ID GET4_HUMAN Reviewed; 327 AA. AC Q7L5D6; A4D2Q1; B3KNC7; Q9UFC9; Q9Y309; DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 10-JUN-2026, entry version 165. DE RecName: Full=Golgi to ER traffic protein 4 homolog {ECO:0000305}; DE AltName: Full=Conserved edge-expressed protein; DE AltName: Full=Transmembrane domain recognition complex 35 kDa subunit; DE Short=TRC35; GN Name=GET4 {ECO:0000312|HGNC:HGNC:21690}; Synonyms=C7orf20, CEE, TRC35; GN ORFNames=CGI-20; 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 2). RC TISSUE=Ovary, Testis, and Thymus; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Testis; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12690205; DOI=10.1126/science.1083423; RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D., RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., RA Adams M.D., Tsui L.-C.; RT "Human chromosome 7: DNA sequence and biology."; RL Science 300:767-772(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Placenta; 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 PROTEIN SEQUENCE OF 2-14 AND 111-122, CLEAVAGE OF INITIATOR METHIONINE, RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lung carcinoma; RA Bienvenut W.V., Vousden K.H., Lukashchuk N.; RL Submitted (MAR-2008) to UniProtKB. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-327 (ISOFORM 1). RX PubMed=10810093; DOI=10.1101/gr.10.5.703; RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.; RT "Identification of novel human genes evolutionarily conserved in RT Caenorhabditis elegans by comparative proteomics."; RL Genome Res. 10:703-713(2000). RN [7] RP IDENTIFICATION. RX PubMed=18249086; DOI=10.1016/j.ygeno.2007.10.017; RA Fernandes J.M.O., Macqueen D.J., Lee H.-T., Johnston I.A.; RT "Genomic, evolutionary, and expression analyses of cee, an ancient gene RT involved in normal growth and development."; RL Genomics 91:315-325(2008). 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, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND RP IDENTIFICATION IN THE BAG6/BAT3 COMPLEX. RX PubMed=20676083; DOI=10.1038/nature09296; RA Mariappan M., Li X., Stefanovic S., Sharma A., Mateja A., Keenan R.J., RA Hegde R.S.; RT "A ribosome-associating factor chaperones tail-anchored membrane RT proteins."; RL Nature 466:1120-1124(2010). 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 FUNCTION, INTERACTION WITH BAG6, AND SUBCELLULAR LOCATION. RX PubMed=21636303; DOI=10.1016/j.molcel.2011.05.010; RA Wang Q., Liu Y., Soetandyo N., Baek K., Hegde R., Ye Y.; RT "A ubiquitin ligase-associated chaperone holdase maintains polypeptides in RT soluble states for proteasome degradation."; RL Mol. Cell 42:758-770(2011). RN [12] RP FUNCTION. RX PubMed=21743475; DOI=10.1038/nature10181; RA Hessa T., Sharma A., Mariappan M., Eshleman H.D., Gutierrez E., Hegde R.S.; RT "Protein targeting and degradation are coupled for elimination of RT mislocalized proteins."; RL Nature 475:394-397(2011). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [14] 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=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [15] 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 [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 [17] RP INTERACTION WITH BAG6, IDENTIFICATION IN THE BAG6/BAT3 COMPLEX, FUNCTION, RP AND MUTAGENESIS OF ASP-84. RX PubMed=25535373; DOI=10.1073/pnas.1402745112; RA Mock J.Y., Chartron J.W., Zaslaver M., Xu Y., Ye Y., Clemons W.M. Jr.; RT "Bag6 complex contains a minimal tail-anchor-targeting module and a mock RT BAG domain."; RL Proc. Natl. Acad. Sci. U.S.A. 112:106-111(2015). RN [18] RP FUNCTION. RX PubMed=28104892; DOI=10.1126/science.aah6130; RA Shao S., Rodrigo-Brenni M.C., Kivlen M.H., Hegde R.S.; RT "Mechanistic basis for a molecular triage reaction."; RL Science 355:298-302(2017). RN [19] RP INVOLVEMENT IN CDG2Y, VARIANTS CDG2Y HIS-122 AND MET-279, FUNCTION, AND RP SUBCELLULAR LOCATION. RX PubMed=32395830; DOI=10.1002/jimd.12249; RG Undiagnosed Diseases Network; RA Tambe M.A., Ng B.G., Shimada S., Wolfe L.A., Adams D.R., Gahl W.A., RA Bamshad M.J., Nickerson D.A., Malicdan M.C.V., Freeze H.H.; RT "Mutations in GET4 disrupt the transmembrane domain recognition complex RT pathway."; RL J. Inherit. Metab. Dis. 43:1037-1045(2020). RN [20] {ECO:0007744|PDB:6AU8} RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 23-305 IN COMPLEX WITH BAG6, RP SUBCELLULAR LOCATION, INTERACTION WITH BAG6, MUTAGENESIS OF TYR-182; RP PHE-188; PHE-195; TRP-241; PHE-242; VAL-257; LEU-258; CYS-259; TYR-262 AND RP LEU-266, AND UBIQUITINATION BY RNF126. RX PubMed=29042515; DOI=10.1073/pnas.1702940114; RA Mock J.Y., Xu Y., Ye Y., Clemons W.M. Jr.; RT "Structural basis for regulation of the nucleo-cytoplasmic distribution of RT Bag6 by TRC35."; RL Proc. Natl. Acad. Sci. U.S.A. 114:11679-11684(2017). RN [21] {ECO:0007744|PDB:7RU9, ECO:0007744|PDB:7RUA, ECO:0007744|PDB:7RUC} RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS) IN COMPLEX WITH BAG6; RP UBL4A AND GET3, INTERACTION WITH GET3, AND MUTAGENESIS OF ARG-25; LYS-29 RP AND ARG-278. RX PubMed=34887561; DOI=10.1038/s41594-021-00690-7; RA Keszei A.F.A., Yip M.C.J., Hsieh T.C., Shao S.; RT "Structural insights into metazoan pretargeting GET complexes."; RL Nat. Struct. Mol. Biol. 28:1029-1037(2021). CC -!- FUNCTION: As part of a cytosolic protein quality control complex, the CC BAG6/BAT3 complex, maintains misfolded and hydrophobic patches- CC containing proteins in a soluble state and participates in their proper CC delivery to the endoplasmic reticulum or alternatively can promote CC their sorting to the proteasome where they undergo degradation CC (PubMed:20676083, PubMed:21636303, PubMed:21743475, PubMed:28104892, CC PubMed:32395830). The BAG6/BAT3 complex is involved in the post- CC translational delivery of tail-anchored/type II transmembrane proteins CC to the endoplasmic reticulum membrane. Recruited to ribosomes, it CC interacts with the transmembrane region of newly synthesized tail- CC anchored proteins and together with SGTA and ASNA1 mediates their CC delivery to the endoplasmic reticulum (PubMed:20676083, CC PubMed:25535373, PubMed:28104892). Client proteins that cannot be CC properly delivered to the endoplasmic reticulum are ubiquitinated and