PDIA2_MOUSE
ID PDIA2_MOUSE Reviewed; 527 AA.
AC D3Z6P0; Q14AV9;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Protein disulfide-isomerase A2 {ECO:0000250|UniProtKB:Q13087};
DE EC=5.3.4.1;
DE AltName: Full=PDIp {ECO:0000250|UniProtKB:Q13087};
DE Flags: Precursor;
GN Name=Pdia2 {ECO:0000312|Ensembl:ENSMUSP00000035584,
GN ECO:0000312|MGI:MGI:1916441}; Synonyms=Pdip {ECO:0000250|UniProtKB:Q13087};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000312|Ensembl:ENSMUSP00000035584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAI16672.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [3] {ECO:0000305}
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity).
CC {ECO:0000250|UniProtKB:Q13087}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC EC=5.3.4.1; Evidence={ECO:0000305};
CC -!- SUBUNIT: Part of a large chaperone multiprotein complex comprising
CC DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGGT1
CC and very small amounts of ERP29, but not, or at very low levels, CALR
CC nor CANX. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000250|UniProtKB:Q13087, ECO:0000255|PROSITE-ProRule:PRU10138}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:19468303};
CC IsoId=D3Z6P0-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334};
CC IsoId=D3Z6P0-2; Sequence=VSP_039293;
CC -!- TISSUE SPECIFICITY: Highly expressed in pancreas.
CC {ECO:0000269|PubMed:9115635}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:9115635}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000255}.
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DR EMBL; AC126438; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC116671; AAI16672.1; -; mRNA.
DR CCDS; CCDS37510.1; -. [D3Z6P0-1]
DR RefSeq; NP_001074539.1; NM_001081070.1. [D3Z6P0-1]
DR AlphaFoldDB; D3Z6P0; -.
DR SMR; D3Z6P0; -.
DR BioGRID; 213283; 1.
DR STRING; 10090.ENSMUSP00000035584; -.
DR GlyGen; D3Z6P0; 3 sites.
DR iPTMnet; D3Z6P0; -.
DR PhosphoSitePlus; D3Z6P0; -.
DR MaxQB; D3Z6P0; -.
DR PaxDb; D3Z6P0; -.
DR PeptideAtlas; D3Z6P0; -.
DR PRIDE; D3Z6P0; -.
DR ProteomicsDB; 288078; -. [D3Z6P0-1]
DR ProteomicsDB; 288079; -. [D3Z6P0-2]
DR Antibodypedia; 22619; 369 antibodies from 30 providers.
DR Ensembl; ENSMUST00000039113; ENSMUSP00000035584; ENSMUSG00000024184. [D3Z6P0-1]
DR Ensembl; ENSMUST00000120333; ENSMUSP00000114080; ENSMUSG00000024184. [D3Z6P0-2]
DR GeneID; 69191; -.
DR KEGG; mmu:69191; -.
DR UCSC; uc008bdo.1; mouse. [D3Z6P0-1]
DR UCSC; uc012ans.1; mouse. [D3Z6P0-2]
DR CTD; 64714; -.
DR MGI; MGI:1916441; Pdia2.
DR VEuPathDB; HostDB:ENSMUSG00000024184; -.
DR eggNOG; KOG0190; Eukaryota.
DR GeneTree; ENSGT00940000161859; -.
DR HOGENOM; CLU_025879_1_0_1; -.
DR InParanoid; D3Z6P0; -.
DR OMA; FPEPRAN; -.
DR OrthoDB; 462118at2759; -.
DR PhylomeDB; D3Z6P0; -.
DR TreeFam; TF106381; -.
DR BioGRID-ORCS; 69191; 1 hit in 76 CRISPR screens.
DR ChiTaRS; Pdia2; mouse.
DR PRO; PR:D3Z6P0; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; D3Z6P0; protein.
DR Bgee; ENSMUSG00000024184; Expressed in epithelium of stomach and 65 other tissues.
DR ExpressionAtlas; D3Z6P0; baseline and differential.
DR Genevisible; D3Z6P0; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0003756; F:protein disulfide isomerase activity; TAS:MGI.
DR GO; GO:0015035; F:protein-disulfide reductase activity; ISO:MGI.
DR GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
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; 1.
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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..527
FT /note="Protein disulfide-isomerase A2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000394671"
FT DOMAIN 29..155
FT /note="Thioredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 355..499
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 20..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 524..527
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT ACT_SITE 74
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P07237"
FT ACT_SITE 77
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P07237"
FT ACT_SITE 421
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q13087"
FT ACT_SITE 424
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q13087"
FT SITE 75
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250|UniProtKB:Q13087"
FT SITE 76
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250|UniProtKB:Q13087"
FT SITE 422
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250|UniProtKB:Q13087"
FT SITE 423
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250|UniProtKB:Q13087"
FT SITE 485
FT /note="Lowers pKa of C-terminal Cys of second active site"
FT /evidence="ECO:0000250|UniProtKB:Q13087"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 518
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 74..77
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:Q13087,
FT ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 421..424
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:Q13087,
FT ECO:0000255|PROSITE-ProRule:PRU00691"
FT VAR_SEQ 184..186
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_039293"
SQ SEQUENCE 527 AA; 58316 MW; CF703D296B634441 CRC64;
MDKQLLPVLL LLLGVSGSWG QGEEPGGPSE VLPEEPTGEE VPKEDGILVL NHRTLSLALQ
EHSALMVEFY APWCGHCKEL APEYSKAAAL LAAESAVVTL AKVDGPAEPE LTKEFEVVGY
PTLKFFQNGN RTNPEEYAGP KTAEGIAEWL RRRVGPSATH LEDEEGVQAL MAKWDMVVIG
FFQDLQGKDM ATFLALAKDA LDMTFGFTDQ PQLFEKFGLT KDTVVLFKKF DEGRADFPVD
KETGLDLGDL SRFLVIHSMH LVTEFNSQTS PKIFAAKILN HLLLFVNQTL AQHRELLTDF
REAAPPFRGQ VLFVMVDVAA DNSHVLNYFG LKAEEAPTLR LINVETTKKY APTGVIAITA
ASVAAFCQAV LHGEIKHYLL SQEIPPDWDQ GPVKTLVSKN FEQVAFDETK NVFVKFYAPW
CSHCKEMAPA WEALAEKYKD REDIVIAELD ATANELEAFS VLGYPTLKFF PAGPDRKVID
YKSTRDLETF SKFLDSGGHL PKEEPKEPAA SAPEAQANST LGPKEEL
