ID COG4_HUMAN Reviewed; 785 AA. AC Q9H9E3; B4DMN8; C9JS23; Q96D40; Q9BRF0; Q9BVZ2; Q9H5Y4; Q9Y3W3; DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 02-NOV-2010, sequence version 3. DT 24-JAN-2024, entry version 182. DE RecName: Full=Conserved oligomeric Golgi complex subunit 4; DE Short=COG complex subunit 4; DE AltName: Full=Component of oligomeric Golgi complex 4; GN Name=COG4; 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 [MRNA] (ISOFORM 2), AND VARIANT ILE-158. RC TISSUE=T-cell; RA Ariga H.; RT "Cog4S, a splicing variant of Cog4."; RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT RP ILE-158. RC TISSUE=Brain, Ileal mucosa, and Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ILE-158. RC TISSUE=Muscle, Placenta, Skin, and Testis; 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 229-785 (ISOFORM 1). RC TISSUE=Uterus; 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 [6] RP SUBCELLULAR LOCATION. 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 [7] RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S). RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8; RA Hillman R.T., Green R.E., Brenner S.E.; RT "An unappreciated role for RNA surveillance."; RL Genome Biol. 5:R8.1-R8.16(2004). RN [8] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [9] RP FUNCTION, AND INTERACTION WITH SCFD1 AND STX5. RX PubMed=19536132; DOI=10.1038/emboj.2009.168; RA Laufman O., Kedan A., Hong W., Lev S.; RT "Direct interaction between the COG complex and the SM protein, Sly1, is RT required for Golgi SNARE pairing."; RL EMBO J. 28:2006-2017(2009). RN [10] 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 [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [13] RP INVOLVEMENT IN SWILS, VARIANT SWILS ARG-512, CHARACTERIZATION OF VARIANT RP SWILS ARG-512, FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=30290151; DOI=10.1016/j.ajhg.2018.09.003; RA Ferreira C.R., Xia Z.J., Clement A., Parry D.A., Davids M., Taylan F., RA Sharma P., Turgeon C.T., Blanco-Sanchez B., Ng B.G., Logan C.V., RA Wolfe L.A., Solomon B.D., Cho M.T., Douglas G., Carvalho D.R., Bratke H., RA Haug M.G., Phillips J.B., Wegner J., Tiemeyer M., Aoki K., Nordgren A., RA Hammarsjoe A., Duker A.L., Rohena L., Hove H.B., Ek J., Adams D., RA Tifft C.J., Onyekweli T., Weixel T., Macnamara E., Radtke K., Powis Z., RA Earl D., Gabriel M., Russi A.H.S., Brick L., Kozenko M., Tham E., RA Raymond K.M., Phillips J.A. III, Tiller G.E., Wilson W.G., Hamid R., RA Malicdan M.C.V., Nishimura G., Grigelioniene G., Jackson A., RA Westerfield M., Bober M.B., Gahl W.A., Freeze H.H.; RT "A recurrent de novo heterozygous COG4 substitution leads to Saul-Wilson RT syndrome, disrupted vesicular trafficking, and altered proteoglycan RT glycosylation."; RL Am. J. Hum. Genet. 