ID G3ND86_GASAC Unreviewed; 625 AA.
AC G3ND86;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 78.
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 Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000003286.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000003286.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000003286.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; G3ND86; -.
DR Ensembl; ENSGACT00000003297.1; ENSGACP00000003286.1; ENSGACG00000002512.2.
DR GeneTree; ENSGT00940000157738; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000002512; Expressed in mesonephros and 13 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; 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; 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 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:UP000007635};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361130}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT CHAIN 24..625
FT /note="Protein disulfide-isomerase"
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT /id="PRO_5005131709"
FT DOMAIN 24..149
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 153..278
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 485..616
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DISULFID 186..189
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
FT DISULFID 535..538
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
SQ SEQUENCE 625 AA; 69923 MW; AA8BA5E601E348A5 CRC64;
MKKKVALLLL LLGVAHFATL SRCETQTQTI SARELVSCPF SSDVLILTNS NYDPFMEGKD
TVLVEFYAPW CGHCKQFAPE YEKIAQTLKE NDPPIPVAKV DATVAKEIAG RFEVTGYPTI
KIIKNGQPVD YDGPRTEKAI VERVKEVARP DWKPPPEATL VLTKDNFDET VNDADIILVE
FYAPWCGHCK SLAPEYEKAA KELSLRSPPI PLAKVDGTVE NELASRFEVT GFPSIKIFRK
GKAFEYNGPR EHRGIVDYMV AQAGPPSKQV QAVKQVQELI KDGDDAVIVG VFSSDEDTAY
ALYTEASNTL REDFTFLHTF SSEVAKLLKA SPGQIVLVQP ERFASKYEPA SHILKVKDST
LVSEVQEFFK KHAIPLVGHR KPSNDAKRYS KRPLVVVYYG VDFSFDYNLA TQFWRSKVLE
VAKDFPEYTF AIGDEEDYAD ELKGLGLSDS GEDVNVGILA EGGKKFAMEP EEFDADVLRE
FVKAFKKGKL KPIIKSAPVP KNNKGPVKVV VGKTFDDIVM DKEKDVLIEF YAPWCGHCKK
LEPDYLALGK KYKGEKNLVI AKMDATANDV PNEHYATEGF PTIYLAPSNN KQNPIKFEGG
DRTVEGFSKF LEKHSTKLSQ KREEL
//
