DJC21_BOVIN
ID DJC21_BOVIN Reviewed; 533 AA.
AC Q0II91;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 2.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=DnaJ homolog subfamily C member 21;
GN Name=DNAJC21;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-186.
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI22751.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AAFC03039458; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03047092; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03047093; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC122750; AAI22751.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001179147.1; NM_001192218.1.
DR AlphaFoldDB; Q0II91; -.
DR SMR; Q0II91; -.
DR STRING; 9913.ENSBTAP00000020793; -.
DR PaxDb; Q0II91; -.
DR PRIDE; Q0II91; -.
DR GeneID; 509302; -.
DR KEGG; bta:509302; -.
DR CTD; 134218; -.
DR eggNOG; KOG0714; Eukaryota.
DR eggNOG; KOG0717; Eukaryota.
DR HOGENOM; CLU_009539_1_0_1; -.
DR InParanoid; Q0II91; -.
DR OrthoDB; 858842at2759; -.
DR TreeFam; TF314518; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
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; 1.10.287.110; -; 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 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; SSF46565; SSF46565; 1.
DR SUPFAM; SSF57667; SSF57667; 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 2: Evidence at transcript level;
KW Chaperone; Cytoplasm; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..533
FT /note="DnaJ homolog subfamily C member 21"
FT /id="PRO_0000413160"
FT DOMAIN 3..70
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT ZN_FING 315..339
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 484..508
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 278..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..437
FT /note="Polar 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 COMPBIAS 508..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5F1R6"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5F1R6"
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 533 AA; 61717 MW; FB5EB0DD3731EA24 CRC64;
MKCHYEALGV RRDASEEELK KAYRKLALKW HPDKNLDNAA EAAEQFKLIQ AAYDVLSDPQ
ERAWYDNHRE ALLKGGLDGE YQDDSLDLLH YFTVTCYSGY GDDEKGFYTV YRNVFEMIAK
EELESALEED MEDFPTFGDS QSDYDTVVHP FYAYWQSFCT QKNFAWKEEY DTRQASNRWE
KRAMEKENKK IRDKARKEKN ELVRQLVAFI RKRDRRVQAH RKLVEEQNAE KARKAEAMRR
QQKLKQAKLA EQYREQSWMA VADLEKELRE MEAQYEKQFG DGSGEDEAED QELRDGQDGK
DSDEAEDAEL YDGLYCPACD KSFKTEKAMR NHEKSKKHRE MVALLKQQLE EEEANFSGPQ
TDENSLNANS EEEMEDAPKQ KLSRKQKKKK QKPAQNYDDN FNENGIGEGV KIDPEDTNLN
QNSAKESEDS LQENVGVTET VELCDDPKTE AKSVSKPKGK KAKDTKKSVR VPAEPQTMSD
VLISCTTCHS EFPSRNKLFD HLKATGHARA PSSSTSLNSV TNSRNKKEKR KNR