103:553-567(2018). RN [14] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 525-785, SUBUNIT, IDENTIFICATION RP OF DOMAINS D AND E, CHARACTERIZATION OF VARIANT CDG2J TRP-729, AND RP MUTAGENESIS OF ARG-729 AND GLU-764. RX PubMed=19651599; DOI=10.1073/pnas.0901966106; RA Richardson B.C., Smith R.D., Ungar D., Nakamura A., Jeffrey P.D., RA Lupashin V.V., Hughson F.M.; RT "Structural basis for a human glycosylation disorder caused by mutation of RT the COG4 gene."; RL Proc. Natl. Acad. Sci. U.S.A. 106:13329-13334(2009). RN [15] RP VARIANT CDG2J TRP-729. RX PubMed=19494034; DOI=10.1093/hmg/ddp262; RA Reynders E., Foulquier F., Leao Teles E., Quelhas D., Morelle W., RA Rabouille C., Annaert W., Matthijs G.; RT "Golgi function and dysfunction in the first COG4-deficient CDG type II RT patient."; RL Hum. Mol. Genet. 18:3244-3256(2009). CC -!- FUNCTION: Required for normal Golgi function (PubMed:19536132, CC PubMed:30290151). Plays a role in SNARE-pin assembly and Golgi-to-ER CC retrograde transport via its interaction with SCFD1 (PubMed:19536132). CC {ECO:0000269|PubMed:19536132, ECO:0000269|PubMed:30290151}. CC -!- SUBUNIT: Monomer. Component of the conserved oligomeric Golgi (COG) CC complex which is composed of eight different subunits and is required CC for normal Golgi morphology and localization (PubMed:19651599). CC Mediates interaction of SCFD1 with the COG complex (PubMed:19536132). CC Interacts with STX5 (PubMed:19536132). {ECO:0000269|PubMed:19536132, CC ECO:0000269|PubMed:19651599}. CC -!- INTERACTION: CC Q9H9E3; X5D778: ANKRD11; NbExp=3; IntAct=EBI-368382, EBI-17183751; CC Q9H9E3; Q9BXY8: BEX2; NbExp=3; IntAct=EBI-368382, EBI-745073; CC Q9H9E3; Q8WTW3: COG1; NbExp=2; IntAct=EBI-368382, EBI-368371; CC Q9H9E3; Q14746: COG2; NbExp=2; IntAct=EBI-368382, EBI-389449; CC Q9H9E3; Q9UP83: COG5; NbExp=2; IntAct=EBI-368382, EBI-389502; CC Q9H9E3; P83436: COG7; NbExp=4; IntAct=EBI-368382, EBI-389534; CC Q9H9E3; Q9UI47-2: CTNNA3; NbExp=3; IntAct=EBI-368382, EBI-11962928; CC Q9H9E3; Q9BQ89: FAM110A; NbExp=3; IntAct=EBI-368382, EBI-1752811; CC Q9H9E3; Q9Y285: FARSA; NbExp=3; IntAct=EBI-368382, EBI-725361; CC Q9H9E3; P25786: PSMA1; NbExp=3; IntAct=EBI-368382, EBI-359352; CC Q9H9E3; Q8WVM8: SCFD1; NbExp=10; IntAct=EBI-368382, EBI-722569; CC Q9H9E3; O60504: SORBS3; NbExp=3; IntAct=EBI-368382, EBI-741237; CC Q9H9E3; Q13190: STX5; NbExp=2; IntAct=EBI-368382, EBI-714206; CC Q9H9E3; O14530: TXNDC9; NbExp=5; IntAct=EBI-368382, EBI-707554; CC Q9H9E3-1; Q9H9E3-1: COG4; NbExp=2; IntAct=EBI-15796331, EBI-15796331; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:30290151}. CC Golgi apparatus membrane {ECO:0000305|PubMed:11703943}; Peripheral CC membrane protein {ECO:0000305|PubMed:11703943}; Cytoplasmic side CC {ECO:0000305|PubMed:11703943}. Note=Mosty cytosolic, with about 5% CC membrane-bound. {ECO:0000269|PubMed:30290151}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9H9E3-1; Sequence=Displayed; CC Name=2; Synonyms=Cog4S; CC IsoId=Q9H9E3-2; Sequence=VSP_001127, VSP_001128; CC Name=3; CC IsoId=Q9H9E3-3; Sequence=VSP_037551; CC -!- DISEASE: Congenital disorder of glycosylation 2J (CDG2J) [MIM:613489]: 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:19494034, ECO:0000269|PubMed:19651599}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Saul-Wilson syndrome (SWILS) [MIM:618150]: A rare skeletal CC dysplasia with characteristic dysmorphic and radiographic findings, as CC well as early developmental delay, primarily involving speech, with CC eventual normal cognition. Clinical findings include marked short CC stature, prominent forehead with an enlarged anterior fontanel, CC prominent eyes with cataracts, narrow nasal bridge with a convex nasal CC ridge, micrognathia, clubfoot, brachydactyly, and short distal CC phalanges of fingers. Radiographic changes include platyspondyly, CC irregular end plates of vertebral bodies, and hypoplasia of the CC odontoid process with cervical instability in the spine, coxa valga, CC overtubulation, metaphyseal flaring and megaepiphyses in the long CC bones, while the hands and feet exhibit short phalanges, metacarpals CC and metatarsals, cone-shaped epiphyses of phalanges, and accessory CC ossification centers of metacarpals and metatarsals. CC {ECO:0000269|PubMed:30290151}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- MISCELLANEOUS: [Isoform 2]: 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 COG4 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB15483.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB088369; BAC05682.1; -; mRNA. DR EMBL; AK022874; BAB14286.1; -; mRNA. DR EMBL; AK026435; BAB15483.1; ALT_INIT; mRNA. DR EMBL; AK297557; BAG59950.1; -; mRNA. DR EMBL; AC106804; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC000796; AAH00796.1; -; mRNA. DR EMBL; BC006306; AAH06306.2; -; mRNA. DR EMBL; BC013347; AAH13347.2; -; mRNA. DR EMBL; BC072438; AAH72438.1; -; mRNA. DR EMBL; AL050101; CAB43272.1; -; mRNA. DR RefSeq; NP_001182068.1; NM_001195139.1. DR RefSeq; NP_056201.2; NM_015386.2. DR PDB; 3HR0; X-ray; 1.90 A; A/B=525-785. DR PDBsum; 3HR0; -. DR AlphaFoldDB; Q9H9E3; -. DR SMR; Q9H9E3; -. DR BioGRID; 117365; 110. DR ComplexPortal; CPX-6199; COG tethering complex. DR CORUM; Q9H9E3; -. DR DIP; DIP-32635N; -. DR IntAct; Q9H9E3; 50. DR MINT; Q9H9E3; -. DR STRING; 9606.ENSP00000315775; -. DR ChEMBL; CHEMBL4105733; -. DR iPTMnet; Q9H9E3; -. DR PhosphoSitePlus; Q9H9E3; -. DR SwissPalm; Q9H9E3; -. DR BioMuta; COG4; -. DR DMDM; 311033464; -. DR EPD; Q9H9E3; -. DR jPOST; Q9H9E3; -. DR MassIVE; Q9H9E3; -. DR MaxQB; Q9H9E3; -. DR PaxDb; 9606-ENSP00000315775; -. DR PeptideAtlas; Q9H9E3; -. DR ProteomicsDB; 81316; -. [Q9H9E3-1] DR ProteomicsDB; 81317; -. [Q9H9E3-2] DR ProteomicsDB; 81318; -. [Q9H9E3-3] DR Pumba; Q9H9E3; -. DR DNASU; 25839; -. DR Ensembl; ENST00000482252.5; ENSP00000432802.1; ENSG00000103051.21. [Q9H9E3-2] DR GeneID; 25839; -. DR KEGG; hsa:25839; -. DR UCSC; uc059wqe.1; human. [Q9H9E3-1] DR AGR; HGNC:18620; -. DR CTD; 25839; -. DR DisGeNET; 25839; -. DR GeneCards; COG4; -. DR GeneReviews; COG4; -. DR HGNC; HGNC:18620; COG4. DR MalaCards; COG4; -. DR MIM; 606976; gene. DR MIM; 613489; phenotype. DR MIM; 618150; phenotype. DR neXtProt; NX_Q9H9E3; -. DR OpenTargets; ENSG00000103051; -. DR Orphanet; 263501; COG4-CDG. DR Orphanet; 85172; Microcephalic osteodysplastic dysplasia, Saul-Wilson type. DR PharmGKB; PA38603; -. DR VEuPathDB; HostDB:ENSG00000103051; -. DR eggNOG; KOG0412; Eukaryota. DR GeneTree; ENSGT00940000154065; -. DR HOGENOM; CLU_014853_0_0_1; -. DR InParanoid; Q9H9E3; -. DR OrthoDB; 7468at2759; -. DR PhylomeDB; Q9H9E3; -. DR PathwayCommons; Q9H9E3; -. 