DJC10_RAT
ID DJC10_RAT Reviewed; 793 AA.
AC Q498R3;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=DnaJ homolog subfamily C member 10;
DE EC=1.8.4.-;
DE Flags: Precursor;
GN Name=Dnajc10;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 262-793.
RC TISSUE=Spleen;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Endoplasmic reticulum disulfide reductase involved both in
CC the correct folding of proteins and degradation of misfolded proteins.
CC Required for efficient folding of proteins in the endoplasmic reticulum
CC by catalyzing the removal of non-native disulfide bonds formed during
CC the folding of proteins, such as LDLR. Also involved in endoplasmic
CC reticulum-associated degradation (ERAD) by reducing incorrect disulfide
CC bonds in misfolded glycoproteins recognized by EDEM1. Interaction with
CC HSPA5 is required its activity, not for the disulfide reductase
CC activity, but to facilitate the release of DNAJC10 from its substrate.
CC Promotes apoptotic signaling pathway in response to endoplasmic
CC reticulum stress (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with HSPA5 (via its J domain). Interacts with EDEM1
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
CC -!- DOMAIN: Thioredoxin domains 3 and 4 are the primary reductase domains.
CC {ECO:0000250}.
CC -!- DOMAIN: The thioredoxin-like regions Trxb 1 and 2 lack a redox-active
CC CXXC motif. {ECO:0000250}.
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DR EMBL; AABR03024291; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC100105; AAI00106.1; -; mRNA.
DR RefSeq; NP_001099956.2; NM_001106486.2.
DR AlphaFoldDB; Q498R3; -.
DR SMR; Q498R3; -.
DR BioGRID; 255075; 1.
DR IntAct; Q498R3; 7.
DR STRING; 10116.ENSRNOP00000009839; -.
DR GlyGen; Q498R3; 1 site.
DR iPTMnet; Q498R3; -.
DR PhosphoSitePlus; Q498R3; -.
DR jPOST; Q498R3; -.
DR PaxDb; Q498R3; -.
DR PRIDE; Q498R3; -.
DR Ensembl; ENSRNOT00000009839; ENSRNOP00000009839; ENSRNOG00000006803.
DR GeneID; 295690; -.
DR KEGG; rno:295690; -.
DR UCSC; RGD:1307813; rat.
DR CTD; 54431; -.
DR RGD; 1307813; Dnajc10.
DR eggNOG; KOG0191; Eukaryota.
DR eggNOG; KOG0713; Eukaryota.
DR GeneTree; ENSGT00940000155558; -.
DR HOGENOM; CLU_023279_0_0_1; -.
DR InParanoid; Q498R3; -.
DR OMA; APTWRKF; -.
DR OrthoDB; 522268at2759; -.
DR PhylomeDB; Q498R3; -.
DR TreeFam; TF105169; -.
DR PRO; PR:Q498R3; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000006803; Expressed in Ammon's horn and 20 other tissues.
DR Genevisible; Q498R3; RN.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0034663; C:endoplasmic reticulum chaperone complex; ISO:RGD.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB.
DR GO; GO:0001671; F:ATPase activator activity; ISO:RGD.
DR GO; GO:0051117; F:ATPase binding; ISO:RGD.
DR GO; GO:0051087; F:chaperone binding; ISO:RGD.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; ISO:RGD.
DR GO; GO:0030544; F:Hsp70 protein binding; ISO:RGD.
DR GO; GO:0051787; F:misfolded protein binding; ISO:RGD.
DR GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; ISS:UniProtKB.
DR GO; GO:0015035; F:protein-disulfide reductase activity; ISS:UniProtKB.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISO:RGD.
DR GO; GO:0036498; P:IRE1-mediated unfolded protein response; IBA:GO_Central.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; ISO:RGD.
DR GO; GO:0034975; P:protein folding in endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISO:RGD.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
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; -; 1.
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 Pfam; PF00226; DnaJ; 1.
DR Pfam; PF00085; Thioredoxin; 4.
DR PIRSF; PIRSF037293; DnaJ_homolog_subfam-C; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF52833; SSF52833; 6.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 3.
PE 2: Evidence at transcript level;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Oxidoreductase;
KW Redox-active center; Reference proteome; Repeat; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..793
FT /note="DnaJ homolog subfamily C member 10"
FT /id="PRO_0000281486"
FT DOMAIN 35..100
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT DOMAIN 130..232
FT /note="Thioredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 454..553
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 557..665
FT /note="Thioredoxin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 671..776
FT /note="Thioredoxin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 235..350
FT /note="Trxb 1"
FT REGION 348..463
FT /note="Trxb 2"
FT MOTIF 790..793
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT CARBOHYD 530
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 158..161
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 480..483
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 588..591
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 700..703
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 793 AA; 90747 MW; 9578A69C36C858C9 CRC64;
MGVWLNRDEF IRDVKRISLC LLVLYVVIVV GTDQNFYSLL GVSKTASSRE IRQAFKKLAL
KLHPDKNPNN PNAHGDFLKI NRAYEVLKDE DLRKKYDKYG EKGLEDNQGG QYESWSYYRY
DFGIYDDDPE IITLERREFD AAVNSGELWF VNFYSPGCSH CHDLAPTWRE FAKEVDGLLR
IGAVNCGDDR MLCRMKGVNS YPSLFIFRSG MAAVKYNGDR SKESLVSFAM QHVRTTVTEL
STGNFVNAIE TAFAAGIGWL ITFCFKGEDC LTPQTRLRLS GMLDGLVNVG WVDCDTQDSL
CKSLDATAST TAYFPPGATL NNKEKSSVLF LNSLDAKEIY MEIIHNLPDF ELLSANKLED
RLAHHRWLVF FHFGKNENAN DPELKKLKTL LKNEHIQVGR FDCSSAPGIC SDLYVFQSCL
AVFKGQGTKE YEIHHGKKIL YDILAFAKES VNSHVTTLGP QNFPASDKEP WLVDFFAPWC
PPCRALLPEL RKASTLLYGQ LKVGTLDCTI HEGLCNMYNI QAYPTTVVFN QSSVHEYEGH
HSAEQILEFI EDLRNPSVVS LTPTTFNELV KQRKHDEVWM VDFYSPWCHP CQVLMPEWKR
MARTLTGLIN VGSVDCQQYH SFCTQENVQR YPEIRFYPQK SSRAYQYHSY NGWNRDAYSL
RSWGLGFLPQ ASIDLTPQTF NEKVLQGKTH WVIDFYAPWC GPCQNFAPEF ELLARMIKGK
VKAGKVDCQA YPQTCQKAGI RAYPSVKLYL YERAKKSIWE EQINSRDAKT IAALIYGKLE
TFQSQVKRNK DEL
