVF MISNRRRKSK TSLQGGNEDA
     TTSDDNPDPL LESYLSSFKN RSILPISPND ADDKSIDSEE STDKISQLQT YYPPLLKTLA
     LLSKIYEMIN SVVFDDLAHH VVHDCIVSLR NAYDMVIKSS AGKSDFNNLD ISLAYLKNLL
     MLRDSIQNFN IQYTVNETYL DFSGVEGFFK SLKENGRNVL KKTKSSSILT LARELVPKVV
     NNMVDARTEL ISELRNVIKD FTESTSLELI DDTLDINSDE DLLSKNVKLR ENIKARLPRI
     YEQILNYIDD QEIVTNLLDA VQELITQSYS KYYETITELA ENGKFAKDQV ADVMYLDVFT
     DFFAKEVADL LRNGDIDTIT K
 
 
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