SMS3_CAEEL
ID SMS3_CAEEL Reviewed; 340 AA.
AC Q965Q4;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Putative phosphatidylcholine:ceramide cholinephosphotransferase 3;
DE EC=2.7.8.27;
DE AltName: Full=Sphingomyelin synthase 3;
GN Name=sms-3; ORFNames=Y22D7AL.8;
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 IDENTIFICATION.
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: Bidirectional lipid cholinephosphotransferase capable of
CC converting phosphatidylcholine (PC) and ceramide to sphingomyelin (SM)
CC and diacylglycerol (DAG) and vice versa. Direction is dependent on the
CC relative concentrations of DAG and ceramide as phosphocholine
CC acceptors. Directly and specifically recognizes the choline head group
CC on the substrate. Also requires two fatty chains on the choline-P donor
CC molecule in order to be recognized efficiently as a substrate. Does not
CC function strictly as a SM synthase (By similarity). {ECO:0000250}.
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 -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
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; FO081783; CCD73749.1; -; Genomic_DNA.
DR RefSeq; NP_497425.1; NM_065024.3.
DR AlphaFoldDB; Q965Q4; -.
DR STRING; 6239.Y22D7AL.8; -.
DR PaxDb; Q965Q4; -.
DR PeptideAtlas; Q965Q4; -.
DR EnsemblMetazoa; Y22D7AL.8a.1; Y22D7AL.8a.1; WBGene00004894.
DR EnsemblMetazoa; Y22D7AL.8a.2; Y22D7AL.8a.2; WBGene00004894.
DR EnsemblMetazoa; Y22D7AL.8a.3; Y22D7AL.8a.3; WBGene00004894.
DR EnsemblMetazoa; Y22D7AL.8a.4; Y22D7AL.8a.4; WBGene00004894.
DR EnsemblMetazoa; Y22D7AL.8a.5; Y22D7AL.8a.5; WBGene00004894.
DR GeneID; 175313; -.
DR UCSC; Y22D7AL.8; c. elegans.
DR CTD; 175313; -.
DR WormBase; Y22D7AL.8a; CE26501; WBGene00004894; sms-3.
DR eggNOG; KOG3058; Eukaryota.
DR HOGENOM; CLU_027104_3_0_1; -.
DR InParanoid; Q965Q4; -.
DR OMA; TLYAMRS; -.
DR PhylomeDB; Q965Q4; -.
DR Reactome; R-CEL-1660661; Sphingolipid de novo biosynthesis.
DR UniPathway; UPA00222; -.
DR PRO; PR:Q965Q4; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00004894; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q965Q4; 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; 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; 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 3: Inferred from homology;
KW Lipid metabolism; Membrane; Reference proteome; Sphingolipid metabolism;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..340
FT /note="Putative phosphatidylcholine:ceramide
FT cholinephosphotransferase 3"
FT /id="PRO_0000221076"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..340
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 183
FT /evidence="ECO:0000250"
FT ACT_SITE 226
FT /evidence="ECO:0000250"
FT ACT_SITE 230
FT /evidence="ECO:0000250"
SQ SEQUENCE 340 AA; 38185 MW; 0C89549F1D91E287 CRC64;
MGSVSKTVIS ARGASPDDEQ NGTKNGISNG SEWAKCIFLF FFLFIAGMSN WAVLAYTHDY
VPRESLPDIV FSLVSEQRWA SSLGDFCVAL CIVMLGALLV IHQHRGTILK RVVFCAGTLY
AMRSVTLAAT QLPSGYTDNQ GRCRDQVESE AGVFFGRLFE QTIRIGFQSK DQMLCGDLLF
SGHTLVMVTC SLAVAYYLPK SIKPLQWVSH VACLIGMICM TISRTHYTID VVIAYWLSNM
VFRMYHAYCE VDMCMERRKS ILYSWWPCRI VDWLEQDIVP GRLENRCQLP WRRSTPRGQE
RGGASAESSD SSVTMCDNIT TSHHQKHVSI SSSSTYPLPC
