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 28-JAN-2026, entry version 186. DE RecName: Full=Endoplasmic reticulum disulfide reductase DNAJC10 {ECO:0000305|PubMed:23769672}; DE EC=1.8.4.2 {ECO:0000269|PubMed:23769672, ECO:0000269|PubMed:37739037}; DE AltName: Full=DnaJ homolog subfamily C member 10 {ECO:0000312|HGNC:HGNC:24637}; DE AltName: Full=Endoplasmic reticulum DNA J domain-containing protein 5 {ECO:0000305|PubMed:12411443}; DE Short=ER-resident protein ERdj5 {ECO:0000305|PubMed:12411443}; DE AltName: Full=Macrothioredoxin {ECO:0000303|PubMed:14587667}; DE Short=MTHr {ECO:0000303|PubMed:14587667}; DE Flags: Precursor; GN Name=DNAJC10 {ECO:0000312|HGNC:HGNC:24637}; GN Synonyms=ERDJ5 {ECO:0000303|PubMed:12411443}; 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, RP INTERACTION WITH HSPA5, AND INDUCTION. 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, CATALYTIC ACTIVITY, INTERACTION WITH HSPA5, SUBCELLULAR LOCATION, RP DOMAIN, MUTAGENESIS OF HIS-63; CYS-161; CYS-483; CYS-591 AND CYS-703, AND RP MOTIF. 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). RN [15] RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH HSPA5, AND DOMAIN. RX PubMed=37739037; DOI=10.1016/j.jbc.2023.105274; RA Cai X., Ito S., Noi K., Inoue M., Ushioda R., Kato Y., Nagata K., Inaba K.; RT "Mechanistic characterization of disulfide bond reduction of an ERAD RT substrate mediated by cooperation between ERdj5 and BiP."; RL J. Biol. Chem. 299:105274-105274(2023). CC -!- FUNCTION: Endoplasmic reticulum disulfide reductase that collaborates CC directly with the chaperone BIP/HSPA5 (GRP78) to maintain protein CC quality control by facilitating either the correct folding or the CC targeted degradation of misfolded proteins (PubMed:12411443, CC PubMed:23769672, PubMed:37739037). Essential for efficient maturation CC of newly synthesized polypeptides in the endoplasmic reticulum, binds CC to substrate proteins and specifically catalyzes the reduction and CC removal of improper (non-native) disulfide bonds during the folding CC process (PubMed:23769672, PubMed:37739037). In endoplasmic reticulum- CC associated degradation (ERAD), DNAJC10 reduces incorrect disulfide CC bonds specifically in misfolded glycoproteins that have been recognized CC by EDEM1, a key component of the ERAD pathway, thereby enabling their CC retrotranslocation and degradation (PubMed:18400946). Promotes CC apoptotic signaling pathway in response to endoplasmic reticulum stress CC (PubMed:19122239). {ECO:0000269|PubMed:12411443, CC ECO:0000269|PubMed:18400946, ECO:0000269|PubMed:19122239, CC ECO:0000269|PubMed:23769672, ECO:0000269|PubMed:37739037}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[protein]-disulfide + 2 glutathione = [protein]-dithiol + CC glutathione disulfide; Xref=Rhea:RHEA:21064, Rhea:RHEA-COMP:10593, CC Rhea:RHEA-COMP:10594, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.8.4.2; CC Evidence={ECO:0000305|PubMed:23769672, ECO:0000305|PubMed:37739037}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21065; CC Evidence={ECO:0000305|PubMed:23769672}; CC -!- SUBUNIT: Interacts with EDEM1 (By similarity). Interacts (via its J CC domain) with HSPA5; this interaction is required for DNAJC10 activity CC in both protein folding and degradation. While not essential for its CC intrinsic disulfide reductase activity, HSPA5 binding may facilitate CC substrate release. {ECO:0000250|UniProtKB:Q9DC23, CC ECO:0000269|PubMed:12411443, ECO:0000269|PubMed:23769672, CC ECO:0000269|PubMed:37739037}. 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 {ECO:0000269|PubMed:12411443}. CC -!- DOMAIN: The J domain and more specifically the HPD motif mediates CC interaction with HSPA5. {ECO:0000269|PubMed:23769672}. CC -!- DOMAIN: The thioredoxin-like regions Trxb 1 and 2 lack a redox-active CC CXXC motif. {ECO:0000250|UniProtKB:Q9DC23}. CC -!- DOMAIN: Thioredoxin domains 3 and 4 are the primary reductase domains. CC The thioredoxin domain 4 is the most efficient at reducing disulfide CC bonds. {ECO:0000269|PubMed:37739037}. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_001271581.3. [Q8IXB1-2] DR RefSeq; NP_061854.1; NM_018981.4. [Q8IXB1-1] DR AlphaFoldDB; Q8IXB1; -. DR SMR; Q8IXB1; -. DR BioGRID; 119947; 276. DR CORUM; Q8IXB1; -. DR DIP; DIP-48947N; -. DR FunCoup; Q8IXB1; 2640. DR IntAct; Q8IXB1; 110. DR MINT; Q8IXB1; -. DR STRING; 9606.ENSP00000264065; -. DR GlyCosmos; Q8IXB1; 1 site, No reported glycans. 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 jPOST; Q8IXB1; -. DR MassIVE; Q8IXB1; -. DR PaxDb; 9606-ENSP00000264065; -. DR PeptideAtlas; Q8IXB1; -. DR ProteomicsDB; 61664; -. DR ProteomicsDB; 70980; -. [Q8IXB1-1] DR ProteomicsDB; 70981; -. [Q8IXB1-2] DR Pumba; Q8IXB1; -. DR Antibodypedia; 33990; 227 antibodies from 29 providers. DR DNASU; 54431; -. DR Ensembl; ENST00000264065.12; ENSP00000264065.6; ENSG00000077232.20. [Q8IXB1-1] DR Ensembl; ENST00000537515.5; ENSP00000441560.1; ENSG00000077232.20. [Q8IXB1-3] DR Ensembl; ENST00000616986.5; ENSP00000479930.1; ENSG00000077232.20. [Q8IXB1-2] DR Ensembl; ENST00000680480.1; ENSP00000505358.1; ENSG00000077232.20. [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 AGR; HGNC:24637; -. DR ClinPGx; PA134917195; -. 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 OpenTargets; ENSG00000077232; -. 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; 5810603at2759; -. DR PAN-GO; Q8IXB1; 5 GO annotations based on evolutionary models. DR PhylomeDB; Q8IXB1; -. DR PathwayCommons; Q8IXB1; -. DR SignaLink; Q8IXB1; -. DR Agora; ENSG00000077232; -. DR BioGRID-ORCS; 54431; 12 hits in 1156 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 198 other cell types or tissues. DR ExpressionAtlas; Q8IXB1; baseline and differential. 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; IEA:Ensembl. DR GO; GO:0051117; F:ATPase binding; IPI: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:0051087; F:protein-folding chaperone binding; IDA:UniProtKB. DR GO; GO:0036503; P:ERAD pathway; IMP: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:0034975; P:protein folding in endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:UniProtKB. DR CDD; cd06257; DnaJ; 1. DR CDD; cd03004; PDI_a_ERdj5_C; 3. DR CDD; cd03003; PDI_a_ERdj5_N; 1. DR FunFam; 1.10.287.110:FF:000029; DnaJ homolog subfamily C member 10; 1. DR FunFam; 3.40.30.10:FF:000087; DnaJ homolog subfamily C member 10; 1. DR FunFam; 3.40.30.10:FF:000106; DnaJ homolog subfamily C member 10; 1. DR FunFam; 3.40.30.10:FF:000125; DnaJ homolog subfamily C member 10; 1. DR FunFam; 3.40.30.10:FF:000135; DnaJ homolog subfamily C member 10; 1. DR FunFam; 3.40.30.10:FF:000137; DnaJ homolog subfamily C member 10; 1. DR FunFam; 3.40.30.10:FF:000169; DnaJ homolog subfamily C member 10; 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; IPR052460; ER_disulfide_reductase. 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; 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; Proteomics identification; Redox-active center; KW Reference proteome; Repeat; Signal. FT SIGNAL 1..32 FT /evidence="ECO:0000255" FT CHAIN 33..793 FT /note="Endoplasmic reticulum disulfide reductase DNAJC10" 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 /evidence="ECO:0000305|PubMed:23769672" FT REGION 348..463 FT /note="Trxb 2" FT /evidence="ECO:0000305|PubMed:23769672" FT MOTIF 63..65 FT /note="HPD" FT /evidence="ECO:0000269|PubMed:23769672" FT MOTIF 790..793 FT /note="Prevents secretion from ER" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138, FT ECO:0000269|PubMed:23769672" FT CARBOHYD 530 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 158..161 FT /note="Redox-active" FT /evidence="ECO:0000269|PubMed:23769672" FT DISULFID 480..483 FT /note="Redox-active" FT /evidence="ECO:0000269|PubMed:23769672" FT DISULFID 588..591 FT /note="Redox-active" FT /evidence="ECO:0000269|PubMed:23769672" FT DISULFID 700..703 FT /note="Redox-active" FT /evidence="ECO:0000269|PubMed:23769672" 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 //