[1]	NUCLEOTIDE SEQUENCE [MRNA]. Van Veldhoven P.P.; "Comparison of sphingosine-1-phosphate lyases."; Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Cleaves phosphorylated sphingoid bases (PSBs), such as sphingosine-1-phosphate, into fatty aldehydes and phosphoethanolamine. Elevates stress-induced ceramide production and apoptosis (By similarity).
CATALYTIC ACTIVITY: Sphinganine 1-phosphate = phosphoethanolamine + palmitaldehyde.
COFACTOR: Pyridoxal phosphate (By similarity).
PATHWAY: Lipid metabolism; sphingolipid metabolism .
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type III membrane protein (By similarity).
SIMILARITY: Belongs to the group II decarboxylase family. Sphingosine-1-phosphate lyase subfamily.

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

AJ512838; CAD55407.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_775139.1; -.

UniGene

Rn.26953

3D structure databases

ModBase

Q8CHN6.

Organism-specific databases

RGD

628599; Sgpl1.

Gene expression databases

ArrayExpress

Q8CHN6; -.

GermOnline

ENSRNOG00000000565; Rattus norvegicus.

Ontologies

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:0006915;	Biological process: apoptosis (inferred from sequence or structural similarity from UniProtKB).
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

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

PF00282; Pyridoxal_deC; 1.
Pfam graphical view of domain structure.

PROSITE

PS00392; DDC_GAD_HDC_YDC; FALSE_NEG.

Genome annotation databases

Ensembl

ENSRNOG00000000565; Rattus norvegicus. [Contig view]

GeneID

286896; -.

KEGG

rno:286896; -.

Phylogenomic databases

HOVERGEN

Q8CHN6; -.

Other

NextBio

624977; -.

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

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 568`	`568`	`Sphingosine-1-phosphate lyase 1.`	`PRO_0000147014`
`TOPO_DOM`	`1 41`	`41`	`Lumenal (Potential).`
`TRANSMEM`	`42 62`	`21`	`Signal-anchor for type III membrane protein (Potential).`
`TOPO_DOM`	`63 568`	`506`	`Cytoplasmic (Potential).`
`BINDING`	`353 353`		`Pyridoxal phosphate (covalent) (By similarity).`

Sequence information

Length: 568 AA [This is the length of the unprocessed precursor]

Molecular weight: 63758 Da [This is the MW of the unprocessed precursor]

CRC64: A0B59A072CC79F48 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPSTDLLKLK DFEPYLEILE AYSTKAKNYV NGYCTKYEPW QLIAGSVLCT LLVVWVYELI 

        70         80         90        100        110        120 
FQPESLWSRF KNKLFRLIRK MPFIGRKIQQ QLTKAKKDLV KNMPFLKLDK DYVKTLPAQG 

       130        140        150        160        170        180 
LSTAEVLERL KEYSSMDVFW QEGKASGAVY SGEPKLTELL VQAYGEFTWS NPLHPDIFPG 

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

       250        260        270        280        290        300 
AHAAFDKAAH YFGMKIVRVA QKKNMEVDVR AMKRAISRNT AMLVCSAPQF PHGVIDPIPE 

       310        320        330        340        350        360 
VAKLAVKYKI PFHVDACLGG FLIVFMEKAG YPLEKPFDFR VKGVTSISAD THKYGYAPKG 

       370        380        390        400        410        420 
SSVVMYSNEK YRKYQFFVDA DWQGGIYASP SIAGSRPGGI IAACWAALMH FGENGYVEAT 

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

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

       550        560 
ISSVFLDSLY STDPVTQGNQ MNGSPKPR

Q8CHN6 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools