ID   SGPL1_RAT               Reviewed;         568 AA.
AC   Q8CHN6;
DT   24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   26-MAY-2009, entry version 44.
DE   RecName: Full=Sphingosine-1-phosphate lyase 1;
DE            Short=SP-lyase;
DE            Short=SPL;
DE            EC=4.1.2.27;
DE   AltName: Full=Sphingosine-1-phosphate aldolase;
GN   Name=Sgpl1; Synonyms=Spl;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Van Veldhoven P.P.;
RT   "Comparison of sphingosine-1-phosphate lyases.";
RL   Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cleaves phosphorylated sphingoid bases (PSBs), such as
CC       sphingosine-1-phosphate, into fatty aldehydes and
CC       phosphoethanolamine. Elevates stress-induced ceramide production
CC       and apoptosis (By similarity).
CC   -!- CATALYTIC ACTIVITY: Sphinganine 1-phosphate = phosphoethanolamine
CC       + palmitaldehyde.
CC   -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC   -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC       type III membrane protein (By similarity).
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       Sphingosine-1-phosphate lyase subfamily.
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DR   EMBL; AJ512838; CAD55407.1; -; mRNA.
DR   IPI; IPI00193172; -.
DR   RefSeq; NP_775139.1; -.
DR   UniGene; Rn.26953; -.
DR   PRIDE; Q8CHN6; -.
DR   Ensembl; ENSRNOG00000000565; Rattus norvegicus.
DR   GeneID; 286896; -.
DR   KEGG; rno:286896; -.
DR   RGD; 628599; Sgpl1.
DR   HOVERGEN; Q8CHN6; -.
DR   BRENDA; 4.1.2.27; 248.
DR   NextBio; 624977; -.
DR   ArrayExpress; Q8CHN6; -.
DR   GermOnline; ENSRNOG00000000565; Rattus norvegicus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008117; F:sphinganine-1-phosphate aldolase activity; IEA:EC.
DR   GO; GO:0006915; P:apoptosis; ISS:UniProtKB.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   GO; GO:0006672; P:ceramide metabolic process; ISS:UniProtKB.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
DR   PANTHER; PTHR11999; Pyridoxal_deC; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Apoptosis; Endoplasmic reticulum; Lipid metabolism; Lyase; Membrane;
KW   Pyridoxal phosphate; Signal-anchor; Transmembrane.
FT   CHAIN         1    568       Sphingosine-1-phosphate lyase 1.
FT                                /FTId=PRO_0000147014.
FT   TOPO_DOM      1     41       Lumenal (Potential).
FT   TRANSMEM     42     62       Signal-anchor for type III membrane
FT                                protein (Potential).
FT   TOPO_DOM     63    568       Cytoplasmic (Potential).
FT   MOD_RES     353    353       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   568 AA;  63758 MW;  A0B59A072CC79F48 CRC64;
     MPSTDLLKLK DFEPYLEILE AYSTKAKNYV NGYCTKYEPW QLIAGSVLCT LLVVWVYELI
     FQPESLWSRF KNKLFRLIRK MPFIGRKIQQ QLTKAKKDLV KNMPFLKLDK DYVKTLPAQG
     LSTAEVLERL KEYSSMDVFW QEGKASGAVY SGEPKLTELL VQAYGEFTWS NPLHPDIFPG
     LRKLEAEIVR MTCSLFNGGP DSCGCVTSGG TESILMACKA YRDLALEKGI KTPEIVAPES
     AHAAFDKAAH YFGMKIVRVA QKKNMEVDVR AMKRAISRNT AMLVCSAPQF PHGVIDPIPE
     VAKLAVKYKI PFHVDACLGG FLIVFMEKAG YPLEKPFDFR VKGVTSISAD THKYGYAPKG
     SSVVMYSNEK YRKYQFFVDA DWQGGIYASP SIAGSRPGGI IAACWAALMH FGENGYVEAT
     KQIIKTARFL KSELENIKNI FILGDPQLSV IALGSNDFDI YRLSNMMSAK GWNFNYLQFP
     RSIHFCITLV HTRKRVAIQF LKDIRESVTQ IMKNPKAKTT GMGAIYGMAQ ATIDRKMVAE
     ISSVFLDSLY STDPVTQGNQ MNGSPKPR
//