COG6_HUMAN
ID COG6_HUMAN Reviewed; 657 AA.
AC Q9Y2V7; Q5T0U1; Q6AI19; Q86V49; Q9ULT5;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Conserved oligomeric Golgi complex subunit 6;
DE Short=COG complex subunit 6;
DE AltName: Full=Component of oligomeric Golgi complex 6;
GN Name=COG6; Synonyms=KIAA1134;
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] (ISOFORM 1), AND VARIANTS THR-10 AND
RP SER-32.
RC TISSUE=Fetal skin;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-657 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT "Characterization of cDNA clones selected by the GeneMark analysis from
RT size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-657 (ISOFORM 4), AND VARIANTS THR-10 AND
RP SER-32.
RC TISSUE=Aorta;
RA Wei Y.J., Ding J.F., Xiong H., Zhou Y., Hui R.T., Liew C.C.;
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP IDENTIFICATION.
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
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).
RN [10]
RP INVOLVEMENT IN SHNS.
RX PubMed=23606727; DOI=10.1136/jmedgenet-2013-101527;
RA Shaheen R., Ansari S., Alshammari M.J., Alkhalidi H., Alrukban H.,
RA Eyaid W., Alkuraya F.S.;
RT "A novel syndrome of hypohidrosis and intellectual disability is linked to
RT COG6 deficiency.";
RL J. Med. Genet. 50:431-436(2013).
RN [11]
RP VARIANT CDG2L VAL-549.
RX PubMed=20605848; DOI=10.1093/hmg/ddq278;
RA Lubbehusen J., Thiel C., Rind N., Ungar D., Prinsen B.H., de Koning T.J.,
RA van Hasselt P.M., Korner C.;
RT "Fatal outcome due to deficiency of subunit 6 of the conserved oligomeric
RT Golgi complex leading to a new type of congenital disorders of
RT glycosylation.";
RL Hum. Mol. Genet. 19:3623-3633(2010).
CC -!- FUNCTION: Required for normal Golgi function. {ECO:0000250}.
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:0000250}.
CC -!- INTERACTION:
CC Q9Y2V7; Q12774: ARHGEF5; NbExp=5; IntAct=EBI-3866319, EBI-602199;
CC Q9Y2V7; Q9UQB8-6: BAIAP2; NbExp=3; IntAct=EBI-3866319, EBI-9092016;
CC Q9Y2V7; O95999: BCL10; NbExp=5; IntAct=EBI-3866319, EBI-958922;
CC Q9Y2V7; Q8IYX3: CCDC116; NbExp=3; IntAct=EBI-3866319, EBI-744311;
CC Q9Y2V7; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-3866319, EBI-744556;
CC Q9Y2V7; Q8TD31-3: CCHCR1; NbExp=5; IntAct=EBI-3866319, EBI-10175300;
CC Q9Y2V7; Q8NE01: CNNM3; NbExp=3; IntAct=EBI-3866319, EBI-741032;
CC Q9Y2V7; Q16527: CSRP2; NbExp=3; IntAct=EBI-3866319, EBI-2959737;
CC Q9Y2V7; Q93034: CUL5; NbExp=3; IntAct=EBI-3866319, EBI-1057139;
CC Q9Y2V7; Q8NF50-4: DOCK8; NbExp=3; IntAct=EBI-3866319, EBI-12021848;
CC Q9Y2V7; O60941-5: DTNB; NbExp=3; IntAct=EBI-3866319, EBI-11984733;
CC Q9Y2V7; Q9BQ89: FAM110A; NbExp=3; IntAct=EBI-3866319, EBI-1752811;
CC Q9Y2V7; Q86YD7: FAM90A1; NbExp=5; IntAct=EBI-3866319, EBI-6658203;
CC Q9Y2V7; Q9BVV2: FNDC11; NbExp=3; IntAct=EBI-3866319, EBI-744935;
CC Q9Y2V7; O95995: GAS8; NbExp=3; IntAct=EBI-3866319, EBI-1052570;
CC Q9Y2V7; P55040: GEM; NbExp=3; IntAct=EBI-3866319, EBI-744104;
CC Q9Y2V7; Q86VF2-5: IGFN1; NbExp=3; IntAct=EBI-3866319, EBI-11955401;
CC Q9Y2V7; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-3866319, EBI-2556193;
CC Q9Y2V7; P61968: LMO4; NbExp=3; IntAct=EBI-3866319, EBI-2798728;
CC Q9Y2V7; P55081: MFAP1; NbExp=3; IntAct=EBI-3866319, EBI-1048159;
CC Q9Y2V7; Q8IVT4: MGC50722; NbExp=3; IntAct=EBI-3866319, EBI-14086479;
CC Q9Y2V7; Q9BV20: MRI1; NbExp=3; IntAct=EBI-3866319, EBI-747381;
CC Q9Y2V7; Q9HC98-4: NEK6; NbExp=3; IntAct=EBI-3866319, EBI-11750983;
CC Q9Y2V7; Q96HA8: NTAQ1; NbExp=5; IntAct=EBI-3866319, EBI-741158;
CC Q9Y2V7; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-3866319, EBI-2811583;
CC Q9Y2V7; P00973-2: OAS1; NbExp=3; IntAct=EBI-3866319, EBI-12081862;
CC Q9Y2V7; Q9HB19: PLEKHA2; NbExp=3; IntAct=EBI-3866319, EBI-4401947;
CC Q9Y2V7; Q96HA1-2: POM121; NbExp=3; IntAct=EBI-3866319, EBI-11956563;
CC Q9Y2V7; Q6NYC8: PPP1R18; NbExp=3; IntAct=EBI-3866319, EBI-2557469;
CC Q9Y2V7; Q7Z5V6-2: PPP1R32; NbExp=3; IntAct=EBI-3866319, EBI-12000762;
CC Q9Y2V7; P25786: PSMA1; NbExp=3; IntAct=EBI-3866319, EBI-359352;
CC Q9Y2V7; P20618: PSMB1; NbExp=3; IntAct=EBI-3866319, EBI-372273;
CC Q9Y2V7; P47897: QARS1; NbExp=3; IntAct=EBI-3866319, EBI-347462;
CC Q9Y2V7; Q8TBN0: RAB3IL1; NbExp=3; IntAct=EBI-3866319, EBI-743796;
CC Q9Y2V7; Q9NRW1: RAB6B; NbExp=5; IntAct=EBI-3866319, EBI-1760079;
CC Q9Y2V7; Q9UHP6: RSPH14; NbExp=3; IntAct=EBI-3866319, EBI-748350;
CC Q9Y2V7; Q14D33: RTP5; NbExp=3; IntAct=EBI-3866319, EBI-10217913;
CC Q9Y2V7; Q06455-2: RUNX1T1; NbExp=3; IntAct=EBI-3866319, EBI-11984663;
CC Q9Y2V7; Q9BWG6: SCNM1; NbExp=5; IntAct=EBI-3866319, EBI-748391;
CC Q9Y2V7; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-3866319, EBI-358489;
CC Q9Y2V7; O95863: SNAI1; NbExp=3; IntAct=EBI-3866319, EBI-1045459;
CC Q9Y2V7; O95721: SNAP29; NbExp=3; IntAct=EBI-3866319, EBI-490676;
CC Q9Y2V7; P14678-2: SNRPB; NbExp=3; IntAct=EBI-3866319, EBI-372475;
CC Q9Y2V7; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-3866319, EBI-742688;
CC Q9Y2V7; Q9BSW7: SYT17; NbExp=3; IntAct=EBI-3866319, EBI-745392;
CC Q9Y2V7; Q9NU19: TBC1D22B; NbExp=3; IntAct=EBI-3866319, EBI-8787464;
CC Q9Y2V7; P62328: TMSB4X; NbExp=3; IntAct=EBI-3866319, EBI-712598;
CC Q9Y2V7; Q9BZW7: TSGA10; NbExp=3; IntAct=EBI-3866319, EBI-744794;
CC Q9Y2V7; Q63HK5: TSHZ3; NbExp=3; IntAct=EBI-3866319, EBI-9053916;
CC Q9Y2V7; Q99598: TSNAX; NbExp=3; IntAct=EBI-3866319, EBI-742638;
CC Q9Y2V7; Q86TV6: TTC7B; NbExp=3; IntAct=EBI-3866319, EBI-12006098;
CC Q9Y2V7; Q6NVU6: UFSP1; NbExp=3; IntAct=EBI-3866319, EBI-12068150;
CC Q9Y2V7; Q9Y3C0: WASHC3; NbExp=4; IntAct=EBI-3866319, EBI-712969;
CC Q9Y2V7; Q05516: ZBTB16; NbExp=5; IntAct=EBI-3866319, EBI-711925;
CC Q9Y2V7; G3V1X1: ZFC3H1; NbExp=3; IntAct=EBI-3866319, EBI-6448783;
CC Q9Y2V7; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-3866319, EBI-740727;
CC Q9Y2V7; PRO_0000449631 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-3866319, EBI-25475920;
CC Q9Y2V7; PRO_0000449633 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-3866319, EBI-25492395;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Y2V7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y2V7-2; Sequence=VSP_001131, VSP_001132;
CC Name=4;
CC IsoId=Q9Y2V7-4; Sequence=VSP_040375, VSP_040376;
CC -!- DISEASE: Congenital disorder of glycosylation 2L (CDG2L) [MIM:614576]:
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 Clinical features of CDG2L include neonatal intractable focal seizures,
CC vomiting, loss of consciousness, intracranial bleeding due to vitamin K
CC deficiency, and death in infancy. {ECO:0000269|PubMed:20605848}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- DISEASE: Shaheen syndrome (SHNS) [MIM:615328]: An autosomal recessive
CC syndrome characterized by severe intellectual disability, hypohidrosis,
CC dental enamel hypoplasia, and hyperkeratosis of the palms and soles.
