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Protein disulfide-isomerase A2 (EC 5.3.4.1) (Pancreas-specific protein disulfide isomerase) (PDIp)

 PDIA2_HUMAN             Reviewed;         525 AA.
Q13087; A6ZJ64; B4DI27; Q2WGM4; Q4TT67; Q6B010; Q96KJ6; Q9BW95;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
27-MAY-2002, sequence version 2.
28-FEB-2018, entry version 173.
RecName: Full=Protein disulfide-isomerase A2;
EC=5.3.4.1;
AltName: Full=Pancreas-specific protein disulfide isomerase;
Short=PDIp;
Flags: Precursor;
Name=PDIA2; Synonyms=PDIP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-502.
Hayashi A., Tabata Y., Sato S., Mitsuyama M., Kanai S., Furuya T.,
Saito T.;
"A human polycistronic mRNA composed of ARHGDIG and PDIP.";
Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11157797; DOI=10.1093/hmg/10.4.339;
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.;
"Sequence, structure and pathology of the fully annotated terminal 2
Mb of the short arm of human chromosome 16.";
Hum. Mol. Genet. 10:339-352(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
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.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-525 (ISOFORM 1), AND
VARIANT SER-502.
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 16-525 (ISOFORM 1), TISSUE SPECIFICITY,
AND VARIANT SER-502.
TISSUE=Pancreas;
PubMed=8561901; DOI=10.1089/dna.1996.15.9;
Desilva M.G., Lu J., Donadel G., Modi W.S., Xie H., Notkins A.L.,
Lan M.S.;
"Characterization and chromosomal localization of a new protein
disulfide isomerase, PDIp, highly expressed in human pancreas.";
DNA Cell Biol. 15:9-16(1996).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 20-525 (ISOFORM 1).
TISSUE=Corpus callosum;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
TISSUE SPECIFICITY, AND GLYCOSYLATION.
PubMed=9115635; DOI=10.1089/dna.1997.16.269;
Desilva M.G., Notkins A.L., Lan M.S.;
"Molecular characterization of a pancreas-specific protein disulfide
isomerase, PDIp.";
DNA Cell Biol. 16:269-274(1997).
[9]
COMPONENT OF A CHAPERONE COMPLEX.
PubMed=12475965; DOI=10.1091/mbc.E02-05-0311;
Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.;
"A subset of chaperones and folding enzymes form multiprotein
complexes in endoplasmic reticulum to bind nascent proteins.";
Mol. Biol. Cell 13:4456-4469(2002).
[10]
FUNCTION, SUBUNIT, DISULFIDE BOND, AND MUTAGENESIS OF CYS-18 AND
CYS-364.
PubMed=19150607; DOI=10.1016/j.abb.2008.12.021;
Fu X., Zhu B.T.;
"Human pancreas-specific protein disulfide isomerase homolog (PDIp) is
redox-regulated through formation of an inter-subunit disulfide
bond.";
Arch. Biochem. Biophys. 485:1-9(2009).
[11]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=19429457; DOI=10.1016/j.jsbmb.2009.02.008;
Fu X.M., Zhu B.T.;
"Human pancreas-specific protein disulfide isomerase homolog (PDIp) is
an intracellular estrogen-binding protein that modulates estrogen
levels and actions in target cells.";
J. Steroid Biochem. Mol. Biol. 115:20-29(2009).
[12]
GLYCOSYLATION AT ASN-127; ASN-284 AND ASN-516, AND MUTAGENESIS OF
ASN-284.
PubMed=23167757; DOI=10.1111/febs.12063;
Walker A.K., Soo K.Y., Levina V., Talbo G.H., Atkin J.D.;
"N-linked glycosylation modulates dimerization of protein disulfide
isomerase family A member 2 (PDIA2).";
FEBS J. 280:233-243(2013).
-!- 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. {ECO:0000269|PubMed:19150607,
ECO:0000269|PubMed:19429457}.
-!- CATALYTIC ACTIVITY: Catalyzes the rearrangement of -S-S- bonds in
proteins.
-!- SUBUNIT: Monomer; predominantly as monomer under reducing
conditions. Homodimer; disulfide-linked. 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.
{ECO:0000269|PubMed:19150607}.
-!- INTERACTION:
P16333:NCK1; NbExp=3; IntAct=EBI-1752525, EBI-389883;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
{ECO:0000255|PROSITE-ProRule:PRU10138}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q13087-1; Sequence=Displayed;
Name=2;
IsoId=Q13087-2; Sequence=VSP_039292;
-!- TISSUE SPECIFICITY: Highly expressed in pancreas (at protein
level). {ECO:0000269|PubMed:19429457, ECO:0000269|PubMed:8561901,
ECO:0000269|PubMed:9115635}.
