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Protein

DnaJ homolog subfamily C member 10

Gene

DNAJC10

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Endoplasmic reticulum disulfide reductase involved both in the correct folding of proteins and degradation of misfolded proteins. Required for efficient folding of proteins in the endoplasmic reticulum by catalyzing the removal of non-native disulfide bonds formed during the folding of proteins, such as LDLR. Also involved in endoplasmic reticulum-associated degradation (ERAD) by reducing incorrect disulfide bonds in misfolded glycoproteins recognized by EDEM1. Interaction with HSPA5 is required its activity, not for the disulfide reductase activity, but to facilitate the release of DNAJC10 from its substrate. Promotes apoptotic signaling pathway in response to endoplasmic reticulum stress (By similarity).By similarity

GO - Molecular functioni

  1. oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor Source: UniProtKB
  2. protein disulfide oxidoreductase activity Source: UniProtKB

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
  3. protein folding in endoplasmic reticulum Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Names & Taxonomyi

Protein namesi
Recommended name:
DnaJ homolog subfamily C member 10 (EC:1.8.4.-)
Gene namesi
Name:DNAJC10
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
ProteomesiUP000001595 Componenti: Unplaced

Subcellular locationi

Endoplasmic reticulum lumen PROSITE-ProRule annotation

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3232Sequence AnalysisAdd
BLAST
Chaini33 – 793761DnaJ homolog subfamily C member 10PRO_0000281485Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi158 ↔ 161Redox-activePROSITE-ProRule annotation
Disulfide bondi480 ↔ 483Redox-activePROSITE-ProRule annotation
Glycosylationi530 – 5301N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi588 ↔ 591Redox-activePROSITE-ProRule annotation
Disulfide bondi700 ↔ 703Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Interacts with HSPA5 (via its J domain). Interacts with EDEM1 (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ5R5L3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini35 – 10066JPROSITE-ProRule annotationAdd
BLAST
Domaini130 – 232103Thioredoxin 1PROSITE-ProRule annotationAdd
BLAST
Domaini454 – 553100Thioredoxin 2PROSITE-ProRule annotationAdd
BLAST
Domaini557 – 662106Thioredoxin 3PROSITE-ProRule annotationAdd
BLAST
Domaini671 – 778108Thioredoxin 4PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni235 – 350116Trxb 1Add
BLAST
Regioni348 – 463116Trxb 2Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi790 – 7934Prevents secretion from ERPROSITE-ProRule annotation

Domaini

Thioredoxin domains 3 and 4 are the primary reductase domains.By similarity
The thioredoxin-like regions Trxb 1 and 2 lack a redox-active CXXC motif.By similarity

Sequence similaritiesi

Contains 1 J domain.PROSITE-ProRule annotation
Contains 4 thioredoxin domains.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center, Repeat, Signal

Phylogenomic databases

HOVERGENiHBG057048.
InParanoidiQ5R5L3.
KOiK09530.

Family and domain databases

Gene3Di1.10.287.110. 1 hit.
3.40.30.10. 5 hits.
InterProiIPR001623. DnaJ_domain.
IPR021170. ERdj5.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00226. DnaJ. 1 hit.
PF00085. Thioredoxin. 4 hits.
[Graphical view]
PIRSFiPIRSF037293. DnaJ_homolog_subfam-C. 1 hit.
PRINTSiPR00625. JDOMAIN.
SMARTiSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
SSF52833. SSF52833. 6 hits.
PROSITEiPS50076. DNAJ_2. 1 hit.
PS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5R5L3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGVWLSKDDY IRDLKRIILC FLIVYMAILV GTEQDFYSLL GVSKTASSRE
60 70 80 90 100
IRQAFKKLAL KLHPDKNPNN PNAHGNFLKI NRAYEVLKDE DLRKKYDKYG
110 120 130 140 150
EKGLEDNQGG QYESWNYYRY DFGIYDDDPE IITLERREFD AAVNSGELWF
160 170 180 190 200
VNFYSPGCSH CHDLAPTWRD FAKEVDGLLR IGAVNCGDDR MLCRMKGVNS
210 220 230 240 250
YPSLFIFRSG MAPVKYHGDR SKESLVSFAM QHVRSTVTEL WTGNFVNSIQ
260 270 280 290 300
TAFAAGIGWL ITFCSKGGDC LTSQTRLRLS GMLDGLVNVG WMDCATQDNL
310 320 330 340 350
CKSLDITTST TAYFPPGATL NNKEKNSILF LNSLDAKEIY LEVIHNLPDF
360 370 380 390 400
ELLSAHTLED RLAHHRWLLF FHFGKNENSN DPELKKLKTL LKNDHIQVGR
410 420 430 440 450
FDCSSAPDIC SNLYVFQPSL AVFKGQGTKE YEIHHGKKIL YDILAFAKES
460 470 480 490 500
VNSHVTTLGP QNFPANDKEP WLVDFFAPWC PPCRALLPEL RRASNLLYGQ
510 520 530 540 550
LKFGTLDCTV HEGLCNMYNI QAYPTTVVFN QSNIHEYEGH HSAEQILEFI
560 570 580 590 600
EDLMNPSVVS LTPTTFNELV TQRKHNEVWM VDFYSPWCHP CQVLMPEWKR
610 620 630 640 650
MARTLTGLIN VGSIDCQQYH SFCAQENVQR YPEIRFFPPK SNKAYQYHSY
660 670 680 690 700
NGWNRDAYSL RIWGLGFLPQ VSTGLTPQTF SEKVLQGKNH WVIDFYAPWC
710 720 730 740 750
GPCQNFAPEF ELLARMIKGK VKAGKVDCQA YAQTCQKAGI RAYPTVKFYF
760 770 780 790
YESAKRTFQE EQINIRDAKA IAALINEKLE TLQNQGKRNK DEL
Length:793
Mass (Da):90,951
Last modified:December 20, 2004 - v1
Checksum:iFADC1167FC65121E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR860844 mRNA. Translation: CAH92953.1.
RefSeqiNP_001126740.1. NM_001133268.1.
UniGeneiPab.5348.

Genome annotation databases

GeneIDi100173742.
KEGGipon:100173742.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR860844 mRNA. Translation: CAH92953.1.
RefSeqiNP_001126740.1. NM_001133268.1.
UniGeneiPab.5348.

3D structure databases

ProteinModelPortaliQ5R5L3.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100173742.
KEGGipon:100173742.

Organism-specific databases

CTDi54431.

Phylogenomic databases

HOVERGENiHBG057048.
InParanoidiQ5R5L3.
KOiK09530.

Family and domain databases

Gene3Di1.10.287.110. 1 hit.
3.40.30.10. 5 hits.
InterProiIPR001623. DnaJ_domain.
IPR021170. ERdj5.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00226. DnaJ. 1 hit.
PF00085. Thioredoxin. 4 hits.
[Graphical view]
PIRSFiPIRSF037293. DnaJ_homolog_subfam-C. 1 hit.
PRINTSiPR00625. JDOMAIN.
SMARTiSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
SSF52833. SSF52833. 6 hits.
PROSITEiPS50076. DNAJ_2. 1 hit.
PS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. The German cDNA consortium
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.

Entry informationi

Entry nameiDJC10_PONAB
AccessioniPrimary (citable) accession number: Q5R5L3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 19, 2007
Last sequence update: December 20, 2004
Last modified: March 31, 2015
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.