DJC10_HUMAN
ID DJC10_HUMAN Reviewed; 793 AA.
AC Q8IXB1; Q17RJ6; Q3B7W8; Q4ZG06; Q53QT7; Q6UWZ6; Q86T61; Q8NC82; Q8TD87;
AC Q96K38; Q96K44; Q96K54; Q9NSY6;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=DnaJ homolog subfamily C member 10;
DE EC=1.8.4.-;
DE AltName: Full=Endoplasmic reticulum DNA J domain-containing protein 5;
DE Short=ER-resident protein ERdj5;
DE Short=ERdj5;
DE AltName: Full=Macrothioredoxin;
DE Short=MTHr;
DE Flags: Precursor;
GN Name=DNAJC10; Synonyms=ERDJ5; ORFNames=UNQ495/PRO1012;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH HSPA5.
RX PubMed=12411443; DOI=10.1074/jbc.m206995200;
RA Cunnea P.M., Miranda-Vizuete A., Bertoli G., Simmen T., Damdimopoulos A.E.,
RA Hermann S., Leinonen S., Huikko M.P., Gustafsson J.-A., Sitia R.,
RA Spyrou G.;
RT "ERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ and
RT thioredoxin domains, is expressed in secretory cells or following ER
RT stress.";
RL J. Biol. Chem. 278:1059-1066(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT ASN-76.
RC TISSUE=Fetal brain;
RX PubMed=14587667; DOI=10.1023/a:1025510502147;
RA Gu S.-H., Chen J.-Z., Ying K., Wang S., Jin W., Qian J., Zhao E.-P.,
RA Xie Y., Mao Y.-M.;
RT "Cloning and identification of a novel cDNA which encodes a putative
RT protein with a DnaJ domain and a thioredoxin active motif, human
RT macrothioredoxin.";
RL Biochem. Genet. 41:245-253(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT GLN-646.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP GLN-646.
RC TISSUE=Colon, and Placenta;
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).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-793 (ISOFORM 1), AND VARIANTS
RP ASN-76 AND GLN-646.
RC TISSUE=Spinal cord, and Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 414-793.
RC TISSUE=Teratocarcinoma;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [10]
RP FUNCTION.
RX PubMed=18400946; DOI=10.1091/mbc.e07-07-0674;
RA Dong M., Bridges J.P., Apsley K., Xu Y., Weaver T.E.;
RT "ERdj4 and ERdj5 are required for endoplasmic reticulum-associated protein
RT degradation of misfolded surfactant protein C.";
RL Mol. Biol. Cell 19:2620-2630(2008).
RN [11]
RP FUNCTION.
RX PubMed=19122239; DOI=10.1074/jbc.m806189200;
RA Thomas C.G., Spyrou G.;
RT "ERdj5 sensitizes neuroblastoma cells to endoplasmic reticulum stress-
RT induced apoptosis.";
RL J. Biol. Chem. 284:6282-6290(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HSPA5, AND MUTAGENESIS OF
RP HIS-63; CYS-161; CYS-483; CYS-591 AND CYS-703.
RX PubMed=23769672; DOI=10.1016/j.molcel.2013.05.014;
RA Oka O.B., Pringle M.A., Schopp I.M., Braakman I., Bulleid N.J.;
RT "ERdj5 is the ER reductase that catalyzes the removal of non-native
RT disulfides and correct folding of the LDL receptor.";
RL Mol. Cell 50:793-804(2013).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
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. {ECO:0000269|PubMed:12411443,
CC ECO:0000269|PubMed:18400946, ECO:0000269|PubMed:19122239,
CC ECO:0000269|PubMed:23769672}.
CC -!- SUBUNIT: Interacts with EDEM1 (By similarity). Interacts with HSPA5
CC (via its J domain). {ECO:0000250, ECO:0000269|PubMed:12411443,
CC ECO:0000269|PubMed:23769672}.
