ID A0A091JVM0_COLST Unreviewed; 425 AA.
AC A0A091JVM0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
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=N325_08768 {ECO:0000313|EMBL:KFP28146.1};
OS Colius striatus (Speckled mousebird).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Coliiformes; Coliidae; Colius.
OX NCBI_TaxID=57412 {ECO:0000313|EMBL:KFP28146.1, ECO:0000313|Proteomes:UP000053615};
RN [1] {ECO:0000313|EMBL:KFP28146.1, ECO:0000313|Proteomes:UP000053615}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N325 {ECO:0000313|EMBL:KFP28146.1};
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; KK531416; KFP28146.1; -; Genomic_DNA.
DR RefSeq; XP_010206154.1; XM_010207852.1.
DR AlphaFoldDB; A0A091JVM0; -.
DR GeneID; 104561969; -.
DR KEGG; csti:104561969; -.
DR CTD; 2923; -.
DR OrthoDB; 5399045at2759; -.
DR Proteomes; UP000053615; 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:UP000053615};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 261..403
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP28146.1"
FT NON_TER 425
FT /evidence="ECO:0000313|EMBL:KFP28146.1"
SQ SEQUENCE 425 AA; 47628 MW; 270EDB2BD63B9009 CRC64;
VDCTANSNTC NKYGVSGYPT LKIFRDGEEA GTYDGPRTAD GIVSHLKKQA GPASVALSSV
ADFEKFIGDK DASVVGFFAD ASGDAYSEFV KAANNLRDNY RFAHTSEEQL VQKYEEDGEG
IVLFRPPRLA NKFEDSSIKY PEDKVTSGKI KKFIQENIFG ICPHMTEDNK DLIQGKDLLV
AYYDVDYEKN AKGSNYWRNR VMMIAKKFLD AGHKLSFAVA SRKTFAHELS EFGLDSSVGE
APVVAIRTAK GEKYVMQEEF SRDGKALERF LQDYFDGNLK KYLKSEPIPD SNDGPVKVVV
AENFDEIVNA EDKDVLIEFY APWCGHCKNL EPKYKELGEK LSKDPNIIIA KMDATANDVP
SPYEVRGFPT IYFAPAGKKQ NPKKYEGGRE VSDFISYLKR EATNTPVLQE EDKAKKSKKK
VKEDL
//