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Q498R3

- DJC10_RAT

UniProt

Q498R3 - DJC10_RAT

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Protein

DnaJ homolog subfamily C member 10

Gene

Dnajc10

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 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. ATPase activator activity Source: Ensembl
  2. oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor Source: UniProtKB
  3. 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. intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: Ensembl
  4. negative regulation of protein phosphorylation Source: Ensembl
  5. 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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 3

Organism-specific databases

RGDi1307813. Dnajc10.

Subcellular locationi

Endoplasmic reticulum lumen PROSITE-ProRule annotation

GO - Cellular componenti

  1. endoplasmic reticulum chaperone complex Source: Ensembl
  2. 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_0000281486Add
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

Proteomic databases

PaxDbiQ498R3.
PRIDEiQ498R3.

PTM databases

PhosphoSiteiQ498R3.

Expressioni

Gene expression databases

GenevestigatoriQ498R3.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiQ498R3. 5 interactions.
MINTiMINT-4572149.
STRINGi10116.ENSRNOP00000009839.

Structurei

3D structure databases

ProteinModelPortaliQ498R3.
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 – 665109Thioredoxin 3PROSITE-ProRule annotationAdd
BLAST
Domaini671 – 776106Thioredoxin 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

eggNOGiCOG0526.
GeneTreeiENSGT00730000110455.
HOGENOMiHOG000231882.
HOVERGENiHBG057048.
InParanoidiQ498R3.
KOiK09530.
OMAiYPSLFIF.
OrthoDBiEOG7RZ5QH.
PhylomeDBiQ498R3.
TreeFamiTF105169.

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. 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.

Q498R3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGVWLNRDEF IRDVKRISLC LLVLYVVIVV GTDQNFYSLL GVSKTASSRE
60 70 80 90 100
IRQAFKKLAL KLHPDKNPNN PNAHGDFLKI NRAYEVLKDE DLRKKYDKYG
110 120 130 140 150
EKGLEDNQGG QYESWSYYRY DFGIYDDDPE IITLERREFD AAVNSGELWF
160 170 180 190 200
VNFYSPGCSH CHDLAPTWRE FAKEVDGLLR IGAVNCGDDR MLCRMKGVNS
210 220 230 240 250
YPSLFIFRSG MAAVKYNGDR SKESLVSFAM QHVRTTVTEL STGNFVNAIE
260 270 280 290 300
TAFAAGIGWL ITFCFKGEDC LTPQTRLRLS GMLDGLVNVG WVDCDTQDSL
310 320 330 340 350
CKSLDATAST TAYFPPGATL NNKEKSSVLF LNSLDAKEIY MEIIHNLPDF
360 370 380 390 400
ELLSANKLED RLAHHRWLVF FHFGKNENAN DPELKKLKTL LKNEHIQVGR
410 420 430 440 450
FDCSSAPGIC SDLYVFQSCL AVFKGQGTKE YEIHHGKKIL YDILAFAKES
460 470 480 490 500
VNSHVTTLGP QNFPASDKEP WLVDFFAPWC PPCRALLPEL RKASTLLYGQ
510 520 530 540 550
LKVGTLDCTI HEGLCNMYNI QAYPTTVVFN QSSVHEYEGH HSAEQILEFI
560 570 580 590 600
EDLRNPSVVS LTPTTFNELV KQRKHDEVWM VDFYSPWCHP CQVLMPEWKR
610 620 630 640 650
MARTLTGLIN VGSVDCQQYH SFCTQENVQR YPEIRFYPQK SSRAYQYHSY
660 670 680 690 700
NGWNRDAYSL RSWGLGFLPQ ASIDLTPQTF NEKVLQGKTH WVIDFYAPWC
710 720 730 740 750
GPCQNFAPEF ELLARMIKGK VKAGKVDCQA YPQTCQKAGI RAYPSVKLYL
760 770 780 790
YERAKKSIWE EQINSRDAKT IAALIYGKLE TFQSQVKRNK DEL
Length:793
Mass (Da):90,747
Last modified:March 20, 2007 - v2
Checksum:i9578A69C36C858C9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03024291 Genomic DNA. No translation available.
BC100105 mRNA. Translation: AAI00106.1.
RefSeqiNP_001099956.2. NM_001106486.2.
UniGeneiRn.8642.

Genome annotation databases

EnsembliENSRNOT00000009839; ENSRNOP00000009839; ENSRNOG00000006803.
GeneIDi295690.
KEGGirno:295690.
UCSCiRGD:1307813. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03024291 Genomic DNA. No translation available.
BC100105 mRNA. Translation: AAI00106.1 .
RefSeqi NP_001099956.2. NM_001106486.2.
UniGenei Rn.8642.

3D structure databases

ProteinModelPortali Q498R3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q498R3. 5 interactions.
MINTi MINT-4572149.
STRINGi 10116.ENSRNOP00000009839.

PTM databases

PhosphoSitei Q498R3.

Proteomic databases

PaxDbi Q498R3.
PRIDEi Q498R3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000009839 ; ENSRNOP00000009839 ; ENSRNOG00000006803 .
GeneIDi 295690.
KEGGi rno:295690.
UCSCi RGD:1307813. rat.

Organism-specific databases

CTDi 54431.
RGDi 1307813. Dnajc10.

Phylogenomic databases

eggNOGi COG0526.
GeneTreei ENSGT00730000110455.
HOGENOMi HOG000231882.
HOVERGENi HBG057048.
InParanoidi Q498R3.
KOi K09530.
OMAi YPSLFIF.
OrthoDBi EOG7RZ5QH.
PhylomeDBi Q498R3.
TreeFami TF105169.

Miscellaneous databases

NextBioi 639891.
PROi Q498R3.

Gene expression databases

Genevestigatori Q498R3.

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. 2 hits.
PS51352. THIOREDOXIN_2. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 262-793.
    Tissue: Spleen.

Entry informationi

Entry nameiDJC10_RAT
AccessioniPrimary (citable) accession number: Q498R3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: March 20, 2007
Last modified: October 1, 2014
This is version 88 of the entry and version 2 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