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
//