ID Q864B5_PIG Unreviewed; 397 AA.
AC Q864B5;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 150.
DE SubName: Full=PDJA1 chaperone {ECO:0000313|EMBL:AAP22730.1};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|EMBL:AAP22730.1};
RN [1] {ECO:0000313|EMBL:AAP22730.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12667953; DOI=10.1016/S0008-6363(02)00845-3;
RA Depre C., Wang L., Tomlinson J.E., Gaussin V., Abdellatif M., Topper J.N.,
RA Vatner S.F.;
RT "Characterization of pDJA1, a cardiac-specific chaperone found by genomic
RT profiling of the post-ischemic swine heart.";
RL Cardiovasc. Res. 58:126-135(2003).
CC -!- INTERACTION:
CC Q864B5; Q5U8X5; Xeno; NbExp=4; IntAct=EBI-12591842, EBI-12557210;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid-
CC anchor {ECO:0000256|ARBA:ARBA00004635}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY267904; AAP22730.1; -; mRNA.
DR RefSeq; NP_999504.1; NM_214339.1.
DR AlphaFoldDB; Q864B5; -.
DR IntAct; Q864B5; 1.
DR PeptideAtlas; Q864B5; -.
DR GeneID; 397613; -.
DR KEGG; ssc:397613; -.
DR CTD; 55466; -.
DR HOGENOM; CLU_017633_10_0_1; -.
DR OMA; FPDVINP; -.
DR OrthoDB; 2785358at2759; -.
DR TreeFam; TF105141; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0009408; P:response to heat; IEA:InterPro.
DR CDD; cd06257; DnaJ; 1.
DR CDD; cd10747; DnaJ_C; 1.
DR CDD; cd10719; DnaJ_zf; 1.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 2.10.230.10; Heat shock protein DnaJ, cysteine-rich domain; 1.
DR Gene3D; 2.60.260.20; Urease metallochaperone UreE, N-terminal domain; 2.
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:SF9; DNAJ HOMOLOG SUBFAMILY A MEMBER 4; 1.
DR PANTHER; PTHR43888; DNAJ-LIKE-2, ISOFORM A-RELATED; 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; Chaperone J-domain; 1.
DR SUPFAM; SSF57938; DnaJ/Hsp40 cysteine-rich domain; 1.
DR SUPFAM; SSF49493; HSP40/DnaJ peptide-binding domain; 2.
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00546}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00546};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00546}.
FT DOMAIN 6..68
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 122..206
FT /note="CR-type"
FT /evidence="ECO:0000259|PROSITE:PS51188"
FT ZN_FING 122..206
FT /note="CR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT REGION 365..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 397 AA; 44839 MW; 93ED32298B5ACE90 CRC64;
MVKETQYYDI LGVKPSASPE EIKKAYRKLA LKYHPDKNPD EGEKFKLISQ AYEVLSDPKK
RDIYDQGGEQ AIKEGGSGSP SFSSPMDIFD MFFGGGGRMA RERRGKNVVH QLSVTLEDLY
NGVTKKLALQ KNVICEKCEG VGGKKGSVEK CPVCKGRGMQ IHIQQIGPGM VQQIQTVCIE
CKGQGERINP KDRCENCSGA KVIREKKIIE VHVEKGMKDG QKILFHGEGD QEPELEPGDV
IIVLDQKDHS VFQRRGHDLI MKMKIQLCEA LCGFKKTIKT LDDRVLVITS KSGEVIKHGD
LKCVRNEGMP IYKAPLEKGT LIIQFLVIFP EKHWLPQDKL PQLEALLPPR QKVRITDDMD
QVELKEFNPN EQNWRQHREA YEEDDDGPRA GVQCQTA
//
