PDI1_SCHPO
ID PDI1_SCHPO Reviewed; 492 AA.
AC Q10057;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Putative protein disulfide-isomerase C1F5.02;
DE EC=5.3.4.1;
DE Flags: Precursor;
GN ORFNames=SPAC1F5.02;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC EC=5.3.4.1;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAA92230.1; -; Genomic_DNA.
DR PIR; T38093; T38093.
DR RefSeq; NP_592871.1; NM_001018271.2.
DR AlphaFoldDB; Q10057; -.
DR SMR; Q10057; -.
DR BioGRID; 277962; 4.
DR STRING; 4896.SPAC1F5.02.1; -.
DR iPTMnet; Q10057; -.
DR MaxQB; Q10057; -.
DR PaxDb; Q10057; -.
DR PRIDE; Q10057; -.
DR EnsemblFungi; SPAC1F5.02.1; SPAC1F5.02.1:pep; SPAC1F5.02.
DR GeneID; 2541460; -.
DR KEGG; spo:SPAC1F5.02; -.
DR PomBase; SPAC1F5.02; -.
DR VEuPathDB; FungiDB:SPAC1F5.02; -.
DR eggNOG; KOG0190; Eukaryota.
DR HOGENOM; CLU_025879_5_0_1; -.
DR InParanoid; Q10057; -.
DR OMA; YIAKHAT; -.
DR PhylomeDB; Q10057; -.
DR Reactome; R-SPO-901042; Calnexin/calreticulin cycle.
DR PRO; PR:Q10057; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; ISO:PomBase.
DR GO; GO:0003756; F:protein disulfide isomerase activity; ISO:PomBase.
DR GO; GO:0015035; F:protein-disulfide reductase activity; ISO:PomBase.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0034975; P:protein folding in endoplasmic reticulum; IC:PomBase.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central.
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; PS00014; ER_TARGET; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 3: Inferred from homology;
KW 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..492
FT /note="Putative protein disulfide-isomerase C1F5.02"
FT /id="PRO_0000034216"
FT DOMAIN 23..128
FT /note="Thioredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 323..462
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 468..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 489..492
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT ACT_SITE 51
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 54
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 385
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 388
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 52
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 53
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 114
FT /note="Lowers pKa of C-terminal Cys of first active site"
FT /evidence="ECO:0000250"
FT SITE 386
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 387
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 448
FT /note="Lowers pKa of C-terminal Cys of second active site"
FT /evidence="ECO:0000250"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 51..54
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 385..388
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 492 AA; 54880 MW; C50B592365666667 CRC64;
MKISNLLAAF LAFSGGFFCA SAEVPKVNKE GLNELITADK VLMVKFYAPW CGHCKALAPE
YESAADELEK DGISLVEVDC TEEGDLCSEY SIRGYPTLNV FKNGKQISQY SGPRKHDALV
KYMRKQLLPT VKPISKDTLE NFVEKADDLA VVAFFKDQKL NDTYTEVAEV MKDDFVFAAS
DDKELAKSLG SNFPGIVAFT KDAAQDSDKL VYTGDWDPAS IADFIGVSSI PLLDELNQMT
FGKYQQSGLP LGIIFYNSTE SRDELYDVFQ PLAKKYQDTL RFAFLDAVRY GAVAKQMNVE
SDWPAFVIAN LKSMLKYPFP TTELTAKAMT KFVGDFVDGK LQPKIKSQPI PESQEDLVVL
VADNFDDIVM DETKDVLVEF YAPWCGHCKN LAPTYEKLAE EYSDDSNVVV AKIDATENDI
SVSISGFPTI MFFKANDKVN PVRYEGDRTL EDLSAFIDKH ASFEPIKKEK ESVPAPDLED
QVAVEDEMAD EL
