SMS2_MACFA
ID SMS2_MACFA Reviewed; 365 AA.
AC Q4R763;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Phosphatidylcholine:ceramide cholinephosphotransferase 2;
DE EC=2.7.8.27 {ECO:0000250|UniProtKB:Q8NHU3};
DE AltName: Full=Sphingomyelin synthase 2;
GN Name=SGMS2; ORFNames=QtsA-16184;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Sphingomyelin synthase that primarily contributes to
CC sphingomyelin synthesis and homeostasis at the plasma membrane.
CC Catalyzes the reversible transfer of phosphocholine moiety in
CC sphingomyelin biosynthesis: in the forward reaction transfers
CC phosphocholine head group of phosphatidylcholine (PC) on to ceramide
CC (CER) to form ceramide phosphocholine (sphingomyelin, SM) and
CC diacylglycerol (DAG) as by-product, and in the reverse reaction
CC transfers phosphocholine from SM to DAG to form PC and CER. The
CC direction of the reaction appears to depend on the levels of CER and
CC DAG in the plasma membrane. Does not use free phosphorylcholine or CDP-
CC choline as donors. Can also transfer phosphoethanolamine head group of
CC phosphatidylethanolamine (PE) on to ceramide (CER) to form ceramide
CC phosphoethanolamine (CPE). Regulates receptor-mediated signal
CC transduction via mitogenic DAG and proapoptotic CER, as well as via SM,
CC a structural component of membrane rafts that serve as platforms for
CC signal transduction and protein sorting. To a lesser extent, plays a
CC role in secretory transport via regulation of DAG pool at the Golgi
CC apparatus and its downstream effects on PRKD1. Required for normal bone
CC matrix mineralization. {ECO:0000250|UniProtKB:Q8NHU3}.
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:0000250|UniProtKB:Q8NHU3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18766;
CC Evidence={ECO:0000250|UniProtKB:Q8NHU3};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18767;
CC Evidence={ECO:0000250|UniProtKB:Q8NHU3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + an N-
CC acylsphing-4-enine = 1,2-dihexadecanoyl-sn-glycerol + a
CC sphingomyelin; Xref=Rhea:RHEA:43324, ChEBI:CHEBI:17636,
CC ChEBI:CHEBI:52639, ChEBI:CHEBI:72999, ChEBI:CHEBI:82929;
CC Evidence={ECO:0000250|UniProtKB:Q8NHU3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43325;
CC Evidence={ECO:0000250|UniProtKB:Q8NHU3};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:43326;
CC Evidence={ECO:0000250|UniProtKB:Q8NHU3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-2-acyl-sn-3-glycerol + a sphingomyelin = a
CC 1-(9Z-octadecenoyl)-2-acyl-sn-glycero-3-phosphocholine + an N-
CC acylsphing-4-enine; Xref=Rhea:RHEA:43320, ChEBI:CHEBI:17636,
CC ChEBI:CHEBI:52639, ChEBI:CHEBI:78421, ChEBI:CHEBI:82983;
CC Evidence={ECO:0000250|UniProtKB:Q8NHU3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43321;
CC Evidence={ECO:0000250|UniProtKB:Q8NHU3};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:43322;
CC Evidence={ECO:0000250|UniProtKB:Q8NHU3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + N-
CC hexadecanoylsphinganine = a 1,2-diacyl-sn-glycerol + N-hexadecanoyl-
CC sphinganine-1-phosphocholine; Xref=Rhea:RHEA:41796,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:57643, ChEBI:CHEBI:67042,
CC ChEBI:CHEBI:78647; Evidence={ECO:0000250|UniProtKB:Q8NHU3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41797;
CC Evidence={ECO:0000250|UniProtKB:Q8NHU3};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:41798;
CC Evidence={ECO:0000250|UniProtKB:Q8NHU3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + N-hexadecanoyl-
CC (4R)-hydroxysphinganine = a 1,2-diacyl-sn-glycerol + N-hexadecanoyl-
CC (4R)-hydroxysphinganine-phosphocholine; Xref=Rhea:RHEA:42140,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:57643, ChEBI:CHEBI:65107,
CC ChEBI:CHEBI:78650; Evidence={ECO:0000250|UniProtKB:Q8NHU3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42141;
CC Evidence={ECO:0000250|UniProtKB:Q8NHU3};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42142;
CC Evidence={ECO:0000250|UniProtKB:Q8NHU3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + N-
CC hexadecanoylsphinganine = a 1,2-diacyl-sn-glycerol + N-hexadecanoyl-
CC sphinganine-1-phosphoethanolamine; Xref=Rhea:RHEA:42128,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:64612, ChEBI:CHEBI:67042,
CC ChEBI:CHEBI:78654; Evidence={ECO:0000250|UniProtKB:Q8NHU3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42129;
CC Evidence={ECO:0000250|UniProtKB:Q8NHU3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + N-
CC hexadecanoyl-(4R)-hydroxysphinganine = a 1,2-diacyl-sn-glycerol + N-
CC hexadecanoyl-(4R)-hydroxysphinganine-1-phosphoethanolamine;
CC Xref=Rhea:RHEA:42144, ChEBI:CHEBI:17815, ChEBI:CHEBI:64612,
CC ChEBI:CHEBI:65107, ChEBI:CHEBI:78656;
CC Evidence={ECO:0000250|UniProtKB:Q8NHU3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42145;
CC Evidence={ECO:0000250|UniProtKB:Q8NHU3};
CC -!- PATHWAY: Sphingolipid metabolism. {ECO:0000250|UniProtKB:Q8NHU3}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8NHU3};
CC Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q8NHU3}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Primarily localized at the plasma membrane with a
CC small fraction at the Golgi apparatus. {ECO:0000250|UniProtKB:Q8NHU3}.
CC -!- PTM: Palmitoylated on Cys-331, Cys-332, Cys-343 and Cys-348; which
CC plays an important role in plasma membrane localization. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sphingomyelin synthase family.
CC {ECO:0000305}.
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DR EMBL; AB168962; BAE01060.1; -; mRNA.
DR RefSeq; NP_001270184.1; NM_001283255.1.
DR AlphaFoldDB; Q4R763; -.
DR STRING; 9541.XP_005555687.1; -.
DR PRIDE; Q4R763; -.
DR GeneID; 101867034; -.
DR CTD; 166929; -.
DR eggNOG; KOG3058; Eukaryota.
DR OrthoDB; 599210at2759; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0033188; F:sphingomyelin synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0030500; P:regulation of bone mineralization; ISS:UniProtKB.
DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Cell membrane; Golgi apparatus; Kinase; Lipid metabolism; Lipoprotein;
KW Membrane; Palmitate; Reference proteome; Sphingolipid metabolism;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..365
FT /note="Phosphatidylcholine:ceramide
FT cholinephosphotransferase 2"
FT /id="PRO_0000290122"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..365
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 229
FT /evidence="ECO:0000250"
FT ACT_SITE 272
FT /evidence="ECO:0000250"
FT ACT_SITE 276
FT /evidence="ECO:0000250"
FT LIPID 331
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 332
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 343
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 348
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 365 AA; 42352 MW; BAC33D21106F8E8D CRC64;
MDIIETAKLE EHLENQPSDP TNTYTRPTEP VEEENKNGNG KPKSLSSGLR KGTKKYPDYI
QIAMPTESRN KFPLEWWKTG IAFIYAVFNL VLTTVMITVV HERVPPKELS PPLPDKFFDY
IDRVKWAFSV SEINGIILVG LWITQWLFLR YKSIVGRRFC FIIGTLYLYR CITMYVTTLP
VPGMHFQCAP KLNGDSQAKV QRILRLISGG GLSITGSHIL CGDFLFSGHT VTLTLTYLFI
KEYSPRHFWW YHLICWLLSA AGIICILVAH EHYTVDVIIA YYITTRLFWW YHSMANEKNL
KVSLQTNFLS RAWWFPIFYF FEKNVQGSIP CCFSWPLSWP PGCFKSSCKK YSRVQKIGED
NEKST
