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UniProtKB/Swiss-Prot entry P21696


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GPD1_SCHPO
Primary accession number P21696
Secondary accession numbers O94310 P78927
Integrated into Swiss-Prot on May 1, 1991
Sequence was last modified on January 11, 2001 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 74)
Name and origin of the protein
Protein name Glycerol-3-phosphate dehydrogenase [NAD+] 1
Synonyms EC 1.1.1.8
GPDH-C
GPD-C
Gene name
Name: gpd1
ORFNames: SPBC215.05
From
Schizosaccharomyces pombe (Fission yeast) [TaxID: 4896] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1093/nar/18.23.7145; PubMed=2263480 [NCBI, ExPASy, EBI, Israel, Japan]
Pidoux A.L., Fawell E.H., Armstrong J.;
"Glycerol-3-phosphate dehydrogenase homologue from Schizosaccharomyces pombe.";
Nucleic Acids Res. 18:7145-7145(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 38366 / 972;
DOI=10.1038/nature724; PubMed=11859360 [NCBI, ExPASy, EBI, Israel, Japan]
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-77.
PubMed=8825100 [NCBI, ExPASy, EBI, Israel, Japan]
Ohmiya R., Yamada H., Nakashima K., Aiba H., Mizuno T.;
"Osmoregulation of fission yeast: cloning of two distinct genes encoding glycerol-3-phosphate dehydrogenase, one of which is responsible for osmotolerance for growth.";
Mol. Microbiol. 18:963-973(1995).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-376 AND THR-382, AND MASS SPECTROMETRY.
DOI=10.1021/pr7006335; PubMed=18257517 [NCBI, ExPASy, EBI, Israel, Japan]
Wilson-Grady J.T., Villen J., Gygi S.P.;
"Phosphoproteome analysis of fission yeast.";
J. Proteome Res. 7:1088-1097(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X56162; CAA39630.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CU329671; CAA22119.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D50796; BAA09424.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T39895; T39895.
RefSeq NP_596682.1; -.
3D structure databases
HSSP P90551; 1EVY. [HSSP ENTRY / PDB]
ModBase P21696.
Enzyme and pathway databases
BioCyc SPOM-XXX-01:SPOM-XXX-01-004669-MON; -.
Organism-specific databases
GeneDB_Spombe SPBC215.05; -.
Gene expression databases
ArrayExpress P21696; -.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from GeneDB_SPombe).
GO:0005634; Cellular component: nucleus (inferred from direct assay from GeneDB_SPombe).
GO:0006970; Biological process: response to osmotic stress (inferred from expression pattern from GeneDB_SPombe).
QuickGo view.
Family and domain databases
InterPro IPR013328; DHase_multihelical.
IPR016040; NAD(P)-bd.
IPR017751; NAD-dep_Gly3P_DH_euk.
IPR006168; NAD-dep_Gly3P_DHase.
IPR011128; NAD-dep_Gly3P_DHase_N.
IPR006109; NAD_Gly3P_DHase_C.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
G3DSA:1.10.1040.10; Opine_DH; 1.
PANTHER PTHR11728; NAD_Gly3P_DH; 1.
Pfam PF07479; NAD_Gly3P_dh_C; 1.
PF01210; NAD_Gly3P_dh_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000114; Glycerol-3-P_dh; 1.
PRINTS PR00077; GPDHDRGNASE.
ProDom PD001278; NAD_Gly3P_C; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00957; NAD_G3PDH; 1.
BLOCKS P21696.
Genome annotation databases
GeneID 2540455; -.
KEGG spo:SPBC215.05; -.
NMPDR fig|4896.1.peg.2548; -.
Other
ProtoNet P21696.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; NAD; Oxidoreductase; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   385  385     Glycerol-3-phosphate dehydrogenase [NAD+] 1. PRO_0000138095
NP_BIND   29    34  6     NAD (By similarity). 
REGION   296   297  2     Substrate binding (By similarity). 
ACT_SITE   232   232        Proton acceptor (By similarity). 
BINDING   121   121        NAD (By similarity). 
BINDING   144   144        NAD; via amide nitrogen (By similarity). 
BINDING   144   144        Substrate (By similarity). 
BINDING   177   177        NAD; via amide nitrogen (By similarity). 
BINDING   296   296        NAD (By similarity). 
BINDING   325   325        NAD (By similarity). 
MOD_RES   376   376        Phosphoserine. 
MOD_RES   382   382        Phosphothreonine. 
CONFLICT   54    56        SKV -> GKG (in Ref. 1; CAA39630). 
CONFLICT   126   127        CD -> WH (in Ref. 1; CAA39630). 
CONFLICT   153   153        Missing (in Ref. 1). 
CONFLICT   209   209        F -> S (in Ref. 1; CAA39630). 
Sequence information
Length: 385 AA [This is the length of the unprocessed precursor] Molecular weight: 41995 Da [This is the MW of the unprocessed precursor] CRC64: 8061C294196516E1 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSGYGQQGVS AANIDSIRPK KRLSIGVVGS GNWGTAIAKI CGENARAHGH HFRSKVRMWV 

        70         80         90        100        110        120 
FEEEIEYKGE KRKLTEVFNE AHENVKYLPG IECPPNVIAV PDVREVARRA DILVFVVPHQ 

       130        140        150        160        170        180 
FIERVCDQMV GLIRPGAVGI SCIKGVAVSK EGVRLYSEVI SEKLGIYCGV LSGANVANEV 

       190        200        210        220        230        240 
AREQFCETTI GFNPPNEVDI PREQIAAVFD RPYFSVVSVD DVAGVALGGA LKNVVAMAVG 

       250        260        270        280        290        300 
FADGLEWGGN TKAAIMRRGL LEMQKFATTF FDSDPRTMVE QSCGIADLVT SCLGGRNNRC 

       310        320        330        340        350        360 
AEAFVKTGKS LETLEKELLG GQLLQGAATS KDVHEFLLTK DMVKDFPLFT AVYNISYEDM 

       370        380 
DPKDLIIVLQ PLKEDSENEG GTETE 

P21696 in FASTA format

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