-!- PTM: The disulfide-linked homodimer exhibits an enhanced chaperone
activity.
-!- PTM: Glycosylated. {ECO:0000269|PubMed:23167757,
ECO:0000269|PubMed:9115635}.
-!- SIMILARITY: Belongs to the protein disulfide isomerase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC50401.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
Sequence=AAH75029.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
Sequence=BAG58339.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AB127078; BAE48734.1; -; mRNA.
EMBL; AE006463; AAK61223.1; -; Genomic_DNA.
EMBL; Z69667; CAI95586.1; -; Genomic_DNA.
EMBL; Z69667; CAO78188.1; -; Genomic_DNA.
EMBL; CH471112; EAW85838.1; -; Genomic_DNA.
EMBL; BC000537; AAH00537.2; -; mRNA.
EMBL; BC075029; AAH75029.1; ALT_SEQ; mRNA.
EMBL; U19948; AAC50401.1; ALT_SEQ; mRNA.
EMBL; AK295383; BAG58339.1; ALT_INIT; mRNA.
CCDS; CCDS42089.1; -. [Q13087-1]
RefSeq; NP_006840.2; NM_006849.2. [Q13087-1]
UniGene; Hs.66581; -.
ProteinModelPortal; Q13087; -.
SMR; Q13087; -.
BioGrid; 122240; 19.
IntAct; Q13087; 12.
MINT; Q13087; -.
STRING; 9606.ENSP00000219406; -.
iPTMnet; Q13087; -.
PhosphoSitePlus; Q13087; -.
BioMuta; PDIA2; -.
DMDM; 21264492; -.
MaxQB; Q13087; -.
PaxDb; Q13087; -.
PeptideAtlas; Q13087; -.
PRIDE; Q13087; -.
DNASU; 64714; -.
Ensembl; ENST00000219406; ENSP00000219406; ENSG00000185615. [Q13087-1]
Ensembl; ENST00000404312; ENSP00000384410; ENSG00000185615. [Q13087-2]
GeneID; 64714; -.
KEGG; hsa:64714; -.
UCSC; uc002cgo.2; human. [Q13087-1]
CTD; 64714; -.
DisGeNET; 64714; -.
EuPathDB; HostDB:ENSG00000185615.15; -.
GeneCards; PDIA2; -.
H-InvDB; HIX0202311; -.
HGNC; HGNC:14180; PDIA2.
HPA; HPA051692; -.
HPA; HPA053492; -.
MIM; 608012; gene.
neXtProt; NX_Q13087; -.
OpenTargets; ENSG00000185615; -.
PharmGKB; PA33153; -.
eggNOG; KOG0190; Eukaryota.
eggNOG; COG0526; LUCA.
GeneTree; ENSGT00860000133691; -.
HOVERGEN; HBG005920; -.
InParanoid; Q13087; -.
KO; K09581; -.
OMA; TTKKYAP; -.
OrthoDB; EOG091G08WM; -.
PhylomeDB; Q13087; -.
TreeFam; TF106381; -.
BRENDA; 5.3.4.1; 2681.
GenomeRNAi; 64714; -.
PRO; PR:Q13087; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000185615; -.
CleanEx; HS_PDIA2; -.
ExpressionAtlas; Q13087; baseline and differential.
Genevisible; Q13087; HS.
GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc.
GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
GO; GO:0015036; F:disulfide oxidoreductase activity; TAS:ParkinsonsUK-UCL.
GO; GO:0015037; F:peptide disulfide oxidoreductase activity; IDA:UniProtKB.
GO; GO:0003756; F:protein disulfide isomerase activity; IBA:GO_Central.
GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0019511; P:peptidyl-proline hydroxylation; IEA:GOC.
GO; GO:0006457; P:protein folding; TAS:ProtInc.
GO; GO:0034975; P:protein folding in endoplasmic reticulum; TAS:ParkinsonsUK-UCL.
GO; GO:0006621; P:protein retention in ER lumen; TAS:ProtInc.
GO; GO:1902175; P:regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IBA:GO_Central.
GO; GO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central.
InterPro; IPR005792; Prot_disulphide_isomerase.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR017937; Thioredoxin_CS.
InterPro; IPR013766; Thioredoxin_domain.
Pfam; PF00085; Thioredoxin; 2.
SUPFAM; SSF52833; SSF52833; 4.
TIGRFAMs; TIGR01130; ER_PDI_fam; 1.
PROSITE; PS00014; ER_TARGET; 1.
PROSITE; PS00194; THIOREDOXIN_1; 2.
PROSITE; PS51352; THIOREDOXIN_2; 2.
