ID A0A183GY87_9BILA Unreviewed; 630 AA.
AC A0A183GY87;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 13-SEP-2023, entry version 42.
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 ORFNames=OFLC_LOCUS197 {ECO:0000313|EMBL:VDO24938.1};
OS Onchocerca flexuosa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX NCBI_TaxID=387005 {ECO:0000313|Proteomes:UP000050787, ECO:0000313|WBParaSite:OFLC_0000019601-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:OFLC_0000019601-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDO24938.1, ECO:0000313|Proteomes:UP000267606}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000256|ARBA:ARBA00006347, ECO:0000256|RuleBase:RU004208}.
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DR EMBL; UZAJ01000053; VDO24938.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A183GY87; -.
DR STRING; 387005.A0A183GY87; -.
DR WBParaSite; OFLC_0000019601-mRNA-1; OFLC_0000019601-mRNA-1; OFLC_0000019601.
DR Proteomes; UP000050787; Unplaced.
DR Proteomes; UP000267606; 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; cd02961; PDI_a_family; 2.
DR CDD; cd02995; PDI_a_PDI_a'_C; 1.
DR CDD; cd03073; PDI_b'_ERp72_ERp57; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 5.
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; 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; PR00312; CALSEQUESTRN.
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}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361130}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT CHAIN 19..630
FT /note="Protein disulfide-isomerase"
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT /id="PRO_5033791510"
FT DOMAIN 12..130
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 132..246
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 506..621
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DISULFID 170..173
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
FT DISULFID 542..545
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
SQ SEQUENCE 630 AA; 72303 MW; B793CD8B2045D6DD CRC64;
MLLRVILILP YLFQCVSAEE SEFEQDDGIF VLNERNFMSF LQQHPTTLVK FYAPWCGHCK
ALAPEYAKAA KKVKVPLAKV DATIETNLAK TCFSYNIEGF PTLKFWQNGE DPIDYDGGRE
SDEIVKWISE KTDPTYKPPP SVVTKLTKEE FTEFITLHQL VLVKFYAPWC GHCKKLAPEY
EKAAKILKDK GIMLAEVDST VEQSLSADFN VTGYPKLYIF RNSKKFDYKG PRDAEGIVRY
MLEQSEPALR KITSVKEAQR FMRKDDVTVI GFFSNEKAEL LDSLNDAAEM MRNDFSIAVC
LEADLKKHFE IDSDQIVIFF PEIYWSKYEP KQIVYKKAYV FSYYFPAIEL SAFGNQYLQE
VSTVEDLVTF IRENSTPLVG HRTKKNVATR YIQFPLVVVY YNVDFSLEYR EGTQYWRKKV
LEIASQYRKD KYHFAISDEN EFADELAAVG LGDSGLEHNV LVFGNDGKKY PMRPNEFDGE
LTENLSAFMK KLSSGQIKSF VKSAPLPKND KNPVKTVVAL NFAQVVFDET KDVLVELYAP
WCGHCKAFES KYKELAMKLK SESNVLLVKI DATANDIPTN YAVSGFPTIY FAPVGRKKEP
IKYEGNRDLD DLIDFMKKHA SVSFRSKDEL
//