CC sorted to the proteasome (PubMed:28104892). Similarly, the BAG6/BAT3 CC complex also functions as a sorting platform for proteins of the CC secretory pathway that are mislocalized to the cytosol either CC delivering them to the proteasome for degradation or to the endoplasmic CC reticulum (PubMed:21743475). The BAG6/BAT3 complex also plays a role in CC the endoplasmic reticulum-associated degradation (ERAD), a quality CC control mechanism that eliminates unwanted proteins of the endoplasmic CC reticulum through their retrotranslocation to the cytosol and their CC targeting to the proteasome. It maintains these retrotranslocated CC proteins in an unfolded yet soluble state condition in the cytosol to CC ensure their proper delivery to the proteasome (PubMed:21636303). CC {ECO:0000269|PubMed:20676083, ECO:0000269|PubMed:21636303, CC ECO:0000269|PubMed:21743475, ECO:0000269|PubMed:25535373, CC ECO:0000269|PubMed:28104892, ECO:0000269|PubMed:32395830}. CC -!- SUBUNIT: Component of the BAG6/BAT3 complex, at least composed of BAG6, CC UBL4A and GET4/TRC35 (PubMed:20676083, PubMed:25535373). Interacts with CC BAG6; the interaction is direct and localizes BAG6 to the cytosol CC (PubMed:21636303, PubMed:25535373, PubMed:29042515). Interacts with CC GET3 (PubMed:34887561). {ECO:0000269|PubMed:20676083, CC ECO:0000269|PubMed:21636303, ECO:0000269|PubMed:25535373, CC ECO:0000269|PubMed:29042515, ECO:0000269|PubMed:34887561}. CC -!- INTERACTION: CC Q7L5D6; Q9NX04: AIRIM; NbExp=3; IntAct=EBI-711823, EBI-8643161; CC Q7L5D6; P46379-2: BAG6; NbExp=4; IntAct=EBI-711823, EBI-10988864; CC Q7L5D6; Q9H596: DUSP21; NbExp=3; IntAct=EBI-711823, EBI-7357329; CC Q7L5D6; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-711823, EBI-744099; CC Q7L5D6; P35555: FBN1; NbExp=3; IntAct=EBI-711823, EBI-2505934; CC Q7L5D6; O43681: GET3; NbExp=7; IntAct=EBI-711823, EBI-2515857; CC Q7L5D6; Q14161-11: GIT2; NbExp=3; IntAct=EBI-711823, EBI-12028686; CC Q7L5D6; Q9BYQ3: KRTAP9-3; NbExp=3; IntAct=EBI-711823, EBI-1043191; CC Q7L5D6; P69849: NOMO3; NbExp=2; IntAct=EBI-711823, EBI-947048; CC Q7L5D6; Q9BW27: NUP85; NbExp=3; IntAct=EBI-711823, EBI-716392; CC Q7L5D6; O43741: PRKAB2; NbExp=8; IntAct=EBI-711823, EBI-1053424; CC Q7L5D6; O00560: SDCBP; NbExp=3; IntAct=EBI-711823, EBI-727004; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:20676083, CC ECO:0000269|PubMed:21636303, ECO:0000269|PubMed:29042515, CC ECO:0000269|PubMed:32395830}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q7L5D6-1; Sequence=Displayed; CC Name=2; CC IsoId=Q7L5D6-2; Sequence=VSP_017652; CC -!- PTM: Ubiquitinated by RNF12, leading to proteasomal degradation. When CC unassembled from BAG6; ubiquitinylation is modulated by BAG6 quality CC control role and effectuated by RNF126. {ECO:0000269|PubMed:29042515}. CC -!