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Q9DC23 (DJC10_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DnaJ homolog subfamily C member 10
Alternative name(s):
ER-resident protein ERdj5
Endoplasmic reticulum DnaJ-PDI fusion protein 1
J domain-containing protein disulfide isomerase-like protein
Short name=J domain-containing PDI-like protein
Short name=JPDI
Gene names
Name:Dnajc10
Synonyms:Erdj5, Jpdi
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length793 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This endoplasmic reticulum co-chaperone may play a role in protein folding and translocation across the endoplasmic reticulum membrane. May be involved in disulfide formation. May act as a co-chaperone for Hspa5. Ref.1 Ref.6

Subunit structure

Interacts with HSPA5 via its J domain. Ref.6

Subcellular location

Secreted Potential. Endoplasmic reticulum lumen Ref.6.

Tissue specificity

Ubiquitous. Particularly abundant in secretory tissues. Ubiquitous in fetal tissues and tumor tissues. Higher expression in fetal tissues than in adult tissues. Expressed in testis, pancreas, fetal thymus and fetal kidney. High expression in heart, liver, kidney, and testis. Low expression in spleen and skeletal muscle. Ref.1 Ref.6

Sequence similarities

Contains 1 J domain.

Contains 4 thioredoxin domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232 Potential
Chain33 – 793761DnaJ homolog subfamily C member 10
PRO_0000281484

Regions

Domain35 – 10066J
Domain130 – 232103Thioredoxin 1
Domain454 – 553100Thioredoxin 2
Domain557 – 665109Thioredoxin 3
Domain671 – 776106Thioredoxin 4
Motif790 – 7934Prevents secretion from ER Potential

Amino acid modifications

Glycosylation5301N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict911D → H in BAB23413. Ref.3
Sequence conflict3101T → A in AAQ14555. Ref.2
Sequence conflict3241E → G in AAH33461. Ref.4
Sequence conflict4331I → T in AAH33461. Ref.4
Sequence conflict5381E → G in AAQ14555. Ref.2
Sequence conflict651 – 6522NG → RP in AAQ14555. Ref.2
Sequence conflict6541N → NS in AAN73273. Ref.1
Sequence conflict6801F → FR in AAN73273. Ref.1
Sequence conflict7671D → M in AAQ14555. Ref.2

Secondary structure

1 ...................................................................................................................................... 793
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9DC23 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 00C88EF3F5497BE1

FASTA79390,583
        10         20         30         40         50         60 
MGVWLNKDDF IRDLKRISLC LLILYVVVVV GTDQNFYSLL GVSKTASSRE IRQAFKKLAL 

        70         80         90        100        110        120 
KLHPDKNPNN PNAHGDFLKI NRAYEVLKDE DLRKKYDKYG EKGLEDNQGG QYESWSYYRY 

       130        140        150        160        170        180 
DFGIYDDDPE IITLERREFD AAVNSGELWF VNFYSPGCSH CHDLAPTWRE FAKEVDGLLR 

       190        200        210        220        230        240 
IGAVNCGDDR MLCRMKGVNS YPSLFIFRSG MAAVKYNGDR SKESLVAFAM QHVRSTVTEL 

       250        260        270        280        290        300 
STGNFVNAIE TAFAAGVGWL ITFCSKGEDC LTSQTRLRLS GMLDGLVNVG WVDCDAQDSL 

       310        320        330        340        350        360 
CKSLDTTAST TAYFPPGATL NDREKSSVLF LNSLDAKEIY MEIIHNLPDF ELLSANQLED 

       370        380        390        400        410        420 
RLAHHRWLVF FHFGKNENAN DPELKKLKTL LKNEHIQVGR FDCSSAPGIC SDLYVFQPCL 

       430        440        450        460        470        480 
AVFKGQGTKE YEIHHGKKIL YDILAFAKES VNSHVTTLGP QNFPASDKEP WLVDFFAPWC 

       490        500        510        520        530        540 
PPCRALLPEL RKASTLLYGQ LKVGTLDCTI HEGLCNMYNI QAYPTTVVFN QSSIHEYEGH 

       550        560        570        580        590        600 
HSAEQILEFI EDLRNPSVVS LTPSTFNELV KQRKHDEVWM VDFYSPWCHP CQVLMPEWKR 

