DNJB3_MOUSE
ID DNJB3_MOUSE Reviewed; 242 AA.
AC O35723; Q9DAN3; Q9DAN4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=DnaJ homolog subfamily B member 3;
DE Short=DnaJ protein homolog 3;
DE AltName: Full=Heat shock protein J3;
DE Short=HSJ-3;
DE AltName: Full=MSJ-1;
GN Name=Dnajb3; Synonyms=Hsj3, Msj1;
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 [MRNA].
RC TISSUE=Testis;
RX PubMed=9521861; DOI=10.1006/excr.1997.3879;
RA Berruti G., Perego L., Borgonovo B., Martegani E.;
RT "MSJ-1, a new member of the DNAJ family of proteins, is a male germ cell-
RT specific gene product.";
RL Exp. Cell Res. 239:430-441(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=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).
CC -!- FUNCTION: May operate as a co-chaperone of the male germ cell- and
CC haploid stage-specific Hsp70 proteins. {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Testis specific. Expression is confined to the
CC germline without any contribution of the somatic components.
CC -!- DEVELOPMENTAL STAGE: Its expression occurs in the postmeiotic phase of
CC male germ cell development. First detected in 30 days old mice and
CC thereafter into adulthood. Barely detectable in 20 days old mice and
CC absent before this period.
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DR EMBL; U95607; AAC13944.1; -; mRNA.
DR EMBL; AK005690; BAB24188.1; -; mRNA.
DR EMBL; AK005688; BAB24186.1; -; mRNA.
DR CCDS; CCDS15142.1; -.
DR RefSeq; NP_032325.2; NM_008299.3.
DR AlphaFoldDB; O35723; -.
DR SMR; O35723; -.
DR BioGRID; 200447; 2.
DR STRING; 10090.ENSMUSP00000112703; -.
DR iPTMnet; O35723; -.
DR PhosphoSitePlus; O35723; -.
DR REPRODUCTION-2DPAGE; IPI00133874; -.
DR REPRODUCTION-2DPAGE; O35723; -.
DR MaxQB; O35723; -.
DR PaxDb; O35723; -.
DR PeptideAtlas; O35723; -.
DR PRIDE; O35723; -.
DR ProteomicsDB; 277349; -.
DR DNASU; 15504; -.
DR GeneID; 15504; -.
DR KEGG; mmu:15504; -.
DR CTD; 414061; -.
DR MGI; MGI:1306822; Dnajb3.
DR eggNOG; KOG0714; Eukaryota.
DR InParanoid; O35723; -.
DR OrthoDB; 1152652at2759; -.
DR PhylomeDB; O35723; -.
DR BioGRID-ORCS; 15504; 1 hit in 72 CRISPR screens.
DR PRO; PR:O35723; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O35723; protein.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:MGI.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR036869; J_dom_sf.
DR Pfam; PF00226; DnaJ; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 2: Evidence at transcript level;
KW Chaperone; Reference proteome.
FT CHAIN 1..242
FT /note="DnaJ homolog subfamily B member 3"
FT /id="PRO_0000071020"
FT DOMAIN 1..69
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT CONFLICT 71
FT /note="V -> M (in Ref. 2; BAB24186)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="F -> I (in Ref. 2; BAB24188)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="R -> K (in Ref. 2; BAB24188/BAB24186)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 242 AA; 26679 MW; 5F54F48A00094D84 CRC64;
MVDYYEVLGV PRQASAEAIR KAYRKLALKW HPDKNPEHKE EAERRFKQVA QAYEVLSDVR
KREVYDRCGE VGEVGGGGAA GSPFHDAFQY VFSFRDPAEV FREFFGGHDP FSFDFFGGDP
LENFFGDRRS TRGSRSRGAV PFSTSFTEFP GFGGGFASLD TGFTSFGSPG NSGLSSFSMS
CGGGAAGNYK SVSTSTEIIN GKKITTKRIV ENGQERVEVE EDGELKSLII NGREQLLRIN
TQ
