Reviewed, UniProtKB/Swiss-Prot Q9DC23 (DJC10_MOUSE)

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	793 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.5
Subunit structure	Interacts with HSPA5 via its J domain. Ref.5
Subcellular location	Secreted Potential. Endoplasmic reticulum lumen.
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.5
Sequence similarities	Contains 1 J domain. Contains 4 thioredoxin domains.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Secreted
Domain	Repeat Signal
Molecular function	Chaperone
PTM	Glycoprotein
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro protein folding Inferred from electronic annotation. Source: InterPro
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	heat shock protein binding Inferred from electronic annotation. Source: InterPro unfolded protein binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 32	32	Potential
	Chain	33 – 793	761	DnaJ homolog subfamily C member 10		PRO_0000281484
Regions
	Domain	35 – 100	66	J
	Domain	130 – 232	103	Thioredoxin 1
	Domain	454 – 553	100	Thioredoxin 2
	Domain	557 – 665	109	Thioredoxin 3
	Domain	671 – 776	106	Thioredoxin 4
	Motif	790 – 793	4	Prevents secretion from ER Potential
Amino acid modifications
	Glycosylation	530	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	91	1	H → D in AAN73273. Ref.1
	Sequence conflict	91	1	H → D in AAQ14555. Ref.2
	Sequence conflict	91	1	H → D in AAH33461. Ref.4
	Sequence conflict	310	1	T → A in AAQ14555. Ref.2
	Sequence conflict	324	1	E → G in AAH33461. Ref.4
	Sequence conflict	433	1	I → T in AAH33461. Ref.4
	Sequence conflict	538	1	E → G in AAQ14555. Ref.2
	Sequence conflict	651 – 652	2	NG → RP in AAQ14555. Ref.2
	Sequence conflict	654	1	N → NS in AAN73273. Ref.1
	Sequence conflict	680	1	F → FR in AAN73273. Ref.1
	Sequence conflict	767	1	D → M in AAQ14555. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9DC23-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: D5BCCE36B1C572EE	FASTA	793	90,605
	10 20 30 40 50 60 MGVWLNKDDF IRDLKRISLC LLILYVVVVV GTDQNFYSLL GVSKTASSRE IRQAFKKLAL 70 80 90 100 110 120 KLHPDKNPNN PNAHGDFLKI NRAYEVLKDE HLRKKYDKYG 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

References

	« Hide 'large scale' referencesShow '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: 12411443] [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. , 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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Lung.
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Czech II and FVB/N x C57BL/6J. Tissue: Mammary tumor.
[5]	"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: 12446677] [Abstract] Cited for: CHARACTERIZATION, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION, INTERACTION WITH HSPA5.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF255459 mRNA. Translation: AAN73273.1. AF314002 mRNA. Translation: AAQ14555.1. AK004617 mRNA. Translation: BAB23413.1. BC002207 mRNA. Translation: AAH02207.1. BC033461 mRNA. Translation: AAH33461.1.
IPI	IPI00844664.
UniGene	Mm.21762
3D structure databases
HSSP	HSSP built from PDB template 1BQZ based on UniProtKB P08622.
ModBase	Search...
Proteomic databases
PRIDE	Q9DC23.
Genome annotation databases
Ensembl	ENSMUSG00000027006. Mus musculus. [Contig view]
Organism-specific databases
MGI	MGI:1914111. Dnajc10.
Phylogenomic databases
HOVERGEN	Q9DC23.
Gene expression databases
ArrayExpress	Q9DC23.
Bgee	Q9DC23.
CleanEx	MM_DNAJC10.
Family and domain databases
InterPro	IPR001623. DnaJ_N. IPR000886. ER_targeting_sequence. IPR018253. Heat_shock_DnaJ_CS. IPR015609. Hsp40/DnaJ_Rel. IPR003095. Hsp_DnaJ. IPR017936. Thioredoxin-like. IPR017937. Thioredoxin_CS. IPR013766. Thioredoxin_domain. IPR012335. Thioredoxin_fold. [Graphical view]
Gene3D	G3DSA:1.10.287.110. DnaJ_N. 1 hit. G3DSA:3.40.30.10. Thioredoxin_fold. 4 hits.
PANTHER	PTHR11821. Hsp40/DnaJ_Rel. 1 hit.
Pfam	PF00226. DnaJ. 1 hit. PF00085. Thioredoxin. 4 hits. [Graphical view]
PRINTS	PR00625. DNAJPROTEIN.
SMART	SM00271. DnaJ. 1 hit. [Graphical view]
PROSITE	PS00636. 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]
ProtoNet	Search...
Other Resources
SOURCE	Search...

Entry information

Entry name

DJC10_MOUSE

Accession

Primary (citable) accession number: Q9DC23
Secondary accession number(s): Q71S84 , Q8CH78, Q8CIB0, Q99LV4

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 2007
Last sequence update:	June 1, 2001
Last modified:	June 16, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)