PDIA3_PONAB
ID PDIA3_PONAB Reviewed; 505 AA.
AC Q5RDG4;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Protein disulfide-isomerase A3;
DE EC=5.3.4.1 {ECO:0000250|UniProtKB:P30101};
DE Flags: Precursor;
GN Name=PDIA3;
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: Disulfide isomerase which catalyzes the formation,
CC isomerization, and reduction or oxidation of disulfide bonds (By
CC similarity). Associates with calcitriol, the active form of vitamin D3
CC which mediates the action of this vitamin on cells (By similarity).
CC Association with calcitriol does not affect its enzymatic activity (By
CC similarity). {ECO:0000250|UniProtKB:P30101}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC EC=5.3.4.1; Evidence={ECO:0000250|UniProtKB:P30101};
CC -!- SUBUNIT: Subunit of the TAP complex, also known as the peptide loading
CC complex (PLC). Can form disulfide-linked heterodimers with TAPBP.
CC Interacts with ERP27 and CANX (By similarity). Interacts with MZB1 in a
CC calcium-dependent manner (By similarity). Interacts with SERPINA2 and
CC with the S and Z variants of SERPINA1. Interacts with ATP2A2 (By
CC similarity). {ECO:0000250|UniProtKB:P27773,
CC ECO:0000250|UniProtKB:P30101}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P30101}. Endoplasmic reticulum lumen
CC {ECO:0000250}. Melanosome {ECO:0000250|UniProtKB:P30101}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
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DR EMBL; CR857946; CAH90193.1; -; mRNA.
DR RefSeq; NP_001127250.1; NM_001133778.1.
DR AlphaFoldDB; Q5RDG4; -.
DR BMRB; Q5RDG4; -.
DR SMR; Q5RDG4; -.
DR STRING; 9601.ENSPPYP00000007276; -.
DR PRIDE; Q5RDG4; -.
DR GeneID; 100174305; -.
DR KEGG; pon:100174305; -.
DR CTD; 2923; -.
DR eggNOG; KOG0190; Eukaryota.
DR InParanoid; Q5RDG4; -.
DR OrthoDB; 462118at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC.
DR CDD; cd03069; PDI_b_ERp57; 1.
DR InterPro; IPR005788; Disulphide_isomerase.
DR InterPro; IPR041868; PDIA3_PDI_b.
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 TIGRFAMs; TIGR01126; pdi_dom; 2.
DR PROSITE; PS00194; THIOREDOXIN_1; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 2: Evidence at transcript level;
KW Acetylation; Disulfide bond; Endoplasmic reticulum; Isomerase; Methylation;
KW Phosphoprotein; Redox-active center; Reference proteome; Repeat; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..505
FT /note="Protein disulfide-isomerase A3"
FT /id="PRO_0000292595"
FT DOMAIN 25..133
FT /note="Thioredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 343..485
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 484..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 502..505
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000250"
FT COMPBIAS 489..505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 57
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 60
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 406
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 409
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 58
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 59
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 119
FT /note="Lowers pKa of C-terminal Cys of first active site"
FT /evidence="ECO:0000250"
FT SITE 407
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 408
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 471
FT /note="Lowers pKa of C-terminal Cys of second active site"
FT /evidence="ECO:0000250"
FT MOD_RES 61
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P30101"
FT MOD_RES 129
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P27773"
FT MOD_RES 152
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P27773"
FT MOD_RES 218
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P27773"
FT MOD_RES 252
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P27773"
FT MOD_RES 319
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P30101"
FT MOD_RES 362
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P27773"
FT MOD_RES 494
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P27773"
FT DISULFID 57..60
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 57
FT /note="Interchain (with C-115 in TAPBP); in linked form"
FT /evidence="ECO:0000250"
FT DISULFID 85..92
FT /evidence="ECO:0000250"
FT DISULFID 406..409
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 505 AA; 56782 MW; 529E5B6692D0D7E9 CRC64;
MRLRRLALFP GVALLLAAAR LAAASDVLEL TDDNFESRIS DTGSAGLMLV EFFAPWCGHC
KRLAPEYEAA ATRLKGIVPL AKVDCTANTN TCNKYGVSGY PTLKIFRDGE EAGAYDGPRT
ADGIVSHLKK QAGPASVPLR TEEEFKKFIS DKDASIVGFF DDSFSEAHSE FLKAASNLRD
NYRFAHTNVE SLVNEYDDNG EGIILFRPSH LTNKFEDKTV AYTEQKMTSG KIKKFIQENI
FGICPHMTED NKDLIQGKDL LIAYYDVDYE KNAKGSNYWR NRVMMVAKKF LDAGHKLNFA
VASRKTFSHE LSDFGLESTA GEIPVVAIRT AKGEKFVMQE EFSRDGKALE RFLQDYFDGN
LKRYLKSEPI PESNDGPVKV VVAENFDEIV NNENKDVLIE FYAPWCGHCK NLEPKYKELG
EKLSKDPNIV IAKMDATAND VPSPYEVRGF PTIYFSPANK KLNPKKYEGG RELSDFISYL
QREATNPPVI QEEKPKKKKK AQEDL
