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PDI_ARTBC
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   25-MAY-2022, entry version 60.
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   EnsemblFungi; EFE30464; EFE30464; ARB_02626.
DR   GeneID; 9523678; -.
DR   KEGG; abe:ARB_02626; -.
DR   eggNOG; KOG0190; Eukaryota.
DR   HOGENOM; CLU_025879_5_0_1; -.
DR   OMA; YIAKHAT; -.
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   InterPro; IPR005788; Disulphide_isomerase.
DR   InterPro; IPR005792; Prot_disulphide_isomerase.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF00085; Thioredoxin; 2.
DR   SUPFAM; SSF52833; SSF52833; 4.
DR   TIGRFAMs; TIGR01130; ER_PDI_fam; 1.
DR   TIGRFAMs; TIGR01126; pdi_dom; 2.
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
 
 
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