- DISEASE: Congenital disorder of glycosylation 2Y (CDG2Y) [MIM:620200]: CC A form of congenital disorder of glycosylation, a genetically CC heterogeneous group of multisystem disorders caused by a defect in CC glycoprotein biosynthesis and characterized by under-glycosylated serum CC glycoproteins. Congenital disorders of glycosylation result in a wide CC variety of clinical features, such as defects in the nervous system CC development, psychomotor retardation, dysmorphic features, hypotonia, CC coagulation disorders, and immunodeficiency. The broad spectrum of CC features reflects the critical role of N-glycoproteins during embryonic CC development, differentiation, and maintenance of cell functions. CDG2Y CC is an autosomal recessive form characterized by poor overall growth and CC global developmental delay with impaired intellectual development. CC Other features may include hypotonia, seizures, brain imaging CC abnormalities, dysmorphic features, and various skeletal defects. CC {ECO:0000269|PubMed:32395830}. Note=The disease may be caused by CC variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the GET4 family. {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; AK024305; BAG51289.1; -; mRNA. DR EMBL; AK097899; BAG53546.1; -; mRNA. DR EMBL; AK125863; BAG54258.1; -; mRNA. DR EMBL; AL133014; CAB61355.1; -; mRNA. DR EMBL; CH236965; EAL23708.1; -; Genomic_DNA. DR EMBL; BC003550; AAH03550.2; -; mRNA. DR EMBL; AF132954; AAD27729.1; -; mRNA. DR CCDS; CCDS5317.1; -. [Q7L5D6-1] DR PIR; T42648; T42648. DR RefSeq; NP_057033.2; NM_015949.2. [Q7L5D6-1] DR PDB; 6AU8; X-ray; 1.80 A; A=23-305. DR PDB; 7RU9; EM; 3.30 A; C/F=1-327. DR PDB; 7RUA; EM; 3.40 A; C/F=1-327. DR PDB; 7RUC; EM; 3.60 A; C/F=1-327. DR PDBsum; 6AU8; -. DR PDBsum; 7RU9; -. DR PDBsum; 7RUA; -. DR PDBsum; 7RUC; -. DR AlphaFoldDB; Q7L5D6; -. DR EMDB; EMD-24700; -. DR EMDB; EMD-24701; -. DR EMDB; EMD-24702; -. DR SMR; Q7L5D6; -. DR BioGRID; 119636; 194. DR ComplexPortal; CPX-132; BAT3 complex. DR CORUM; Q7L5D6; -. DR FunCoup; Q7L5D6; 3528. DR IntAct; Q7L5D6; 122. DR MINT; Q7L5D6; -. DR NDEx; IQUERY-CP-GET4; 1 NDEx IQuery Curated Pathway. DR STRING; 9606.ENSP00000265857; -. DR MoonDB; Q7L5D6; Predicted. DR iPTMnet; Q7L5D6; -. DR MetOSite; Q7L5D6; -. DR PhosphoSitePlus; Q7L5D6; -. DR BioMuta; GET4; -. DR DMDM; 74738593; -. DR jPOST; Q7L5D6; -. DR MassIVE; Q7L5D6; -. DR PaxDb; 9606-ENSP00000265857; -. DR PeptideAtlas; Q7L5D6; -. DR ProteomicsDB; 68807; -. [Q7L5D6-1] DR ProteomicsDB; 68808; -. [Q7L5D6-2] DR Pumba; Q7L5D6; -. DR Antibodypedia; 34834; 57 antibodies from 16 providers. DR DNASU; 51608; -. DR Ensembl; ENST00000265857.8; ENSP00000265857.3; ENSG00000239857.8. [Q7L5D6-1] DR Ensembl; ENST00000407192.5; ENSP00000385646.1; ENSG00000239857.8. [Q7L5D6-2] DR GeneID; 51608; -. DR KEGG; hsa:51608; -. DR MANE-Select; ENST00000265857.8; ENSP00000265857.3; NM_015949.3; NP_057033.2. DR UCSC; uc003sjl.2; human. [Q7L5D6-1] DR AGR; HGNC:21690; -. DR ClinPGx; PA165618100; -. DR CTD; 51608; -. DR DisGeNET; 51608; -. DR GeneCards; GET4; -. DR HGNC; HGNC:21690; GET4. DR HPA; ENSG00000239857; Low tissue specificity. DR MalaCards; GET4; -. DR MIM; 612056; gene. DR MIM; 620200; phenotype. DR OpenTargets; ENSG00000239857; -. DR VEuPathDB; HostDB:ENSG00000239857; -. DR eggNOG; KOG3024; Eukaryota. DR GeneTree; ENSGT00390000015750; -. DR HOGENOM; CLU_046061_2_0_1; -. DR InParanoid; Q7L5D6; -. DR OMA; LMDMMGM; -. DR OrthoDB; 10252405at2759; -. DR PAN-GO; Q7L5D6; 4 GO