SMS2_CAEEL
ID SMS2_CAEEL Reviewed; 335 AA.
AC Q20735;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Phosphatidylcholine:ceramide cholinephosphotransferase 2;
DE Short=PC:ceramide cholinephosphotransferase 2 {ECO:0000303|PubMed:14685263};
DE EC=2.7.8.27 {ECO:0000269|PubMed:14685263};
DE AltName: Full=Sphingomyelin synthase 2 {ECO:0000303|PubMed:14685263};
DE Short=CSS3alpha2 {ECO:0000303|PubMed:14685263};
DE Short=SMS-2 {ECO:0000303|PubMed:14685263};
GN Name=sms-2; ORFNames=F53H8.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=14685263; DOI=10.1038/sj.emboj.7600034;
RA Huitema K., Van Den Dikkenberg J., Brouwers J.F.H.M., Holthuis J.C.;
RT "Identification of a family of animal sphingomyelin synthases.";
RL EMBO J. 23:33-44(2004).
CC -!- FUNCTION: Sphingomyelin synthases (SM synthase or SMS) synthesize the
CC sphingolipid sphingomyelin (SM) through transfer of the phosphatidyl
CC head group of 1,2-diacyl-sn-glycero-3-phosphocholine
CC (phosphatidylcholine, PC) on to the primary hydroxyl of ceramide (N-
CC acylsphingoid base), yielding 1,2-diacyl-sn-glycerol (diacylglycerol,
CC DAG) as a side product. Functions as a bidirectional lipid
CC cholinephosphotransferases capable of converting PC and ceramide to SM
CC and DAG and vice versa depending on the respective levels of ceramide
CC and DAG as phosphocholine acceptors, respectively.
CC {ECO:0000269|PubMed:14685263}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + an N-acylsphing-4-
CC enine = a 1,2-diacyl-sn-glycerol + a sphingomyelin;
CC Xref=Rhea:RHEA:18765, ChEBI:CHEBI:17636, ChEBI:CHEBI:17815,
CC ChEBI:CHEBI:52639, ChEBI:CHEBI:57643; EC=2.7.8.27;
CC Evidence={ECO:0000269|PubMed:14685263};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18766;
CC Evidence={ECO:0000269|PubMed:14685263};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18767;
CC Evidence={ECO:0000269|PubMed:14685263};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + N-acyl-15-
CC methylhexadecasphing-4-enine = a 1,2-diacyl-sn-glycerol + N-acyl-15-
CC methylhexadecasphing-4-enine-1-phosphocholine; Xref=Rhea:RHEA:34607,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:57643, ChEBI:CHEBI:70775,
CC ChEBI:CHEBI:70846; Evidence={ECO:0000305|PubMed:14685263};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34608;
CC Evidence={ECO:0000305|PubMed:14685263};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:34609;
CC Evidence={ECO:0000305|PubMed:14685263};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000269|PubMed:14685263}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the sphingomyelin synthase family.
CC {ECO:0000305}.
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DR EMBL; FO080855; CCD67244.1; -; Genomic_DNA.
DR PIR; T34296; T34296.
DR RefSeq; NP_508182.1; NM_075781.3.
DR AlphaFoldDB; Q20735; -.
DR STRING; 6239.F53H8.4; -.
DR SwissLipids; SLP:000000014; -.
DR EPD; Q20735; -.
DR PaxDb; Q20735; -.
DR EnsemblMetazoa; F53H8.4.1; F53H8.4.1; WBGene00004893.
DR GeneID; 180445; -.
DR KEGG; cel:CELE_F53H8.4; -.
DR UCSC; F53H8.4; c. elegans.
DR CTD; 180445; -.
DR WormBase; F53H8.4; CE04657; WBGene00004893; sms-2.
DR eggNOG; KOG3058; Eukaryota.
DR HOGENOM; CLU_027104_3_0_1; -.
DR InParanoid; Q20735; -.
DR OMA; RLWWFWL; -.
DR OrthoDB; 599210at2759; -.
DR PhylomeDB; Q20735; -.
DR BRENDA; 2.7.8.27; 1045.
DR Reactome; R-CEL-1660661; Sphingolipid de novo biosynthesis.
DR UniPathway; UPA00222; -.
DR PRO; PR:Q20735; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00004893; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0030173; C:integral component of Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0047493; F:ceramide cholinephosphotransferase activity; ISS:UniProtKB.
DR GO; GO:0033188; F:sphingomyelin synthase activity; ISS:UniProtKB.
DR GO; GO:0046513; P:ceramide biosynthetic process; IBA:GO_Central.
DR GO; GO:0006686; P:sphingomyelin biosynthetic process; ISS:UniProtKB.
DR InterPro; IPR045221; Sphingomyelin_synth-like.
DR InterPro; IPR025749; Sphingomyelin_synth-like_dom.
DR PANTHER; PTHR21290; PTHR21290; 1.
DR Pfam; PF14360; PAP2_C; 1.
PE 1: Evidence at protein level;
KW Lipid metabolism; Membrane; Reference proteome; Sphingolipid metabolism;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..335
FT /note="Phosphatidylcholine:ceramide
FT cholinephosphotransferase 2"
FT /id="PRO_0000221075"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..335
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 210
FT /evidence="ECO:0000250"
FT ACT_SITE 253
FT /evidence="ECO:0000250"
FT ACT_SITE 257
FT /evidence="ECO:0000250"
SQ SEQUENCE 335 AA; 38737 MW; 7FCA39B7B849A4A4 CRC64;
MTNSSEFTDV LQSRDPCVSN GIVINIDPID PEPTPIRKEF TCEDTFHHEH HGNSEGFKTL
TAFLCLMLSA FLNFFLLTVI HDVVPRQPLP DLTFMIIPQQ RWAWSVGDVL STVSSVVAFT
IIFLHHQRWI VLRRTFLLGA IMYGLRAVIL GVTFLPPSFH NRDEICQPQV NRTAMYGMEI
ATRFLTYVIT LGLTSGQDKI LCGDLMFSGH TVVLTIMYFV QLQYTPRGLV ILRYIAAPIT
FLGIAALVVS GGHYTMDVLI AYWLTSHVFW SYHQIFEMRK DDRPQAPLSR LWWFWLCYWF
ESDVADGKLV NKWNWPLEGP QRMHTIMNRI NYKLQ
