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Database: UniProt
Entry: A0A183GY87_9BILA
LinkDB: A0A183GY87_9BILA
Original site: A0A183GY87_9BILA 
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
//
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