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Q5R5L3

- DJC10_PONAB

UniProt

Q5R5L3 - DJC10_PONAB

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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: 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.

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: Unplaced

Subcellular locationi

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 – 3232 Reviewed predictionAdd
BLAST
Chaini33 – 793761DnaJ homolog subfamily C member 10PRO_0000281485Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi158 ↔ 161Redox-active By similarity
Disulfide bondi480 ↔ 483Redox-active By similarity
Glycosylationi530 – 5301N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi588 ↔ 591Redox-active By similarity
Disulfide bondi700 ↔ 703Redox-active By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliQ5R5L3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini35 – 10066JAdd
BLAST
Domaini130 – 232103Thioredoxin 1Add
BLAST
Domaini454 – 553100Thioredoxin 2Add
BLAST
Domaini557 – 662106Thioredoxin 3Add
BLAST
Domaini671 – 778108Thioredoxin 4Add
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 ER Reviewed prediction

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.
Contains 4 thioredoxin domains.

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. DnaJ_homolog_subfam-C.
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

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MGVWLSKDDY IRDLKRIILC FLIVYMAILV GTEQDFYSLL GVSKTASSRE    50
IRQAFKKLAL KLHPDKNPNN PNAHGNFLKI NRAYEVLKDE DLRKKYDKYG 100
EKGLEDNQGG QYESWNYYRY DFGIYDDDPE IITLERREFD AAVNSGELWF 150
VNFYSPGCSH CHDLAPTWRD FAKEVDGLLR IGAVNCGDDR MLCRMKGVNS 200
YPSLFIFRSG MAPVKYHGDR SKESLVSFAM QHVRSTVTEL WTGNFVNSIQ 250
TAFAAGIGWL ITFCSKGGDC LTSQTRLRLS GMLDGLVNVG WMDCATQDNL 300
CKSLDITTST TAYFPPGATL NNKEKNSILF LNSLDAKEIY LEVIHNLPDF 350
ELLSAHTLED RLAHHRWLLF FHFGKNENSN DPELKKLKTL LKNDHIQVGR 400
FDCSSAPDIC SNLYVFQPSL AVFKGQGTKE YEIHHGKKIL YDILAFAKES 450
VNSHVTTLGP QNFPANDKEP WLVDFFAPWC PPCRALLPEL RRASNLLYGQ 500
LKFGTLDCTV HEGLCNMYNI QAYPTTVVFN QSNIHEYEGH HSAEQILEFI 550
EDLMNPSVVS LTPTTFNELV TQRKHNEVWM VDFYSPWCHP CQVLMPEWKR 600
MARTLTGLIN VGSIDCQQYH SFCAQENVQR YPEIRFFPPK SNKAYQYHSY 650
NGWNRDAYSL RIWGLGFLPQ VSTGLTPQTF SEKVLQGKNH WVIDFYAPWC 700
GPCQNFAPEF ELLARMIKGK VKAGKVDCQA YAQTCQKAGI RAYPTVKFYF 750
YESAKRTFQE EQINIRDAKA IAALINEKLE TLQNQGKRNK DEL 793
Length:793
Mass (Da):90,951
Last modified:December 21, 2004 - v1
Checksum:iFADC1167FC65121E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
CR860844 mRNA. Translation: CAH92953.1 .
RefSeqi NP_001126740.1. NM_001133268.1.
UniGenei Pab.5348.

3D structure databases

ProteinModelPortali Q5R5L3.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100173742.
KEGGi pon:100173742.

Organism-specific databases

CTDi 54431.

Phylogenomic databases

HOVERGENi HBG057048.
InParanoidi Q5R5L3.
KOi K09530.

Family and domain databases

Gene3Di 1.10.287.110. 1 hit.
3.40.30.10. 5 hits.
InterProi IPR001623. DnaJ_domain.
IPR021170. DnaJ_homolog_subfam-C.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view ]
Pfami PF00226. DnaJ. 1 hit.
PF00085. Thioredoxin. 4 hits.
[Graphical view ]
PIRSFi PIRSF037293. DnaJ_homolog_subfam-C. 1 hit.
PRINTSi PR00625. JDOMAIN.
SMARTi SM00271. DnaJ. 1 hit.
[Graphical view ]
SUPFAMi SSF46565. SSF46565. 1 hit.
SSF52833. SSF52833. 6 hits.
PROSITEi PS50076. DNAJ_2. 1 hit.
PS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. The German cDNA consortium
    Submitted (NOV-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 20, 2007
Last sequence update: December 21, 2004
Last modified: September 3, 2014
This is version 73 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

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