DJC10_PONAB
ID DJC10_PONAB Reviewed; 793 AA.
AC Q5R5L3;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=DnaJ homolog subfamily C member 10;
DE EC=1.8.4.-;
DE Flags: Precursor;
GN Name=DNAJC10;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-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, 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; CR860844; CAH92953.1; -; mRNA.
DR RefSeq; NP_001126740.1; NM_001133268.1.
DR AlphaFoldDB; Q5R5L3; -.
DR SMR; Q5R5L3; -.
DR STRING; 9601.ENSPPYP00000014516; -.
DR GeneID; 100173742; -.
DR KEGG; pon:100173742; -.
DR CTD; 54431; -.
DR eggNOG; KOG0191; Eukaryota.
DR eggNOG; KOG0713; Eukaryota.
DR InParanoid; Q5R5L3; -.
DR OrthoDB; 522268at2759; -.
DR Proteomes; UP000001595; Unplaced.
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; 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_0000281485"
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 /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; 90951 MW; FADC1167FC65121E CRC64;
MGVWLSKDDY IRDLKRIILC FLIVYMAILV GTEQDFYSLL GVSKTASSRE IRQAFKKLAL
KLHPDKNPNN PNAHGNFLKI 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 ELLSAHTLED
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 SNKAYQYHSY NGWNRDAYSL
RIWGLGFLPQ VSTGLTPQTF SEKVLQGKNH WVIDFYAPWC GPCQNFAPEF ELLARMIKGK
VKAGKVDCQA YAQTCQKAGI RAYPTVKFYF YESAKRTFQE EQINIRDAKA IAALINEKLE
TLQNQGKRNK DEL
