PDIA2_PONAB
ID PDIA2_PONAB Reviewed; 525 AA.
AC Q5RCH2; Q5R6G7;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Protein disulfide-isomerase A2;
DE EC=5.3.4.1;
DE Flags: Precursor;
GN Name=PDIA2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
CC -!- PTM: The disulfide-linked homodimer exhibits an enhanced chaperone
CC activity. {ECO:0000250}.
CC -!- PTM: Glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR858298; CAH90535.1; -; mRNA.
DR EMBL; CR860523; CAH92649.1; -; mRNA.
DR RefSeq; NP_001125285.1; NM_001131813.1.
DR AlphaFoldDB; Q5RCH2; -.
DR SMR; Q5RCH2; -.
DR STRING; 9601.ENSPPYP00000007818; -.
DR PRIDE; Q5RCH2; -.
DR GeneID; 100172183; -.
DR KEGG; pon:100172183; -.
DR CTD; 64714; -.
DR eggNOG; KOG0190; Eukaryota.
DR InParanoid; Q5RCH2; -.
DR OrthoDB; 462118at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Chaperone; Disulfide bond; Endoplasmic reticulum; Glycoprotein; Isomerase;
KW Lipid-binding; Redox-active center; Reference proteome; Repeat; Signal;
KW Steroid-binding.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..525
FT /note="Protein disulfide-isomerase A2"
FT /id="PRO_0000034223"
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 498..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:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 516
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 18
FT /note="Interchain"
FT /evidence="ECO:0000250"
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 CONFLICT 342
FT /note="E -> G (in Ref. 1; CAH92649)"
FT /evidence="ECO:0000305"
FT CONFLICT 485
FT /note="G -> E (in Ref. 1; CAH92649)"
FT /evidence="ECO:0000305"
FT CONFLICT 505
FT /note="E -> G (in Ref. 1; CAH92649)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 525 AA; 58124 MW; 0C402549E70D3F32 CRC64;
MSCQLLPVLL LLLLRASCPW GHEQGPRSPS EEPPEEEIPK EDGILVLSRH TLGLALREHP
ALLVEFYAPW CGHCQALAPE YSKAAAVLAA ESSVVMLAKV DGPAQPELAE EFGVTEYPTL
KFFRDGNRTH PEEYTGPREA EGIAEWLRRR VGPSAMRLED EAAAQALIDG RDLVVIGFFQ
DLHDEDVATF LALAQDALDM TFGLTDRPQL FQQFGLTKDT VVLFKKFDEG RADFPVDEEL
GLDLGDLSRF LVTHSMRLVT EFNSQTSAKI FAARILNHLL LFVNQTLAAH RELLVGFGEA
APHFRGQVLF VVVDVAADNE HVLQYFGLKA EAAPTLRLVN LETTKKYAPV DGGPVTTASI
TAFCHAVLNG QVKPYLLSQE VPPDWDQRPV KTLVGKNFEQ VAFDETKNVF VKFYAPWCTH
CKEMAPAWEA LAEKYQDHED VIIAELDATA NELDAFAVHG FPTLKYFPAG PGRKVIEYKS
TRDLGTFSKF LDNGGVLPTE EPLEEPAAPF PEPPANSTMG SKEEL
