ID A0A0D0BTN6_9AGAM Unreviewed; 503 AA.
AC A0A0D0BTN6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 13-SEP-2023, entry version 47.
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=CY34DRAFT_518279 {ECO:0000313|EMBL:KIK48927.1};
OS Suillus luteus UH-Slu-Lm8-n1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Suillineae; Suillaceae; Suillus.
OX NCBI_TaxID=930992 {ECO:0000313|EMBL:KIK48927.1, ECO:0000313|Proteomes:UP000054485};
RN [1] {ECO:0000313|EMBL:KIK48927.1, ECO:0000313|Proteomes:UP000054485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UH-Slu-Lm8-n1 {ECO:0000313|EMBL:KIK48927.1,
RC ECO:0000313|Proteomes:UP000054485};
RG DOE Joint Genome Institute;
RA Kuo A., Ruytinx J., Rineau F., Colpaert J., Kohler A., Nagy L.G.,
RA Floudas D., Copeland A., Barry K.W., Cichocki N., Veneault-Fourrey C.,
RA LaButti K., Lindquist E.A., Lipzen A., Lundell T., Morin E., Murat C.,
RA Sun H., Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.,
RA Nordberg H.P., Cantor M.N., Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UH-Slu-Lm8-n1 {ECO:0000313|Proteomes:UP000054485};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Participates in the folding of proteins containing disulfide
CC bonds, may be involved in glycosylation, prolyl hydroxylation and
CC triglyceride transfer. {ECO:0000256|ARBA:ARBA00002692}.
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; KN835135; KIK48927.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0BTN6; -.
DR STRING; 930992.A0A0D0BTN6; -.
DR HOGENOM; CLU_025879_5_0_1; -.
DR InParanoid; A0A0D0BTN6; -.
DR OrthoDB; 5399045at2759; -.
DR Proteomes; UP000054485; 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: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:UP000054485};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361130}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT CHAIN 22..503
FT /note="Protein disulfide-isomerase"
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT /id="PRO_5005112159"
FT DOMAIN 10..134
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 345..476
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 478..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 57..60
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
FT DISULFID 395..398
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
SQ SEQUENCE 503 AA; 55077 MW; D41599DCF1BB6A7F CRC64;
MRFSSLVSVA SAIALASLVT AEDAAESSDV LSLTKDTFSS VVNPESLILV EFYAPWCGHC
KALAPHYEEA ATTLKDKDIK LTKVDCVDQA DLCQSHGVQG YPTLKVFRNG ESTDYSGPRK
ADGIISYMLK QSLPAVSDVT ASNLVEFQNA DKLVVLAYVS STTKAPAPEF TATAEKLRDD
YLFGITSDAA AIAAAGVTPP AIVVYRNFDE HVTEYPNPAS AATIPELEAW IQQLSIPILG
EVNGETYAMY AASGKPIGYL FLDPADEKSD ETIAALKPVA AKYRGEIHFV WIDATKFGDH
AKALNLAEPK WPSFVIQRLE DQLKYPYDQS KPIEAEAVSA MVGEYLAGTL LPTLKSQPIP
ETQDGNVFTL VGKQFDEVVY DDSKDVFVEF YATWCGHCKR LTPIWESLGD HFAEVKDQLV
IAKMESTEND LPASAPFRIS GFPTLKFKPA GSREFLEYNG DRELESLVAY VEEHAKNSLK
PAAKAPENDS QATFEAREVH DEL
//