CC -!- INTERACTION:
CC Q8IXB1; Q8IWF2: FOXRED2; NbExp=2; IntAct=EBI-2949763, EBI-10763361;
CC Q8IXB1-2; P43364-2: MAGEA11; NbExp=3; IntAct=EBI-10262451, EBI-10178634;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138, ECO:0000269|PubMed:12411443,
CC ECO:0000269|PubMed:23769672}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8IXB1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IXB1-2; Sequence=VSP_024011;
CC Name=3;
CC IsoId=Q8IXB1-3; Sequence=VSP_054434, VSP_054435;
CC -!- INDUCTION: By endoplasmic reticulum stress.
CC -!- DOMAIN: The thioredoxin-like regions Trxb 1 and 2 lack a redox-active
CC CXXC motif. {ECO:0000250}.
CC -!- DOMAIN: Thioredoxin domains 3 and 4 are the primary reductase domains.
CC {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB55121.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC11281.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF038503; AAN73271.1; -; mRNA.
DR EMBL; AF490904; AAM09527.1; -; mRNA.
DR EMBL; AY358577; AAQ88940.1; -; mRNA.
DR EMBL; AK027450; BAB55121.1; ALT_INIT; mRNA.
DR EMBL; AK027647; BAB55263.1; -; mRNA.
DR EMBL; AK027696; BAB55304.1; -; mRNA.
DR EMBL; AC073951; AAX88931.1; -; Genomic_DNA.
DR EMBL; AC105396; AAY24240.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX10960.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX10963.1; -; Genomic_DNA.
DR EMBL; BC107425; AAI07426.1; -; mRNA.
DR EMBL; BC117299; AAI17300.1; -; mRNA.
DR EMBL; BC126168; AAI26169.1; -; mRNA.
DR EMBL; AL137648; CAB70858.1; -; mRNA.
DR EMBL; AL832646; CAD89982.1; -; mRNA.
DR EMBL; AK074905; BAC11281.1; ALT_INIT; mRNA.
DR CCDS; CCDS33345.1; -. [Q8IXB1-1]
DR CCDS; CCDS74613.1; -. [Q8IXB1-2]
DR PIR; T46333; T46333.
DR RefSeq; NP_001258510.1; NM_001271581.1. [Q8IXB1-2]
DR RefSeq; NP_061854.1; NM_018981.2. [Q8IXB1-1]
DR AlphaFoldDB; Q8IXB1; -.
DR SMR; Q8IXB1; -.
DR BioGRID; 119947; 197.
DR DIP; DIP-48947N; -.
DR IntAct; Q8IXB1; 73.
DR MINT; Q8IXB1; -.
DR STRING; 9606.ENSP00000264065; -.
DR GlyGen; Q8IXB1; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q8IXB1; -.
DR PhosphoSitePlus; Q8IXB1; -.
DR SwissPalm; Q8IXB1; -.
DR BioMuta; DNAJC10; -.
DR DMDM; 142981524; -.
DR EPD; Q8IXB1; -.
DR jPOST; Q8IXB1; -.
DR MassIVE; Q8IXB1; -.
DR MaxQB; Q8IXB1; -.
DR PaxDb; Q8IXB1; -.
DR PeptideAtlas; Q8IXB1; -.
DR PRIDE; Q8IXB1; -.
DR ProteomicsDB; 61664; -.
DR ProteomicsDB; 70980; -. [Q8IXB1-1]
DR ProteomicsDB; 70981; -. [Q8IXB1-2]
DR Antibodypedia; 33990; 232 antibodies from 29 providers.
DR DNASU; 54431; -.
DR Ensembl; ENST00000264065.12; ENSP00000264065.6; ENSG00000077232.19. [Q8IXB1-1]
DR Ensembl; ENST00000537515.5; ENSP00000441560.1; ENSG00000077232.19. [Q8IXB1-3]
DR Ensembl; ENST00000616986.5; ENSP00000479930.1; ENSG00000077232.19. [Q8IXB1-2]
DR Ensembl; ENST00000680480.1; ENSP00000505358.1; ENSG00000077232.19. [Q8IXB1-3]
DR GeneID; 54431; -.
