P27773 (PDIA3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein disulfide-isomerase A3
EC=5.3.4.1

Alternative name(s):
58 kDa glucose-regulated protein
58 kDa microsomal protein
Short name=p58
Disulfide isomerase ER-60
Endoplasmic reticulum resident protein 57
Short name=ER protein 57
Short name=ERp57
Endoplasmic reticulum resident protein 60
Short name=ER protein 60
Short name=ERp60

Gene names

Name:	Pdia3
Synonyms:	Erp, Erp60, Grp58

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	505 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)

Catalytic activity	Catalyzes the rearrangement of -S-S- bonds in proteins.
Subunit structure	Subunit of the TAP complex, also known as the peptide loading complex (PLC). Can form disulfide-linked heterodimers with TAPBP. Interacts with ERP27 and CANX By similarity. Interacts with MZB1 in a calcium-dependent manner. Ref.10
Subcellular location	Endoplasmic reticulum lumen By similarity. Melanosome By similarity.
Tissue specificity	In caput and cauda epididymal spermatozoa, detected in the acrosome and principal piece (at protein level). Ref.9
Post-translational modification	Phosphorylated. Ref.7
Sequence similarities	Belongs to the protein disulfide isomerase family. Contains 2 thioredoxin domains.
Caution	Was originally (Ref.1) thought to be a phosphatidylinositol 4,5-bisphosphate phosphodiesterase type I (phospholipase C-alpha).

