D3Z6P0 (PDIA2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein disulfide-isomerase A2
EC=5.3.4.1

Alternative name(s):
PDIp

Gene names

Name:	Pdia2
Synonyms:	Pdip

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	527 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	Acts as an intracellular estrogen-binding protein. May be involved in modulating cellular levels and biological functions of estrogens in the pancreas. May act as a chaperone that inhibits aggregation of misfolded proteins By similarity. UniProtKB Q13087
Catalytic activity	Catalyzes the rearrangement of -S-S- bonds in proteins.
Subunit structure	Part of a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX By similarity.
Subcellular location	Endoplasmic reticulum lumen By similarity UniProtKB Q13087.
Tissue specificity	Highly expressed in pancreas. Ref.3
Post-translational modification	Glycosylated. Ref.3
Sequence similarities	Belongs to the protein disulfide isomerase family. Contains 2 thioredoxin domains.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Coding sequence diversity	Alternative splicing
Domain	Redox-active center Repeat Signal
Ligand	Lipid-binding Steroid-binding
Molecular function	Chaperone Isomerase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: Compara cell redox homeostasis Inferred from electronic annotation. Source: InterPro glycerol ether metabolic process Inferred from electronic annotation. Source: InterPro response to hypoxia Inferred from electronic annotation. Source: Compara
Cellular_component	endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	electron carrier activity Inferred from electronic annotation. Source: InterPro protein disulfide isomerase activity Traceable author statement Ref.3. Source: MGI protein disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro steroid binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 Ref.1 (identifier: D3Z6P0-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 Ref.2 (identifier: D3Z6P0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     184-186: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Potential
	Chain	21 – 527	507	Protein disulfide-isomerase A2		PRO_0000394671
Regions
	Domain	29 – 155	127	Thioredoxin 1
	Domain	355 – 499	145	Thioredoxin 2
	Motif	524 – 527	4	Prevents secretion from ER Potential
Sites
	Active site	74	1	Nucleophile By similarity UniProtKB P07237
	Active site	77	1	Nucleophile By similarity UniProtKB P07237
	Active site	421	1	Nucleophile By similarity UniProtKB Q13087
	Active site	424	1	Nucleophile By similarity UniProtKB Q13087
	Site	75	1	Contributes to redox potential value By similarity UniProtKB Q13087
	Site	76	1	Contributes to redox potential value By similarity UniProtKB Q13087
	Site	422	1	Contributes to redox potential value By similarity UniProtKB Q13087
	Site	423	1	Contributes to redox potential value By similarity UniProtKB Q13087
	Site	485	1	Lowers pKa of C-terminal Cys of second active site By similarity UniProtKB Q13087
Amino acid modifications
	Glycosylation	130	1	N-linked (GlcNAc...) Potential
	Glycosylation	287	1	N-linked (GlcNAc...) Potential
	Glycosylation	518	1	N-linked (GlcNAc...) Potential
	Disulfide bond	74 ↔ 77		Redox-active By similarity UniProtKB Q13087
	Disulfide bond	421 ↔ 424		Redox-active By similarity UniProtKB Q13087
Natural variations
	Alternative sequence	184 – 186	3	Missing in isoform 2. Ref.2		VSP_039293

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 20, 2010. Version 1. Checksum: CF703D296B634441	FASTA	527	58,316
	10 20 30 40 50 60 MDKQLLPVLL LLLGVSGSWG QGEEPGGPSE VLPEEPTGEE VPKEDGILVL NHRTLSLALQ 70 80 90 100 110 120 EHSALMVEFY APWCGHCKEL APEYSKAAAL LAAESAVVTL AKVDGPAEPE LTKEFEVVGY 130 140 150 160 170 180 PTLKFFQNGN RTNPEEYAGP KTAEGIAEWL RRRVGPSATH LEDEEGVQAL MAKWDMVVIG 190 200 210 220 230 240 FFQDLQGKDM ATFLALAKDA LDMTFGFTDQ PQLFEKFGLT KDTVVLFKKF DEGRADFPVD 250 260 270 280 290 300 KETGLDLGDL SRFLVIHSMH LVTEFNSQTS PKIFAAKILN HLLLFVNQTL AQHRELLTDF 310 320 330 340 350 360 REAAPPFRGQ VLFVMVDVAA DNSHVLNYFG LKAEEAPTLR LINVETTKKY APTGVIAITA 370 380 390 400 410 420 ASVAAFCQAV LHGEIKHYLL SQEIPPDWDQ GPVKTLVSKN FEQVAFDETK NVFVKFYAPW 430 440 450 460 470 480 CSHCKEMAPA WEALAEKYKD REDIVIAELD ATANELEAFS VLGYPTLKFF PAGPDRKVID 490 500 510 520 YKSTRDLETF SKFLDSGGHL PKEEPKEPAA SAPEAQANST LGPKEEL
	Isoform 2 [UniParc]. Checksum: 4233CC4C3942C17D	FASTA	524	57,960
	10 20 30 40 50 60 MDKQLLPVLL LLLGVSGSWG QGEEPGGPSE VLPEEPTGEE VPKEDGILVL NHRTLSLALQ 70 80 90 100 110 120 EHSALMVEFY APWCGHCKEL APEYSKAAAL LAAESAVVTL AKVDGPAEPE LTKEFEVVGY 130 140 150 160 170 180 PTLKFFQNGN RTNPEEYAGP KTAEGIAEWL RRRVGPSATH LEDEEGVQAL MAKWDMVVIG 190 200 210 220 230 240 FFQGKDMATF LALAKDALDM TFGFTDQPQL FEKFGLTKDT VVLFKKFDEG RADFPVDKET 250 260 270 280 290 300 GLDLGDLSRF LVIHSMHLVT EFNSQTSPKI FAAKILNHLL LFVNQTLAQH RELLTDFREA 310 320 330 340 350 360 APPFRGQVLF VMVDVAADNS HVLNYFGLKA EEAPTLRLIN VETTKKYAPT GVIAITAASV 370 380 390 400 410 420 AAFCQAVLHG EIKHYLLSQE IPPDWDQGPV KTLVSKNFEQ VAFDETKNVF VKFYAPWCSH 430 440 450 460 470 480 CKEMAPAWEA LAEKYKDRED IVIAELDATA NELEAFSVLG YPTLKFFPAG PDRKVIDYKS 490 500 510 520 TRDLETFSKF LDSGGHLPKE EPKEPAASAP EAQANSTLGP KEEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[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] (ISOFORM 2).
[3]	"Molecular characterization of a pancreas-specific protein disulfide isomerase, PDIp." Desilva M.G., Notkins A.L., Lan M.S. DNA Cell Biol. 16:269-274(1997) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, GLYCOSYLATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC126438 Genomic DNA. No translation available. BC116671 mRNA. Translation: AAI16672.1.
IPI	IPI00347894. IPI00880560.
RefSeq	NP_001074539.1. NM_001081070.1.
UniGene	Mm.32631.
3D structure databases
ProteinModelPortal	D3Z6P0.
SMR	D3Z6P0. Positions 43-499.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000035584.
Proteomic databases
PRIDE	D3Z6P0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000039113; ENSMUSP00000035584; ENSMUSG00000024184. ENSMUST00000120333; ENSMUSP00000114080; ENSMUSG00000024184.
GeneID	69191.
KEGG	mmu:69191.
UCSC	uc008bdo.1. mouse. uc012ans.1. mouse.
Organism-specific databases
CTD	64714.
MGI	MGI:1916441. Pdia2.
Phylogenomic databases
GeneTree	ENSGT00700000104429.
HOGENOM	HOG000162459.
HOVERGEN	HBG005920.
KO	K09581.
OMA	TEFNSQT.
OrthoDB	EOG4JWVDB.
Gene expression databases
Bgee	D3Z6P0.
Family and domain databases
Gene3D	3.40.30.10. 4 hits.
InterPro	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.
PROSITE	PS00014. ER_TARGET. 1 hit. PS00194. THIOREDOXIN_1. 1 hit. PS51352. THIOREDOXIN_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	PDIA2. mouse.
NextBio	328852.
SOURCE	Search...

Entry information

Entry name

PDIA2_MOUSE

Accession

Primary (citable) accession number: D3Z6P0
Secondary accession number(s): Q14AV9

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 15, 2010
Last sequence update:	April 20, 2010
Last modified:	May 1, 2013
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program