ID   COG7_HUMAN              Reviewed;         770 AA.
AC   P83436; Q6UWU7;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2002, sequence version 1.
DT   27-MAR-2024, entry version 166.
DE   RecName: Full=Conserved oligomeric Golgi complex subunit 7;
DE            Short=COG complex subunit 7;
DE   AltName: Full=Component of oligomeric Golgi complex 7;
GN   Name=COG7; ORFNames=UNQ3082/PRO10013;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 257-770.
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [3]
RP   IDENTIFICATION, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=11980916; DOI=10.1083/jcb.200202016;
RA   Ungar D., Oka T., Brittle E.E., Vasile E., Lupashin V.V., Chatterton J.E.,
RA   Heuser J.E., Krieger M., Waters M.G.;
RT   "Characterization of a mammalian Golgi-localized protein complex, COG, that
RT   is required for normal Golgi morphology and function.";
RL   J. Cell Biol. 157:405-415(2002).
RN   [4]
RP   INVOLVEMENT IN CDG2E.
RX   PubMed=15107842; DOI=10.1038/nm1041;
RA   Wu X., Steet R.A., Bohorov O., Bakker J., Newell J., Krieger M.,
RA   Spaapen L., Kornfeld S., Freeze H.H.;
RT   "Mutation of the COG complex subunit gene COG7 causes a lethal congenital
RT   disorder.";
RL   Nat. Med. 10:518-523(2004).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
CC   -!- FUNCTION: Required for normal Golgi function.
CC       {ECO:0000269|PubMed:11980916}.
CC   -!- SUBUNIT: Component of the conserved oligomeric Golgi complex which is
CC       composed of eight different subunits and is required for normal Golgi
CC       morphology and localization. {ECO:0000269|PubMed:11980916}.
CC   -!- INTERACTION:
CC       P83436; Q9H9E3: COG4; NbExp=4; IntAct=EBI-389534, EBI-368382;
CC       P83436; Q9UP83: COG5; NbExp=2; IntAct=EBI-389534, EBI-389502;
CC       P83436; Q9BVG8-5: KIFC3; NbExp=6; IntAct=EBI-389534, EBI-14069005;
CC       P83436; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-389534, EBI-16439278;
CC       P83436; Q86VP1: TAX1BP1; NbExp=10; IntAct=EBI-389534, EBI-529518;
CC       P83436; P70191: Traf5; Xeno; NbExp=2; IntAct=EBI-389534, EBI-523899;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000269|PubMed:11980916}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:11980916}.
CC   -!- DISEASE: Congenital disorder of glycosylation 2E (CDG2E) [MIM:608779]:
CC       A multisystem disorder caused by a defect in glycoprotein biosynthesis
CC       and characterized by under-glycosylated serum glycoproteins. Congenital
CC       disorders of glycosylation result in a wide variety of clinical
CC       features, such as defects in the nervous system development,
CC       psychomotor retardation, dysmorphic features, hypotonia, coagulation
CC       disorders, and immunodeficiency. The broad spectrum of features
CC       reflects the critical role of N-glycoproteins during embryonic
CC       development, differentiation, and maintenance of cell functions.
CC       {ECO:0000269|PubMed:15107842}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the COG7 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAQ88995.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC000549; AAH00549.1; -; mRNA.
DR   EMBL; BC037563; AAH37563.1; -; mRNA.
DR   EMBL; AY358632; AAQ88995.1; ALT_INIT; mRNA.
DR   CCDS; CCDS10610.1; -.
DR   RefSeq; NP_705831.1; NM_153603.3.
DR   AlphaFoldDB; P83436; -.
DR   BioGRID; 124896; 81.
DR   ComplexPortal; CPX-6199; COG tethering complex.
DR   CORUM; P83436; -.
DR   IntAct; P83436; 27.
DR   MINT; P83436; -.
DR   STRING; 9606.ENSP00000305442; -.
DR   ChEMBL; CHEMBL4105843; -.
DR   GlyCosmos; P83436; 1 site, 1 glycan.
DR   GlyGen; P83436; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P83436; -.
DR   PhosphoSitePlus; P83436; -.
DR   BioMuta; COG7; -.
DR   DMDM; 22653684; -.
DR   EPD; P83436; -.
DR   jPOST; P83436; -.
DR   MassIVE; P83436; -.
DR   MaxQB; P83436; -.
DR   PaxDb; 9606-ENSP00000305442; -.
DR   PeptideAtlas; P83436; -.
DR   ProteomicsDB; 57736; -.
DR   Pumba; P83436; -.
DR   Antibodypedia; 25940; 219 antibodies from 32 providers.
DR   DNASU; 91949; -.
DR   Ensembl; ENST00000307149.10; ENSP00000305442.5; ENSG00000168434.13.
DR   GeneID; 91949; -.
DR   KEGG; hsa:91949; -.
DR   MANE-Select; ENST00000307149.10; ENSP00000305442.5; NM_153603.4; NP_705831.1.
DR   UCSC; uc002dlo.4; human.
DR   AGR; HGNC:18622; -.
DR   CTD; 91949; -.
DR   DisGeNET; 91949; -.
DR   GeneCards; COG7; -.
DR   GeneReviews; COG7; -.
