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Golgi to ER traffic protein 4 homolog (Conserved edge-expressed protein) (Transmembrane domain recognition complex 35 kDa subunit) (TRC35)

 GET4_HUMAN              Reviewed;         327 AA.
Q7L5D6; A4D2Q1; B3KNC7; Q9UFC9; Q9Y309;
21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
25-OCT-2017, entry version 116.
RecName: Full=Golgi to ER traffic protein 4 homolog;
AltName: Full=Conserved edge-expressed protein;
AltName: Full=Transmembrane domain recognition complex 35 kDa subunit;
Short=TRC35;
Name=GET4; Synonyms=C7orf20, CEE, TRC35; ORFNames=CGI-20;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Ovary, Testis, and Thymus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 2-14 AND 111-122, CLEAVAGE OF INITIATOR
METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Lung carcinoma;
Bienvenut W.V., Vousden K.H., Lukashchuk N.;
Submitted (MAR-2008) to UniProtKB.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-327 (ISOFORM 1).
PubMed=10810093; DOI=10.1101/gr.10.5.703;
Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
"Identification of novel human genes evolutionarily conserved in
Caenorhabditis elegans by comparative proteomics.";
Genome Res. 10:703-713(2000).
[7]
IDENTIFICATION.
PubMed=18249086; DOI=10.1016/j.ygeno.2007.10.017;
Fernandes J.M.O., Macqueen D.J., Lee H.-T., Johnston I.A.;
"Genomic, evolutionary, and expression analyses of cee, an ancient
gene involved in normal growth and development.";
Genomics 91:315-325(2008).
[8]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[9]
FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY,
AND IDENTIFICATION IN THE BAG6/BAT3 COMPLEX.
PubMed=20676083; DOI=10.1038/nature09296;
Mariappan M., Li X., Stefanovic S., Sharma A., Mateja A., Keenan R.J.,
Hegde R.S.;
"A ribosome-associating factor chaperones tail-anchored membrane
proteins.";
Nature 466:1120-1124(2010).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
FUNCTION, INTERACTION WITH BAG6, AND SUBCELLULAR LOCATION.
PubMed=21636303; DOI=10.1016/j.molcel.2011.05.010;
Wang Q., Liu Y., Soetandyo N., Baek K., Hegde R., Ye Y.;
"A ubiquitin ligase-associated chaperone holdase maintains
polypeptides in soluble states for proteasome degradation.";
Mol. Cell 42:758-770(2011).
[12]
FUNCTION.
PubMed=21743475; DOI=10.1038/nature10181;
Hessa T., Sharma A., Mariappan M., Eshleman H.D., Gutierrez E.,
Hegde R.S.;
"Protein targeting and degradation are coupled for elimination of
mislocalized proteins.";
Nature 475:394-397(2011).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
FUNCTION.
PubMed=28104892; DOI=10.1126/science.aah6130;
Shao S., Rodrigo-Brenni M.C., Kivlen M.H., Hegde R.S.;
"Mechanistic basis for a molecular triage reaction.";
Science 355:298-302(2017).
-!- FUNCTION: As part of a cytosolic protein quality control complex,
the BAG6/BAT3 complex, maintains misfolded and hydrophobic
patches-containing proteins in a soluble state and participates to
their proper delivery to the endoplasmic reticulum or
alternatively can promote their sorting to the proteasome where
they undergo degradation (PubMed:20676083, PubMed:21636303,
PubMed:21743475, PubMed:28104892). The BAG6/BAT3 complex is
involved in the post-translational delivery of tail-anchored/type
II transmembrane proteins to the endoplasmic reticulum membrane.
Recruited to ribosomes, it interacts with the transmembrane region
of newly synthesized tail-anchored proteins and together with SGTA
and ASNA1 mediates their delivery to the endoplasmic reticulum
(PubMed:20676083, PubMed:28104892). Client proteins that cannot be
properly delivered to the endoplasmic reticulum are ubiquitinated
and sorted to the proteasome (PubMed:28104892). Similarly, the
BAG6/BAT3 complex also functions as a sorting platform for
proteins of the secretory pathway that are mislocalized to the
cytosol either delivering them to the proteasome for degradation
or to the endoplasmic reticulum (PubMed:21743475). The BAG6/BAT3
complex also plays a role in the endoplasmic reticulum-associated
degradation (ERAD), a quality control mechanism that eliminates
unwanted proteins of the endoplasmic reticulum through their
retrotranslocation to the cytosol and their targeting to the
proteasome. It maintains these retrotranslocated proteins in an
unfolded yet soluble state condition in the cytosol to ensure
their proper delivery to the proteasome (PubMed:21636303).
{ECO:0000269|PubMed:20676083, ECO:0000269|PubMed:21636303,
ECO:0000269|PubMed:21743475, ECO:0000269|PubMed:28104892}.
