ID A0A091ESI3_CORBR Unreviewed; 615 AA.
AC A0A091ESI3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 13-SEP-2023, entry version 48.
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};
DE Flags: Fragment;
GN ORFNames=N302_15994 {ECO:0000313|EMBL:KFO59264.1};
OS Corvus brachyrhynchos (American crow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Corvoidea; Corvidae;
OC Corvus.
OX NCBI_TaxID=85066 {ECO:0000313|EMBL:KFO59264.1, ECO:0000313|Proteomes:UP000052976};
RN [1] {ECO:0000313|EMBL:KFO59264.1, ECO:0000313|Proteomes:UP000052976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N302 {ECO:0000313|EMBL:KFO59264.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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}.
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DR EMBL; KK718893; KFO59264.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091ESI3; -.
DR STRING; 85066.A0A091ESI3; -.
DR Proteomes; UP000052976; 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:UP000052976};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 8..137
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 139..255
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 475..606
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 176..179
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
FT DISULFID 525..528
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO59264.1"
FT NON_TER 615
FT /evidence="ECO:0000313|EMBL:KFO59264.1"
SQ SEQUENCE 615 AA; 69473 MW; E660BC24C671F49D CRC64;
ESVTKEVDDD GDDDDDEEDD EDDNDSVVKE ENGVLVLNDA NFDTFTADKD TVLLEFYAPW
CGHCKQFAPE YEKIAKTLKE NDPPIPVAKI DATAATSLSS RFDVSGYPTI KILKKGQAVD
YDGSRTEDAI VAKVKEVSDP NWTPPPEATL VLTQDNFDEV VNGADIILVE FYAPWCGHCK
RLAPEYEKAA QELSKRTPPI PLAKVDATAE TELAKKFDVT GYPTLKIFRK GKPYDYSGPR
EKYGIVDYMI EQAGPPSKQI QATKQVQEFL RDGDDVIIIG VFSGENDKTY QLYQEAANSL
REDYKFHHTF SNEIAKLLKA SPGKLVVMQP EKFQSKHEPK MHVLNLKDST DGSEIKEHVL
KHALPLVGHR KPSNDAKRYS KRPLVVVYYS VDFGFDYRVA TQYWRGKVLE VAKDFPEYVF
AVSDEEDYSS EIKDLGLLES GEDVNAAILD EGGKKYAMEP EEFDSDVLRQ FVLAFKKGKL
KPIVKSQPVP KNNKGPVKVV VGKTFDTIVM DPKNDVLIEF YAPWCGHCKK LEPVYNELGK
KYKNEKNLII AKMDATANDV TNDHYKVEGF PTIYFAPKDK KNNPIKFEGG DRDLEHLSKF
IEEHATKLSR TKEEL
//
