ID A0A091HN69_BUCRH Unreviewed; 431 AA.
AC A0A091HN69;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Protein disulfide-isomerase {ECO:0000256|RuleBase:RU361130};
DE EC=5.3.4.1 {ECO:0000256|RuleBase:RU361130};
DE Flags: Fragment;
GN ORFNames=N320_00613 {ECO:0000313|EMBL:KFO88773.1};
OS Buceros rhinoceros silvestris.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Bucerotiformes; Bucerotidae; Buceros.
OX NCBI_TaxID=175836 {ECO:0000313|EMBL:KFO88773.1, ECO:0000313|Proteomes:UP000054064};
RN [1] {ECO:0000313|EMBL:KFO88773.1, ECO:0000313|Proteomes:UP000054064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N320 {ECO:0000313|EMBL:KFO88773.1};
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}. Melanosome
CC {ECO:0000256|ARBA:ARBA00004223}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000256|ARBA:ARBA00006347, ECO:0000256|RuleBase:RU004208}.
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DR EMBL; KL518347; KFO88773.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091HN69; -.
DR Proteomes; UP000054064; 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; cd02995; PDI_a_PDI_a'_C; 1.
DR CDD; cd03073; PDI_b'_ERp72_ERp57; 1.
DR CDD; cd03069; PDI_b_ERp57; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 4.
DR InterPro; IPR005788; PDI_thioredoxin-like_dom.
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 NCBIfam; TIGR01130; ER_PDI_fam; 1.
DR NCBIfam; TIGR01126; pdi_dom; 1.
DR PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1.
DR PANTHER; PTHR18929:SF132; PROTEIN DISULFIDE-ISOMERASE A3; 1.
DR Pfam; PF00085; Thioredoxin; 2.
DR Pfam; PF13848; Thioredoxin_6; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 4.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000054064};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 267..409
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 411..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO88773.1"
FT NON_TER 431
FT /evidence="ECO:0000313|EMBL:KFO88773.1"
SQ SEQUENCE 431 AA; 48343 MW; BBD8467F8A24D8C2 CRC64;
VLLLLQVDCT ANSNTCNKYG VSGYPTLKIF RDGEEAGTYD GPRTADGIVS HLKKQAGPAS
VALNSAAEFE KFIGDKDASV VGFFGDTSSD AYSEFMKAAN NLRDNYRFAH TSEDQLVQKY
EEDGEGVVLF RPPRLTNKFE DSSIKYPDDK ITSGKIKKFI QENIFGICPH MTEDNKDLIQ
GKDLLVAYYD VDYEKNAKGS NYWRNRVMMI AKKFLDAGHK LSFAVASRKT FGHELSEFGL
DSSVGEAPVV AIRTAKGDKY VMQEEFSRDG KALERFLQDY FDGNLKKYLK SEPVPESNDG
PVKVVVAENF DEIVNADDKD VLIEFYAPWC GHCKNLEPKY KELGEKLSKD PNIVIAKMDA
TANDVPSPYE VRGFPTIYFA PAGKKQSPKK YEGGREVSDF ISYLKREATN TPVLQEEDKP
KKSKKKVKED L
//