DR   HGNC; HGNC:18622; COG7.
DR   HPA; ENSG00000168434; Low tissue specificity.
DR   MalaCards; COG7; -.
DR   MIM; 606978; gene.
DR   MIM; 608779; phenotype.
DR   neXtProt; NX_P83436; -.
DR   OpenTargets; ENSG00000168434; -.
DR   Orphanet; 79333; COG7-CDG.
DR   PharmGKB; PA38605; -.
DR   VEuPathDB; HostDB:ENSG00000168434; -.
DR   eggNOG; KOG4182; Eukaryota.
DR   GeneTree; ENSGT00390000001260; -.
DR   HOGENOM; CLU_006044_2_0_1; -.
DR   InParanoid; P83436; -.
DR   OMA; FAQVNHS; -.
DR   OrthoDB; 455037at2759; -.
DR   PhylomeDB; P83436; -.
DR   TreeFam; TF324498; -.
DR   PathwayCommons; P83436; -.
DR   Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR   Reactome; R-HSA-6811438; Intra-Golgi traffic.
DR   Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network.
DR   SignaLink; P83436; -.
DR   BioGRID-ORCS; 91949; 192 hits in 1159 CRISPR screens.
DR   ChiTaRS; COG7; human.
DR   GeneWiki; COG7; -.
DR   GenomeRNAi; 91949; -.
DR   Pharos; P83436; Tbio.
DR   PRO; PR:P83436; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; P83436; Protein.
DR   Bgee; ENSG00000168434; Expressed in right uterine tube and 191 other cell types or tissues.
DR   ExpressionAtlas; P83436; baseline and differential.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR   GO; GO:0017119; C:Golgi transport complex; IDA:UniProtKB.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
DR   GO; GO:0070085; P:glycosylation; IMP:ComplexPortal.
DR   GO; GO:0007030; P:Golgi organization; IMP:ComplexPortal.
DR   GO; GO:0006886; P:intracellular protein transport; IMP:UniProtKB.
DR   GO; GO:0006486; P:protein glycosylation; IMP:UniProtKB.
DR   GO; GO:0034067; P:protein localization to Golgi apparatus; IMP:UniProtKB.
DR   GO; GO:0033365; P:protein localization to organelle; IMP:UniProtKB.
DR   GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
DR   GO; GO:0000301; P:retrograde transport, vesicle recycling within Golgi; IMP:ComplexPortal.
DR   GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IMP:UniProtKB.
DR   InterPro; IPR019335; COG7.
DR   PANTHER; PTHR21443; CONSERVED OLIGOMERIC GOLGI COMPLEX COMPONENT 7; 1.
DR   PANTHER; PTHR21443:SF0; CONSERVED OLIGOMERIC GOLGI COMPLEX SUBUNIT 7; 1.
DR   Pfam; PF10191; COG7; 1.
DR   Genevisible; P83436; HS.
PE   1: Evidence at protein level;
KW   Congenital disorder of glycosylation; Golgi apparatus; Membrane;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..770
FT                   /note="Conserved oligomeric Golgi complex subunit 7"
FT                   /id="PRO_0000213518"
FT   VARIANT         605
FT                   /note="T -> M (in dbSNP:rs16940094)"
FT                   /id="VAR_048762"
SQ   SEQUENCE   770 AA;  86344 MW;  14DAC431B291582C CRC64;
     MDFSKFLADD FDVKEWINAA FRAGSKEAAS GKADGHAATL VMKLQLFIQE VNHAVEETSH
     QALQNMPKVL RDVEALKQEA SFLKEQMILV KEDIKKFEQD TSQSMQVLVE IDQVKSRMQL
     AAESLQEADK WSTLSADIEE TFKTQDIAVI SAKLTGMQNS LMMLVDTPDY SEKCVHLEAL
     KNRLEALASP QIVAAFTSQA VDQSKVFVKV FTEIDRMPQL LAYYYKCHKV QLLAAWQELC
     QSDLSLDRQL TGLYDALLGA WHTQIQWATQ VFQKPHEVVM VLLIQTLGAL MPSLPSCLSN
     GVERAGPEQE LTRLLEFYDA TAHFAKGLEM ALLPHLHEHN LVKVTELVDA VYDPYKPYQL
     KYGDMEESNL LIQMSAVPLE HGEVIDCVQE LSHSVNKLFG LASAAVDRCV RFTNGLGTCG
     LLSALKSLFA KYVSDFTSTL QSIRKKCKLD HIPPNSLFQE DWTAFQNSIR IIATCGELLR
     HCGDFEQQLA NRILSTAGKY LSDSCSPRSL AGFQESILTD KKNSAKNPWQ EYNYLQKDNP
     AEYASLMEIL YTLKEKGSSN HNLLAAPRAA LTRLNQQAHQ LAFDSVFLRI KQQLLLISKM
     DSWNTAGIGE TLTDELPAFS LTPLEYISNI GQYIMSLPLN LEPFVTQEDS ALELALHAGK
     LPFPPEQGDE LPELDNMADN WLGSIARATM QTYCDAILQI PELSPHSAKQ LATDIDYLIN
     VMDALGLQPS RTLQHIVTLL KTRPEDYRQV SKGLPRRLAT TVATMRSVNY
//