ID   PDIA2_HUMAN             Reviewed;         525 AA.
AC   Q13087; A6ZJ64; B4DI27; Q2WGM4; Q4TT67; Q6B010; Q96KJ6; Q9BW95;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 2.
DT   27-MAR-2024, entry version 209.
DE   RecName: Full=Protein disulfide-isomerase A2;
DE            EC=5.3.4.1;
DE   AltName: Full=Pancreas-specific protein disulfide isomerase;
DE            Short=PDIp;
DE   Flags: Precursor;
GN   Name=PDIA2; Synonyms=PDIP;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-502.
RA   Hayashi A., Tabata Y., Sato S., Mitsuyama M., Kanai S., Furuya T.,
RA   Saito T.;
RT   "A human polycistronic mRNA composed of ARHGDIG and PDIP.";
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11157797; DOI=10.1093/hmg/10.4.339;
RA   Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C.,
RA   Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.;
RT   "Sequence, structure and pathology of the fully annotated terminal 2 Mb of
RT   the short arm of human chromosome 16.";
RL   Hum. Mol. Genet. 10:339-352(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA   Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA   Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA   Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA   Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA   Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA   Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA   Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA   Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA   Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA   Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA   Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA   Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA   Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA   Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA   Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA   Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA   DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA   Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA   Myers R.M., Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-525 (ISOFORM 1), AND VARIANT
RP   SER-502.
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 16-525 (ISOFORM 1), TISSUE SPECIFICITY, AND
RP   VARIANT SER-502.
RC   TISSUE=Pancreas;
RX   PubMed=8561901; DOI=10.1089/dna.1996.15.9;
RA   Desilva M.G., Lu J., Donadel G., Modi W.S., Xie H., Notkins A.L., Lan M.S.;
RT   "Characterization and chromosomal localization of a new protein disulfide
RT   isomerase, PDIp, highly expressed in human pancreas.";
RL   DNA Cell Biol. 15:9-16(1996).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 20-525 (ISOFORM 1).
RC   TISSUE=Corpus callosum;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [8]
RP   TISSUE SPECIFICITY, AND GLYCOSYLATION.
RX   PubMed=9115635; DOI=10.1089/dna.1997.16.269;
RA   Desilva M.G., Notkins A.L., Lan M.S.;
RT   "Molecular characterization of a pancreas-specific protein disulfide
RT   isomerase, PDIp.";
RL   DNA Cell Biol. 16:269-274(1997).
RN   [9]
RP   COMPONENT OF A CHAPERONE COMPLEX.
RX   PubMed=12475965; DOI=10.1091/mbc.e02-05-0311;
RA   Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.;
RT   "A subset of chaperones and folding enzymes form multiprotein complexes in
RT   endoplasmic reticulum to bind nascent proteins.";
RL   Mol. Biol. Cell 13:4456-4469(2002).
RN   [10]
RP   FUNCTION, SUBUNIT, DISULFIDE BOND, AND MUTAGENESIS OF CYS-18 AND CYS-364.
RX   PubMed=19150607; DOI=10.1016/j.abb.2008.12.021;
RA   Fu X., Zhu B.T.;
RT   "Human pancreas-specific protein disulfide isomerase homolog (PDIp) is
RT   redox-regulated through formation of an inter-subunit disulfide bond.";
RL   Arch. Biochem. Biophys. 485:1-9(2009).
RN   [11]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=19429457; DOI=10.1016/j.jsbmb.2009.02.008;
RA   Fu X.M., Zhu B.T.;
RT   "Human pancreas-specific protein disulfide isomerase homolog (PDIp) is an
RT   intracellular estrogen-binding protein that modulates estrogen levels and
RT   actions in target cells.";
RL   J. Steroid Biochem. Mol. Biol. 115:20-29(2009).
RN   [12]
RP   GLYCOSYLATION AT ASN-127; ASN-284 AND ASN-516, AND MUTAGENESIS OF ASN-284.
RX   PubMed=23167757; DOI=10.1111/febs.12063;
RA   Walker A.K., Soo K.Y., Levina V., Talbo G.H., Atkin J.D.;
RT   "N-linked glycosylation modulates dimerization of protein disulfide
RT   isomerase family A member 2 (PDIA2).";
RL   FEBS J. 280:233-243(2013).
CC   -!- FUNCTION: Acts as an intracellular estrogen-binding protein. May be
CC       involved in modulating cellular levels and biological functions of
CC       estrogens in the pancreas. May act as a chaperone that inhibits
CC       aggregation of misfolded proteins. {ECO:0000269|PubMed:19150607,
CC       ECO:0000269|PubMed:19429457}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC         EC=5.3.4.1;
CC   -!- SUBUNIT: Monomer; predominantly as monomer under reducing conditions.