DR KEGG; hsa:54431; -.
DR MANE-Select; ENST00000264065.12; ENSP00000264065.6; NM_018981.4; NP_061854.1.
DR UCSC; uc002uow.3; human. [Q8IXB1-1]
DR CTD; 54431; -.
DR DisGeNET; 54431; -.
DR GeneCards; DNAJC10; -.
DR HGNC; HGNC:24637; DNAJC10.
DR HPA; ENSG00000077232; Tissue enhanced (epididymis).
DR MIM; 607987; gene.
DR neXtProt; NX_Q8IXB1; -.
DR OpenTargets; ENSG00000077232; -.
DR PharmGKB; PA134917195; -.
DR VEuPathDB; HostDB:ENSG00000077232; -.
DR eggNOG; KOG0191; Eukaryota.
DR eggNOG; KOG0713; Eukaryota.
DR GeneTree; ENSGT00940000155558; -.
DR HOGENOM; CLU_023279_0_0_1; -.
DR InParanoid; Q8IXB1; -.
DR OMA; APTWRKF; -.
DR OrthoDB; 522268at2759; -.
DR PhylomeDB; Q8IXB1; -.
DR TreeFam; TF105169; -.
DR PathwayCommons; Q8IXB1; -.
DR SignaLink; Q8IXB1; -.
DR BioGRID-ORCS; 54431; 12 hits in 1078 CRISPR screens.
DR ChiTaRS; DNAJC10; human.
DR GeneWiki; DNAJC10; -.
DR GenomeRNAi; 54431; -.
DR Pharos; Q8IXB1; Tbio.
DR PRO; PR:Q8IXB1; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8IXB1; protein.
DR Bgee; ENSG00000077232; Expressed in corpus epididymis and 196 other tissues.
DR ExpressionAtlas; Q8IXB1; baseline and differential.
DR Genevisible; Q8IXB1; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0034663; C:endoplasmic reticulum chaperone complex; IDA:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0001671; F:ATPase activator activity; ISS:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; IPI:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; IDA:UniProtKB.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; ISS:UniProtKB.
DR GO; GO:0030544; F:Hsp70 protein binding; IPI:UniProtKB.
DR GO; GO:0051787; F:misfolded protein binding; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IDA:UniProtKB.
DR GO; GO:0036498; P:IRE1-mediated unfolded protein response; IBA:GO_Central.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; ISS:UniProtKB.
DR GO; GO:0034975; P:protein folding in endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:UniProtKB.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP: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 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Oxidoreductase; 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_0000281483"
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..662
FT /note="Thioredoxin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 671..778
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 DISULFID 480..483
FT /note="Redox-active"
FT DISULFID 588..591
FT /note="Redox-active"
FT DISULFID 700..703
FT /note="Redox-active"
FT VAR_SEQ 284..329
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309,
FT ECO:0000303|PubMed:14587667"
FT /id="VSP_024011"
FT VAR_SEQ 330..332
FT /note="FLN -> LLH (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054434"
FT VAR_SEQ 333..793
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054435"
FT VARIANT 76
FT /note="D -> N (in dbSNP:rs6729801)"
FT /evidence="ECO:0000269|PubMed:14587667,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_031247"
FT VARIANT 347
FT /note="L -> I (in dbSNP:rs13414223)"
FT /id="VAR_048912"
FT VARIANT 414
FT /note="Y -> C (in dbSNP:rs11681366)"
FT /id="VAR_031248"
FT VARIANT 646
FT /note="H -> Q (in dbSNP:rs288334)"
FT /evidence="ECO:0000269|PubMed:12975309,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005"
FT /id="VAR_031249"
FT MUTAGEN 63
FT /note="H->Q: Prevents interaction with HSPA5, leading to
FT prolonged interaction with substrate proteins."
