PDIA2_HUMAN
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 03-AUG-2022, entry version 200.
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 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; Q13087; -.
DR PeptideAtlas; Q13087; -.
DR PRIDE; Q13087; -.
DR ProteomicsDB; 59143; -. [Q13087-1]
DR ProteomicsDB; 59144; -. [Q13087-2]
DR Antibodypedia; 22619; 369 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 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; FPEPRAN; -.
DR OrthoDB; 462118at2759; -.
DR PhylomeDB; Q13087; -.
DR TreeFam; TF106381; -.
DR BRENDA; 5.3.4.1; 2681.
DR PathwayCommons; Q13087; -.
DR SignaLink; Q13087; -.
DR BioGRID-ORCS; 64714; 10 hits in 1062 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 113 other tissues.
DR ExpressionAtlas; Q13087; baseline and differential.
DR Genevisible; Q13087; HS.
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: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 InterPro; IPR005792; Prot_disulphide_isomerase.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 2.
DR SUPFAM; SSF52833; SSF52833; 4.
DR TIGRFAMs; TIGR01130; ER_PDI_fam; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
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
