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Protein

DnaJ homolog subfamily C member 10

Gene

dnajc10

Organism
Xenopus laevis (African clawed frog)
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. Also involved in endoplasmic reticulum-associated degradation (ERAD) by reducing incorrect disulfide bonds in misfolded glycoproteins (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

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

  • Endoplasmic reticulum lumen PROSITE-ProRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 33Sequence analysisAdd BLAST33
ChainiPRO_000028148734 – 796DnaJ homolog subfamily C member 10Add BLAST763

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi159 ↔ 162Redox-activePROSITE-ProRule annotation
Disulfide bondi481 ↔ 484Redox-activePROSITE-ProRule annotation
Glycosylationi531N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi589 ↔ 592Redox-activePROSITE-ProRule annotation
Disulfide bondi701 ↔ 704Redox-activePROSITE-ProRule annotation
Glycosylationi753N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ6NRT6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini36 – 100JPROSITE-ProRule annotationAdd BLAST65
Domaini131 – 233Thioredoxin 1PROSITE-ProRule annotationAdd BLAST103
Domaini455 – 554Thioredoxin 2PROSITE-ProRule annotationAdd BLAST100
Domaini558 – 668Thioredoxin 3PROSITE-ProRule annotationAdd BLAST111
Domaini672 – 780Thioredoxin 4PROSITE-ProRule annotationAdd BLAST109

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni236 – 351Trxb 1Add BLAST116
Regioni349 – 464Trxb 2Add BLAST116

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi793 – 796Prevents secretion from ERPROSITE-ProRule annotation4

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.
KOiK09530.

Family and domain databases

CDDicd06257. DnaJ. 1 hit.
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. 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

        10         20         30         40         50
MKHSLNTATS SSSVLKRTIL YLVLISLAAL VYCDDDYYDL LGVSKAATNR
60 70 80 90 100
EIRQAFKKLA LKLHPDKNKD PDAHNKFLKI NRAYEVLKDE DLRKKYDKYG
110 120 130 140 150
EKGLDEQNQG GGYQSWSYYR YDFGIYDDDL EIITLDRGEF DGAVNSGELW
160 170 180 190 200
FINFYSPGCS HCHDLAPTWR QFAKEMDGLL RIGAVNCGDN RMLCRSQGIN
210 220 230 240 250
SYPNLYIFKS GMNPVKYYGE RSKERLVNFA MPYISSTVTE LWAGNFRSSI
260 270 280 290 300
EDAFSSGVGW LITFCSDTGD CLNSQTRSKL AGLLEGLVKV GWMDCATQGD
310 320 330 340 350
LCDNLEITSS ATVYFPPGST LTDKENGDVL FLNSLDAREI YKEVLNHLPD
360 370 380 390 400
LETISPESLQ GKLSHHRWLL FFTFGTDEQS SLPEFKKLTV HLRSEHVQVG
410 420 430 440 450
KFDCYSSPSI CSELYIHKPC VAAFKGKGIS AYEIHHGKVQ LYDLVSFAKE
460 470 480 490 500
SVNSHVITLG PTNFPGKDRD TWLVDFFAPW CPPCRALLPE LRIASKRLFG
510 520 530 540 550
QIKFGTLDCT IHEGLCNMHN IRAYPTTVVF NHSNIHEYAG HNNAEEILEF
560 570 580 590 600
IEDLRNPSVV TLTPETFQSL VRNRRGDEMW MVDFYAPWCG PCQALMPEWK
610 620 630 640 650
RMARHINGLI SVGSIDCQKY SLFCTQERVN GYPEIRLYPA NINPQHTYYR
660 670 680 690 700
YTGWHRDSQS LRNWALMYLP KASFDLTPES FHEHVINGKD NWVLDFYAPW
710 720 730 740 750
CGPCQNFNPE FEILARAVKG KIKAGKVNCQ AYEHLCNSAS IRSYPTVRLY
760 770 780 790
PYNGSKKKDY FGEQIDSRDA KEIAQIITKR IEAIKRVKEA YNKDEL
Length:796
Mass (Da):90,984
Last modified:July 5, 2004 - v1
Checksum:iF3AB8453C8397F37
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
BC070632 mRNA. Translation: AAH70632.1.
RefSeqiNP_001084933.1. NM_001091464.1.
UniGeneiXl.47147.

3D structure databases

ProteinModelPortaliQ6NRT6.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi431990.
KEGGixla:431990.

Organism-specific databases

CTDi54431.
XenbaseiXB-GENE-981000. dnajc10.

Phylogenomic databases

HOVERGENiHBG057048.
KOiK09530.

Family and domain databases

CDDicd06257. DnaJ. 1 hit.
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. 3 hits.
PS51352. THIOREDOXIN_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 80 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

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 one 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.