ID   COG6_YEAST              Reviewed;         839 AA.
AC   P53959; D6W1D8;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 170.
DE   RecName: Full=Conserved oligomeric Golgi complex subunit 6;
DE            Short=COG complex subunit 6;
DE   AltName: Full=Complexed with DOR1 protein 2;
DE   AltName: Full=Component of oligomeric Golgi complex 6;
DE   AltName: Full=Protein SEC37;
GN   Name=COG6; Synonyms=COD2, SEC37, TFI2; OrderedLocusNames=YNL041C;
GN   ORFNames=N2675;
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=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   [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   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   [4]
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   [5]
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   [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   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).
CC   -!- FUNCTION: Acts as a component of the peripheral membrane COG complex
CC       that is involved in intra-Golgi protein trafficking. COG is located at
CC       the cis-Golgi, and regulates tethering of retrograde intra-Golgi
CC       vesicles and possibly a number of other membrane trafficking events.
CC       {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       P53959; P53079: COG1; NbExp=5; IntAct=EBI-4829, EBI-4835;
CC       P53959; P53271: COG2; NbExp=3; IntAct=EBI-4829, EBI-16614;
CC       P53959; P40094: COG3; NbExp=3; IntAct=EBI-4829, EBI-16605;
CC       P53959; P53951: COG5; NbExp=2; IntAct=EBI-4829, EBI-4841;
CC       P53959; P53195: COG7; NbExp=3; IntAct=EBI-4829, EBI-4847;
CC       P53959; Q04632: COG8; NbExp=5; IntAct=EBI-4829, EBI-6035;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}.
CC   -!- MISCELLANEOUS: Present with 1720 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the COG6 family. {ECO:0000305}.
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DR   EMBL; Z71317; CAA95908.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10504.1; -; Genomic_DNA.
DR   PIR; S62963; S62963.
DR   RefSeq; NP_014357.1; NM_001182880.1.
DR   AlphaFoldDB; P53959; -.
DR   SMR; P53959; -.
DR   BioGRID; 35783; 535.
DR   ComplexPortal; CPX-1840; COG Golgi transport complex.
DR   DIP; DIP-4373N; -.
DR   IntAct; P53959; 18.
DR   MINT; P53959; -.
DR   STRING; 4932.YNL041C; -.
DR   iPTMnet; P53959; -.
DR   MaxQB; P53959; -.
DR   PaxDb; 4932-YNL041C; -.
DR   PeptideAtlas; P53959; -.
DR   EnsemblFungi; YNL041C_mRNA; YNL041C; YNL041C.
DR   GeneID; 855687; -.
DR   KEGG; sce:YNL041C; -.
DR   AGR; SGD:S000004986; -.
DR   SGD; S000004986; COG6.
DR   VEuPathDB; FungiDB:YNL041C; -.
DR   eggNOG; KOG3758; Eukaryota.
DR   GeneTree; ENSGT00390000013518; -.
DR   HOGENOM; CLU_017837_0_0_1; -.
DR   InParanoid; P53959; -.
DR   OMA; IINMICP; -.
DR   OrthoDB; 276556at2759; -.
DR   BioCyc; YEAST:G3O-33077-MONOMER; -.
DR   BioGRID-ORCS; 855687; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P53959; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P53959; Protein.
DR   GO; GO:0000139; C:Golgi membrane; NAS:ComplexPortal.
DR   GO; GO:0017119; C:Golgi transport complex; IMP:SGD.
DR   GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IMP:SGD.
DR   GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IMP:SGD.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0000301; P:retrograde transport, vesicle recycling within Golgi; NAS:ComplexPortal.
DR   InterPro; IPR010490; COG6.
DR   InterPro; IPR048369; COG6_C.
DR   InterPro; IPR048368; COG6_N.
DR   PANTHER; PTHR21506; COMPONENT OF OLIGOMERIC GOLGI COMPLEX 6; 1.
DR   PANTHER; PTHR21506:SF0; CONSERVED OLIGOMERIC GOLGI COMPLEX SUBUNIT 6; 1.
DR   Pfam; PF20653; COG6_C; 1.
DR   Pfam; PF06419; COG6_N; 1.
DR   SMART; SM01087; COG6; 1.
PE   1: Evidence at protein level;
KW   Golgi apparatus; Membrane; Protein transport; Reference proteome;
KW   Transport.
FT   CHAIN           1..839
FT                   /note="Conserved oligomeric Golgi complex subunit 6"
FT                   /id="PRO_0000213517"
FT   REGION          14..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   839 AA;  96976 MW;  6484A40F999AD787 CRC64;
     MDFVVDYQTY AMADTATPEL PEPEPRLNLT SDAQSQPTGK LDLQFKLPDL QRYSNNNATL
     PVDNDGAGSK DLHKKMTHYA MSSIDKIQLS NPSKQLGQNS QDEKLSQQES QNFTNYEPKN
     LDLSKLVSPS SGSNKNTTNL VLSNKLSKIL NNYTLINYQA TVQLRKSLKV LEENKERLSL
     DEQKLMNPEY VGTLARRALR TDLESQLLKE HITVLEEFKP IIRRIKRLSS SVEKIQRTSE
     KLLSNETNEV PTNNVVLQEI DQYRLKAEQL KLKKKILLSI RDRFTLNQVE DDVITNGTID
     NIFFEVVKKV INIKDESSFL LTLPNLNAGN ALIMGVNEIL EKTNKKIFNY LIDFLYSFES
     SSNLLNDHGT TEQESLNIFR KSLVFLSSDL ELFNELLKRV TTLRSKSILD EFLSQFDMNS
     TTSKPIILSA HDPIRYIGDV LASVHSIIAN EADFVKSLFD FQDEDLKDTP ISILQQNKTF
     LKGIDNKLLN DIIQSLSNSC RIRIEQIVRF EENPIINFEI VRLLKLYRVM FERKGIQDDS
     SIINNLKSLE DISKNRIIGY YEDYMKQTVM AETKNSSDDL LPPEWLSEYM NKLVELFEIY
     EKTHAAEDEE SEDNKLLSSK NLQTIVEQPI KDVLLKQLQT SFPLAKKNEK EKASLLTIEI
     NCFDLIKSRL QPFEGLFAQD DDSRKITIWV CDKLKEYTKQ MLTLQIKFLF ENTGLDLYSN
     LVNMIFPVDS VKDELDYDMY LALRDNSLME LDMVRKNVHD KLNYYLPQAL TDVQGNLLFK
     LTSPMIADEI CDECFKKLSL FYNIFRKLLI HLYPNKKDQV FEILNFSTDE FDMLIGIDH
//