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Database: UniProt
Entry: H0ZH31_TAEGU
LinkDB: H0ZH31_TAEGU
Original site: H0ZH31_TAEGU 
ID   H0ZH31_TAEGU            Unreviewed;       797 AA.
AC   H0ZH31;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 2.
DT   24-JAN-2024, entry version 73.
DE   RecName: Full=DnaJ homolog subfamily C member 10 {ECO:0000256|ARBA:ARBA00020920};
GN   Name=DNAJC10 {ECO:0000313|Ensembl:ENSTGUP00000009895.2};
OS   Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC   Estrildinae; Taeniopygia.
OX   NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000009895.2, ECO:0000313|Proteomes:UP000007754};
RN   [1] {ECO:0000313|Ensembl:ENSTGUP00000009895.2, ECO:0000313|Proteomes:UP000007754}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20360741; DOI=10.1038/nature08819;
RA   Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA   Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA   Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA   Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA   Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA   Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA   Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA   McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA   Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA   Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA   Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA   Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA   Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA   Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT   "The genome of a songbird.";
RL   Nature 464:757-762(2010).
RN   [2] {ECO:0000313|Ensembl:ENSTGUP00000009895.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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DR   AlphaFoldDB; H0ZH31; -.
DR   STRING; 59729.ENSTGUP00000009895; -.
DR   Ensembl; ENSTGUT00000010002.2; ENSTGUP00000009895.2; ENSTGUG00000009565.2.
DR   GeneTree; ENSGT00940000155558; -.
DR   HOGENOM; CLU_023279_0_0_1; -.
DR   InParanoid; H0ZH31; -.
DR   OMA; APTWRKF; -.
DR   OrthoDB; 52245at2759; -.
DR   TreeFam; TF105169; -.
DR   Proteomes; UP000007754; Chromosome 7.
DR   GO; GO:0034663; C:endoplasmic reticulum chaperone complex; IEA:Ensembl.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:Ensembl.
DR   GO; GO:0001671; F:ATPase activator activity; IEA:Ensembl.
DR   GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
DR   GO; GO:0030544; F:Hsp70 protein binding; IEA:Ensembl.
DR   GO; GO:0051787; F:misfolded protein binding; IEA:Ensembl.
DR   GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IEA:Ensembl.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IEA:Ensembl.
DR   GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IEA:Ensembl.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
DR   GO; GO:0034975; P:protein folding in endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:Ensembl.
DR   CDD; cd06257; DnaJ; 1.
DR   CDD; cd03004; PDI_a_ERdj5_C; 3.
DR   CDD; cd03003; PDI_a_ERdj5_N; 1.
DR   Gene3D; 1.10.287.110; DnaJ domain; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 6.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR021170; ERdj5.
DR   InterPro; IPR035674; ERdj5_TRX_C.
DR   InterPro; IPR035673; ERdj5_TRX_N.
DR   InterPro; IPR036869; J_dom_sf.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR44340; DNAJ HOMOLOG SUBFAMILY C MEMBER 10; 1.
DR   PANTHER; PTHR44340:SF1; DNAJ HOMOLOG SUBFAMILY C MEMBER 10; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF00085; Thioredoxin; 4.
DR   PIRSF; PIRSF037293; DnaJ_homolog_subfam-C; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; Chaperone J-domain; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 6.
DR   PROSITE; PS50076; DNAJ_2; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 3.
DR   PROSITE; PS51352; THIOREDOXIN_2; 4.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR037293-1};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007754};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          34..99
FT                   /note="J"
FT                   /evidence="ECO:0000259|PROSITE:PS50076"
FT   DOMAIN          120..234
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          437..555
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          556..652
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          659..780
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   COILED          765..792
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   DISULFID        158..161
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037293-1"
FT   DISULFID        480..483
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037293-1"
FT   DISULFID        588..591
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037293-1"
FT   DISULFID        700..703
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037293-1"
SQ   SEQUENCE   797 AA;  91438 MW;  01582B414942ED34 CRC64;
     MEFLASKGDC TRYFKRSLLL VLVCVIVLVC TDQDYYSLLG VSKEASSREI RQAFKKLALK
     LHPDKNQNDP NAHENFLKIN RAYEVLKDED LRKKYDKYGE KGLEDQQQGG RYESWHFYRY
     DFGIYDDDPE ILTLDRGEFD AAVNSGELWF VNFYSPRCSH CHDLAPTWRE FAKELDGVIR
     IGAVNCGDNR MLCRIKGINS YPSLYVFKTG MQPVKYYGDR SKESLKNFAM QYVTSRVTEL
     WAGNFVNAIE TSFASGIGWL ITFCAERGDC LSYQTRLKLA GMLEGLVNVG WMDCGTQGEL
     CDNLDVSSST TAYFPPGATI NNKEKGGVLF LNSLDAREIY QEVMQHLPDF EIISATSLED
     RLAHHRWLLF FQFGEGDKSN VQEFKKLKFL LKDEHIQVGK FDCLSSPTIC NKLYVYQPCL
     AVFKGKGTGD YEIHHGKKIL YDIVAFAKES VNSHVITLGP QNFPDKDKEP WLVDFFAPWC
     PPCRALLPEL RKASKHLYGQ LKFGTLDCTV HEGLCNMHNI RAYPTTVVFN QSDVHEYEGH
     HSAEQILEFI EDLRNPSVVS LTPETFAELV QRRKREEIWM VDFYAPWCGP CQALMPEWKK
     MARMLNGLIS VGSVDCQKYY SFCHQESVRG YPEIRLFPQK SNTAYQYYSY NGWHRDAYSL
     RGWALGYLPQ VSVDLTPHSF TEKVLNGKDH WVIDFYAPWC GPCQNFAPEF EMLARAVKGK
     VKAGKVDCQA YGQTCQTADI RAYPTVKFYP YQGTKKSVLG EYIDSRDAKG IADLLNEKLE
     AMENKGKRKK SRSKDEL
//
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