CC Some may develop mild microcephaly. {ECO:0000269|PubMed:23606727}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- MISCELLANEOUS: [Isoform 4]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the COG6 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD29633.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
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DR EMBL; CR627406; CAH10495.1; -; mRNA.
DR EMBL; AL512505; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471075; EAX08619.1; -; Genomic_DNA.
DR EMBL; BC051723; AAH51723.1; -; mRNA.
DR EMBL; AB032960; BAA86448.1; -; mRNA.
DR EMBL; AF116827; AAD29633.1; ALT_SEQ; mRNA.
DR CCDS; CCDS45042.1; -. [Q9Y2V7-2]
DR CCDS; CCDS9370.1; -. [Q9Y2V7-1]
DR RefSeq; NP_001138551.1; NM_001145079.1. [Q9Y2V7-2]
DR RefSeq; NP_065802.1; NM_020751.2. [Q9Y2V7-1]
DR AlphaFoldDB; Q9Y2V7; -.
DR SMR; Q9Y2V7; -.
DR BioGRID; 121575; 170.
DR ComplexPortal; CPX-6199; COG tethering complex.
DR CORUM; Q9Y2V7; -.
DR DIP; DIP-48931N; -.
DR IntAct; Q9Y2V7; 132.
DR MINT; Q9Y2V7; -.
DR STRING; 9606.ENSP00000397441; -.
DR ChEMBL; CHEMBL4105962; -.
DR iPTMnet; Q9Y2V7; -.
DR MetOSite; Q9Y2V7; -.
DR PhosphoSitePlus; Q9Y2V7; -.
DR BioMuta; COG6; -.
DR DMDM; 182676410; -.
DR EPD; Q9Y2V7; -.
DR jPOST; Q9Y2V7; -.
DR MassIVE; Q9Y2V7; -.
DR MaxQB; Q9Y2V7; -.
DR PaxDb; Q9Y2V7; -.
DR PeptideAtlas; Q9Y2V7; -.
DR PRIDE; Q9Y2V7; -.
DR ProteomicsDB; 85911; -. [Q9Y2V7-1]
DR ProteomicsDB; 85912; -. [Q9Y2V7-2]
DR ProteomicsDB; 85913; -. [Q9Y2V7-4]
DR Antibodypedia; 23303; 228 antibodies from 25 providers.
DR DNASU; 57511; -.
DR Ensembl; ENST00000356576.8; ENSP00000348983.4; ENSG00000133103.17. [Q9Y2V7-4]
DR Ensembl; ENST00000416691.5; ENSP00000403733.1; ENSG00000133103.17. [Q9Y2V7-2]
DR Ensembl; ENST00000455146.8; ENSP00000397441.2; ENSG00000133103.17. [Q9Y2V7-1]
DR GeneID; 57511; -.
DR KEGG; hsa:57511; -.
DR MANE-Select; ENST00000455146.8; ENSP00000397441.2; NM_020751.3; NP_065802.1.
DR UCSC; uc001uxh.3; human. [Q9Y2V7-1]
DR CTD; 57511; -.
DR DisGeNET; 57511; -.
DR GeneCards; COG6; -.
DR GeneReviews; COG6; -.
DR HGNC; HGNC:18621; COG6.
DR HPA; ENSG00000133103; Low tissue specificity.
DR MalaCards; COG6; -.
DR MIM; 606977; gene.
DR MIM; 614576; phenotype.
DR MIM; 615328; phenotype.
DR neXtProt; NX_Q9Y2V7; -.
DR OpenTargets; ENSG00000133103; -.
DR Orphanet; 464443; COG6-CGD.
DR Orphanet; 363523; Hypohidrosis-enamel hypoplasia-palmoplantar keratoderma-intellectual disability syndrome.
DR PharmGKB; PA38604; -.
DR VEuPathDB; HostDB:ENSG00000133103; -.
DR eggNOG; KOG3758; Eukaryota.
DR GeneTree; ENSGT00390000013518; -.
DR HOGENOM; CLU_011361_3_0_1; -.
