ID A0A090MY70_STRRB Unreviewed; 619 AA.
AC A0A090MY70;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 63.
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=SRAE_2000133600 {ECO:0000313|EMBL:CEF66669.1,
GN ECO:0000313|WBParaSite:SRAE_2000133600.1,
GN ECO:0000313|WormBase:SRAE_2000133600};
OS Strongyloides ratti (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=34506 {ECO:0000313|EMBL:CEF66669.1};
RN [1] {ECO:0000313|EMBL:CEF66669.1, ECO:0000313|Proteomes:UP000035682}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ED321 {ECO:0000313|Proteomes:UP000035682,
RC ECO:0000313|WBParaSite:SRAE_2000133600.1}, and ED321 Heterogonic
RC {ECO:0000313|EMBL:CEF66669.1};
RA Martin A.A.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:SRAE_2000133600.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (DEC-2020) 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; LN609529; CEF66669.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090MY70; -.
DR STRING; 34506.A0A090MY70; -.
DR EnsemblMetazoa; SRAE_2000133600.1; SRAE_2000133600.1; WBGene00261540.
DR WBParaSite; SRAE_2000133600.1; SRAE_2000133600.1; WBGene00261540.
DR WormBase; SRAE_2000133600; SRP09500; WBGene00261540; -.
DR eggNOG; KOG0190; Eukaryota.
DR OMA; FRSKHEP; -.
DR OrthoDB; 5399045at2759; -.
DR Proteomes; UP000035682; Chromosome X.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000035682};
KW 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..619
FT /note="Protein disulfide-isomerase"
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT /id="PRO_5015017758"
FT DOMAIN 8..115
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 116..241
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 449..595
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 597..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 164..167
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
FT DISULFID 515..518
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
SQ SEQUENCE 619 AA; 70128 MW; 79E05ECD85C11E59 CRC64;
MKILKCLILL SILYSGYAVD VDTDDNVYIL TEANFDDFLE ENPIVMVKFY APWCGHCKKL
APDYATASRH IKFPLAKVDA TIEKALGEKY NVQGYPTIKL FKNGEVLDYN GARDVASIVD
WAEEVTDPNY KPPSNEVVAL TSETFDEFVS DKPLMLVEFY APWCGHCKQL APELEKAASA
LKDENIVIAK VDATVEKKLA DQFGVKGYPT MKVLRNGKRY DYNGPRDSIG IMEYMLKQAE
PAAKKLNSVM EAKRIMKKTD VTIIGFFANE DGPQYNAFFE ASEKVREELP GMGFTTDPDV
IKAFKAQPGD VIIFYPDVFW TKYEEKQKKY NKDASTAEDL LAFLKDNIAP MVGQITQENA
AFRYSKLPLC VVYYNVDFSP EYREGTNYWR NKVVEVAKNY KDSKYTFAVG DEEEFSDELA
NVGLGDSGLE HNVIVFGFDG KKYPMDPEKY DGELDENLEQ FMKDINSGKV KAFIKSSPPP
KHQKGPVKVL VGSTFSSIVD DETKDVLVEF YAPWCGHCKS FEPEYNKLAE KLKKEQPNIV
IAKMDATAND PPSGYKVEGF PTIYFAPSGM KSKPIKYTGN RDLDDLEKFM KKHAVKSYTD
KTEEVEKEDK TKTDKKEEL
//
