DNJB4_MOUSE
ID DNJB4_MOUSE Reviewed; 337 AA.
AC Q9D832; Q3TS92; Q9D9U2;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=DnaJ homolog subfamily B member 4;
GN Name=Dnajb4;
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].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Egg, Small intestine, and Testis;
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].
RC TISSUE=Eye;
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, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC 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: Probable chaperone. Stimulates ATP hydrolysis and the folding
CC of unfolded proteins mediated by HSPA1A/B (in vitro).
CC {ECO:0000250|UniProtKB:Q9UDY4}.
CC -!- SUBUNIT: Homodimer. The C-terminal section interacts with the C-
CC terminal tail of OPRM1. Interacts also with SDIM1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9UDY4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UDY4}. Cell
CC membrane {ECO:0000250|UniProtKB:Q9UDY4}.
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DR EMBL; AK006478; BAB24608.1; -; mRNA.
DR EMBL; AK008537; BAB25729.1; -; mRNA.
DR EMBL; AK028049; BAC25720.1; -; mRNA.
DR EMBL; AK136240; BAE22891.1; -; mRNA.
DR EMBL; AK162194; BAE36783.1; -; mRNA.
DR EMBL; BC017161; AAH17161.1; -; mRNA.
DR CCDS; CCDS17915.1; -.
DR RefSeq; NP_080202.1; NM_025926.4.
DR RefSeq; NP_081563.2; NM_027287.4.
DR RefSeq; XP_006501983.1; XM_006501920.3.
DR AlphaFoldDB; Q9D832; -.
DR SMR; Q9D832; -.
DR BioGRID; 211889; 17.
DR IntAct; Q9D832; 3.
DR MINT; Q9D832; -.
DR STRING; 10090.ENSMUSP00000114356; -.
DR iPTMnet; Q9D832; -.
DR PhosphoSitePlus; Q9D832; -.
DR EPD; Q9D832; -.
DR MaxQB; Q9D832; -.
DR PaxDb; Q9D832; -.
DR PeptideAtlas; Q9D832; -.
DR PRIDE; Q9D832; -.
DR ProteomicsDB; 277350; -.
DR Antibodypedia; 33498; 273 antibodies from 31 providers.
DR DNASU; 67035; -.
DR Ensembl; ENSMUST00000029669; ENSMUSP00000029669; ENSMUSG00000028035.
DR Ensembl; ENSMUST00000050073; ENSMUSP00000053916; ENSMUSG00000028035.
DR Ensembl; ENSMUST00000144950; ENSMUSP00000114356; ENSMUSG00000028035.
DR GeneID; 67035; -.
DR KEGG; mmu:67035; -.
DR UCSC; uc008rsq.3; mouse.
DR CTD; 11080; -.
DR MGI; MGI:1914285; Dnajb4.
DR VEuPathDB; HostDB:ENSMUSG00000028035; -.
DR eggNOG; KOG0714; Eukaryota.
DR GeneTree; ENSGT00940000156826; -.
DR HOGENOM; CLU_017633_0_0_1; -.
DR InParanoid; Q9D832; -.
DR OMA; DVNFPET; -.
DR OrthoDB; 1393097at2759; -.
DR PhylomeDB; Q9D832; -.
DR TreeFam; TF105141; -.
DR BioGRID-ORCS; 67035; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Dnajb4; mouse.
DR PRO; PR:Q9D832; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9D832; protein.
DR Bgee; ENSMUSG00000028035; Expressed in ascending aorta and 249 other tissues.
DR ExpressionAtlas; Q9D832; baseline and differential.
DR Genevisible; Q9D832; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0001671; F:ATPase activator activity; ISS:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; ISO:MGI.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR002939; DnaJ_C.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR InterPro; IPR036869; J_dom_sf.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF01556; DnaJ_C; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF49493; SSF49493; 2.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Chaperone; Cytoplasm; Membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..337
FT /note="DnaJ homolog subfamily B member 4"
FT /id="PRO_0000071022"
FT DOMAIN 4..68
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY4"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY4"
FT CONFLICT 66
FT /note="Q -> L (in Ref. 1; BAB24608)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="P -> T (in Ref. 1; BAB24608)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="I -> S (in Ref. 1; BAB24608)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 337 AA; 37782 MW; BEE4A0E25BCEEFF4 CRC64;
MGKDYYHILG IDKGATDEDV KKAYRKQALK FHPDKNKSPQ AEEKFKEVAE AYEVLSDPKK
REIYDQFGEE GLKGGAGGTD GQGGTFRYTF HGDPHATFAA FFGGSNPFEI FFGRRMGGGR
DSEEMEIDGD PFSAFGFSMN GYPRDRNSVG PSRLKQDPPI IHELKVSLEE IYSGCTKRMK
ISRKRLNPDG RSYRSEDKIL TIEIKKGWKE GTKITFPREG DETPNSIPAD IVFVIKDKEH
PKFKRDGSNI VYTAKISLRE ALCGCSLNVP TMDGRNLPMS VTDIVKPGMR RRVIGYGLPF
PKNPDQRGDL LIEFDVSFPD VISAASKEIL RKHLPAS
