PDIA3_CHICK
ID PDIA3_CHICK Reviewed; 505 AA.
AC Q8JG64;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Protein disulfide-isomerase A3;
DE EC=5.3.4.1 {ECO:0000250|UniProtKB:P30101};
DE AltName: Full=Endoplasmic reticulum resident protein 57;
DE Short=ER protein 57;
DE Short=ERp57;
DE AltName: Full=Glucose-regulated thiol oxidoreductase 58 kDa protein;
DE Flags: Precursor;
GN Name=PDIA3; Synonyms=ERP57, GRP58;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=White leghorn; TISSUE=Liver;
RA Gao B.;
RT "The amino-acid sequence of chicken homologue of ERp57.";
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Disulfide isomerase which catalyzes the formation,
CC isomerization, and reduction or oxidation of disulfide bonds.
CC {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 -!- 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; AY122886; AAM82759.1; -; mRNA.
DR RefSeq; NP_989441.1; NM_204110.3.
DR AlphaFoldDB; Q8JG64; -.
DR SMR; Q8JG64; -.
DR BioGRID; 674949; 1.
DR STRING; 9031.ENSGALP00000013574; -.
DR PaxDb; Q8JG64; -.
DR Ensembl; ENSGALT00000013589; ENSGALP00000013574; ENSGALG00000008348.
DR GeneID; 373899; -.
DR KEGG; gga:373899; -.
DR CTD; 2923; -.
DR VEuPathDB; HostDB:geneid_373899; -.
DR eggNOG; KOG0190; Eukaryota.
DR GeneTree; ENSGT00940000155425; -.
DR HOGENOM; CLU_025879_6_0_1; -.
DR InParanoid; Q8JG64; -.
DR OMA; YIAKHAT; -.
DR OrthoDB; 462118at2759; -.
DR PhylomeDB; Q8JG64; -.
DR TreeFam; TF106382; -.
DR Reactome; R-GGA-1236974; ER-Phagosome pathway.
DR Reactome; R-GGA-901042; Calnexin/calreticulin cycle.
DR Reactome; R-GGA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR PRO; PR:Q8JG64; -.
DR Proteomes; UP000000539; Chromosome 10.
DR Bgee; ENSGALG00000008348; Expressed in spermatocyte and 13 other tissues.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0061779; C:Tapasin-ERp57 complex; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IBA:GO_Central.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:Ensembl.
DR GO; GO:0098761; P:cellular response to interleukin-7; IEA:Ensembl.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0002502; P:peptide antigen assembly with MHC class I protein complex; IEA:Ensembl.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central.
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; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 2: Evidence at transcript level;
KW Disulfide bond; Endoplasmic reticulum; Isomerase; Redox-active center;
KW 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_5000088911"
FT DOMAIN 25..131
FT /note="Thioredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 341..483
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 486..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 ACT_SITE 55
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 58
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 404
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 407
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 56
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 57
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 117
FT /note="Lowers pKa of C-terminal Cys of first active site"
FT /evidence="ECO:0000250"
FT SITE 405
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 406
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 469
FT /note="Lowers pKa of C-terminal Cys of second active site"
FT /evidence="ECO:0000250"
FT DISULFID 55..58
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 83..90
FT /evidence="ECO:0000250"
FT DISULFID 404..407
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 505 AA; 56182 MW; 996509BBDC2D000A CRC64;
MSVPRPSRAA LLLLVPLLAL SAGASDVVEL SDADFESGLA ERPGLVLVEF FAPWCGHCKR
LAPEYEAAAT RLKGIVPLVK VDCTANSNTC NKYGVSGYPT LKIFRDGEES GTYDGPRTAD
GIVSHLKKQA GPASVALSSV ADFEKFIGDK DASVVGFFRD ASGDAYSEFM KAANNLRDNY
RFAHTSEEQL VQKYEEDGEG VVLYRPSRLA NKFEDSTVKY TEDKITSAKI KKFIQENIFG
ICPHMTEDNK DLIQGKDLLV AYYDVDYEKN AKGSNYWRNR VMMIAKKFLD AGHKLSFAVA
SRKTFGHELS EFGLDNSVGE APVVAIRTAK GDKFVMQEEF SRDGKALERF LQDYFDGNLK
KYLKSEPVPE NNDGPVKVVV AENFDEIVNA EDKDVLIEFY APWCGHCKNL EPKYKELGEK
LSKDPNIVIA KMDATANDVP SPYEVRGFPT IYFAPAGKKQ SPKKYEGGRE VSDFISYLKR
EATSTPVLQE EDKAKKSKKK AKEDL
