PDI2_SCHPO
ID PDI2_SCHPO Reviewed; 359 AA.
AC O13811; Q4F7X2;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Protein disulfide-isomerase C17H9.14c;
DE EC=5.3.4.1;
DE Flags: Precursor;
GN ORFNames=SPAC17H9.14c;
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 [GENOMIC DNA].
RA Choi Y.-S., Kim H.-G., Lim H.-W., Lim C.-J.;
RT "Physiological roles and regulation of protein disulfide isomerase in the
RT fission yeast Schizosaccharomyces pombe.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
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DR EMBL; DQ104736; AAZ13768.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB11223.1; -; Genomic_DNA.
DR PIR; T37880; T37880.
DR RefSeq; NP_593584.1; NM_001019016.2.
DR AlphaFoldDB; O13811; -.
DR SMR; O13811; -.
DR BioGRID; 278739; 7.
DR STRING; 4896.SPAC17H9.14c.1; -.
DR iPTMnet; O13811; -.
DR MaxQB; O13811; -.
DR PaxDb; O13811; -.
DR PRIDE; O13811; -.
DR EnsemblFungi; SPAC17H9.14c.1; SPAC17H9.14c.1:pep; SPAC17H9.14c.
DR GeneID; 2542270; -.
DR KEGG; spo:SPAC17H9.14c; -.
DR PomBase; SPAC17H9.14c; -.
DR VEuPathDB; FungiDB:SPAC17H9.14c; -.
DR eggNOG; KOG0191; Eukaryota.
DR HOGENOM; CLU_038617_1_1_1; -.
DR InParanoid; O13811; -.
DR OMA; FINEHAG; -.
DR PhylomeDB; O13811; -.
DR BRENDA; 5.3.4.1; 5613.
DR PRO; PR:O13811; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:PomBase.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IMP:PomBase.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IMP:PomBase.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:PomBase.
DR GO; GO:0006457; P:protein folding; IMP:PomBase.
DR GO; GO:0034975; P:protein folding in endoplasmic reticulum; IC:PomBase.
DR CDD; cd00238; ERp29c; 1.
DR Gene3D; 1.20.1150.12; -; 1.
DR InterPro; IPR005788; Disulphide_isomerase.
DR InterPro; IPR011679; ERp29_C.
DR InterPro; IPR036356; ERp29_C_sf.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF07749; ERp29; 1.
DR Pfam; PF00085; Thioredoxin; 2.
DR SUPFAM; SSF47933; SSF47933; 1.
DR SUPFAM; SSF52833; SSF52833; 2.
DR TIGRFAMs; TIGR01126; pdi_dom; 2.
DR PROSITE; PS00194; THIOREDOXIN_1; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 3: Inferred from homology;
KW Disulfide bond; Isomerase; Redox-active center; Reference proteome; Repeat;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..359
FT /note="Protein disulfide-isomerase C17H9.14c"
FT /id="PRO_0000034217"
FT DOMAIN 20..130
FT /note="Thioredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 134..250
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 51
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 54
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 116
FT /note="Lowers pKa of C-terminal Cys of first active site"
FT /evidence="ECO:0000250"
FT DISULFID 51..54
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 170..173
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 359 AA; 40692 MW; A2FB610518DA2E50 CRC64;
MRLPLLSFVI FALFALVFAS GVVELQSLNE LENTIRASKK GALIEFYATW CGHCKSLAPV
YEELGALFED HNDVLIGKID ADTHSDVADK YHITGFPTLI WFPPDGSEPV QYSNARDVDS
LTQFVSEKTG IKKRKIVLPS NVVELDSLNF DKVVMDDKKD VLVEFYADWC GYCKRLAPTY
ETLGKVFKNE PNVEIVKINA DVFADIGRLH EVASFPTIKF FPKDDKDKPE LYEGDRSLES
LIEYINKKSG TQRSPDGTLL STAGRIPTFD EFAAEFLDMS NAAKEVVLEK VKQLALEDSS
RWTKYYKKVF EKILNDENWV HKEAKRLSKL LRQKSIALAS ADDFKTRLNI LNSFLPGNH
