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Database: UniProt
Entry: A0A0R3VX09_TAEAS
LinkDB: A0A0R3VX09_TAEAS
Original site: A0A0R3VX09_TAEAS 
ID   A0A0R3VX09_TAEAS        Unreviewed;       483 AA.
AC   A0A0R3VX09;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 46.
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=TASK_LOCUS1954 {ECO:0000313|EMBL:VDK24008.1};
OS   Taenia asiatica (Asian tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Taeniidae; Taenia.
OX   NCBI_TaxID=60517 {ECO:0000313|Proteomes:UP000046400, ECO:0000313|WBParaSite:TASK_0000195301-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:TASK_0000195301-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDK24008.1, ECO:0000313|Proteomes:UP000282613}
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; UYRS01000776; VDK24008.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R3VX09; -.
DR   STRING; 60517.A0A0R3VX09; -.
DR   WBParaSite; TASK_0000195301-mRNA-1; TASK_0000195301-mRNA-1; TASK_0000195301.
DR   Proteomes; UP000046400; Unplaced.
DR   Proteomes; UP000282613; 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; 1.
DR   CDD; cd02995; PDI_a_PDI_a'_C; 1.
DR   CDD; cd02982; PDI_b'_family; 1.
DR   CDD; cd02981; PDI_b_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 4.
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:SF246; PROTEIN DISULFIDE-ISOMERASE; 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:UP000282613};
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..483
FT                   /note="Protein disulfide-isomerase"
FT                   /evidence="ECO:0000256|RuleBase:RU361130"
FT                   /id="PRO_5033766137"
FT   DOMAIN          7..130
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          329..470
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DISULFID        52..55
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
FT   DISULFID        393..396
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
SQ   SEQUENCE   483 AA;  55250 MW;  C1F8C98A02D32978 CRC64;
     MFGSVFAFGV LAFLSVVLSD DTSKVIVLTE SNFDEIISTH KYVLVEFYAP WCGHCQRLEP
     EYNRASILLD EENSEIRLAK VDATKETGLA SKYEVGGYPT LKLFREGSPI EFDGERSAEG
     IVSWLRRKTG PAVLTVESAD EYEAIVEKNK FLVIGITDNT ESEEWKVFHT VASDSDEVYV
     RPTVKSVLDH FKYKDGVMVV IVRKFDDPVV VYEGKMTVDE LSKFIKTEKV PLVTEFNEES
     AVVVFSSDIK RHIIVFMRKS DDAYQPYMDV LRQVAIEFRG RAHVVHIDVD DENHERILSF
     FAIKKEECPT YRVIELDDSV VKFKPDVLEF TFDSMRAFTN DAIERKIKPY LQSDDIPNDW
     DSEPVKVLVG KNFDSVARDP SKAVFVEFYA PWCGHCKQLK PLWDQLGEAY KDHPEVIIAK
     MDATTNEVEN IKIGSFPTIK LFPKNSDDVI DYTGDRTVDA FKKFIQKEGK ITKPVEEIVK
     EEL
//
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