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DNJA4_MOUSE
ID   DNJA4_MOUSE             Reviewed;         397 AA.
AC   Q9JMC3; B2RW09; Q543S9; Q9CTD6; Q9CUD4;
DT   11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 160.
DE   RecName: Full=DnaJ homolog subfamily A member 4;
DE   AltName: Full=MmDjA4;
DE   Flags: Precursor;
GN   Name=Dnaja4;
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   STRAIN=CD-1;
RX   PubMed=10978524; DOI=10.1016/s0167-4781(00)00136-6;
RA   Hata M., Ohtsuka K.;
RT   "Murine cDNA encoding a novel type I HSP40/DNAJ homolog, mmDjA4.";
RL   Biochim. Biophys. Acta 1493:208-210(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Brain, Corpora quadrigemina, Embryo, Spinal ganglion, 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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Lung, 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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in testis and heart.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB30367.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB032401; BAA92775.1; -; mRNA.
DR   EMBL; AK003903; BAB23067.1; -; mRNA.
DR   EMBL; AK016666; BAB30367.2; ALT_INIT; mRNA.
DR   EMBL; AK046476; BAC32747.1; -; mRNA.
DR   EMBL; AK076175; BAC36232.1; -; mRNA.
DR   EMBL; AK141909; BAE24880.1; -; mRNA.
DR   EMBL; BC147484; AAI47485.1; -; mRNA.
DR   EMBL; BC147486; AAI47487.1; -; mRNA.
DR   CCDS; CCDS23193.1; -.
DR   RefSeq; NP_067397.1; NM_021422.4.
DR   AlphaFoldDB; Q9JMC3; -.
DR   SMR; Q9JMC3; -.
DR   BioGRID; 208406; 4.
DR   IntAct; Q9JMC3; 1.
DR   STRING; 10090.ENSMUSP00000070413; -.
DR   iPTMnet; Q9JMC3; -.
DR   PhosphoSitePlus; Q9JMC3; -.
DR   REPRODUCTION-2DPAGE; Q9JMC3; -.
DR   EPD; Q9JMC3; -.
DR   MaxQB; Q9JMC3; -.
DR   PaxDb; Q9JMC3; -.
DR   PeptideAtlas; Q9JMC3; -.
DR   PRIDE; Q9JMC3; -.
DR   ProteomicsDB; 277348; -.
DR   Antibodypedia; 27578; 144 antibodies from 25 providers.
DR   DNASU; 58233; -.
DR   Ensembl; ENSMUST00000070070; ENSMUSP00000070413; ENSMUSG00000032285.
DR   Ensembl; ENSMUST00000120452; ENSMUSP00000112520; ENSMUSG00000032285.
DR   GeneID; 58233; -.
DR   KEGG; mmu:58233; -.
DR   UCSC; uc009prk.2; mouse.
DR   CTD; 55466; -.
DR   MGI; MGI:1927638; Dnaja4.
DR   VEuPathDB; HostDB:ENSMUSG00000032285; -.
DR   eggNOG; KOG0712; Eukaryota.
DR   GeneTree; ENSGT00940000155707; -.
DR   HOGENOM; CLU_017633_10_0_1; -.
DR   InParanoid; Q9JMC3; -.
DR   OMA; NALCTKC; -.
DR   PhylomeDB; Q9JMC3; -.
DR   TreeFam; TF105141; -.
DR   Reactome; R-MMU-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR   BioGRID-ORCS; 58233; 1 hit in 71 CRISPR screens.
DR   ChiTaRS; Dnaja4; mouse.
DR   PRO; PR:Q9JMC3; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q9JMC3; protein.
DR   Bgee; ENSMUSG00000032285; Expressed in seminiferous tubule of testis and 215 other tissues.
DR   ExpressionAtlas; Q9JMC3; baseline and differential.
DR   Genevisible; Q9JMC3; MM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0051087; F:chaperone binding; ISO:MGI.
DR   GO; GO:0030544; F:Hsp70 protein binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051082; F:unfolded protein binding; ISO:MGI.
DR   GO; GO:0010596; P:negative regulation of endothelial cell migration; ISO:MGI.
DR   GO; GO:0090084; P:negative regulation of inclusion body assembly; ISO:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR   GO; GO:0042026; P:protein refolding; ISO:MGI.
DR   GO; GO:0009408; P:response to heat; IEA:InterPro.
DR   CDD; cd06257; DnaJ; 1.
DR   CDD; cd10719; DnaJ_zf; 1.
DR   Gene3D; 1.10.287.110; -; 1.
DR   HAMAP; MF_01152; DnaJ; 1.
DR   InterPro; IPR012724; DnaJ.
DR   InterPro; IPR002939; DnaJ_C.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR018253; DnaJ_domain_CS.
DR   InterPro; IPR044713; DNJA1/2-like.
DR   InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR   InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom.
DR   InterPro; IPR036410; HSP_DnaJ_Cys-rich_dom_sf.
DR   InterPro; IPR036869; J_dom_sf.
DR   PANTHER; PTHR43888; PTHR43888; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF01556; DnaJ_C; 1.
DR   Pfam; PF00684; DnaJ_CXXCXGXG; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; SSF46565; 1.
DR   SUPFAM; SSF49493; SSF49493; 2.
DR   SUPFAM; SSF57938; SSF57938; 1.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
DR   PROSITE; PS51188; ZF_CR; 1.
PE   1: Evidence at protein level;
KW   Chaperone; Lipoprotein; Membrane; Metal-binding; Methylation;
KW   Phosphoprotein; Prenylation; Reference proteome; Repeat; Zinc; Zinc-finger.
FT   CHAIN           1..394
FT                   /note="DnaJ homolog subfamily A member 4"
FT                   /id="PRO_0000071015"
FT   PROPEP          395..397
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000396761"
FT   DOMAIN          4..70
FT                   /note="J"
FT   REPEAT          135..142
FT                   /note="CXXCXGXG motif"
FT   REPEAT          151..158
FT                   /note="CXXCXGXG motif"
FT   REPEAT          178..185
FT                   /note="CXXCXGXG motif"
FT   REPEAT          194..201
FT                   /note="CXXCXGXG motif"
FT   ZN_FING         122..206
FT                   /note="CR-type"
FT   REGION          366..397
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        366..390
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         135
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         138
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         151
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         154
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         178
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         181
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         194
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         197
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         18
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WW22"
FT   MOD_RES         394
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           394
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   397 AA;  44902 MW;  EF47E79FADDD9055 CRC64;
     MVKETQYYDI LGVKPSASPE EIKKAYRKLA LKYHPDKNPD EGEKFKLISQ AYEVLSDPKK
     RDIYDQGGEQ AIKEGGSGSP SFSSPMDIFD MFFGGGGRMT RERRGKNVVH QLSVTLEDLY
     NGITKKLALQ KNVICEKCEG IGGKKGSVEK CPLCKGRGMQ VHIQQIGPGM VQQIQTVCIE
     CKGQGERINP KDRCENCSGA KVTREKKIIE VHVEKGMKDG QKILFHGEGD QEPELDPGDV
     IIVLDQKDHS VFQRRGQDLI MKMKIQLSEA LCGFKKTIKT LDDRVLVISS KSGEVIKHGD
     LKCIRNEGMP IYKAPLEKGV MIIQFLVVFP EKQWLSQEKL PQLEALLPPR QKVRITDDMD
     QVELKEFNPN EQSWRQHREA YEEDDEEPRA GVQCQTA
 
 
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