DR InParanoid; Q9Y2V7; -.
DR OMA; RFYQQIM; -.
DR OrthoDB; 1370285at2759; -.
DR PhylomeDB; Q9Y2V7; -.
DR TreeFam; TF314527; -.
DR PathwayCommons; Q9Y2V7; -.
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; Q9Y2V7; -.
DR BioGRID-ORCS; 57511; 185 hits in 1083 CRISPR screens.
DR ChiTaRS; COG6; human.
DR GenomeRNAi; 57511; -.
DR Pharos; Q9Y2V7; Tbio.
DR PRO; PR:Q9Y2V7; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q9Y2V7; protein.
DR Bgee; ENSG00000133103; Expressed in secondary oocyte and 188 other tissues.
DR ExpressionAtlas; Q9Y2V7; baseline and differential.
DR Genevisible; Q9Y2V7; HS.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0017119; C:Golgi transport complex; IDA:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
DR GO; GO:0070085; P:glycosylation; IMP:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IMP:ComplexPortal.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0000301; P:retrograde transport, vesicle recycling within Golgi; IMP:ComplexPortal.
DR InterPro; IPR010490; COG6.
DR PANTHER; PTHR21506; PTHR21506; 1.
DR Pfam; PF06419; COG6; 1.
DR SMART; SM01087; COG6; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Congenital disorder of glycosylation;
KW Disease variant; Golgi apparatus; Intellectual disability; Membrane;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..657
FT /note="Conserved oligomeric Golgi complex subunit 6"
FT /id="PRO_0000213513"
FT VAR_SEQ 53..75
FT /note="MLEALKALSTFFVENSLRTRRNL -> LGILLLSFSWLLFEDSVRDSRRC
FT (in isoform 4)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_040375"
FT VAR_SEQ 76..657
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_040376"
FT VAR_SEQ 610..615
FT /note="EQIVKQ -> RPPNGP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10574461"
FT /id="VSP_001131"
FT VAR_SEQ 616..657
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10574461"
FT /id="VSP_001132"
FT VARIANT 10
FT /note="A -> T (in dbSNP:rs3812882)"
FT /evidence="ECO:0000269|PubMed:17974005, ECO:0000269|Ref.6"
FT /id="VAR_048759"
FT VARIANT 32
FT /note="C -> S (in dbSNP:rs3812883)"
FT /evidence="ECO:0000269|PubMed:17974005, ECO:0000269|Ref.6"
FT /id="VAR_048760"
FT VARIANT 300
FT /note="H -> Y (in dbSNP:rs34555836)"
FT /id="VAR_048761"
FT VARIANT 447
FT /note="M -> T (in dbSNP:rs41286961)"
FT /id="VAR_061110"
FT VARIANT 549
FT /note="G -> V (in CDG2L; dbSNP:rs387906959)"
FT /evidence="ECO:0000269|PubMed:20605848"
FT /id="VAR_068240"
FT CONFLICT 158
FT /note="S -> F (in Ref. 2; CAH10495)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="N -> S (in Ref. 2; CAH10495)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 657 AA; 73279 MW; 0F29785E722B5185 CRC64;
MAEGSGEVVA VSATGAANGL NNGAGGTSAT TCNPLSRKLH KILETRLDND KEMLEALKAL
STFFVENSLR TRRNLRGDIE RKSLAINEEF VSIFKEVKEE LESISEDVQA MSNCCQDMTS
RLQAAKEQTQ DLIVKTTKLQ SESQKLEIRA QVADAFLSKF QLTSDEMSLL RGTREGPITE
DFFKALGRVK QIHNDVKVLL RTNQQTAGLE IMEQMALLQE TAYERLYRWA QSECRTLTQE
SCDVSPVLTQ AMEALQDRPV LYKYTLDEFG TARRSTVVRG FIDALTRGGP GGTPRPIEMH
SHDPLRYVGD MLAWLHQATA SEKEHLEALL KHVTTQGVEE NIQEVVGHIT EGVCRPLKVR
IEQVIVAEPG AVLLYKISNL LKFYHHTISG IVGNSATALL TTIEEMHLLS KKIFFNSLSL
HASKLMDKVE LPPPDLGPSS ALNQTLMLLR EVLASHDSSV VPLDARQADF VQVLSCVLDP
LLQMCTVSAS NLGTADMATF MVNSLYMMKT TLALFEFTDR RLEMLQFQIE AHLDTLINEQ
ASYVLTRVGL SYIYNTVQQH KPEQGSLANM PNLDSVTLKA AMVQFDRYLS APDNLLIPQL
NFLLSATVKE QIVKQSTELV CRAYGEVYAA VMNPINEYKD PENILHRSPQ QVQTLLS
