ID A0A072PKP9_9EURO Unreviewed; 539 AA.
AC A0A072PKP9;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Protein disulfide-isomerase {ECO:0000256|ARBA:ARBA00039846, ECO:0000256|RuleBase:RU361130};
DE EC=5.3.4.1 {ECO:0000256|ARBA:ARBA00012723, ECO:0000256|RuleBase:RU361130};
GN ORFNames=A1O9_05143 {ECO:0000313|EMBL:KEF60292.1};
OS Exophiala aquamarina CBS 119918.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF60292.1, ECO:0000313|Proteomes:UP000027920};
RN [1] {ECO:0000313|EMBL:KEF60292.1, ECO:0000313|Proteomes:UP000027920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF60292.1,
RC ECO:0000313|Proteomes:UP000027920};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala aquamarina CBS 119918.";
RL Submitted (MAR-2013) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KEF60292.1}.
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DR EMBL; AMGV01000003; KEF60292.1; -; Genomic_DNA.
DR RefSeq; XP_013262882.1; XM_013407428.1.
DR AlphaFoldDB; A0A072PKP9; -.
DR STRING; 1182545.A0A072PKP9; -.
DR GeneID; 25280069; -.
DR VEuPathDB; FungiDB:A1O9_05143; -.
DR HOGENOM; CLU_025879_5_0_1; -.
DR OrthoDB; 5399045at2759; -.
DR Proteomes; UP000027920; 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; 3.
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:UP000027920};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361130}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT CHAIN 21..539
FT /note="Protein disulfide-isomerase"
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT /id="PRO_5005104217"
FT DOMAIN 8..127
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 321..464
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DISULFID 50..53
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
FT DISULFID 384..387
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
SQ SEQUENCE 539 AA; 57375 MW; 220038AE78548E4C CRC64;
MRSFKSLAAA SIALAGFAAA SDVHDLKTDN FKQFISENDL VLAEFFAPWC GHCKALAPEY
EEAATTLKEK NIALVKVDCT VEGDLCKEYG VEGYPTVKVF RGLDNIKPYS GARKAPAIVS
YMTKQGLPAV SLLTSETLEE FKTTDKVVVV AYIAADDKAS NQTYTTLADT LRDDYIFGAT
NDAALAKTEG AKQPSIVLYK DFDEGKNVFD SAFDDEAITK FIKAAATPLI GEVGPETYAG
YIGAGIPLAY IFSETAEERA SLAETLKSVA EKHKGVINFA VIDAKAFGAH AGNLNLPTDK
FPSFAIQETV KNEKYPFEGD ALTEKTIGAF VQSFVDGKLE PSIKSEPIPE KQEGPVTVVV
ANSYKDIVLD DSKDVLIEFY APWCGHCKSL APIYEKLAEL YTSSDLSSKV TVAKVDATLN
DVPDEISGFP TIKLYPAGAK DSPVEYSGSR TLEDLAAFIK DNGKHAADGL AAQADAEDVV
MEDASAAADQ ETLAKAAPAA TTDGEGVVDA VKSAVSGAAD AASTFVADDD AGVQEHDEL
//