CC       Homodimer; disulfide-linked. Part of a large chaperone multiprotein
CC       complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6,
CC       PPIB, SDF2L1, UGGT1 and very small amounts of ERP29, but not, or at
CC       very low levels, CALR nor CANX. {ECO:0000269|PubMed:19150607}.
CC   -!- INTERACTION:
CC       Q13087; P59990: KRTAP12-1; NbExp=3; IntAct=EBI-1752525, EBI-10210845;
CC       Q13087; Q3LI64: KRTAP6-1; NbExp=3; IntAct=EBI-1752525, EBI-12111050;
CC       Q13087; P16333: NCK1; NbExp=3; IntAct=EBI-1752525, EBI-389883;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC       ProRule:PRU10138}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q13087-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q13087-2; Sequence=VSP_039292;
CC   -!- TISSUE SPECIFICITY: Highly expressed in pancreas (at protein level).
CC       {ECO:0000269|PubMed:19429457, ECO:0000269|PubMed:8561901,
CC       ECO:0000269|PubMed:9115635}.
CC   -!- PTM: The disulfide-linked homodimer exhibits an enhanced chaperone
CC       activity.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:23167757,
CC       ECO:0000269|PubMed:9115635}.
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC50401.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
CC       Sequence=AAH75029.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
CC       Sequence=BAG58339.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB127078; BAE48734.1; -; mRNA.
DR   EMBL; AE006463; AAK61223.1; -; Genomic_DNA.
DR   EMBL; Z69667; CAI95586.1; -; Genomic_DNA.
DR   EMBL; Z69667; CAO78188.1; -; Genomic_DNA.
DR   EMBL; CH471112; EAW85838.1; -; Genomic_DNA.
DR   EMBL; BC000537; AAH00537.2; -; mRNA.
DR   EMBL; BC075029; AAH75029.1; ALT_SEQ; mRNA.
DR   EMBL; U19948; AAC50401.1; ALT_SEQ; mRNA.
DR   EMBL; AK295383; BAG58339.1; ALT_INIT; mRNA.
DR   CCDS; CCDS42089.1; -. [Q13087-1]
DR   RefSeq; NP_006840.2; NM_006849.2. [Q13087-1]
DR   AlphaFoldDB; Q13087; -.
DR   SMR; Q13087; -.
DR   BioGRID; 122240; 25.
DR   IntAct; Q13087; 12.
DR   MINT; Q13087; -.
DR   STRING; 9606.ENSP00000219406; -.
DR   ChEMBL; CHEMBL4739853; -.
DR   GlyConnect; 1655; 6 N-Linked glycans (1 site).
DR   GlyCosmos; Q13087; 3 sites, 8 glycans.
DR   GlyGen; Q13087; 3 sites, 8 N-linked glycans (1 site).
DR   iPTMnet; Q13087; -.
DR   PhosphoSitePlus; Q13087; -.
DR   BioMuta; PDIA2; -.
DR   DMDM; 21264492; -.
DR   MassIVE; Q13087; -.
DR   MaxQB; Q13087; -.
DR   PaxDb; 9606-ENSP00000219406; -.
DR   PeptideAtlas; Q13087; -.
DR   ProteomicsDB; 59143; -. [Q13087-1]
DR   ProteomicsDB; 59144; -. [Q13087-2]
DR   Antibodypedia; 22619; 413 antibodies from 30 providers.
DR   DNASU; 64714; -.
DR   Ensembl; ENST00000219406.11; ENSP00000219406.7; ENSG00000185615.16. [Q13087-1]
DR   Ensembl; ENST00000404312.5; ENSP00000384410.1; ENSG00000185615.16. [Q13087-2]
DR   GeneID; 64714; -.
DR   KEGG; hsa:64714; -.
DR   MANE-Select; ENST00000219406.11; ENSP00000219406.7; NM_006849.4; NP_006840.2.
DR   UCSC; uc002cgo.2; human. [Q13087-1]
DR   AGR; HGNC:14180; -.
DR   CTD; 64714; -.
DR   DisGeNET; 64714; -.
DR   GeneCards; PDIA2; -.
DR   HGNC; HGNC:14180; PDIA2.
DR   HPA; ENSG00000185615; Tissue enriched (pancreas).
DR   MIM; 608012; gene.
DR   neXtProt; NX_Q13087; -.
DR   OpenTargets; ENSG00000185615; -.
DR   PharmGKB; PA33153; -.
DR   VEuPathDB; HostDB:ENSG00000185615; -.
DR   eggNOG; KOG0190; Eukaryota.
DR   GeneTree; ENSGT00940000161859; -.
DR   HOGENOM; CLU_025879_1_0_1; -.
DR   InParanoid; Q13087; -.
DR   OMA; FCHSVFS; -.
DR   OrthoDB; 5399045at2759; -.
DR   PhylomeDB; Q13087; -.
DR   TreeFam; TF106381; -.
DR   BRENDA; 5.3.4.1; 2681.
