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UniProtKB/Swiss-Prot entry Q8R0X7


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

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Entry information
Entry name SGPL1_MOUSE
Primary accession number Q8R0X7
Secondary accession numbers O54955 Q8C942
Integrated into Swiss-Prot on October 24, 2003
Sequence was last modified on June 1, 2002 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 51)
Name and origin of the protein
Protein name Sphingosine-1-phosphate lyase 1
Synonyms SP-lyase
mSPL
EC 4.1.2.27
Sphingosine-1-phosphate aldolase
Gene name
Name: Sgpl1
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J;
DOI=10.1006/bbrc.1997.7993; PubMed=9464245 [NCBI, ExPASy, EBI, Israel, Japan]
Zhou J., Saba J.D.;
"Identification of the first mammalian sphingosine phosphate lyase gene and its functional expression in yeast.";
Biochem. Biophys. Res. Commun. 242:502-507(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Bone, and Thymus;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
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
AF036894; AAC03768.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK036747; BAC29562.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK037789; BAC29872.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK043024; BAC31437.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK049342; BAC33695.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC026135; AAH26135.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JC5923; JC5923.
RefSeq NP_033189.2; -.
UniGene Mm.412319
3D structure databases
ModBase Q8R0X7.
Organism-specific databases
MGI MGI:1261415; Sgpl1.
Gene expression databases
ArrayExpress Q8R0X7; -.
CleanEx MM_SGPL1; -.
GermOnline ENSMUSG00000020097; Mus musculus.
Ontologies
GO
GO:0005789; Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0016831; Molecular function: carboxy-lyase activity (inferred from electronic annotation from InterPro).
GO:0030170; Molecular function: pyridoxal phosphate binding (inferred from electronic annotation from InterPro).
GO:0008117; Molecular function: sphinganine-1-phosphate aldolase activity (inferred from electronic annotation from EC).
GO:0016769; Molecular function: transferase activity, transferring nitrogenous groups (inferred from electronic annotation from InterPro).
GO:0006915; Biological process: apoptosis (inferred from sequence or structural similarity from UniProtKB).
GO:0009058; Biological process: biosynthetic process (inferred from electronic annotation from InterPro).
GO:0019752; Biological process: carboxylic acid metabolic process (inferred from electronic annotation from InterPro).
GO:0006672; Biological process: ceramide metabolic process (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR004839; Aminotrans_I/II.
IPR002129; PyrdxlP-dep_de-COase.
IPR015421; PyrdxlP-dep_Trfase_major_sub1.
Graphical view of domain structure.
Gene3D G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
PANTHER PTHR11999; Pyridoxal_deC; 1.
Pfam PF00155; Aminotran_1_2; 1.
Pfam graphical view of domain structure.
PROSITE PS00392; DDC_GAD_HDC_YDC; FALSE_NEG.
ProtoNet Q8R0X7.
Genome annotation databases
Ensembl ENSMUSG00000020097; Mus musculus. [Contig view]
GeneID 20397; -.
KEGG mmu:20397; -.
Phylogenomic databases
HOVERGEN Q8R0X7; -.
Other
NextBio 298346; -.
SOURCE Sgpl1; Mus musculus.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Apoptosis; Endoplasmic reticulum; Lipid metabolism; Lyase; Membrane; Pyridoxal phosphate; Signal-anchor; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   568  568     Sphingosine-1-phosphate lyase 1. PRO_0000147013
TOPO_DOM   1    40  40     Lumenal (Potential). 
TRANSMEM   41    61  21     Signal-anchor for type III membrane protein (Potential). 
TOPO_DOM   62   568  507     Cytoplasmic (Potential). 
BINDING   353   353        Pyridoxal phosphate (covalent) (By similarity). 
CONFLICT   305   305        A -> T (in Ref. 1; AAC03768). 
CONFLICT   473   473        N -> K (in Ref. 2; BAC31437). 
Sequence information
Length: 568 AA [This is the length of the unprocessed precursor] Molecular weight: 63677 Da [This is the MW of the unprocessed precursor] CRC64: FA5D52E4E49DF09E [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPGTDLLKLK DFEPYLEILE SYSTKAKNYV NGYCTKYEPW QLIAWSVLCT LLIVWVYELI 

        70         80         90        100        110        120 
FQPESLWSRF KKKLFKLIRK MPFIGRKIEQ QVSKAKKDLV KNMPFLKVDK DYVKTLPAQG 

       130        140        150        160        170        180 
MGTAEVLERL KEYSSMDGSW QEGKASGAVY NGEPKLTELL VQAYGEFTWS NPLHPDIFPG 

       190        200        210        220        230        240 
LRKLEAEIVR MTCSLFNGGP DSCGCVTSGG TESILMACKA YRDLALEKGI KTPEIVAPES 

       250        260        270        280        290        300 
AHAAFDKAAH YFGMKIVRVA LKKNMEVDVQ AMKRAISRNT AMLVCSTPQF PHGVMDPVPE 

       310        320        330        340        350        360 
VAKLAVRYKI PLHVDACLGG FLIVFMEKAG YPLEKPFDFR VKGVTSISAD THKYGYAPKG 

       370        380        390        400        410        420 
SSVVMYSNEK YRTYQFFVGA DWQGGVYASP SIAGSRPGGI IAACWAALMH FGENGYVEAT 

       430        440        450        460        470        480 
KQIIKTARFL KSELENIKNI FIFGDPQLSV IALGSNDFDI YRLSNMMSAK GWNFNYLQFP 

       490        500        510        520        530        540 
RSIHFCITLV HTRKRVAIQF LKDIRESVTQ IMKNPKAKTT GMGAIYGMAQ ATIDRKLVAE 

       550        560 
ISSVFLDCLY TTDPVTQGNQ MNGSPKPR 

Q8R0X7 in FASTA format

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