annotations based on evolutionary models. DR PhylomeDB; Q7L5D6; -. DR PathwayCommons; Q7L5D6; -. DR Reactome; R-HSA-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane. DR SignaLink; Q7L5D6; -. DR Agora; ENSG00000239857; -. DR BioGRID-ORCS; 51608; 231 hits in 1167 CRISPR screens. DR ChiTaRS; GET4; human. DR GeneWiki; C7orf20; -. DR GenomeRNAi; 51608; -. DR Pharos; Q7L5D6; Tbio. DR PRO; PR:Q7L5D6; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; Q7L5D6; protein. DR Bgee; ENSG00000239857; Expressed in left testis and 95 other cell types or tissues. DR ExpressionAtlas; Q7L5D6; baseline and differential. DR GO; GO:0071818; C:BAT3 complex; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0140597; F:protein carrier chaperone; IMP:ParkinsonsUK-UCL. DR GO; GO:0051087; F:protein-folding chaperone binding; IPI:BHF-UCL. DR GO; GO:0036503; P:ERAD pathway; IMP:ParkinsonsUK-UCL. DR GO; GO:0036506; P:maintenance of unfolded protein; IMP:ParkinsonsUK-UCL. DR GO; GO:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; IDA:ComplexPortal. DR GO; GO:0045048; P:protein insertion into ER membrane; IMP:UniProtKB. DR GO; GO:0031647; P:regulation of protein stability; IDA:ComplexPortal. DR GO; GO:0071816; P:tail-anchored membrane protein insertion into ER membrane; IDA:UniProtKB. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:ComplexPortal. DR FunFam; 1.25.40.10:FF:000060; Golgi to ER traffic protein 4 homolog; 1. DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1. DR InterPro; IPR007317; GET4. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR PANTHER; PTHR12875; GOLGI TO ER TRAFFIC PROTEIN 4 HOMOLOG; 1. DR PANTHER; PTHR12875:SF0; GOLGI TO ER TRAFFIC PROTEIN 4 HOMOLOG; 1. DR Pfam; PF04190; GET4; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; KW Congenital disorder of glycosylation; Cytoplasm; Direct protein sequencing; KW Disease variant; Phosphoprotein; Proteomics identification; KW Reference proteome; Transport; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT CHAIN 2..327 FT /note="Golgi to ER traffic protein 4 homolog" FT /id="PRO_0000228104" FT REGION 195..271 FT /note="Interacts with BAG6" FT /evidence="ECO:0000269|PubMed:25535373, FT ECO:0000269|PubMed:29042515" FT REGION 307..327 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT MOD_RES 12 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..53 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:17974005" FT /id="VSP_017652" FT VARIANT 122 FT /note="R -> H (in CDG2Y; uncertain significance; FT dbSNP:rs1268790820)" FT /evidence="ECO:0000269|PubMed:32395830" FT /id="VAR_088084" FT VARIANT 279 FT /note="I -> M (in CDG2Y; uncertain significance; FT dbSNP:rs1844404490)" FT /evidence="ECO:0000269|PubMed:32395830" FT /id="VAR_088085" FT MUTAGEN 25 FT /note="R->D: Loss of interaction with GET3; when associated FT with D-29. Impairs tail-anchored protein delivery; when FT associetd with D-29." FT /evidence="ECO:0000269|PubMed:34887561" FT MUTAGEN 29 FT /note="K->D: Loss of interaction with GET3; when associated FT with D-25. Impairs tail-anchored protein delivery; when FT associetd with D-25." FT /evidence="ECO:0000269|PubMed:34887561" FT MUTAGEN 84 FT /note="D->K: Reduces tail-anchored protein delivery." FT /evidence="ECO:0000269|PubMed:25535373" FT MUTAGEN 182 FT /note="Y->A: No effect on interaction with BAG6." FT /evidence="ECO:0000269|PubMed:29042515" FT MUTAGEN 188 FT /note="F->A: No effect on interaction with BAG6." FT /evidence="ECO:0000269|PubMed:29042515" FT MUTAGEN 195 FT /note="F->A: No effect on interaction with BAG6." FT /evidence="ECO:0000269|PubMed:29042515" FT MUTAGEN 241 FT /note="W->A: No effect on interaction with BAG6." FT /evidence="ECO:0000269|PubMed:29042515" FT MUTAGEN 242 FT /note="F->A: No effect on interaction with BAG6." FT /evidence="ECO:0000269|PubMed:29042515" FT MUTAGEN 257 FT /note="V->A: No effect on interaction with BAG6." FT /evidence="ECO:0000269|PubMed:29042515" FT MUTAGEN 258 FT /note="L->A: No effect on interaction with BAG6." FT /evidence="ECO:0000269|PubMed:29042515" FT MUTAGEN 259 FT /note="C->A: No effect on interaction with BAG6." FT /evidence="ECO:0000269|PubMed:29042515" FT MUTAGEN 262 FT /note="Y->A: Inhibits interaction with BAG6." FT /evidence="ECO:0000269|PubMed:29042515" FT MUTAGEN 266 FT /note="L->A: No effect on interaction with BAG6." FT /evidence="ECO:0000269|PubMed:29042515" FT MUTAGEN 278 FT /note="R->E: No effect on interaction with GET3. No effect FT on tail-anchored protein delivery." FT /evidence="ECO:0000269|PubMed:34887561" FT CONFLICT 9..22 FT /note="EQESARNGGRNRGG -> DRRAPATALQPRA (in Ref. 6; FT AAD27729)" FT /evidence="ECO:0000305" FT CONFLICT 177 FT /note="N -> D (in Ref. 6; AAD27729)" FT /evidence="ECO:0000305" FT HELIX 26..35 FT /evidence="ECO:0007829|PDB:6AU8" FT HELIX 39..55 FT /evidence="ECO:0007829|PDB:6AU8" FT HELIX 59..75 FT /evidence="ECO:0007829|PDB:6AU8" FT HELIX 79..95 FT /evidence="ECO:0007829|PDB:6AU8" FT HELIX 98..100 FT /evidence="ECO:0007829|PDB:6AU8" FT HELIX 102..114 FT /evidence="ECO:0007829|PDB:6AU8" FT HELIX 120..134 FT /evidence="ECO:0007829|PDB:6AU8" FT HELIX 143..155 FT /evidence="ECO:0007829|PDB:6AU8" FT HELIX 159..167 FT /evidence="ECO:0007829|PDB:6AU8" FT HELIX 172..186 FT /evidence="ECO:0007829|PDB:6AU8" FT HELIX 189..191 FT /evidence="ECO:0007829|PDB:6AU8" FT HELIX 192..205 FT /evidence="ECO:0007829|PDB:6AU8" FT HELIX 209..222 FT /evidence="ECO:0007829|PDB:6AU8" FT STRAND 228..231 FT /evidence="ECO:0007829|PDB:7RU9" FT HELIX 235..248 FT /evidence="ECO:0007829|PDB:6AU8" FT HELIX 252..261 FT /evidence="ECO:0007829|PDB:6AU8" FT HELIX 263..266 FT /evidence="ECO:0007829|PDB:6AU8" FT HELIX 272..284 FT /evidence="ECO:0007829|PDB:6AU8" FT HELIX 286..288 FT /evidence="ECO:0007829|PDB:6AU8" FT HELIX 294..298 FT /evidence="ECO:0007829|PDB:6AU8" FT HELIX 301..303 FT /evidence="ECO:0007829|PDB:6AU8" SQ SEQUENCE 327 AA; 36504 MW; 4D6C4233181B0512 CRC64; MAAAAAMAEQ ESARNGGRNR GGVQRVEGKL RASVEKGDYY EAHQMYRTLF FRYMSQSKHT EARELMYSGA LLFFSHGQQN SAADLSMLVL ESLEKAEVEV ADELLENLAK VFSLMDPNSP ERVTFVSRAL KWSSGGSGKL GHPRLHQLLA LTLWKEQNYC ESRYHFLHSA DGEGCANMLV EYSTSRGFRS EVDMFVAQAV LQFLCLKNKS SASVVFTTYT QKHPSIEDGP PFVEPLLNFI WFLLLAVDGG KLTVFTVLCE QYQPSLRRDP MYNEYLDRIG QLFFGVPPKQ TSSYGGLLGN LLTSLMGSSE QEDGEESPSD GSPIELD //