GET4_HUMAN
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 03-AUG-2022, entry version 147.
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] {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).
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 The BAG6/BAT3 complex is involved in the post-translational delivery of
CC tail-anchored/type II transmembrane proteins to the endoplasmic
CC reticulum membrane. Recruited to ribosomes, it interacts with the
CC transmembrane region of newly synthesized tail-anchored proteins and
CC together with SGTA and ASNA1 mediates their delivery to the endoplasmic
CC reticulum (PubMed:20676083, PubMed:28104892, PubMed:25535373). Client
CC proteins that cannot be properly delivered to the endoplasmic reticulum
CC are ubiquitinated and sorted to the proteasome (PubMed:28104892).
CC Similarly, the BAG6/BAT3 complex also functions as a sorting platform
CC for proteins of the secretory pathway that are mislocalized to the
CC cytosol either delivering them to the proteasome for degradation or to
CC the endoplasmic reticulum (PubMed:21743475). The BAG6/BAT3 complex also
CC plays a role in the endoplasmic reticulum-associated degradation
CC (ERAD), a quality control mechanism that eliminates unwanted proteins
CC of the endoplasmic reticulum through their retrotranslocation to the
CC cytosol and their targeting to the proteasome. It maintains these
CC retrotranslocated proteins in an unfolded yet soluble state condition
CC in the cytosol to ensure their proper delivery to the proteasome
CC (PubMed:21636303). {ECO:0000269|PubMed:20676083,
CC ECO:0000269|PubMed:21636303, ECO:0000269|PubMed:21743475,
CC ECO:0000269|PubMed:25535373, ECO:0000269|PubMed:28104892}.
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:29042515, PubMed:25535373).
CC {ECO:0000269|PubMed:20676083, ECO:0000269|PubMed:21636303,
CC ECO:0000269|PubMed:25535373, ECO:0000269|PubMed:29042515}.
CC -!- INTERACTION:
CC Q7L5D6; P46379-2: BAG6; NbExp=4; IntAct=EBI-711823, EBI-10988864;
CC Q7L5D6; Q9NX04: C1orf109; NbExp=3; IntAct=EBI-711823, EBI-8643161;
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=4; 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; 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 -!- 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 -!- SIMILARITY: Belongs to the GET4 family. {ECO:0000305}.
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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 SMR; Q7L5D6; -.
DR BioGRID; 119636; 138.
DR ComplexPortal; CPX-132; BAT3 complex.
DR CORUM; Q7L5D6; -.
DR IntAct; Q7L5D6; 56.
DR MINT; Q7L5D6; -.
DR STRING; 9606.ENSP00000265857; -.
DR MoonDB; Q7L5D6; Predicted.
DR iPTMnet; Q7L5D6; -.
DR MetOSite; Q7L5D6; -.
DR PhosphoSitePlus; Q7L5D6; -.
DR BioMuta; GET4; -.
DR DMDM; 74738593; -.
DR EPD; Q7L5D6; -.
DR jPOST; Q7L5D6; -.
DR MassIVE; Q7L5D6; -.
DR MaxQB; Q7L5D6; -.
DR PaxDb; Q7L5D6; -.
DR PeptideAtlas; Q7L5D6; -.
DR PRIDE; Q7L5D6; -.
DR ProteomicsDB; 68807; -. [Q7L5D6-1]
DR ProteomicsDB; 68808; -. [Q7L5D6-2]
DR Antibodypedia; 34834; 59 antibodies from 15 providers.
DR DNASU; 51608; -.
DR Ensembl; ENST00000265857.8; ENSP00000265857.3; ENSG00000239857.7. [Q7L5D6-1]
DR Ensembl; ENST00000407192.5; ENSP00000385646.1; ENSG00000239857.7. [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 CTD; 51608; -.
DR DisGeNET; 51608; -.
DR GeneCards; GET4; -.
DR HGNC; HGNC:21690; GET4.
DR HPA; ENSG00000239857; Low tissue specificity.
DR MIM; 612056; gene.
DR neXtProt; NX_Q7L5D6; -.
DR OpenTargets; ENSG00000239857; -.
DR PharmGKB; PA165618100; -.
DR VEuPathDB; HostDB:ENSG00000239857; -.
DR eggNOG; KOG3024; Eukaryota.
DR GeneTree; ENSGT00390000015750; -.
DR HOGENOM; CLU_046061_2_0_1; -.
DR InParanoid; Q7L5D6; -.
DR OMA; QIGEMYF; -.
DR OrthoDB; 1030907at2759; -.
DR PhylomeDB; Q7L5D6; -.
DR TreeFam; TF315163; -.
DR PathwayCommons; Q7L5D6; -.
DR Reactome; R-HSA-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR SignaLink; Q7L5D6; -.
DR BioGRID-ORCS; 51608; 206 hits in 1082 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 93 other tissues.
DR ExpressionAtlas; Q7L5D6; baseline and differential.
DR Genevisible; Q7L5D6; HS.
DR GO; GO:0071818; C:BAT3 complex; IDA:UniProtKB.
DR GO; GO:0005694; C:chromosome; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0051087; F:chaperone binding; IPI:BHF-UCL.
DR GO; GO:0051220; P:cytoplasmic sequestering of protein; IMP:ParkinsonsUK-UCL.
DR GO; GO:1904378; P:maintenance of unfolded protein involved in ERAD pathway; 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; IBA:GO_Central.
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 Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR007317; GET4.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR12875; PTHR12875; 1.
DR Pfam; PF04190; GET4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Phosphoprotein; Reference proteome; Transport;
KW 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 COMPBIAS 313..327
FT /note="Acidic residues"
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 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 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 102..114
FT /evidence="ECO:0007829|PDB:6AU8"
FT HELIX 120..133
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 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
