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Database: UniProt
Entry: O13811
LinkDB: O13811
Original site: O13811 
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   29-OCT-2014, entry version 104.
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;
OC   Schizosaccharomycetaceae; 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
RT   the 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.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- FUNCTION: Participates in the folding of proteins containing
CC       disulfide bonds, may be involved in glycosylation, prolyl
CC       hydroxylation and triglyceride transfer. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: Catalyzes the rearrangement of -S-S- bonds in
CC       proteins.
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 2 thioredoxin domains. {ECO:0000255|PROSITE-
CC       ProRule:PRU00691}.
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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   ProteinModelPortal; O13811; -.
DR   BioGrid; 278739; 6.
DR   STRING; 4896.SPAC17H9.14c-1; -.
DR   MaxQB; O13811; -.
DR   PaxDb; 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   eggNOG; COG0526; -.
DR   HOGENOM; HOG000176389; -.
DR   InParanoid; O13811; -.
DR   KO; K09584; -.
DR   OMA; GTSRDTK; -.
DR   OrthoDB; EOG71CFZN; -.
DR   PhylomeDB; O13811; -.
DR   BRENDA; 5.3.4.1; 5615.
DR   Reactome; REACT_188301; XBP1(S) activates chaperone genes.
DR   NextBio; 20803334; -.
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 oxidoreductase activity; IMP:PomBase.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IMP:PomBase.
DR   GO; GO:0055114; P:oxidation-reduction process; IMP:GOC.
DR   GO; GO:0006457; P:protein folding; IMP:PomBase.
DR   Gene3D; 1.20.1150.12; -; 1.
DR   Gene3D; 3.40.30.10; -; 2.
DR   InterPro; IPR005788; Disulphide_isomerase.
DR   InterPro; IPR011679; ER_p29_C.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
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   Complete proteome; Disulfide bond; Isomerase; Redox-active center;
KW   Reference proteome; Repeat; Signal.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   CHAIN        20    359       Protein disulfide-isomerase C17H9.14c.
FT                                /FTId=PRO_0000034217.
FT   DOMAIN       20    130       Thioredoxin 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00691}.
FT   DOMAIN      134    250       Thioredoxin 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00691}.
FT   ACT_SITE     51     51       Nucleophile. {ECO:0000250}.
FT   ACT_SITE     54     54       Nucleophile. {ECO:0000250}.
FT   SITE         52     52       Contributes to redox potential value.
FT                                {ECO:0000250}.
FT   SITE         53     53       Contributes to redox potential value.
FT                                {ECO:0000250}.
FT   SITE        116    116       Lowers pKa of C-terminal Cys of first
FT                                active site. {ECO:0000250}.
FT   DISULFID     51     54       Redox-active. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00691}.
FT   DISULFID    170    173       Redox-active. {ECO:0000255|PROSITE-
FT                                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
//
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