1: Evidence at protein level;
Alternative splicing; Chaperone; Complete proteome; Disulfide bond;
Endoplasmic reticulum; Glycoprotein; Isomerase; Lipid-binding;
Polymorphism; Redox-active center; Reference proteome; Repeat; Signal;
Steroid-binding.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 525 Protein disulfide-isomerase A2.
/FTId=PRO_0000034222.
DOMAIN 27 152 Thioredoxin 1. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
DOMAIN 367 496 Thioredoxin 2. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
MOTIF 522 525 Prevents secretion from ER.
{ECO:0000255|PROSITE-ProRule:PRU10138}.
ACT_SITE 71 71 Nucleophile. {ECO:0000250}.
ACT_SITE 74 74 Nucleophile. {ECO:0000250}.
ACT_SITE 418 418 Nucleophile. {ECO:0000250}.
ACT_SITE 421 421 Nucleophile. {ECO:0000250}.
SITE 72 72 Contributes to redox potential value.
{ECO:0000250}.
SITE 73 73 Contributes to redox potential value.
{ECO:0000250}.
SITE 138 138 Lowers pKa of C-terminal Cys of first
active site. {ECO:0000250}.
SITE 419 419 Contributes to redox potential value.
{ECO:0000250}.
SITE 420 420 Contributes to redox potential value.
{ECO:0000250}.
SITE 482 482 Lowers pKa of C-terminal Cys of second
active site. {ECO:0000250}.
CARBOHYD 127 127 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:23167757}.
CARBOHYD 284 284 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:23167757}.
CARBOHYD 516 516 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:23167757}.
DISULFID 18 18 Interchain.
{ECO:0000269|PubMed:19150607}.
DISULFID 71 74 Redox-active. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
DISULFID 418 421 Redox-active. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
VAR_SEQ 181 183 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_039292.
VARIANT 39 39 P -> S (in dbSNP:rs45455191).
/FTId=VAR_048087.
VARIANT 119 119 T -> R (in dbSNP:rs45614840).
/FTId=VAR_048088.
VARIANT 185 185 E -> K (in dbSNP:rs419949).
/FTId=VAR_048089.
VARIANT 286 286 T -> M (in dbSNP:rs2685127).
/FTId=VAR_048090.
VARIANT 382 382 P -> A (in dbSNP:rs45529833).
/FTId=VAR_048091.
VARIANT 388 388 R -> Q (in dbSNP:rs400037).
/FTId=VAR_048092.
VARIANT 502 502 P -> S (in dbSNP:rs1048786).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:8561901,
ECO:0000269|Ref.1}.
/FTId=VAR_048093.
MUTAGEN 18 18 C->A: Impairs interchain disulfide bridge
formation. {ECO:0000269|PubMed:19150607}.
MUTAGEN 284 284 N->Q: Increases formation of a highly
stable disulfide-bonded PDIA2 dimer.
{ECO:0000269|PubMed:23167757}.
MUTAGEN 364 364 C->A: No effect on interchain disulfide
bridge formation.
{ECO:0000269|PubMed:19150607}.
CONFLICT 96 96 T -> M (in Ref. 7; BAG58339).
{ECO:0000305}.
CONFLICT 484 484 L -> Q (in Ref. 7; BAG58339).
{ECO:0000305}.
SEQUENCE 525 AA; 58206 MW; B741851AA2C40540 CRC64;
MSRQLLPVLL LLLLRASCPW GQEQGARSPS EEPPEEEIPK EDGILVLSRH TLGLALREHP
ALLVEFYAPW CGHCQALAPE YSKAAAVLAA ESMVVTLAKV DGPAQRELAE EFGVTEYPTL
KFFRNGNRTH PEEYTGPRDA EGIAEWLRRR VGPSAMRLED EAAAQALIGG RDLVVIGFFQ
DLQDEDVATF LALAQDALDM TFGLTDRPRL FQQFGLTKDT VVLFKKFDEG RADFPVDEEL
GLDLGDLSRF LVTHSMRLVT EFNSQTSAKI FAARILNHLL LFVNQTLAAH RELLAGFGEA
APRFRGQVLF VVVDVAADNE HVLQYFGLKA EAAPTLRLVN LETTKKYAPV DGGPVTAASI
TAFCHAVLNG QVKPYLLSQE IPPDWDQRPV KTLVGKNFEQ VAFDETKNVF VKFYAPWCTH
CKEMAPAWEA LAEKYQDHED IIIAELDATA NELDAFAVHG FPTLKYFPAG PGRKVIEYKS
TRDLETFSKF LDNGGVLPTE EPPEEPAAPF PEPPANSTMG SKEEL


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