Protein disulfide-isomerase A2 precursor

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

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	525 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Catalytic activity	Catalyzes the rearrangement of -S-S- bonds in proteins.
Subunit structure	Part a large chaperone multiprotein complex comprising CABP1, DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX.
Subcellular location	Endoplasmic reticulum lumen By similarity.
Tissue specificity	Highly expressed in pancreas.
Sequence similarities	Belongs to the protein disulfide isomerase family. Contains 2 thioredoxin domains.

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Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Coding sequence diversity	Polymorphism
Domain	Redox-active center Repeat Signal
Molecular function	Isomerase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro protein folding Ref.6 Traceable author statement. Source: ProtInc protein retention in ER lumen Ref.6 Traceable author statement. Source: ProtInc response to hypoxia Inferred from mutant phenotype. Source: HGNC
Cellular component	endoplasmic reticulum Ref.6 Inferred from direct assay. Source: HGNC endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein binding Inferred from physical interaction. Source: IntAct protein disulfide isomerase activity Ref.6 Traceable author statement. Source: ProtInc
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
ABL1	P00519	1	EBI-1752525,EBI-375543
CRK	P46108	1	EBI-1752525,EBI-886
FYN	P06241	1	EBI-1752525,EBI-515315
GRB2	P62993	1	EBI-1752525,EBI-401755
NCK1	P16333	1	EBI-1752525,EBI-389883
PIK3R1	P27986	1	EBI-1752525,EBI-79464
PLCG1	P19174	1	EBI-1752525,EBI-79387
SRC	P12931	1	EBI-1752525,EBI-621482

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Potential

Chain

22 – 525

504

Protein disulfide-isomerase A2

PRO_0000034222

Regions

Domain

27 – 152

126

Thioredoxin 1

Domain

367 – 496

130

Thioredoxin 2

Motif

522 – 525

4

Prevents secretion from ER Potential

Sites

Active site

71

1

Nucleophile By similarity

Active site

74

1

Nucleophile By similarity

Active site

418

1

Nucleophile By similarity

Active site

421

1

Nucleophile By similarity

Site

72

1

Contributes to redox potential value By similarity

Site

73

1

Contributes to redox potential value By similarity

Site

138

1

Lowers pKa of C-terminal Cys of first active site By similarity

Site

419

1

Contributes to redox potential value By similarity

Site

420

1

Contributes to redox potential value By similarity

Site

482

1

Lowers pKa of C-terminal Cys of second active site By similarity

Amino acid modifications

Glycosylation

127

1

N-linked (GlcNAc...) Potential

Glycosylation

284

1

N-linked (GlcNAc...) Potential

Glycosylation

516

1

N-linked (GlcNAc...) Potential

Disulfide bond

71 ↔ 74

Redox-active By similarity

Disulfide bond

418 ↔ 421

Redox-active By similarity

Natural variations

Natural variant

39

1

P → S: dbSNP rs45455191.

VAR_048087

Natural variant

119

1

T → R: dbSNP rs45614840.

VAR_048088

Natural variant

185

1

E → K: dbSNP rs419949.

VAR_048089

Natural variant

286

1

T → M: dbSNP rs2685127.

VAR_048090

Natural variant

382

1

P → A: dbSNP rs45529833.

VAR_048091

Natural variant

388

1

R → Q: dbSNP rs400037.

VAR_048092

Natural variant

502

1

P → S: dbSNP rs1048786. Ref.1 Ref.5 Ref.6

VAR_048093

Experimental info

Sequence conflict

15

1

R → M in AAC50401. Ref.6

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Sequences

Sequence

Length

Mass (Da)

Tools

Q13087-1 [UniParc].

Last modified May 27, 2002. Version 2.
Checksum: B741851AA2C40540
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FASTA

525

58,206

        10         20         30         40         50         60 
MSRQLLPVLL LLLLRASCPW GQEQGARSPS EEPPEEEIPK EDGILVLSRH TLGLALREHP 

        70         80         90        100        110        120 
ALLVEFYAPW CGHCQALAPE YSKAAAVLAA ESMVVTLAKV DGPAQRELAE EFGVTEYPTL 

       130        140        150        160        170        180 
KFFRNGNRTH PEEYTGPRDA EGIAEWLRRR VGPSAMRLED EAAAQALIGG RDLVVIGFFQ 

       190        200        210        220        230        240 
DLQDEDVATF LALAQDALDM TFGLTDRPRL FQQFGLTKDT VVLFKKFDEG RADFPVDEEL 

       250        260        270        280        290        300 
GLDLGDLSRF LVTHSMRLVT EFNSQTSAKI FAARILNHLL LFVNQTLAAH RELLAGFGEA 

       310        320        330        340        350        360 
APRFRGQVLF VVVDVAADNE HVLQYFGLKA EAAPTLRLVN LETTKKYAPV DGGPVTAASI 

       370        380        390        400        410        420 
TAFCHAVLNG QVKPYLLSQE IPPDWDQRPV KTLVGKNFEQ VAFDETKNVF VKFYAPWCTH 

       430        440        450        460        470        480 
CKEMAPAWEA LAEKYQDHED IIIAELDATA NELDAFAVHG FPTLKYFPAG PGRKVIEYKS 

       490        500        510        520 
TRDLETFSKF LDNGGVLPTE EPPEEPAAPF PEPPANSTMG SKEEL

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A human polycistronic mRNA composed of ARHGDIG and PDIP." Hayashi A., Tabata Y., Sato S., Mitsuyama M., Kanai S., Furuya T., Saito T. Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-502.
[2]	"Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16." Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R. Hum. Mol. Genet. 10:339-352(2001) [PubMed: 11157797] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"The sequence and analysis of duplication-rich human chromosome 16." Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. Pennacchio L.A. Nature 432:988-994(2004) [PubMed: 15616553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-525, VARIANT SER-502. Tissue: Brain.
[6]	"Characterization and chromosomal localization of a new protein disulfide isomerase, PDIp, highly expressed in human pancreas." Desilva M.G., Lu J., Donadel G., Modi W.S., Xie H., Notkins A.L., Lan M.S. DNA Cell Biol. 15:9-16(1996) [PubMed: 8561901] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 15-525, VARIANT SER-502. Tissue: Pancreas.
[7]	"A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins." Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M. Mol. Biol. Cell 13:4456-4469(2002) [PubMed: 12475965] [Abstract] Cited for: COMPONENT OF A CHAPERONE COMPLEX.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	AB127078 mRNA. Translation: BAE48734.1. AE006463 Genomic DNA. Translation: AAK61223.1. Z69667 Genomic DNA. Translation: CAI95586.1. CH471112 Genomic DNA. Translation: EAW85838.1. BC000537 mRNA. Translation: AAH00537.2. BC075029 mRNA. Translation: AAH75029.1. Different initiation. U19948 mRNA. Translation: AAC50401.1.
IPI	IPI00011571.
RefSeq	NP_006840.2.
UniGene	Hs.66581
3D structure databases
HSSP	HSSP built from PDB template 1MEK based on UniProtKB P07237.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q13087. 8 interactions.
Proteomic databases
PRIDE	Q13087.
Genome annotation databases
Ensembl	ENSG00000185615. Homo sapiens. [Contig view]
GeneID	64714.
KEGG	hsa:64714.
UCSC	uc002cgn.1. human.
Organism-specific databases
GeneCards	GC16P000274.
H-InvDB	HIX0026950.
HGNC	HGNC:14180. PDIA2.
MIM	608012. gene.
PharmGKB	PA33153.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q13087.
HOVERGEN	Q13087.
OMA	Q13087. KDTVVLF.
Enzyme and pathway databases
BRENDA	5.3.4.1. 247.
Gene expression databases
Bgee	Q13087.
CleanEx	HS_PDIA2.
GermOnline	ENSG00000185615. Homo sapiens.
Family and domain databases
InterPro	IPR005788. Disulphide_isomerase. IPR000886. ER_targeting_sequence. IPR005792. Prot_disulphide_isomerase. IPR017936. Thioredoxin-like. IPR006662. Thioredoxin-like_subdom. IPR017937. Thioredoxin_CS. IPR013766. Thioredoxin_domain. IPR012335. Thioredoxin_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 2 hits.
Pfam	PF00085. Thioredoxin. 2 hits. [Graphical view]
PRINTS	PR00421. THIOREDOXIN.
TIGRFAMs	TIGR01130. ER_PDI_fam. 1 hit. TIGR01126. pdi_dom. 2 hits.
PROSITE	PS00014. ER_TARGET. 1 hit. PS00194. THIOREDOXIN_1. 2 hits. PS51352. THIOREDOXIN_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	66651.
SOURCE	Search...

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Entry information

Entry name

PDIA2_HUMAN

Accession

Primary (citable) accession number: Q13087
Secondary accession number(s): Q2WGM4

Q9BW95

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	May 27, 2002
Last modified:	July 7, 2009
This is version 91 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents