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-APR-2013, entry version 92.
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 (By similarity).
CC -!- CATALYTIC ACTIVITY: Catalyzes the rearrangement of -S-S- bonds in
CC proteins.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC -!- SIMILARITY: Contains 2 thioredoxin domains.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 STRING; 4896.SPAC17H9.14c-1; -.
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 eggNOG; COG0526; -.
DR HOGENOM; HOG000176389; -.
DR KO; K09584; -.
DR OMA; FFPKGST; -.
DR OrthoDB; EOG4X9BS1; -.
DR BRENDA; 5.3.4.1; 5615.
DR NextBio; 20803334; -.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:PomBase.
DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
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:0006662; P:glycerol ether metabolic process; IEA:InterPro.
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; IPR005746; Thioredoxin.
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 PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF47933; ERP29_C; 1.
DR SUPFAM; SSF52833; Thiordxn-like_fd; 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 Potential.
FT CHAIN 20 359 Protein disulfide-isomerase C17H9.14c.
FT /FTId=PRO_0000034217.
FT DOMAIN 20 130 Thioredoxin 1.
FT DOMAIN 134 250 Thioredoxin 2.
FT ACT_SITE 51 51 Nucleophile (By similarity).
FT ACT_SITE 54 54 Nucleophile (By similarity).
FT SITE 52 52 Contributes to redox potential value (By
FT similarity).
FT SITE 53 53 Contributes to redox potential value (By
FT similarity).
FT SITE 116 116 Lowers pKa of C-terminal Cys of first
FT active site (By similarity).
FT DISULFID 51 54 Redox-active (By similarity).
FT DISULFID 170 173 Redox-active (By similarity).
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
//