       610        620        630        640        650        660 
MARTLTGLIN VGSVDCQQYH SFCTQENVQR YPEIRFYPQK SSKAYQYHSY NGWNRDAYSL 

       670        680        690        700        710        720 
RSWGLGFLPQ ASIDLTPQTF NEKVLQGKTH WVVDFYAPWC GPCQNFAPEF ELLARMIKGK 

       730        740        750        760        770        780 
VRAGKVDCQA YPQTCQKAGI KAYPSVKLYQ YERAKKSIWE EQINSRDAKT IAALIYGKLE 

       790 
TLQSQVKRNK DEL

« Hide

References

« Hide 'large scale' references
[1]"ERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ and thioredoxin domains, is expressed in secretory cells or following ER stress."
Cunnea P.M., Miranda-Vizuete A., Bertoli G., Simmen T., Damdimopoulos A.E., Hermann S., Leinonen S., Huikko M.P., Gustafsson J.-A., Sitia R., Spyrou G.
J. Biol. Chem. 278:1059-1066(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
[2]"ERDJPs, a novel family of ER chaperones."
Simmen T., Mezghrani A., Bertoli G., Sitia R.
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Lung.
[4]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[5]"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].
Strain: Czech II and FVB/N x C57BL/6J.
Tissue: Mammary tumor.
[6]"JPDI, a novel endoplasmic reticulum-resident protein containing both a BiP-interacting J-domain and thioredoxin-like motifs."
Hosoda A., Kimata Y., Tsuru A., Kohno K.
J. Biol. Chem. 278:2669-2676(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION, INTERACTION WITH HSPA5.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF255459 mRNA. Translation: AAN73273.1.
AF314002 mRNA. Translation: AAQ14555.1.
AK004617 mRNA. Translation: BAB23413.1.
AL928587 Genomic DNA. Translation: CAM19646.1.
BC002207 mRNA. Translation: AAH02207.1.
BC033461 mRNA. Translation: AAH33461.1.
IPIIPI00844664.
RefSeqNP_077143.2. NM_024181.2.
UniGeneMm.21762.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3APOX-ray2.40A33-793[»]
3APQX-ray1.84A/B34-242[»]
3APSX-ray1.90A/B668-789[»]
ProteinModelPortalQ9DC23.
SMRQ9DC23. Positions 34-782.
ModBaseSearch...

PTM databases

PhosphoSiteQ9DC23.

Proteomic databases

PaxDbQ9DC23.
PRIDEQ9DC23.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028392; ENSMUSP00000028392; ENSMUSG00000027006.
GeneID66861.
KEGGmmu:66861.

Organism-specific databases

CTD54431.
MGIMGI:1914111. Dnajc10.

Phylogenomic databases

eggNOGCOG0526.
GeneTreeENSGT00700000104218.
HOGENOMHOG000231882.
HOVERGENHBG057048.
InParanoidA2ASA2.
KOK09530.
OMAYPSLFIF.
OrthoDBEOG480HW1.

Gene expression databases

ArrayExpressQ9DC23.
BgeeQ9DC23.
CleanExMM_DNAJC10.
GenevestigatorQ9DC23.

Family and domain databases

Gene3D1.10.287.110. 1 hit.
3.40.30.10. 5 hits.
InterProIPR001623. DnaJ_domain.
IPR021170. DnaJ_homolog_subfam-C.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamPF00226. DnaJ. 1 hit.
PF00085. Thioredoxin. 4 hits.
[Graphical view]
PIRSFPIRSF037293. DnaJ_homolog_subfam-C. 1 hit.
PRINTSPR00625. JDOMAIN.
SMARTSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMSSF46565. DnaJ_N. 1 hit.
SSF52833. Thiordxn-like_fd. 6 hits.
PROSITEPS00636. DNAJ_1. False negative.
PS50076. DNAJ_2. 1 hit.
PS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9DC23.
NextBio322847.
SOURCESearch...

Entry information

Entry nameDJC10_MOUSE
AccessionPrimary (citable) accession number: Q9DC23
Secondary accession number(s): A2ASA2 expand/collapse secondary AC list , Q71S84, Q8CH78, Q8CIB0, Q99LV4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: July 27, 2011
Last modified: May 1, 2013
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents