SGPL1_PONAB
ID SGPL1_PONAB Reviewed; 568 AA.
AC Q5R4G0;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 88.
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:0000250|UniProtKB:O95470};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR861289; CAH93356.1; -; mRNA.
DR RefSeq; NP_001126976.1; NM_001133504.1.
DR AlphaFoldDB; Q5R4G0; -.
DR SMR; Q5R4G0; -.
DR STRING; 9601.ENSPPYP00000002746; -.
DR GeneID; 100173995; -.
DR KEGG; pon:100173995; -.
DR CTD; 8879; -.
DR eggNOG; KOG1383; Eukaryota.
DR InParanoid; Q5R4G0; -.
DR UniPathway; UPA00222; -.
DR Proteomes; UP000001595; Unplaced.
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:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006631; P:fatty acid metabolic process; ISS:UniProtKB.
DR GO; GO:0030149; P:sphingolipid catabolic process; ISS:UniProtKB.
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_0000248943"
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; 63472 MW; 0DFA7E82D95C1DA3 CRC64;
MPSTDLLTLK AFEPYLEILE VYSTKAKNYV NGHCTKYEPW QLIAWSVVWT LLIVWGYEFV
FQPESLWSRF KKKCFKLTRK MPIIGRKIQD KLNKTKDDIS KNMSFLKVDK EYVKALPSQG
LSSSAVLEKL KEYSSMDAFW QEGRASGTVY SGEEKLTELL VKAYGDFAWS NPLHPDIFPG
LRKIEAEIVR IACSLFNGGP DSCGCVTSGG TESILMACKA YRDLAFEKGI KTSEIVAPQS
AHAAFNKAAS YFGMKIVRVP LTKMMEVDVR AMRRAISRNT AMLVCSTPQF PHGVIDPVPE
VAKLAVKYKI PLHVDACLGG FLTVFMEKAG YPLEHPFDFR VKGVTSISAD THKYGYAPKG
SSLVLYSDKK YRNYQFFVDT DWQGGIYASP TIAGSRPGGI SAACWAALMH FGENGYVEAT
KQIIKTARFL KSELENIKGI FVFGNPQLSV IALGSRDFDI YRLSNLMTAK GWNLNQLQFP
PSIHFCITLL HARKRVAIQF LKDIRESVTQ IMKNPKAKTT GMGAIYGMAQ TTVDRNMVAE
LSSVFLDSLY STDTVTQGSQ MNGSPKPH
