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   24-JAN-2024, entry version 130.
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   GlyCosmos; Q498R3; 1 site, No reported glycans.
DR   GlyGen; Q498R3; 1 site.
DR   iPTMnet; Q498R3; -.
DR   PhosphoSitePlus; Q498R3; -.
DR   jPOST; Q498R3; -.
DR   PaxDb; 10116-ENSRNOP00000009839; -.
DR   Ensembl; ENSRNOT00000009839.5; ENSRNOP00000009839.4; ENSRNOG00000006803.6.
DR   Ensembl; ENSRNOT00055037024; ENSRNOP00055030112; ENSRNOG00055021622.
DR   Ensembl; ENSRNOT00060025600; ENSRNOP00060020427; ENSRNOG00060014939.
DR   GeneID; 295690; -.
DR   KEGG; rno:295690; -.
DR   UCSC; RGD:1307813; rat.
DR   AGR; RGD:1307813; -.
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; 52245at2759; -.
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 cell types or tissues.
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: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:0051087; F:protein-folding chaperone binding; ISO:RGD.
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: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; 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   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; PS00014; ER_TARGET; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 2.
DR   PROSITE; PS51352; THIOREDOXIN_2; 3.
DR   Genevisible; Q498R3; RN.
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
//