GET4_MOUSE
ID GET4_MOUSE Reviewed; 327 AA.
AC Q9D1H7; Q78J86;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Golgi to ER traffic protein 4 homolog;
GN Name=Get4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Liver;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. The
CC 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. Client proteins that cannot be properly delivered to the
CC endoplasmic reticulum are ubiquitinated and sorted to the proteasome.
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. 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.
CC {ECO:0000250|UniProtKB:Q7L5D6}.
CC -!- SUBUNIT: Component of the BAG6/BAT3 complex, at least composed of BAG6,
CC UBL4A and GET4/TRC35. Interacts with BAG6; the interaction is direct
CC and localizes BAG6 in the cytosol. {ECO:0000250|UniProtKB:Q7L5D6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q7L5D6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D1H7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D1H7-2; Sequence=VSP_017653;
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:0000250|UniProtKB:Q7L5D6}.
CC -!- SIMILARITY: Belongs to the GET4 family. {ECO:0000305}.
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DR EMBL; AK003551; BAB22851.2; -; mRNA.
DR EMBL; BC019557; AAH19557.1; -; mRNA.
DR CCDS; CCDS19805.1; -. [Q9D1H7-1]
DR CCDS; CCDS51682.1; -. [Q9D1H7-2]
DR RefSeq; NP_001156788.1; NM_001163316.1. [Q9D1H7-2]
DR RefSeq; NP_080545.2; NM_026269.2. [Q9D1H7-1]
DR AlphaFoldDB; Q9D1H7; -.
DR SMR; Q9D1H7; -.
DR BioGRID; 212305; 31.
DR ComplexPortal; CPX-133; BAT3 complex.
DR IntAct; Q9D1H7; 23.
DR STRING; 10090.ENSMUSP00000026976; -.
DR iPTMnet; Q9D1H7; -.
DR PhosphoSitePlus; Q9D1H7; -.
DR EPD; Q9D1H7; -.
DR jPOST; Q9D1H7; -.
DR MaxQB; Q9D1H7; -.
DR PaxDb; Q9D1H7; -.
DR PeptideAtlas; Q9D1H7; -.
DR PRIDE; Q9D1H7; -.
DR ProteomicsDB; 271210; -. [Q9D1H7-1]
DR ProteomicsDB; 271211; -. [Q9D1H7-2]
DR Antibodypedia; 34834; 59 antibodies from 15 providers.
DR Ensembl; ENSMUST00000026976; ENSMUSP00000026976; ENSMUSG00000025858. [Q9D1H7-1]
DR Ensembl; ENSMUST00000110878; ENSMUSP00000106502; ENSMUSG00000025858. [Q9D1H7-2]
DR GeneID; 67604; -.
DR KEGG; mmu:67604; -.
DR UCSC; uc009agg.2; mouse. [Q9D1H7-1]
DR CTD; 51608; -.
DR MGI; MGI:1914854; Get4.
DR VEuPathDB; HostDB:ENSMUSG00000025858; -.
DR eggNOG; KOG3024; Eukaryota.
DR GeneTree; ENSGT00390000015750; -.
DR HOGENOM; CLU_046061_2_0_1; -.
DR InParanoid; Q9D1H7; -.
DR OMA; QIGEMYF; -.
DR OrthoDB; 1030907at2759; -.
DR PhylomeDB; Q9D1H7; -.
DR TreeFam; TF315163; -.
DR BioGRID-ORCS; 67604; 19 hits in 72 CRISPR screens.
DR ChiTaRS; Get4; mouse.
DR PRO; PR:Q9D1H7; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9D1H7; protein.
DR Bgee; ENSMUSG00000025858; Expressed in bone marrow and 71 other tissues.
DR ExpressionAtlas; Q9D1H7; baseline and differential.
DR Genevisible; Q9D1H7; MM.
DR GO; GO:0071818; C:BAT3 complex; ISS:UniProtKB.
DR GO; GO:0005694; C:chromosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0051087; F:chaperone binding; ISO:MGI.
DR GO; GO:0051220; P:cytoplasmic sequestering of protein; ISO:MGI.
DR GO; GO:1904378; P:maintenance of unfolded protein involved in ERAD pathway; ISO:MGI.
DR GO; GO:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0045048; P:protein insertion into ER membrane; IBA:GO_Central.
DR GO; GO:0031647; P:regulation of protein stability; ISO:MGI.
DR GO; GO:0071816; P:tail-anchored membrane protein insertion into ER membrane; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISO:MGI.
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 Acetylation; Alternative splicing; Cytoplasm; Reference proteome;
KW Transport; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q7L5D6"
FT CHAIN 2..327
FT /note="Golgi to ER traffic protein 4 homolog"
FT /id="PRO_0000228105"
FT REGION 195..271
FT /note="Interacts with BAG6"
FT /evidence="ECO:0000250|UniProtKB:Q7L5D6"
FT REGION 307..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..327
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q7L5D6"
FT VAR_SEQ 1..53
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017653"
SQ SEQUENCE 327 AA; 36525 MW; 04B8DCC8E75FB022 CRC64;
MAAAAAMAEQ EGARNGARNR GGVQRVEGKL RASVEKGDYY EAHQMYRTLF FRYMSQSKHA
EARELMYSGA LLFFSHGQQN SAADLSMLVL ESLEKAEVDV ADELLENLAK VFSLMDPNSP
ERVAFVSRAL KWSSGGSGKL GHPRLHQLLA LTLWKEQNYC ESRYHFLHSS DGEGCANMLV
EYSTARGFRS EVDMFVAQAV LQFLCLKNKN SALVVFTTYT QKHPSIEDGP PFVQPLLNFI
WFLLLAVDGG KLAVFTVLCE QYQPSLRRDP MYNEYLDRIG QLFFGVPPKQ TSSYGGLLGN
LLSSLMGSSE QEEGEESQDD SSPIELD
