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   16-JUN-2009, entry version 66.
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 (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=4896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38366 / 972;
RX   MEDLINE=21848401; 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   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen (By similarity).
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC   -!- SIMILARITY: Contains 2 thioredoxin domains.
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DR   EMBL; CU329670; CAA92230.1; -; Genomic_DNA.
DR   PIR; T38093; T38093.
DR   RefSeq; NP_592871.1; -.
DR   HSSP; P07237; 1MEK.
DR   GeneID; 2541460; -.
DR   KEGG; spo:SPAC1F5.02; -.
DR   NMPDR; fig|4896.1.peg.2841; -.
DR   GeneDB_Spombe; SPAC1F5.02; -.
DR   OMA; Q10057; EETINGN.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-000606-MON; -.
DR   BRENDA; 5.3.4.1; 653.
DR   ArrayExpress; Q10057; -.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:GeneDB_SPombe.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IEA:EC.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   InterPro; IPR005788; Disulphide_isomerase.
DR   InterPro; IPR000886; ER_targeting_sequence.
DR   InterPro; IPR005792; Prot_disulphide_isomerase.
DR   InterPro; IPR017936; Thioredoxin-like.
DR   InterPro; IPR006662; Thioredoxin-like_subdom.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 3.
DR   Pfam; PF00085; Thioredoxin; 2.
DR   PRINTS; PR00421; THIOREDOXIN.
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   2: Evidence at transcript level;
KW   Complete proteome; Disulfide bond; Endoplasmic reticulum;
KW   Glycoprotein; Isomerase; Redox-active center; Repeat; Signal.
FT   SIGNAL        1     22       Potential.
FT   CHAIN        23    492       Putative protein disulfide-isomerase
FT                                C1F5.02.
FT                                /FTId=PRO_0000034216.
FT   DOMAIN       23    128       Thioredoxin 1.
FT   DOMAIN      323    462       Thioredoxin 2.
FT   MOTIF       489    492       Prevents secretion from ER (Potential).
FT   ACT_SITE     51     51       Nucleophile (By similarity).
FT   ACT_SITE     54     54       Nucleophile (By similarity).
FT   ACT_SITE    385    385       Nucleophile (By similarity).
FT   ACT_SITE    388    388       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        114    114       Lowers pKa of C-terminal Cys of first
FT                                active site (By similarity).
FT   SITE        386    386       Contributes to redox potential value (By
FT                                similarity).
FT   SITE        387    387       Contributes to redox potential value (By
FT                                similarity).
FT   SITE        448    448       Lowers pKa of C-terminal Cys of second
FT                                active site (By similarity).
FT   CARBOHYD    161    161       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    257    257       N-linked (GlcNAc...) (Potential).
FT   DISULFID     51     54       Redox-active (By similarity).
FT   DISULFID    385    388       Redox-active (By similarity).
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
//