-!- SUBUNIT: Component of the BAG6/BAT3 complex, at least composed of
BAG6, UBL4A and GET4/TRC35 (PubMed:20676083). Interacts with BAG6;
the interaction is direct and localizes BAG6 to the cytosol
(PubMed:21636303). {ECO:0000269|PubMed:20676083,
ECO:0000269|PubMed:21636303}.
-!- INTERACTION:
O43681:ASNA1; NbExp=3; IntAct=EBI-711823, EBI-2515857;
O43741:PRKAB2; NbExp=6; IntAct=EBI-711823, EBI-1053424;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:20676083, ECO:0000269|PubMed:21636303}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q7L5D6-1; Sequence=Displayed;
Note=No experimental confirmation available.;
Name=2;
IsoId=Q7L5D6-2; Sequence=VSP_017652;
-!- SIMILARITY: Belongs to the GET4 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AK024305; BAG51289.1; -; mRNA.
EMBL; AK097899; BAG53546.1; -; mRNA.
EMBL; AK125863; BAG54258.1; -; mRNA.
EMBL; AL133014; CAB61355.1; -; mRNA.
EMBL; CH236965; EAL23708.1; -; Genomic_DNA.
EMBL; BC003550; AAH03550.2; -; mRNA.
EMBL; AF132954; AAD27729.1; -; mRNA.
CCDS; CCDS5317.1; -. [Q7L5D6-1]
PIR; T42648; T42648.
RefSeq; NP_057033.2; NM_015949.2. [Q7L5D6-1]
UniGene; Hs.107387; -.
UniGene; Hs.743756; -.
ProteinModelPortal; Q7L5D6; -.
SMR; Q7L5D6; -.
BioGrid; 119636; 63.
IntAct; Q7L5D6; 46.
MINT; MINT-1852978; -.
STRING; 9606.ENSP00000265857; -.
iPTMnet; Q7L5D6; -.
PhosphoSitePlus; Q7L5D6; -.
BioMuta; GET4; -.
DMDM; 74738593; -.
EPD; Q7L5D6; -.
MaxQB; Q7L5D6; -.
PaxDb; Q7L5D6; -.
PeptideAtlas; Q7L5D6; -.
PRIDE; Q7L5D6; -.
DNASU; 51608; -.
Ensembl; ENST00000265857; ENSP00000265857; ENSG00000239857. [Q7L5D6-1]
Ensembl; ENST00000407192; ENSP00000385646; ENSG00000239857. [Q7L5D6-2]
GeneID; 51608; -.
KEGG; hsa:51608; -.
UCSC; uc003sjl.2; human. [Q7L5D6-1]
CTD; 51608; -.
EuPathDB; HostDB:ENSG00000239857.6; -.
GeneCards; GET4; -.
H-InvDB; HIX0033841; -.
H-InvDB; HIX0201122; -.
HGNC; HGNC:21690; GET4.
HPA; HPA019765; -.
MIM; 612056; gene.
neXtProt; NX_Q7L5D6; -.
OpenTargets; ENSG00000239857; -.
PharmGKB; PA165618100; -.
eggNOG; KOG3024; Eukaryota.
eggNOG; ENOG410XRWE; LUCA.
GeneTree; ENSGT00390000015750; -.
HOGENOM; HOG000264232; -.
HOVERGEN; HBG059877; -.
InParanoid; Q7L5D6; -.
OMA; QMYRTLF; -.
OrthoDB; EOG091G0DTD; -.
PhylomeDB; Q7L5D6; -.
TreeFam; TF315163; -.
GeneWiki; C7orf20; -.
GenomeRNAi; 51608; -.
PRO; PR:Q7L5D6; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000239857; -.
CleanEx; HS_C7orf20; -.
ExpressionAtlas; Q7L5D6; baseline and differential.
Genevisible; Q7L5D6; HS.
GO; GO:0071818; C:BAT3 complex; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0051087; F:chaperone binding; IPI:BHF-UCL.
GO; GO:0051220; P:cytoplasmic sequestering of protein; IMP:ParkinsonsUK-UCL.
GO; GO:1904378; P:maintenance of unfolded protein involved in ERAD pathway; IMP:ParkinsonsUK-UCL.
GO; GO:0071816; P:tail-anchored membrane protein insertion into ER membrane; IMP:UniProtKB.
GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
InterPro; IPR007317; UPF0363.
PANTHER; PTHR12875; PTHR12875; 1.
Pfam; PF04190; DUF410; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
Direct protein sequencing; Phosphoprotein; Reference proteome;
Transport.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.5}.
CHAIN 2 327 Golgi to ER traffic protein 4 homolog.
/FTId=PRO_0000228104.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.5}.
MOD_RES 12 12 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 53 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_017652.
CONFLICT 9 22 EQESARNGGRNRGG -> DRRAPATALQPRA (in Ref.
6; AAD27729). {ECO:0000305}.
CONFLICT 177 177 N -> D (in Ref. 6; AAD27729).
{ECO:0000305}.
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


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