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Domain	Redox-active center Repeat Signal
Molecular function	Isomerase
PTM	Disulfide bond Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro glycerol ether metabolic process Inferred from electronic annotation. Source: InterPro positive regulation of apoptotic process Inferred from mutant phenotype PubMed 15858817. Source: MGI protein folding Inferred from electronic annotation. Source: GOC
Cellular_component	cell surface Inferred from direct assay PubMed 19995400. Source: MGI endoplasmic reticulum lumen Traceable author statement. Source: Reactome melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	electron carrier activity Inferred from electronic annotation. Source: InterPro protein disulfide isomerase activity Inferred from electronic annotation. Source: EC protein disulfide oxidoreductase activity 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 – 24	24	Ref.6 Ref.7
	Chain	25 – 505	481	Protein disulfide-isomerase A3		PRO_0000034226
Regions
	Domain	25 – 133	109	Thioredoxin 1
	Domain	343 – 485	143	Thioredoxin 2
	Motif	502 – 505	4	Prevents secretion from ER By similarity
Sites
	Active site	57	1	Nucleophile By similarity
	Active site	60	1	Nucleophile By similarity
	Active site	406	1	Nucleophile By similarity
	Active site	409	1	Nucleophile By similarity
	Site	58	1	Contributes to redox potential value By similarity
	Site	59	1	Contributes to redox potential value By similarity
	Site	119	1	Lowers pKa of C-terminal Cys of first active site By similarity
	Site	407	1	Contributes to redox potential value By similarity
	Site	408	1	Contributes to redox potential value By similarity
	Site	471	1	Lowers pKa of C-terminal Cys of second active site By similarity
Amino acid modifications
	Disulfide bond	57 ↔ 60		Redox-active; alternate By similarity
	Disulfide bond	57		Interchain (with C-118 in TAPBP); alternate By similarity
	Disulfide bond	85 ↔ 92		By similarity
	Disulfide bond	406 ↔ 409		Redox-active By similarity
Experimental info
	Sequence conflict	20	1	R → C in BAC40527. Ref.3
	Sequence conflict	20	1	R → C in BAE41259. Ref.3
	Sequence conflict	76	1	Missing in AAA39944. Ref.1
	Sequence conflict	108	1	D → A in AAA39944. Ref.1
	Sequence conflict	230	1	G → A in AAA39944. Ref.1
	Sequence conflict	264	1	Y → F in BAE39834. Ref.3
	Sequence conflict	315	1	G → S in AAA39944. Ref.1
	Sequence conflict	387	1	D → G in BAE39834. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P27773 [UniParc]. Last modified May 1, 2007. Version 2. Checksum: 3A7CD1C35981C4B3	FASTA	505	56,678
	10 20 30 40 50 60 MRFSCLALLP GVALLLASAR LAAASDVLEL TDENFESRVS DTGSAGLMLV EFFAPWCGHC 70 80 90 100 110 120 KRLAPEYEAA ATRLKGIVPL AKVDCTANTN TCNKYGVSGY PTLKIFRDGE EAGAYDGPRT 130 140 150 160 170 180 ADGIVSHLKK QAGPASVPLR TEEEFKKFIS DKDASVVGFF RDLFSDGHSE FLKAASNLRD 190 200 210 220 230 240 NYRFAHTNIE SLVKEYDDNG EGITIFRPLH LANKFEDKTV AYTEKKMTSG KIKKFIQDSI 250 260 270 280 290 300 FGLCPHMTED NKDLIQGKDL LTAYYDVDYE KNAKGSNYWR NRVMMVAKKF LDAGHKLNFA 310 320 330 340 350 360 VASRKTFSHE LSDFGLESTT GEVPVVAIRT AKGEKFVMQE EFSRDGKALE QFLQEYFDGN 370 380 390 400 410 420 LKRYLKSEPI PESNEGPVKV VVAENFDDIV NEEDKDVLIE FYAPWCGHCK NLEPKYKELG 430 440 450 460 470 480 EKLSKDPNIV IAKMDATAND VPSPYEVKGF PTIYFSPANK KLTPKKYEGG RELNDFISYL 490 500 QREATNPPII QEEKPKKKKK AQEDL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Expression of phospholipase C isozymes by murine B lymphocytes." Hempel W.M., Defranco A.L. J. Immunol. 146:3713-3720(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Mouse GRP58 gene structure." Wang W., Jaiswal A.K. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: C57BL/6.
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J, DBA/2 and NOD. Tissue: Thymus.
[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. , 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. Tissue: Mammary tumor.
[6]	"Separation and sequencing of familiar and novel murine proteins using preparative two-dimensional gel electrophoresis." Merrick B.A., Patterson R.M., Wichter L.L., He C., Selkirk J.K. Electrophoresis 15:735-745(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 25-41 AND 306-329. Tissue: Fibroblast.
[7]	"Identification of the two isoforms of phospholipase C-alpha from dividing murine fibroblasts by protein microsequencing." Merrick B.A., Wichter L.L., Patterson R.M., He C., Selkirk J.K. Biochem. Arch. 9:335-340(1993) Cited for: PROTEIN SEQUENCE OF 25-41, PHOSPHORYLATION. Tissue: Fibroblast.
[8]	Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 63-73; 94-103; 119-128; 130-139; 147-172; 183-193; 195-214; 234-251; 258-270; 306-329; 335-343; 347-362; 366-378; 448-459 AND 472-495, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain and Hippocampus.
[9]	"Glucose-regulated protein precursor (GRP78) and tumor rejection antigen (GP96) are unique to hamster caput epididymal spermatozoa." Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S. Asian J. Androl. 12:344-355(2010) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[10]	"Mzb1 protein regulates calcium homeostasis, antibody secretion, and integrin activation in innate-like B cells." Flach H., Rosenbaum M., Duchniewicz M., Kim S., Zhang S.L., Cahalan M.D., Mittler G., Grosschedl R. Immunity 33:723-735(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MZB1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M73329 mRNA. Translation: AAA39944.1. DQ000491 Genomic DNA. Translation: AAY16987.1. AK088721 mRNA. Translation: BAC40527.1. AK133799 mRNA. Translation: BAE21849.1. AK167807 mRNA. Translation: BAE39834.1. AK169611 mRNA. Translation: BAE41259.1. AL845466 Genomic DNA. Translation: CAM24231.1. BC003285 mRNA. Translation: AAH03285.1. BC033439 mRNA. Translation: AAH33439.1.
IPI	IPI00230108.
RefSeq	NP_031978.2. NM_007952.2.
UniGene	Mm.263177.
3D structure databases
ProteinModelPortal	P27773.
SMR	P27773. Positions 25-493.
ModBase	Search...
Protein-protein interaction databases
IntAct	P27773. 3 interactions.
PTM databases
PhosphoSite	P27773.
2D gel databases
REPRODUCTION-2DPAGE	IPI00230108. P27773. Q3TEI9. Q8C2F4.
SWISS-2DPAGE	P27773.
Proteomic databases
PaxDb	P27773.
PRIDE	P27773.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000028683; ENSMUSP00000028683; ENSMUSG00000027248.
GeneID	14827.
KEGG	mmu:14827.
UCSC	uc008lzb.1. mouse.
Organism-specific databases
CTD	2923.
MGI	MGI:95834. Pdia3.
Phylogenomic databases
eggNOG	COG0526.
GeneTree	ENSGT00700000104218.
HOGENOM	HOG000162459.
HOVERGEN	HBG005920.
InParanoid	P27773.
KO	K08056.
OMA	KNPKGTN.
OrthoDB	EOG42Z4PX.
Enzyme and pathway databases
Reactome	REACT_107772. Immune System.
Gene expression databases
ArrayExpress	P27773.
Bgee	P27773.
CleanEx	MM_PDIA3.
Genevestigator	P27773.
GermOnline	ENSMUSG00000027248. Mus musculus.
Family and domain databases
Gene3D	3.40.30.10. 3 hits.
InterPro	IPR005788. Disulphide_isomerase. IPR005792. Prot_disulphide_isomerase. IPR005746. Thioredoxin. IPR012336. Thioredoxin-like_fold. IPR017937. Thioredoxin_CS. IPR013766. Thioredoxin_domain. [Graphical view]
Pfam	PF00085. Thioredoxin. 2 hits. [Graphical view]
PRINTS	PR00421. THIOREDOXIN.
SUPFAM	SSF52833. Thiordxn-like_fd. 4 hits.
TIGRFAMs	TIGR01130. ER_PDI_fam. 1 hit. TIGR01126. pdi_dom. 2 hits.
PROSITE	PS00194. THIOREDOXIN_1. 2 hits. PS51352. THIOREDOXIN_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	PDIA3. mouse.
NextBio	287035.
SOURCE	Search...

Entry information

Entry name

PDIA3_MOUSE

Accession

Primary (citable) accession number: P27773
Secondary accession number(s): Q3TEI9 , Q3TIL2, Q3UZK8, Q8C2F4, Q99LF6

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	May 1, 2007
Last modified:	April 3, 2013
This is version 129 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program