DR   PathwayCommons; Q13087; -.
DR   SignaLink; Q13087; -.
DR   BioGRID-ORCS; 64714; 11 hits in 1138 CRISPR screens.
DR   GenomeRNAi; 64714; -.
DR   Pharos; Q13087; Tbio.
DR   PRO; PR:Q13087; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; Q13087; Protein.
DR   Bgee; ENSG00000185615; Expressed in body of pancreas and 115 other cell types or tissues.
DR   ExpressionAtlas; Q13087; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0015036; F:disulfide oxidoreductase activity; TAS:ParkinsonsUK-UCL.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; TAS:ProtInc.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IDA:UniProtKB.
DR   GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
DR   GO; GO:0070527; P:platelet aggregation; IEA:Ensembl.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0034975; P:protein folding in endoplasmic reticulum; TAS:ParkinsonsUK-UCL.
DR   GO; GO:0006621; P:protein retention in ER lumen; TAS:ProtInc.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central.
DR   CDD; cd02961; PDI_a_family; 1.
DR   CDD; cd02995; PDI_a_PDI_a'_C; 1.
DR   CDD; cd02982; PDI_b'_family; 1.
DR   CDD; cd02981; PDI_b_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 4.
DR   InterPro; IPR005792; Prot_disulphide_isomerase.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   NCBIfam; TIGR01130; ER_PDI_fam; 1.
DR   PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1.
DR   PANTHER; PTHR18929:SF93; PROTEIN DISULFIDE-ISOMERASE A2; 1.
DR   Pfam; PF00085; Thioredoxin; 2.
DR   Pfam; PF13848; Thioredoxin_6; 1.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 4.
DR   PROSITE; PS00014; ER_TARGET; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 2.
DR   PROSITE; PS51352; THIOREDOXIN_2; 2.
DR   Genevisible; Q13087; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chaperone; Disulfide bond; Endoplasmic reticulum;
KW   Glycoprotein; Isomerase; Lipid-binding; Redox-active center;
KW   Reference proteome; Repeat; Signal; Steroid-binding.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..525
FT                   /note="Protein disulfide-isomerase A2"
FT                   /id="PRO_0000034222"
FT   DOMAIN          27..152
FT                   /note="Thioredoxin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DOMAIN          367..496
FT                   /note="Thioredoxin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   REGION          492..525
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           522..525
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   ACT_SITE        71
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        74
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        418
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        421
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   SITE            72
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            73
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            138
FT                   /note="Lowers pKa of C-terminal Cys of first active site"
FT                   /evidence="ECO:0000250"
FT   SITE            419
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            420
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            482
FT                   /note="Lowers pKa of C-terminal Cys of second active site"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        127
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:23167757"
FT   CARBOHYD        284
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:23167757"
FT   CARBOHYD        516
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:23167757"
FT   DISULFID        18
FT                   /note="Interchain"
FT                   /evidence="ECO:0000269|PubMed:19150607"
FT   DISULFID        71..74
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        418..421
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   VAR_SEQ         181..183
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_039292"
FT   VARIANT         39
FT                   /note="P -> S (in dbSNP:rs45455191)"
FT                   /id="VAR_048087"
FT   VARIANT         119
FT                   /note="T -> R (in dbSNP:rs45614840)"
FT                   /id="VAR_048088"
FT   VARIANT         185
FT                   /note="E -> K (in dbSNP:rs419949)"
FT                   /id="VAR_048089"
FT   VARIANT         286
FT                   /note="T -> M (in dbSNP:rs2685127)"
FT                   /id="VAR_048090"
FT   VARIANT         382
FT                   /note="P -> A (in dbSNP:rs45529833)"
FT                   /id="VAR_048091"
FT   VARIANT         388
FT                   /note="R -> Q (in dbSNP:rs400037)"
FT                   /id="VAR_048092"
FT   VARIANT         502
FT                   /note="P -> S (in dbSNP:rs1048786)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:8561901, ECO:0000269|Ref.1"
FT                   /id="VAR_048093"
FT   MUTAGEN         18
FT                   /note="C->A: Impairs interchain disulfide bridge
FT                   formation."
FT                   /evidence="ECO:0000269|PubMed:19150607"
FT   MUTAGEN         284
FT                   /note="N->Q: Increases formation of a highly stable
FT                   disulfide-bonded PDIA2 dimer."
FT                   /evidence="ECO:0000269|PubMed:23167757"
FT   MUTAGEN         364
FT                   /note="C->A: No effect on interchain disulfide bridge
FT                   formation."
FT                   /evidence="ECO:0000269|PubMed:19150607"
FT   CONFLICT        96
FT                   /note="T -> M (in Ref. 7; BAG58339)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        484
FT                   /note="L -> Q (in Ref. 7; BAG58339)"
FT                   /evidence="ECO:0000305"
SQ   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
//