ID PDI_ARTBC Reviewed; 523 AA.
AC D4B2L8;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Protein disulfide-isomerase {ECO:0000250|UniProtKB:P07237};
DE EC=5.3.4.1 {ECO:0000250|UniProtKB:P07237};
DE AltName: Full=Allergen Alt a 4 homolog {ECO:0000305};
DE Flags: Precursor;
GN ORFNames=ARB_02626;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
CC -!- FUNCTION: Participates in the folding of proteins containing disulfide
CC bonds, may be involved in glycosylation, prolyl hydroxylation and
CC triglyceride transfer. {ECO:0000250|UniProtKB:P07237}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC EC=5.3.4.1; Evidence={ECO:0000250|UniProtKB:P07237};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
CC -!- ALLERGEN: May cause an allergic reaction in human. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
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DR EMBL; ABSU01000029; EFE30464.1; -; Genomic_DNA.
DR RefSeq; XP_003011104.1; XM_003011058.1.
DR AlphaFoldDB; D4B2L8; -.
DR SMR; D4B2L8; -.
DR STRING; 663331.D4B2L8; -.
DR GeneID; 9523678; -.
DR KEGG; abe:ARB_02626; -.
DR eggNOG; KOG0190; Eukaryota.
DR HOGENOM; CLU_025879_5_0_1; -.
DR OMA; FFGMKKD; -.
DR OrthoDB; 5399045at2759; -.
DR Proteomes; UP000008866; 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; PS00014; ER_TARGET; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 3: Inferred from homology;
KW Allergen; Disulfide bond; Endoplasmic reticulum; Glycoprotein; Isomerase;
KW Redox-active center; Reference proteome; Repeat; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..523
FT /note="Protein disulfide-isomerase"
FT /evidence="ECO:0000255"
FT /id="PRO_5001341173"
FT DOMAIN 24..137
FT /note="Thioredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 344..475
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 478..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 520..523
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT ACT_SITE 59
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P07237"
FT ACT_SITE 62
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P07237"
FT SITE 60
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250|UniProtKB:P07237"
FT SITE 61
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250|UniProtKB:P07237"
FT SITE 122
FT /note="Lowers pKa of C-terminal Cys of first active site"
FT /evidence="ECO:0000250|UniProtKB:P07237"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 59..62
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 394..397
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 523 AA; 57255 MW; 3E846B95D50891F6 CRC64;
MPGVRSLLLA LAGVSLAPAV LAADASTDSS DVHALKTDTF KDFIKEHDLV LAEFYAPWCG
HCKALAPEYE KAATELKSKN IQLAKVDCTE EADLCQEYGV EGYPTLKVFR GLDSHKPYNG
ARKSPAITSY MIKQSLPSVS VVTAENFEEV KSLDKVVVVA FIGEDDKETN KTYTALADSM
RDDVLFAGTS SAELAKKEGV SLPAVVLYKE FDDRKDVYDG KFEAEALKAF IKSSSTPLVG
EVGPETYSGY MSAGIPLAYI FADTAEEREQ YASDFKDLAK KLKGKINFAT IDSKAFGAHA
ANLNLIPEKF PAFAIQDTVS NKKYPFDQEK KLTKQDITKF VEGVIAGDIA PSVKSEAVPE
TNDGPVTVIV AHTYEEIVMN KDKDVLVEFY APWCGHCKAL APKYDQLGSL YKDNKDFASK
VTIAKVDATA NDIPDEIQGF PTIKLFPADD KDKPVEYTGS RTIEDLANFV RDNGKHKVDA
YDEKKVEKDG SDVTGKPKDA EAPPKPSDAP ESEEKADKEH EEL
//
