COG2_YEAST
ID COG2_YEAST Reviewed; 262 AA.
AC P53271; D6VUQ1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Conserved oligomeric Golgi complex subunit 2;
DE Short=COG complex subunit 2;
DE AltName: Full=Component of oligomeric Golgi complex 2;
DE AltName: Full=Protein SEC35;
GN Name=COG2; Synonyms=SEC35; OrderedLocusNames=YGR120C; ORFNames=G6324;
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 96604 / S288c / FY1679;
RX PubMed=9046098;
RX DOI=10.1002/(sici)1097-0061(199702)13:2<171::aid-yea57>3.0.co;2-v;
RA van Dyck L., Tettelin H., Purnelle B., Goffeau A.;
RT "An 18.3 kb DNA fragment from yeast chromosome VII carries four unknown
RT open reading frames, the gene for an Asn synthase, remnants of Ty and three
RT tRNA genes.";
RL Yeast 13:171-176(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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9606204; DOI=10.1083/jcb.141.5.1107;
RA VanRheenen S.M., Cao X., Lupashin V.V., Barlowe C., Waters M.G.;
RT "Sec35p, a novel peripheral membrane protein, is required for ER to Golgi
RT vesicle docking.";
RL J. Cell Biol. 141:1107-1119(1998).
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 COG COMPLEX, AND SUBUNIT.
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 IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [9]
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 [10]
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 [11]
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 [12]
RP STRUCTURE BY NMR OF 61-262.
RX PubMed=17565980; DOI=10.1074/jbc.m703716200;
RA Cavanaugh L.F., Chen X., Richardson B.C., Ungar D., Pelczer I., Rizo J.,
RA Hughson F.M.;
RT "Structural analysis of conserved oligomeric Golgi complex subunit 2.";
RL J. Biol. Chem. 282:23418-23426(2007).
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. COG2 is
CC required for ER to Golgi vesicle docking. Not essential for viability.
CC {ECO:0000269|PubMed:12006647, ECO:0000269|PubMed:9606204}.
CC -!- SUBUNIT: Component of the conserved oligomeric Golgi (COG or
CC Sec34/Sec35) complex which consists of eight different proteins COG1-
CC COG8. The COG complex interacts with the Rab GTPase YPT1, the Glogi
CC SNAREs GOS1, SEC22, SED5, VTI1 and YKT6 and the COPI coatomer subunit
CC gamma SEC21. {ECO:0000269|PubMed:11703943, ECO:0000269|PubMed:12006647,
CC ECO:0000269|PubMed:12011112, ECO:0000269|PubMed:15047703}.
CC -!- INTERACTION:
CC P53271; P53079: COG1; NbExp=16; IntAct=EBI-16614, EBI-4835;
CC P53271; P40094: COG3; NbExp=16; IntAct=EBI-16614, EBI-16605;
CC P53271; Q06096: COG4; NbExp=15; IntAct=EBI-16614, EBI-4823;
CC P53271; P53951: COG5; NbExp=3; IntAct=EBI-16614, EBI-4841;
CC P53271; P53959: COG6; NbExp=3; IntAct=EBI-16614, EBI-4829;
CC P53271; P53195: COG7; NbExp=2; IntAct=EBI-16614, EBI-4847;
CC P53271; Q04632: COG8; NbExp=4; IntAct=EBI-16614, EBI-6035;
CC P53271; Q01590: SED5; NbExp=2; IntAct=EBI-16614, EBI-16930;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:9606204}; Peripheral
CC membrane protein {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:9606204}; Cytoplasmic side
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:9606204}.
CC -!- MISCELLANEOUS: Present with 3270 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X83099; CAA58155.1; -; Genomic_DNA.
DR EMBL; Z72905; CAA97130.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08212.1; -; Genomic_DNA.
DR PIR; S55978; S55978.
DR RefSeq; NP_011635.2; NM_001181249.1.
DR PDB; 2JQQ; NMR; -; A=61-262.
DR PDBsum; 2JQQ; -.
DR AlphaFoldDB; P53271; -.
DR BMRB; P53271; -.
DR SMR; P53271; -.
DR BioGRID; 33365; 240.
DR ComplexPortal; CPX-1840; COG Golgi transport complex.
DR DIP; DIP-1194N; -.
DR IntAct; P53271; 28.
DR MINT; P53271; -.
DR STRING; 4932.YGR120C; -.
DR MaxQB; P53271; -.
DR PaxDb; P53271; -.
DR PRIDE; P53271; -.
DR EnsemblFungi; YGR120C_mRNA; YGR120C; YGR120C.
DR GeneID; 853017; -.
DR KEGG; sce:YGR120C; -.
DR SGD; S000003352; COG2.
DR VEuPathDB; FungiDB:YGR120C; -.
DR eggNOG; ENOG502RYA4; Eukaryota.
DR HOGENOM; CLU_095072_0_0_1; -.
DR InParanoid; P53271; -.
DR OMA; YVHHLRN; -.
DR BioCyc; YEAST:G3O-30827-MON; -.
DR EvolutionaryTrace; P53271; -.
DR PRO; PR:P53271; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53271; protein.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:SGD.
DR GO; GO:0000139; C:Golgi membrane; IC:ComplexPortal.
DR GO; GO:0017119; C:Golgi transport complex; IMP:SGD.
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: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; IPR024602; COG_su2_N.
DR Pfam; PF06148; COG2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Golgi apparatus; Membrane; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..262
FT /note="Conserved oligomeric Golgi complex subunit 2"
FT /id="PRO_0000213499"
FT HELIX 110..127
FT /evidence="ECO:0007829|PDB:2JQQ"
FT HELIX 133..151
FT /evidence="ECO:0007829|PDB:2JQQ"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:2JQQ"
FT HELIX 158..177
FT /evidence="ECO:0007829|PDB:2JQQ"
FT HELIX 184..208
FT /evidence="ECO:0007829|PDB:2JQQ"
FT HELIX 214..243
FT /evidence="ECO:0007829|PDB:2JQQ"
FT TURN 245..248
FT /evidence="ECO:0007829|PDB:2JQQ"
FT HELIX 249..258
FT /evidence="ECO:0007829|PDB:2JQQ"
SQ SEQUENCE 262 AA; 30325 MW; 0ED457A7466F0F53 CRC64;
MDFLNDDELD LDLPVTAEIS KELFATEIEK YRESETNGTD VDNFDVDRFL VQKNFHYLPL
DSLIRDLSGL SQKMVQTLLE QIRSNYDDYL TFSNTYTDEE NETLINLEKT QSDLQKFMTQ
LDHLIKDDIS NTQEIIKDVL EYLKKLDEIY GSLRNHSQLT EALSLGKRLS KSLHEMCGIE
PLEEEICSGL IEQLYKLITA SRRILESCAD SNSPYIHHLR NDYQDLLQEF QISLKILTEK
CLENPSSLQN LSLTLVSIIK TA
