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Q6NRT6

- DJC10_XENLA

UniProt

Q6NRT6 - DJC10_XENLA

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Protein
DnaJ homolog subfamily C member 10
Gene
dnajc10
Organism
Xenopus laevis (African clawed frog)
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. Also involved in endoplasmic reticulum-associated degradation (ERAD) by reducing incorrect disulfide bonds in misfolded glycoproteins 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. ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
  2. cell redox homeostasis Source: InterPro
  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
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-981000. dnajc10.

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 – 3333 Reviewed prediction
Add
BLAST
Chaini34 – 796763DnaJ homolog subfamily C member 10
PRO_0000281487Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi159 ↔ 162Redox-active By similarity
Disulfide bondi481 ↔ 484Redox-active By similarity
Glycosylationi531 – 5311N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi589 ↔ 592Redox-active By similarity
Disulfide bondi701 ↔ 704Redox-active By similarity
Glycosylationi753 – 7531N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ6NRT6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 10065J
Add
BLAST
Domaini131 – 233103Thioredoxin 1
Add
BLAST
Domaini455 – 554100Thioredoxin 2
Add
BLAST
Domaini558 – 668111Thioredoxin 3
Add
BLAST
Domaini672 – 780109Thioredoxin 4
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni236 – 351116Trxb 1
Add
BLAST
Regioni349 – 464116Trxb 2
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi793 – 7964Prevents 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.
KOiK09530.

Family and domain databases

Gene3Di1.10.287.110. 1 hit.
3.40.30.10. 4 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. 3 hits.
PS51352. THIOREDOXIN_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q6NRT6-1 [UniParc]FASTAAdd to Basket

« Hide

MKHSLNTATS SSSVLKRTIL YLVLISLAAL VYCDDDYYDL LGVSKAATNR    50
EIRQAFKKLA LKLHPDKNKD PDAHNKFLKI NRAYEVLKDE DLRKKYDKYG 100
EKGLDEQNQG GGYQSWSYYR YDFGIYDDDL EIITLDRGEF DGAVNSGELW 150
FINFYSPGCS HCHDLAPTWR QFAKEMDGLL RIGAVNCGDN RMLCRSQGIN 200
SYPNLYIFKS GMNPVKYYGE RSKERLVNFA MPYISSTVTE LWAGNFRSSI 250
EDAFSSGVGW LITFCSDTGD CLNSQTRSKL AGLLEGLVKV GWMDCATQGD 300
LCDNLEITSS ATVYFPPGST LTDKENGDVL FLNSLDAREI YKEVLNHLPD 350
LETISPESLQ GKLSHHRWLL FFTFGTDEQS SLPEFKKLTV HLRSEHVQVG 400
KFDCYSSPSI CSELYIHKPC VAAFKGKGIS AYEIHHGKVQ LYDLVSFAKE 450
SVNSHVITLG PTNFPGKDRD TWLVDFFAPW CPPCRALLPE LRIASKRLFG 500
QIKFGTLDCT IHEGLCNMHN IRAYPTTVVF NHSNIHEYAG HNNAEEILEF 550
IEDLRNPSVV TLTPETFQSL VRNRRGDEMW MVDFYAPWCG PCQALMPEWK 600
RMARHINGLI SVGSIDCQKY SLFCTQERVN GYPEIRLYPA NINPQHTYYR 650
YTGWHRDSQS LRNWALMYLP KASFDLTPES FHEHVINGKD NWVLDFYAPW 700
CGPCQNFNPE FEILARAVKG KIKAGKVNCQ AYEHLCNSAS IRSYPTVRLY 750
PYNGSKKKDY FGEQIDSRDA KEIAQIITKR IEAIKRVKEA YNKDEL 796
Length:796
Mass (Da):90,984
Last modified:July 5, 2004 - v1
Checksum:iF3AB8453C8397F37
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC070632 mRNA. Translation: AAH70632.1.
RefSeqiNP_001084933.1. NM_001091464.1.
UniGeneiXl.47147.

Genome annotation databases

GeneIDi431990.
KEGGixla:431990.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC070632 mRNA. Translation: AAH70632.1 .
RefSeqi NP_001084933.1. NM_001091464.1.
UniGenei Xl.47147.

3D structure databases

ProteinModelPortali Q6NRT6.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 431990.
KEGGi xla:431990.

Organism-specific databases

CTDi 54431.
Xenbasei XB-GENE-981000. dnajc10.

Phylogenomic databases

HOVERGENi HBG057048.
KOi K09530.

Family and domain databases

Gene3Di 1.10.287.110. 1 hit.
3.40.30.10. 4 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. 3 hits.
PS51352. THIOREDOXIN_2. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. NIH - Xenopus Gene Collection (XGC) project
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryo.

Entry informationi

Entry nameiDJC10_XENLA
AccessioniPrimary (citable) accession number: Q6NRT6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: July 5, 2004
Last modified: September 3, 2014
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

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi