ID A0A3P8NY00_ASTCA Unreviewed; 495 AA.
AC A0A3P8NY00;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
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};
OS Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000009676.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000009676.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000009676.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 AlphaFoldDB; A0A3P8NY00; -.
DR Ensembl; ENSACLT00000009900.1; ENSACLP00000009676.1; ENSACLG00000006616.1.
DR GeneTree; ENSGT00940000166438; -.
DR OMA; FRYGRDS; -.
DR OrthoDB; 5399045at2759; -.
DR Proteomes; UP000265100; Chromosome 22.
DR Bgee; ENSACLG00000006616; Expressed in testis and 7 other cell types or tissues.
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; 1.
DR CDD; cd02995; PDI_a_PDI_a'_C; 1.
DR CDD; cd03073; PDI_b'_ERp72_ERp57; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 4.
DR InterPro; IPR005788; PDI_thioredoxin-like_dom.
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:SF45; PROTEIN DISULFIDE-ISOMERASE; 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; 2.
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}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361130}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT CHAIN 26..495
FT /note="Protein disulfide-isomerase"
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT /id="PRO_5017844449"
FT DOMAIN 15..132
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 341..483
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DISULFID 56..59
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
FT DISULFID 404..407
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
SQ SEQUENCE 495 AA; 56149 MW; 548CC5A134626BC4 CRC64;
MAPTLGFFPV VTLVVLSGFP AAVSSRRDVL ELGDADFDYL ATEHETMLVK FYAPWCGHCK
KLAPEFEKAA SRLKGSVQLA KVDCTTNSET CSRFGVSGYP TLRIFRYGKD SAPYDGPRTA
EGIYETMRRQ TGPDSMHLKT KDDLKAFVNN HDASIVGVFS GTDSPRLAEF LKAATLLREQ
FRFAHSTNLQ LAEEHGANSE CVLLFRPPRL ANAFEDSIVI FRDYLTIGSL RRFIRDHIYG
LCPHMTIENR DRLRVRDLLT AYYALDYHHN IPGSNYWRNR VMKVASKYVG RGLTFSIANK
KDFLLELEED FGMGTSDGGE LPFITIRTRL GHKYTMREEF TRDGASLQRF LEDYFAGRLK
RYIKSEPIPE KNSGAVKVVV AESFDQVVND PDKNVLIQFF SPLCPHCKKL EPVYGELAET
LRSDPKIVIA KMNALANDVP LGYDVQGFPT IYFAPVGRKD EPVRYQGTRE LKDFLRFLKR
EASHHLVLSG FKDEL
//