SGPL1_RAT
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 03-AUG-2022, entry version 128.
DE RecName: Full=Sphingosine-1-phosphate lyase 1 {ECO:0000305};
DE Short=S1PL;
DE Short=SP-lyase 1;
DE Short=SPL;
DE Short=SPL 1;
DE EC=4.1.2.27 {ECO:0000250|UniProtKB:O95470};
DE AltName: Full=Sphingosine-1-phosphate aldolase;
GN Name=Sgpl1 {ECO:0000312|RGD:628599}; Synonyms=Spl;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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 phosphoethanolamine.
CC Elevates stress-induced ceramide production and apoptosis (By
CC similarity). Required for global lipid homeostasis in liver and
CC cholesterol homeostasis in fibroblasts. Involved in the regulation of
CC pro-inflammatory response and neutrophil trafficking. Modulates
CC neuronal autophagy via phosphoethanolamine production which regulates
CC accumulation of aggregate-prone proteins such as APP (By similarity).
CC Seems to play a role in establishing neuronal contact sites and axonal
CC maintenance (By similarity). {ECO:0000250|UniProtKB:O95470,
CC ECO:0000250|UniProtKB:Q8R0X7, ECO:0000250|UniProtKB:Q9V7Y2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=sphinganine 1-phosphate = hexadecanal + phosphoethanolamine;
CC Xref=Rhea:RHEA:18593, ChEBI:CHEBI:17600, ChEBI:CHEBI:57939,
CC ChEBI:CHEBI:58190; EC=4.1.2.27;
CC Evidence={ECO:0000250|UniProtKB:O95470};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=sphing-4-enine 1-phosphate = (2E)-hexadecenal +
CC phosphoethanolamine; Xref=Rhea:RHEA:33507, ChEBI:CHEBI:17585,
CC ChEBI:CHEBI:58190, ChEBI:CHEBI:60119; EC=4.1.2.27;
CC Evidence={ECO:0000250|UniProtKB:O95470};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:O95470};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000250|UniProtKB:O95470}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O95470}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O95470}; Single-pass type III membrane protein
CC {ECO:0000255}; Cytoplasmic side {ECO:0000250|UniProtKB:Q8R0X7}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family. Sphingosine-
CC 1-phosphate lyase subfamily. {ECO:0000305}.
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DR EMBL; AJ512838; CAD55407.1; -; mRNA.
DR RefSeq; NP_775139.1; NM_173116.1.
DR RefSeq; XP_008771092.1; XM_008772870.2.
DR RefSeq; XP_008771093.1; XM_008772871.1.
DR RefSeq; XP_008771094.1; XM_008772872.1.
DR RefSeq; XP_008771095.1; XM_008772873.1.
DR AlphaFoldDB; Q8CHN6; -.
DR SMR; Q8CHN6; -.
DR BioGRID; 251889; 1.
DR IntAct; Q8CHN6; 1.
DR STRING; 10116.ENSRNOP00000059089; -.
DR BindingDB; Q8CHN6; -.
DR ChEMBL; CHEMBL3826869; -.
DR iPTMnet; Q8CHN6; -.
DR PhosphoSitePlus; Q8CHN6; -.
DR jPOST; Q8CHN6; -.
DR PaxDb; Q8CHN6; -.
DR PRIDE; Q8CHN6; -.
DR GeneID; 286896; -.
DR KEGG; rno:286896; -.
DR UCSC; RGD:628599; rat.
DR CTD; 8879; -.
DR RGD; 628599; Sgpl1.
DR VEuPathDB; HostDB:ENSRNOG00000000565; -.
DR eggNOG; KOG1383; Eukaryota.
DR InParanoid; Q8CHN6; -.
DR OMA; FKDHQFT; -.
DR OrthoDB; 517323at2759; -.
DR PhylomeDB; Q8CHN6; -.
DR TreeFam; TF300777; -.
DR Reactome; R-RNO-1660661; Sphingolipid de novo biosynthesis.
DR UniPathway; UPA00222; -.
DR PRO; PR:Q8CHN6; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000000565; Expressed in jejunum and 19 other tissues.
DR Genevisible; Q8CHN6; RN.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008117; F:sphinganine-1-phosphate aldolase activity; ISS:UniProtKB.
DR GO; GO:0008209; P:androgen metabolic process; ISO:RGD.
DR GO; GO:0097190; P:apoptotic signaling pathway; ISS:UniProtKB.
DR GO; GO:0006672; P:ceramide metabolic process; ISS:UniProtKB.
DR GO; GO:0008210; P:estrogen metabolic process; ISO:RGD.
DR GO; GO:0060325; P:face morphogenesis; ISO:RGD.
DR GO; GO:0006631; P:fatty acid metabolic process; ISS:UniProtKB.
DR GO; GO:0008585; P:female gonad development; ISO:RGD.
DR GO; GO:0010761; P:fibroblast migration; ISO:RGD.
DR GO; GO:0030097; P:hemopoiesis; ISO:RGD.
DR GO; GO:0001822; P:kidney development; ISO:RGD.
DR GO; GO:0033327; P:Leydig cell differentiation; ISO:RGD.
DR GO; GO:0001553; P:luteinization; ISO:RGD.
DR GO; GO:0006807; P:nitrogen compound metabolic process; ISO:RGD.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0009791; P:post-embryonic development; ISO:RGD.
DR GO; GO:0040014; P:regulation of multicellular organism growth; ISO:RGD.
DR GO; GO:0060021; P:roof of mouth development; ISO:RGD.
DR GO; GO:0048705; P:skeletal system morphogenesis; ISO:RGD.
DR GO; GO:0007283; P:spermatogenesis; ISO:RGD.
DR GO; GO:0030149; P:sphingolipid catabolic process; ISS:UniProtKB.
DR GO; GO:0001570; P:vasculogenesis; ISO:RGD.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Apoptosis; Endoplasmic reticulum; Lipid metabolism; Lyase;
KW Membrane; Nitration; Phosphoprotein; Pyridoxal phosphate;
KW Reference proteome; Signal-anchor; Sphingolipid metabolism; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..568
FT /note="Sphingosine-1-phosphate lyase 1"
FT /id="PRO_0000147014"
FT TOPO_DOM 1..41
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..568
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 353
FT /note="N6-(pyridoxal phosphate)lysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 353
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O95470"
FT MOD_RES 356
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O95470"
FT MOD_RES 366
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O95470"
FT MOD_RES 564
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95470"
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
