ID DJC21_MOUSE Reviewed; 531 AA.
AC E9Q8D0; Q3USP3;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 85.
DE RecName: Full=DnaJ homolog subfamily C member 21;
GN Name=Dnajc21;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-184.
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283 AND SER-302, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283 AND SER-302, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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: May act as a co-chaperone for HSP70. May play a role in
CC ribosomal RNA (rRNA) biogenesis, possibly in the maturation of the 60S
CC subunit. Binds the precursor 45S rRNA. {ECO:0000250|UniProtKB:Q5F1R6}.
CC -!- SUBUNIT: Interacts with HSPA8, PA2G4 and ZNF622.
CC {ECO:0000250|UniProtKB:Q5F1R6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5F1R6}. Nucleus
CC {ECO:0000250|UniProtKB:Q5F1R6}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q5F1R6}. Note=Within the nucleus, localizes
CC primarily to the nucleolus. {ECO:0000250|UniProtKB:Q5F1R6}.
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DR EMBL; AC102101; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK140224; BAE24288.1; -; mRNA.
DR CCDS; CCDS49581.1; -.
DR RefSeq; NP_084322.2; NM_030046.2.
DR AlphaFoldDB; E9Q8D0; -.
DR SMR; E9Q8D0; -.
DR IntAct; E9Q8D0; 1.
DR MINT; E9Q8D0; -.
DR STRING; 10090.ENSMUSP00000116865; -.
DR iPTMnet; E9Q8D0; -.
DR PhosphoSitePlus; E9Q8D0; -.
DR SwissPalm; E9Q8D0; -.
DR EPD; E9Q8D0; -.
DR jPOST; E9Q8D0; -.
DR MaxQB; E9Q8D0; -.
DR PaxDb; 10090-ENSMUSP00000116865; -.
DR PeptideAtlas; E9Q8D0; -.
DR ProteomicsDB; 279669; -.
DR Pumba; E9Q8D0; -.
DR Antibodypedia; 22862; 76 antibodies from 15 providers.
DR Ensembl; ENSMUST00000136591.8; ENSMUSP00000116865.2; ENSMUSG00000044224.17.
DR GeneID; 78244; -.
DR KEGG; mmu:78244; -.
DR UCSC; uc007vgc.2; mouse.
DR AGR; MGI:1925371; -.
DR CTD; 134218; -.
DR MGI; MGI:1925371; Dnajc21.
DR VEuPathDB; HostDB:ENSMUSG00000044224; -.
DR eggNOG; KOG0714; Eukaryota.
DR eggNOG; KOG0717; Eukaryota.
DR GeneTree; ENSGT00510000047097; -.
DR HOGENOM; CLU_009539_1_0_1; -.
DR InParanoid; E9Q8D0; -.
DR OMA; RANHEES; -.
DR OrthoDB; 5491419at2759; -.
DR PhylomeDB; E9Q8D0; -.
DR TreeFam; TF314518; -.
DR BioGRID-ORCS; 78244; 7 hits in 80 CRISPR screens.
DR ChiTaRS; Dnajc21; mouse.
DR PRO; PR:E9Q8D0; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; E9Q8D0; Protein.
DR Bgee; ENSMUSG00000044224; Expressed in cleaving embryo and 266 other cell types or tissues.
DR Genevisible; E9Q8D0; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR022755; Znf_C2H2_jaz.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR44029; DNAJ HOMOLOG SUBFAMILY C MEMBER 21; 1.
DR PANTHER; PTHR44029:SF1; DNAJ HOMOLOG SUBFAMILY C MEMBER 21; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF12171; zf-C2H2_jaz; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SMART; SM00451; ZnF_U1; 1.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW Chaperone; Cytoplasm; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..531
FT /note="DnaJ homolog subfamily C member 21"
FT /id="PRO_0000437995"
FT DOMAIN 3..69
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT ZN_FING 314..338
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 483..507
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 278..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..429
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5F1R6"
FT MOD_RES 512
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5F1R6"
SQ SEQUENCE 531 AA; 61735 MW; 7341A135EEBB5384 CRC64;
MKCHYEALGV RRDASEEELK KAYRKLALRW HPDKNLDNAA EAAEQFKLIQ AAYDVLSDPQ
ERAWYDNHRE ALLKGGLDGE YQDDSLDLLH YFTVTCYSGY GDDERGFYAV YRVVFELIAK
EELECMSEGD VEDFPTFGDS QSDYDTVVHP FYAHWQSFCT QKNFSWKEEY DTRQASNRWE
KRAMEKENKK IRDRARKEKN ELVRQLVAFI RKRDKRVQAH RKLVEEQNAE KARKAEEMRR
QQKLKQAKLA EQYREQSWMT MANLEKELQE MEARYEKEFG DGSDENEVED QEPRNGLDGK
DSEEAEEAEL YQDLYCPACD KSFKTEKAMK NHEKSKKHRE MVALLKQQLE EEEEQFSGVQ
MDENVLNANS EEEMEDTPKQ KLSKKQKKKK QKSAQNFDDN FNENGTEEGG KIAPEKTKSN
EDNAKELENR PQENTCITET TEACEDPKSE AKSVPKSKGK KTKDVKKSVK APAEAQPVSD
VLISCATCHS EFPSRNKLFD HLKATGHARA PSATASLNSV TRNKKEKRRS R
//
