DJB12_MOUSE
ID DJB12_MOUSE Reviewed; 376 AA.
AC Q9QYI4; Q8K037;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=DnaJ homolog subfamily B member 12 {ECO:0000312|MGI:MGI:1931881};
DE AltName: Full=mDj10 {ECO:0000303|PubMed:11147971};
GN Name=Dnajb12 {ECO:0000312|MGI:MGI:1931881};
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].
RX PubMed=11147971; DOI=10.1379/1466-1268(2000)005<0098:mhdhco>2.0.co;2;
RA Ohtsuka K., Hata M.;
RT "Mammalian HSP40/DNAJ homologs: cloning of novel cDNAs and a proposal for
RT their classification and nomenclature.";
RL Cell Stress Chaperones 5:98-112(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Mammary gland, Spinal cord, and Spleen;
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, and Pancreas;
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: Acts as a co-chaperone with HSPA8/Hsc70; required to promote
CC protein folding and trafficking, prevent aggregation of client
CC proteins, and promote unfolded proteins to endoplasmic reticulum-
CC associated degradation (ERAD) pathway. Acts by determining
CC HSPA8/Hsc70's ATPase and polypeptide-binding activities. Can also act
CC independently of HSPA8/Hsc70: together with DNAJB14, acts as a
CC chaperone that promotes maturation of potassium channels KCND2 and
CC KCNH2 by stabilizing nascent channel subunits and assembling them into
CC tetramers. While stabilization of nascent channel proteins is dependent
CC on HSPA8/Hsc70, the process of oligomerization of channel subunits is
CC independent of HSPA8/Hsc70. When overexpressed, forms membranous
CC structures together with DNAJB14 and HSPA8/Hsc70 within the nucleus;
CC the role of these structures, named DJANGOs, is still unclear.
CC {ECO:0000250|UniProtKB:Q9NXW2}.
CC -!- SUBUNIT: Homodimer and homotetramer. Interacts (via J domain) with
CC HSPA8/Hsc70. Forms a multiprotein complex, at least composed of
CC DNAJB12, DNAJB14, HSPA8/Hsc70 and SGTA; interaction with DNAJB14 and
CC HSPA8/Hsc70 is direct. {ECO:0000250|UniProtKB:Q9NXW2}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9NXW2}; Single-pass membrane protein
CC {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:Q9NXW2}; Single-
CC pass membrane protein {ECO:0000250|UniProtKB:Q9NXW2}. Note=Localizes to
CC the endoplasmic reticulum membrane. When overexpressed, forms
CC membranous structures in the nucleus. {ECO:0000250|UniProtKB:Q9NXW2}.
CC -!- PTM: Methylated at His-186 by METTL9. {ECO:0000250|UniProtKB:Q9NXW2}.
CC -!- SIMILARITY: Belongs to the DnaJ family. DNAJB12/DNAJB14 subfamily.
CC {ECO:0000305}.
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DR EMBL; AB028860; BAA88308.1; -; mRNA.
DR EMBL; AK138495; BAE23683.1; -; mRNA.
DR EMBL; AK166224; BAE38642.1; -; mRNA.
DR EMBL; AK172274; BAE42919.1; -; mRNA.
DR EMBL; CH466553; EDL32192.1; -; Genomic_DNA.
DR EMBL; CH466553; EDL32193.1; -; Genomic_DNA.
DR EMBL; CH466553; EDL32195.1; -; Genomic_DNA.
DR EMBL; BC034162; AAH34162.1; -; mRNA.
DR CCDS; CCDS23867.1; -.
DR RefSeq; NP_064349.2; NM_019965.2.
DR AlphaFoldDB; Q9QYI4; -.
DR SMR; Q9QYI4; -.
DR BioGRID; 208137; 6.
DR IntAct; Q9QYI4; 1.
DR STRING; 10090.ENSMUSP00000122056; -.
DR iPTMnet; Q9QYI4; -.
