DJC10_XENLA
ID DJC10_XENLA Reviewed; 796 AA.
AC Q6NRT6;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=DnaJ homolog subfamily C member 10;
DE EC=1.8.4.-;
DE Flags: Precursor;
GN Name=dnajc10;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
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. Also involved in endoplasmic reticulum-
CC associated degradation (ERAD) by reducing incorrect disulfide bonds in
CC misfolded glycoproteins (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; BC070632; AAH70632.1; -; mRNA.
DR RefSeq; NP_001084933.1; NM_001091464.1.
DR AlphaFoldDB; Q6NRT6; -.
DR SMR; Q6NRT6; -.
DR DNASU; 431990; -.
DR GeneID; 431990; -.
DR KEGG; xla:431990; -.
DR CTD; 431990; -.
DR Xenbase; XB-GENE-981000; dnajc10.S.
DR OrthoDB; 522268at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR Bgee; 431990; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; ISS: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; ISS:UniProtKB.
DR GO; GO:0034975; P:protein folding in endoplasmic reticulum; ISS:UniProtKB.
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; 3.
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..33
FT /evidence="ECO:0000255"
FT CHAIN 34..796
FT /note="DnaJ homolog subfamily C member 10"
FT /id="PRO_0000281487"
FT DOMAIN 36..100
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT DOMAIN 131..233
FT /note="Thioredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 455..554
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 558..668
FT /note="Thioredoxin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 672..780
FT /note="Thioredoxin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 236..351
FT /note="Trxb 1"
FT REGION 349..464
FT /note="Trxb 2"
FT MOTIF 793..796
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT CARBOHYD 531
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 753
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 159..162
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 481..484
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 589..592
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 701..704
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 796 AA; 90984 MW; F3AB8453C8397F37 CRC64;
MKHSLNTATS SSSVLKRTIL YLVLISLAAL VYCDDDYYDL LGVSKAATNR EIRQAFKKLA
LKLHPDKNKD PDAHNKFLKI NRAYEVLKDE DLRKKYDKYG EKGLDEQNQG GGYQSWSYYR
YDFGIYDDDL EIITLDRGEF DGAVNSGELW FINFYSPGCS HCHDLAPTWR QFAKEMDGLL
RIGAVNCGDN RMLCRSQGIN SYPNLYIFKS GMNPVKYYGE RSKERLVNFA MPYISSTVTE
LWAGNFRSSI EDAFSSGVGW LITFCSDTGD CLNSQTRSKL AGLLEGLVKV GWMDCATQGD
LCDNLEITSS ATVYFPPGST LTDKENGDVL FLNSLDAREI YKEVLNHLPD LETISPESLQ
GKLSHHRWLL FFTFGTDEQS SLPEFKKLTV HLRSEHVQVG KFDCYSSPSI CSELYIHKPC
VAAFKGKGIS AYEIHHGKVQ LYDLVSFAKE SVNSHVITLG PTNFPGKDRD TWLVDFFAPW
CPPCRALLPE LRIASKRLFG QIKFGTLDCT IHEGLCNMHN IRAYPTTVVF NHSNIHEYAG
HNNAEEILEF IEDLRNPSVV TLTPETFQSL VRNRRGDEMW MVDFYAPWCG PCQALMPEWK
RMARHINGLI SVGSIDCQKY SLFCTQERVN GYPEIRLYPA NINPQHTYYR YTGWHRDSQS
LRNWALMYLP KASFDLTPES FHEHVINGKD NWVLDFYAPW CGPCQNFNPE FEILARAVKG
KIKAGKVNCQ AYEHLCNSAS IRSYPTVRLY PYNGSKKKDY FGEQIDSRDA KEIAQIITKR
IEAIKRVKEA YNKDEL
