DJC14_BOVIN
ID DJC14_BOVIN Reviewed; 699 AA.
AC Q95J56; B0JYR1;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=DnaJ homolog subfamily C member 14;
DE AltName: Full=J domain protein interacting with viral protein;
DE Short=Jiv;
GN Name=DNAJC14;
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 [MRNA], SUBCELLULAR LOCATION, AND INTERACTION WITH
RP PESTIVIRUS NS2.
RX PubMed=11533209; DOI=10.1128/jvi.75.19.9470-9482.2001;
RA Rinck G., Birghan C., Harada T., Meyers G., Thiel H.-J., Tautz N.;
RT "A cellular J-domain protein modulates polyprotein processing and
RT cytopathogenicity of a pestivirus.";
RL J. Virol. 75:9470-9482(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulates the export of target proteins, such as DRD1, from
CC the endoplasmic reticulum to the cell surface (By similarity). Promotes
CC cleavage of pestivirus polyprotein. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the FxxxFxxxF motif of DRD1 via its C-terminal
CC domain (By similarity). Interacts with pestivirus nonstructural protein
CC NS2. {ECO:0000250, ECO:0000269|PubMed:11533209}.
CC -!- INTERACTION:
CC Q95J56; PRO_0000038031 [P19711]; Xeno; NbExp=2; IntAct=EBI-9612178, EBI-9612504;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11533209}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11533209}.
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; AY027881; AAK28650.1; -; mRNA.
DR EMBL; AY027882; AAK28651.1; -; mRNA.
DR EMBL; BT025444; ABF57400.1; -; mRNA.
DR EMBL; BC151599; AAI51600.1; -; mRNA.
DR RefSeq; NP_776699.1; NM_174274.1.
DR AlphaFoldDB; Q95J56; -.
DR SMR; Q95J56; -.
DR IntAct; Q95J56; 1.
DR STRING; 9913.ENSBTAP00000027541; -.
DR PaxDb; Q95J56; -.
DR Ensembl; ENSBTAT00000027541; ENSBTAP00000027541; ENSBTAG00000020664.
DR GeneID; 281691; -.
DR KEGG; bta:281691; -.
DR CTD; 85406; -.
DR VEuPathDB; HostDB:ENSBTAG00000020664; -.
DR eggNOG; KOG0720; Eukaryota.
DR GeneTree; ENSGT00940000155637; -.
DR HOGENOM; CLU_020746_0_0_1; -.
DR InParanoid; Q95J56; -.
DR OMA; VQRGWLE; -.
DR OrthoDB; 1434217at2759; -.
DR TreeFam; TF105173; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000020664; Expressed in granulosa cell and 103 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0050780; F:dopamine receptor binding; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR032843; Jiv.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF14901; Jiv90; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 1: Evidence at protein level;
KW Chaperone; Endoplasmic reticulum; Host-virus interaction; Membrane;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..699
FT /note="DnaJ homolog subfamily C member 14"
FT /id="PRO_0000247492"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 444..508
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 1..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..85
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..699
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 699 AA; 78178 MW; 370F62297595F516 CRC64;
MAQKHPGEGG LCGAHHSGGA SLRTLGPSVD PDILSFSGLR DSAGSAPNGT RCLTEHSSPK
YTQPPNPAHW SDPSHGPPRG PGPPLAEEDP DQSEASSEES GVDQELSREN ETGYQDDGNS
SFLSIPSTCN CQGTPGIPEG PYSEGRDSSS SNFCHHCTSP ALGEDEELEG EYDEEEPLKF
PSDVSRVPSE KKPAPRRQRH RVPAKEDTRE GGRRDPRSPG RHRLGRKRSQ ADKRRGLGLW
GAEELCQLGQ AGFWWLIELL VLVGEYVETC GHLIYACRQL KGSDLDLLRV WVGVWAGRLR
GWAQVMFQFL SQGFCYGAGL FTRFLRLVGA LLLLALALLL GCLQLGWRFL VGLSDRLGWR
DKATWIFSWL ASPTWQRCLI LLRESRPWQQ LVRIVQWGWL ELPWVKQRTN RQANAPVAGG
RYCQPEEEVA RLLTMAGVPE DELNPFHVLG VEATASDVEL KKAYRQLAVM VHPDKNHHPR
AEEAFKVLRA AWDIVSNPER RKEYEMKRMA ENELSRSVNE FLSKLQEAMN TMMCSRCQGK
HRRFEMDREP KSARYCAECN RLHPAEEGDF WAESSMLGLK ITYFALMDGK VYDITEWAGC
QRVGISPDTH RVPYHISFGS RMPGTSGRQR ATPDAPPADL QDFLSRIFQV PPGQMSNGNF
FAAPQPGPGA TAASKPNSTV PKGEAKPKRR KKVRRPFQR