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; Q9H9E3; -. DR BioGRID-ORCS; 25839; 418 hits in 1169 CRISPR screens. DR ChiTaRS; COG4; human. DR EvolutionaryTrace; Q9H9E3; -. DR GeneWiki; COG4; -. DR GenomeRNAi; 25839; -. DR Pharos; Q9H9E3; Tbio. DR PRO; PR:Q9H9E3; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q9H9E3; Protein. DR Bgee; ENSG00000103051; Expressed in lower esophagus mucosa and 191 other cell types or tissues. DR ExpressionAtlas; Q9H9E3; baseline and differential. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. 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:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0070085; P:glycosylation; IMP:ComplexPortal. DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB. DR GO; GO:0048213; P:Golgi vesicle prefusion complex stabilization; IMP:UniProtKB. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. 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 Gene3D; 1.20.58.1970; -; 1. DR Gene3D; 1.10.287.1060; ESAT-6-like; 1. DR InterPro; IPR048682; COG4. DR InterPro; IPR048684; COG4_C. DR InterPro; IPR013167; COG4_M. DR InterPro; IPR048680; COG4_N. DR PANTHER; PTHR24016; CONSERVED OLIGOMERIC GOLGI COMPLEX SUBUNIT 4; 1. DR PANTHER; PTHR24016:SF0; CONSERVED OLIGOMERIC GOLGI COMPLEX SUBUNIT 4; 1. DR Pfam; PF20662; COG4_C; 1. DR Pfam; PF08318; COG4_m; 1. DR Pfam; PF20663; COG4_N; 1. DR SMART; SM00762; Cog4; 1. DR Genevisible; Q9H9E3; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; KW Congenital disorder of glycosylation; Cytoplasm; Disease variant; Dwarfism; KW Golgi apparatus; Membrane; Phosphoprotein; Protein transport; KW Reference proteome; Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22814378" FT CHAIN 2..785 FT /note="Conserved oligomeric Golgi complex subunit 4" FT /id="PRO_0000213504" FT REGION 1..24 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2..84 FT /note="Interaction with SCFD1" FT /evidence="ECO:0000269|PubMed:19536132" FT REGION 85..153 FT /note="Interaction with STX5" FT /evidence="ECO:0000269|PubMed:19536132" FT REGION 618..740 FT /note="D domain" FT /evidence="ECO:0000269|PubMed:19651599" FT REGION 741..785 FT /note="E domain; essential for proper cell surface FT glycosylation" FT /evidence="ECO:0000269|PubMed:19651599" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22814378" FT MOD_RES 6 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..73 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_037551" FT VAR_SEQ 331..337 FT /note="FRHVQNN -> NFVFSFF (in isoform 2)" FT /evidence="ECO:0000303|Ref.1" FT /id="VSP_001127" FT VAR_SEQ 338..785 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.1" FT /id="VSP_001128" FT VARIANT 158 FT /note="T -> I (in dbSNP:rs3931036)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1" FT /id="VAR_058009" FT VARIANT 512 FT /note="G -> R (in SWILS; delayed