ID A0A212FGT6_DANPL Unreviewed; 487 AA.
AC A0A212FGT6;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
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};
GN Name=LOC116778961 {ECO:0000313|RefSeq:XP_032528964.1};
GN ORFNames=KGM_215686 {ECO:0000313|EMBL:OWR52961.1};
OS Danaus plexippus plexippus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Nymphalidae; Danainae; Danaini; Danaina; Danaus; Danaus.
OX NCBI_TaxID=278856 {ECO:0000313|EMBL:OWR52961.1, ECO:0000313|Proteomes:UP000007151};
RN [1] {ECO:0000313|EMBL:OWR52961.1, ECO:0000313|Proteomes:UP000007151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F-2 {ECO:0000313|EMBL:OWR52961.1};
RX PubMed=22118469; DOI=10.1016/j.cell.2011.09.052;
RA Zhan S., Merlin C., Boore J.L., Reppert S.M.;
RT "The monarch butterfly genome yields insights into long-distance
RT migration.";
RL Cell 147:1171-1185(2011).
RN [2] {ECO:0000313|EMBL:OWR52961.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=F-2 {ECO:0000313|EMBL:OWR52961.1};
RA Zhan S., Reppert S.M.;
RT "MonarchBase: the monarch butterfly genome database.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:XP_032528964.1}
RP IDENTIFICATION.
RG RefSeq;
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 EMBL; AGBW02008594; OWR52961.1; -; Genomic_DNA.
DR RefSeq; XP_032528964.1; XM_032673073.1.
DR STRING; 278856.A0A212FGT6; -.
DR EnsemblMetazoa; XM_032673073.1; XP_032528964.1; LOC116778961.
DR KEGG; dpl:KGM_215686; -.
DR eggNOG; KOG0190; Eukaryota.
DR OrthoDB; 5399045at2759; -.
DR Proteomes; UP000007151; Unassembled WGS sequence.
DR Proteomes; UP000596680; Chromosome 4.
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; cd02997; PDI_a_PDIR; 1.
DR CDD; cd03073; PDI_b'_ERp72_ERp57; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 4.
DR InterPro; IPR046374; PDI_a_PDIR.
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; 2.
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; 2.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000007151};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361130}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT CHAIN 20..487
FT /note="Protein disulfide-isomerase"
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT /id="PRO_5041471809"
FT DOMAIN 5..131
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 341..470
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DISULFID 51..54
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
FT DISULFID 391..394
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
SQ SEQUENCE 487 AA; 54736 MW; EB957A399BFEFA18 CRC64;
MLGSIKIFLL LGVIYLCKAS EEDVLELTDS DFESAIGQHE TALVMFYAPW CGHCKRLKPE
YAVAAGILKD DDPPVALAKV DCTEAGKSTC EKFSVSGYPT LKIFRKGELS QEYNGPRESN
GIVKYMRAQV GPSSKELLNV ESFENMISKD EVVVIGFFEK EDDLKGEFLK TADKMREEVS
FAHSSAKDVL EKSGYKNNVV LYRPKRLQNK FEDSFVVYKS GVSLKGFIKE NYHGLVGIRQ
KDNMNDFSNP LVVAYYDVDY VKNPKGTNYW RNRVLKVAKE MKDVNFAVSD KDDFTHELND
FGIDFAKGDK PVVGGKDADG NKFVMSSEFS IENLLAFAKD LLDGKLEPFI KSEPVPENND
GPVKVAVGKN FKELVTDSGR DALVEFYAPW CGHCQKLAPV WEELGEKLKD EDVDIVKIDA
TANDWPKSLY DVSGFPTIFW KPKDNSKKPV RYNGGRALED FVKYVSDNAS NELKGFDRKG
NAKKDEL
//
