ID A0A0Q3MB78_AMAAE Unreviewed; 647 AA.
AC A0A0Q3MB78;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 13-SEP-2023, entry version 41.
DE RecName: Full=Protein disulfide-isomerase {ECO:0000256|ARBA:ARBA00012723, ECO:0000256|RuleBase:RU361130};
DE EC=5.3.4.1 {ECO:0000256|ARBA:ARBA00012723, ECO:0000256|RuleBase:RU361130};
GN ORFNames=AAES_98721 {ECO:0000313|EMBL:KQK79917.1};
OS Amazona aestiva (Blue-fronted Amazon parrot).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona.
OX NCBI_TaxID=12930 {ECO:0000313|EMBL:KQK79917.1, ECO:0000313|Proteomes:UP000051836};
RN [1] {ECO:0000313|EMBL:KQK79917.1, ECO:0000313|Proteomes:UP000051836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FVVF132 {ECO:0000313|EMBL:KQK79917.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC EC=5.3.4.1; Evidence={ECO:0000256|ARBA:ARBA00001182,
CC ECO:0000256|RuleBase:RU361130};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000256|ARBA:ARBA00004319}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000256|ARBA:ARBA00006347, ECO:0000256|RuleBase:RU004208}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQK79917.1}.
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DR EMBL; LMAW01002558; KQK79917.1; -; Genomic_DNA.
DR STRING; 12930.A0A0Q3MB78; -.
DR Proteomes; UP000051836; Unassembled WGS sequence.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC.
DR CDD; cd02961; PDI_a_family; 2.
DR CDD; cd02995; PDI_a_PDI_a'_C; 1.
DR CDD; cd03073; PDI_b'_ERp72_ERp57; 1.
DR CDD; cd03068; PDI_b_ERp72; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 5.
DR InterPro; IPR005788; PDI_thioredoxin-like_dom.
DR InterPro; IPR041866; PDIA4_PDI_b.
DR InterPro; IPR005792; Prot_disulphide_isomerase.
DR InterPro; IPR017068; Protein_diS-isomerase_A4.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR01130; ER_PDI_fam; 1.
DR NCBIfam; TIGR01126; pdi_dom; 3.
DR PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1.
DR PANTHER; PTHR18929:SF210; PROTEIN DISULFIDE-ISOMERASE A4; 1.
DR Pfam; PF00085; Thioredoxin; 3.
DR Pfam; PF13848; Thioredoxin_6; 1.
DR PIRSF; PIRSF036862; Disulphide_isom_A4; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 5.
DR PROSITE; PS00194; THIOREDOXIN_1; 3.
DR PROSITE; PS51352; THIOREDOXIN_2; 3.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR605792-51};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU361130};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|PIRSR:PIRSR605792-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000051836};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361130}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT CHAIN 28..647
FT /note="Protein disulfide-isomerase"
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT /id="PRO_5005965298"
FT DOMAIN 16..171
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 173..334
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 507..638
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 29..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..60
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 208..211
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
FT DISULFID 557..560
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
SQ SEQUENCE 647 AA; 72835 MW; 67470F64CAB83377 CRC64;
MRPSGLWVLL LLLGLAQVAL LARGAAAEEN GDDESVIKET DDDSDDDDDD DEDDEDDSEV
KEEXXVLILN DANFDTFTAD KDTVLLEFYA PWCGHCKQFA PEYEKIAKTL KDNDPPIPVA
KIDATAATSL ASRFDVSGYP TIKILKKGQP VDYDGSRTED AIVAKVKEVS DPSWTPPPEA
TLVLTQDNFD EVVNDADIIL VEFYAPWCGH CKRLAPEYEK AAQELSKRTP PIPLAKVDAT
AETELAKKFD VTGYPTLKIF RKGKAYDYSG PREKYGIVDY MIEQAGPPSK QIQAAKQVQE
FLKDGDDVII IGVFSGETDK AYQLYQEAAN GLREDYKFHH TFSNEIAKLL KASPGTVVVM
QPEKFQSKHE PKMRVLDLKD STNESEIKEH VIKYALPLVG HRKPSNDAKR YAKHPLVVVY
YSVDFSFDYR VATQYWXGKV LEVAKDFPEY VFAVSDEEDY SSEIKDLGLL ESGEDVNVAI
LDEGGKKYAM EPEEFDSDVL RQFVMAFKKG KLKPIVKSQP VPKNNKGPVK VVVGKTFDTI
VMDPKNDVLI EFYAPWCGHC KKLEPVYNEL GKKYKNEKNL IIAKMDATAN DVTSDRYKVE
GFPTIYFAPK DKKNNPIKFE GGDRDLEHLS KFIEEHATKL SRTKEEL
//