anterograde vesicular FT trafficking from the ER to the Golgi and accelerated FT retrograde vesicular recycling from the Golgi to the ER, FT leading to a decrease in Golgi volume, as well as FT morphologic abnormalities with collapse of the Golgi stacks FT in affected fibroblasts; altered decorin/DCNGolgi-dependent FT glycosylation; no effect on protein expression; FT dbSNP:rs1555575860)" FT /evidence="ECO:0000269|PubMed:30290151" FT /id="VAR_081564" FT VARIANT 729 FT /note="R -> W (in CDG2J; severe defects in glycosylation)" FT /evidence="ECO:0000269|PubMed:19494034, FT ECO:0000269|PubMed:19651599" FT /id="VAR_063767" FT MUTAGEN 729 FT /note="R->A: Severe defects in glycosylation." FT /evidence="ECO:0000269|PubMed:19651599" FT MUTAGEN 764 FT /note="E->A: Severe defects in glycosylation." FT /evidence="ECO:0000269|PubMed:19651599" FT CONFLICT 177 FT /note="E -> G (in Ref. 2; BAB14286)" FT /evidence="ECO:0000305" FT CONFLICT 234 FT /note="K -> R (in Ref. 2; BAB14286)" FT /evidence="ECO:0000305" FT CONFLICT 285 FT /note="T -> A (in Ref. 2; BAB14286)" FT /evidence="ECO:0000305" FT CONFLICT 486 FT /note="E -> G (in Ref. 2; BAB15483)" FT /evidence="ECO:0000305" FT CONFLICT 588 FT /note="S -> G (in Ref. 2; BAB14286/BAG59950)" FT /evidence="ECO:0000305" FT CONFLICT 644 FT /note="A -> S (in Ref. 4; AAH06306)" FT /evidence="ECO:0000305" FT HELIX 537..572 FT /evidence="ECO:0007829|PDB:3HR0" FT TURN 573..575 FT /evidence="ECO:0007829|PDB:3HR0" FT HELIX 580..615 FT /evidence="ECO:0007829|PDB:3HR0" FT HELIX 617..625 FT /evidence="ECO:0007829|PDB:3HR0" FT HELIX 626..629 FT /evidence="ECO:0007829|PDB:3HR0" FT HELIX 636..644 FT /evidence="ECO:0007829|PDB:3HR0" FT HELIX 649..666 FT /evidence="ECO:0007829|PDB:3HR0" FT HELIX 669..691 FT /evidence="ECO:0007829|PDB:3HR0" FT HELIX 698..716 FT /evidence="ECO:0007829|PDB:3HR0" FT HELIX 723..726 FT /evidence="ECO:0007829|PDB:3HR0" FT HELIX 728..737 FT /evidence="ECO:0007829|PDB:3HR0" FT HELIX 742..747 FT /evidence="ECO:0007829|PDB:3HR0" FT HELIX 750..753 FT /evidence="ECO:0007829|PDB:3HR0" FT HELIX 762..769 FT /evidence="ECO:0007829|PDB:3HR0" FT HELIX 777..782 FT /evidence="ECO:0007829|PDB:3HR0" SQ SEQUENCE 785 AA; 89083 MW; 93E8597991934AD2 CRC64; MADLDSPPKL SGVQQPSEGV GGGRCSEISA ELIRSLTELQ ELEAVYERLC GEEKVVEREL DALLEQQNTI ESKMVTLHRM GPNLQLIEGD AKQLAGMITF TCNLAENVSS KVRQLDLAKN RLYQAIQRAD DILDLKFCMD GVQTALRSED YEQAAAHTHR YLCLDKSVIE LSRQGKEGSM IDANLKLLQE AEQRLKAIVA EKFAIATKEG DLPQVERFFK IFPLLGLHEE GLRKFSEYLC KQVASKAEEN LLMVLGTDMS DRRAAVIFAD TLTLLFEGIA RIVETHQPIV ETYYGPGRLY TLIKYLQVEC DRQVEKVVDK FIKQRDYHQQ FRHVQNNLMR NSTTEKIEPR ELDPILTEVT LMNARSELYL RFLKKRISSD FEVGDSMASE EVKQEHQKCL DKLLNNCLLS CTMQELIGLY VTMEEYFMRE TVNKAVALDT YEKGQLTSSM VDDVFYIVKK CIGRALSSSS IDCLCAMINL ATTELESDFR DVLCNKLRMG FPATTFQDIQ RGVTSAVNIM HSSLQQGKFD TKGIESTDEA KMSFLVTLNN VEVCSENIST LKKTLESDCT KLFSQGIGGE QAQAKFDSCL SDLAAVSNKF RDLLQEGLTE LNSTAIKPQV QPWINSFFSV SHNIEEEEFN DYEANDPWVQ QFILNLEQQM AEFKASLSPV IYDSLTGLMT SLVAVELEKV VLKSTFNRLG GLQFDKELRS LIAYLTTVTT WTIRDKFARL SQMATILNLE RVTEILDYWG PNSGPLTWRL TPAEVRQVLA LRIDFRSEDI KRLRL //