FT /evidence="ECO:0000269|PubMed:23769672"
FT MUTAGEN 161
FT /note="C->A: Abolishes disulfide reductase activity; when
FT associated with A-483; A-591 and A-703."
FT /evidence="ECO:0000269|PubMed:23769672"
FT MUTAGEN 483
FT /note="C->A: Abolishes disulfide reductase activity; when
FT associated with A-161; A-591 and A-703."
FT /evidence="ECO:0000269|PubMed:23769672"
FT MUTAGEN 591
FT /note="C->A: Abolishes disulfide reductase activity; when
FT associated with A-161; A-483 and A-703."
FT /evidence="ECO:0000269|PubMed:23769672"
FT MUTAGEN 703
FT /note="C->A: Abolishes disulfide reductase activity; when
FT associated with A-161; A-483 and A-591."
FT /evidence="ECO:0000269|PubMed:23769672"
FT CONFLICT 5
FT /note="L -> S (in Ref. 2; AAM09527 and 4; BAB55304)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="P -> A (in Ref. 1; AAN73271)"
FT /evidence="ECO:0000305"
FT CONFLICT 356..359
FT /note="NTLE -> KRVK (in Ref. 1; AAN73271)"
FT /evidence="ECO:0000305"
FT CONFLICT 446
FT /note="F -> S (in Ref. 4; BAB55121)"
FT /evidence="ECO:0000305"
FT CONFLICT 565
FT /note="T -> A (in Ref. 8; CAD89982)"
FT /evidence="ECO:0000305"
FT CONFLICT 633
FT /note="E -> K (in Ref. 8; CAB70858)"
FT /evidence="ECO:0000305"
FT CONFLICT 755
FT /note="K -> N (in Ref. 4; BAB55304)"
FT /evidence="ECO:0000305"
FT CONFLICT 771
FT /note="I -> T (in Ref. 8; CAD89982)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 793 AA; 91080 MW; BD39B64325432D5D CRC64;
MGVWLNKDDY IRDLKRIILC FLIVYMAILV GTDQDFYSLL GVSKTASSRE IRQAFKKLAL
KLHPDKNPNN PNAHGDFLKI NRAYEVLKDE DLRKKYDKYG EKGLEDNQGG QYESWNYYRY
DFGIYDDDPE IITLERREFD AAVNSGELWF VNFYSPGCSH CHDLAPTWRD FAKEVDGLLR
IGAVNCGDDR MLCRMKGVNS YPSLFIFRSG MAPVKYHGDR SKESLVSFAM QHVRSTVTEL
WTGNFVNSIQ TAFAAGIGWL ITFCSKGGDC LTSQTRLRLS GMLDGLVNVG WMDCATQDNL
CKSLDITTST TAYFPPGATL NNKEKNSILF LNSLDAKEIY LEVIHNLPDF ELLSANTLED
RLAHHRWLLF FHFGKNENSN DPELKKLKTL LKNDHIQVGR FDCSSAPDIC SNLYVFQPSL
AVFKGQGTKE YEIHHGKKIL YDILAFAKES VNSHVTTLGP QNFPANDKEP WLVDFFAPWC
PPCRALLPEL RRASNLLYGQ LKFGTLDCTV HEGLCNMYNI QAYPTTVVFN QSNIHEYEGH
HSAEQILEFI EDLMNPSVVS LTPTTFNELV TQRKHNEVWM VDFYSPWCHP CQVLMPEWKR
MARTLTGLIN VGSIDCQQYH SFCAQENVQR YPEIRFFPPK SNKAYHYHSY NGWNRDAYSL
RIWGLGFLPQ VSTDLTPQTF SEKVLQGKNH WVIDFYAPWC GPCQNFAPEF ELLARMIKGK
VKAGKVDCQA YAQTCQKAGI RAYPTVKFYF YERAKRNFQE EQINTRDAKA IAALISEKLE
TLRNQGKRNK DEL
