SMS1_CAEEL
ID SMS1_CAEEL Reviewed; 469 AA.
AC Q9U3D4; B3GWD9; H2L2K5; Q9XTV2;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Phosphatidylcholine:ceramide cholinephosphotransferase 1;
DE Short=PC:ceramide cholinephosphotransferase 1 {ECO:0000303|PubMed:14685263};
DE EC=2.7.8.27 {ECO:0000269|PubMed:14685263};
DE AltName: Full=Sphingomyelin synthase 1 {ECO:0000303|PubMed:14685263};
DE Short=CSS3alpha1 {ECO:0000303|PubMed:14685263};
DE Short=SMS-1 {ECO:0000303|PubMed:14685263};
GN Name=sms-1; ORFNames=H21P03.3;
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], AND ALTERNATIVE SPLICING.
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: Golgi apparatus membrane {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=b {ECO:0000305};
CC IsoId=Q9U3D4-1; Sequence=Displayed;
CC Name=a {ECO:0000305};
CC IsoId=Q9U3D4-2; Sequence=VSP_050674;
CC Name=c;
CC IsoId=Q9U3D4-3; Sequence=VSP_039807;
CC Name=d;
CC IsoId=Q9U3D4-4; Sequence=VSP_061062;
CC -!- SIMILARITY: Belongs to the sphingomyelin synthase family.
CC {ECO:0000305}.
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DR EMBL; Z95619; CAB09114.2; -; Genomic_DNA.
DR EMBL; Z95619; CAB54269.2; -; Genomic_DNA.
DR EMBL; Z95619; CAQ58114.2; -; Genomic_DNA.
DR EMBL; BX284604; CCE72098.1; -; Genomic_DNA.
DR PIR; T23111; T23111.
DR PIR; T23112; T23112.
DR RefSeq; NP_001129861.2; NM_001136389.2. [Q9U3D4-3]
DR RefSeq; NP_001255559.1; NM_001268630.1. [Q9U3D4-4]
DR RefSeq; NP_502168.2; NM_069767.2. [Q9U3D4-1]
DR RefSeq; NP_502169.2; NM_069768.4. [Q9U3D4-2]
DR AlphaFoldDB; Q9U3D4; -.
DR BioGRID; 43169; 2.
DR DIP; DIP-25498N; -.
DR IntAct; Q9U3D4; 1.
DR STRING; 6239.H21P03.3b; -.
DR SwissLipids; SLP:000000013; -.
DR EPD; Q9U3D4; -.
DR PaxDb; Q9U3D4; -.
DR EnsemblMetazoa; H21P03.3a.1; H21P03.3a.1; WBGene00004892. [Q9U3D4-2]
DR EnsemblMetazoa; H21P03.3b.1; H21P03.3b.1; WBGene00004892. [Q9U3D4-1]
DR EnsemblMetazoa; H21P03.3c.1; H21P03.3c.1; WBGene00004892. [Q9U3D4-3]
DR EnsemblMetazoa; H21P03.3d.1; H21P03.3d.1; WBGene00004892. [Q9U3D4-4]
DR GeneID; 178072; -.
DR KEGG; cel:CELE_H21P03.3; -.
DR UCSC; H21P03.3a; c. elegans. [Q9U3D4-1]
DR CTD; 178072; -.
DR WormBase; H21P03.3a; CE44486; WBGene00004892; sms-1. [Q9U3D4-2]
DR WormBase; H21P03.3b; CE44496; WBGene00004892; sms-1. [Q9U3D4-1]
DR WormBase; H21P03.3c; CE44516; WBGene00004892; sms-1. [Q9U3D4-3]
DR WormBase; H21P03.3d; CE46610; WBGene00004892; sms-1.
DR eggNOG; KOG3058; Eukaryota.
DR GeneTree; ENSGT00940000170729; -.
DR InParanoid; Q9U3D4; -.
DR OMA; YGMRCIT; -.
DR OrthoDB; 599210at2759; -.
DR PhylomeDB; Q9U3D4; -.
DR BRENDA; 2.7.8.27; 1045.
DR Reactome; R-CEL-1660661; Sphingolipid de novo biosynthesis.
DR SignaLink; Q9U3D4; -.
DR UniPathway; UPA00222; -.
DR PRO; PR:Q9U3D4; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00004892; Expressed in embryo and 4 other tissues.
DR ExpressionAtlas; Q9U3D4; baseline and differential.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0030173; C:integral component of Golgi membrane; ISS: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; IBA:GO_Central.
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 Alternative splicing; Golgi apparatus; Lipid metabolism; Membrane;
KW Reference proteome; Sphingolipid metabolism; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..469
FT /note="Phosphatidylcholine:ceramide
FT cholinephosphotransferase 1"
FT /id="PRO_0000221074"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 376..469
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 40..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 336
FT /evidence="ECO:0000250"
FT ACT_SITE 379
FT /evidence="ECO:0000250"
FT ACT_SITE 383
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..117
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_039807"
FT VAR_SEQ 1..56
FT /note="MSVTVEVADEETHDVPLVEQVRTTPDQNVDVKVQENNVVTTKIGPKLETIPA
FT AKMQ -> MKMSWNHQYTNYGSIA (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_050674"
FT VAR_SEQ 1..54
FT /note="Missing (in isoform d)"
FT /id="VSP_061062"
SQ SEQUENCE 469 AA; 52642 MW; 62BBE972FC8D1911 CRC64;
MSVTVEVADE ETHDVPLVEQ VRTTPDQNVD VKVQENNVVT TKIGPKLETI PAAKMQDDNG
DEEKAENSEG AAAEKVEKQH DDDGVVVHEE TDGVASSRSS HHDKQKPGET KKSGDGKMDD
DDIITTARSS SRRICGSAAS SSDSETADDA PLLPDEGPSH AVRLEMPGDK PASPHDRFPK
TPLKTLVAFL MLVVAAAGNT ITLSWIHERY PLTPPLPDIV FELIPKIPWG LRLCENLMIG
SFVSLLVLIL FHRHRWIVLR RLCFIGSILY GMRCITMMVT PVPKADEDFE CSPRFGENAT
FSLIVMRGVW SMFGLGLNLF DNQKVVLCGD YIYSGHTLVL VVSALFIGEY SPRRFYILHW
LSWLVCSVGV IFLVLSHGHY TIDVILSYFA CTRVFWAYHT QAAHPSIRLS VQNHQAKEFW
FPLLRWFEGD IRRPVPRRFD CPISYSQVCN AFRRVRPRGR NGAARPAFE