DR PhosphoSitePlus; Q9QYI4; -.
DR EPD; Q9QYI4; -.
DR jPOST; Q9QYI4; -.
DR MaxQB; Q9QYI4; -.
DR PaxDb; Q9QYI4; -.
DR PeptideAtlas; Q9QYI4; -.
DR PRIDE; Q9QYI4; -.
DR ProteomicsDB; 277458; -.
DR Antibodypedia; 2545; 181 antibodies from 25 providers.
DR DNASU; 56709; -.
DR Ensembl; ENSMUST00000020309; ENSMUSP00000020309; ENSMUSG00000020109.
DR Ensembl; ENSMUST00000142819; ENSMUSP00000118088; ENSMUSG00000020109.
DR Ensembl; ENSMUST00000146590; ENSMUSP00000122056; ENSMUSG00000020109.
DR GeneID; 56709; -.
DR KEGG; mmu:56709; -.
DR UCSC; uc007fdz.1; mouse.
DR CTD; 54788; -.
DR MGI; MGI:1931881; Dnajb12.
DR VEuPathDB; HostDB:ENSMUSG00000020109; -.
DR eggNOG; KOG0714; Eukaryota.
DR GeneTree; ENSGT00940000155590; -.
DR HOGENOM; CLU_043579_3_0_1; -.
DR InParanoid; Q9QYI4; -.
DR OrthoDB; 1173544at2759; -.
DR PhylomeDB; Q9QYI4; -.
DR TreeFam; TF105145; -.
DR BioGRID-ORCS; 56709; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Dnajb12; mouse.
DR PRO; PR:Q9QYI4; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9QYI4; protein.
DR Bgee; ENSMUSG00000020109; Expressed in hindlimb stylopod muscle and 234 other tissues.
DR ExpressionAtlas; Q9QYI4; baseline and differential.
DR Genevisible; Q9QYI4; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0030544; F:Hsp70 protein binding; ISO:MGI.
DR GO; GO:0071218; P:cellular response to misfolded protein; ISS:UniProtKB.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; ISS:UniProtKB.
DR GO; GO:0036503; P:ERAD pathway; ISS:UniProtKB.
DR GO; GO:0065003; P:protein-containing complex assembly; ISS:UniProtKB.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; 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; IPR015399; DUF1977_DnaJ-like.
DR InterPro; IPR036869; J_dom_sf.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF09320; DUF1977; 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 1: Evidence at protein level;
KW Acetylation; Chaperone; Endoplasmic reticulum; Membrane; Methylation;
KW Nucleus; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..376
FT /note="DnaJ homolog subfamily B member 12"
FT /id="PRO_0000071038"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 111..175
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 45..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9NXW2"
FT MOD_RES 186
FT /note="Pros-methylhistidine"
FT /evidence="ECO:0000250|UniProtKB:Q9NXW2"
FT CONFLICT 321
FT /note="D -> E (in Ref. 1; BAA88308)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 376 AA; 41988 MW; 33560A17E4B14235 CRC64;
MESNKDEAER CISIALKAIQ SNQPERALRF LEKAQRLYPT PRVSALIESL NQKPQSTGDH
PQPTDTTHTT TKKAGGTETP SANGEAGGGE SAKGYTSEQV AAVKRVKQCK DYYEILGVSR
SASDEDLKKA YRKLALKFHP DKNHAPGATE AFKAIGTAYA VLSNPEKRKQ YDQFGDDKSQ
AARHGHSHGD FHRGFEADIS PEDLFNMFFG GGFPSSNVHV YSNGRMRYTY QQRQDRRDNQ
GDGGLGVFVQ LMPILILILV SALSQLMVSS PPYSLSPRPS VGHIHKRVTD HLNVAYYVAD
TFSEEYTGSS LKTVERNVED DYIANLRNNC WKEKQQKEGL LYRARYFGDT DMYHRAQKMG
TPSCNRLSEV QASLHG
