SMS2_RAT
ID SMS2_RAT Reviewed; 365 AA.
AC Q4JM44; Q5U2Z1;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 92.
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;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Testis;
RX PubMed=17210739; DOI=10.1677/joe-06-0002;
RA Lee N.P.Y., Mruk D.D., Xia W., Cheng C.Y.;
RT "Cellular localization of sphingomyelin synthase 2 in the seminiferous
RT epithelium of adult rat testes.";
RL J. Endocrinol. 192:17-32(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Brown Norway; TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION.
RX PubMed=21980337; DOI=10.1371/journal.pone.0023644;
RA Subathra M., Qureshi A., Luberto C.;
RT "Sphingomyelin synthases regulate protein trafficking and secretion.";
RL PLoS ONE 6:e23644-e23644(2011).
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 (By similarity). Does not use free
CC phosphorylcholine or CDP-choline as donors (By similarity). Can also
CC transfer phosphoethanolamine head group of phosphatidylethanolamine
CC (PE) on to ceramide (CER) to form ceramide phosphoethanolamine (CPE)
CC (By similarity). Regulates receptor-mediated signal transduction via
CC mitogenic DAG and proapoptotic CER, as well as via SM, a structural
CC component of membrane rafts that serve as platforms for signal
CC transduction and protein sorting (By similarity). To a lesser extent,
CC plays a role in secretory transport via regulation of DAG pool at the
CC Golgi apparatus and its downstream effects on PRKD1 (PubMed:21980337).
CC Required for normal bone matrix mineralization (By similarity).
CC {ECO:0000250|UniProtKB:Q8NHU3, ECO:0000269|PubMed:21980337}.
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 -!- TISSUE SPECIFICITY: Expression restricted to late round spermatids and
CC elongating spermatids but not detected in late elongate spermatids and
CC Sertoli cells (at protein level). {ECO:0000269|PubMed:17210739}.
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; DQ071571; AAY84706.2; -; mRNA.
DR EMBL; BC085803; AAH85803.1; -; mRNA.
DR RefSeq; NP_001014065.1; NM_001014043.1.
DR RefSeq; XP_006233373.1; XM_006233311.3.
DR RefSeq; XP_008759723.1; XM_008761501.1.
DR RefSeq; XP_017446423.1; XM_017590934.1.
DR AlphaFoldDB; Q4JM44; -.
DR STRING; 10116.ENSRNOP00000015020; -.
DR PaxDb; Q4JM44; -.
DR GeneID; 310849; -.
DR KEGG; rno:310849; -.
DR CTD; 166929; -.
DR RGD; 1305778; Sgms2.
DR eggNOG; KOG3058; Eukaryota.
DR InParanoid; Q4JM44; -.
DR OrthoDB; 599210at2759; -.
DR PhylomeDB; Q4JM44; -.
DR TreeFam; TF314547; -.
DR BRENDA; 2.7.8.27; 5301.
DR Reactome; R-RNO-1660661; Sphingolipid de novo biosynthesis.
DR PRO; PR:Q4JM44; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0030173; C:integral component of Golgi membrane; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0047493; F:ceramide cholinephosphotransferase activity; ISO:RGD.
DR GO; GO:0002950; F:ceramide phosphoethanolamine synthase activity; ISO:RGD.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0033188; F:sphingomyelin synthase activity; ISO:RGD.
DR GO; GO:0046513; P:ceramide biosynthetic process; ISO:RGD.
DR GO; GO:1905373; P:ceramide phosphoethanolamine biosynthetic process; ISO:RGD.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0030500; P:regulation of bone mineralization; ISS:UniProtKB.
DR GO; GO:0006686; P:sphingomyelin biosynthetic process; ISO:RGD.
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 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_0000290123"
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 219..239
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 9..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..28
FT /note="Polar 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"
FT CONFLICT 264
FT /note="I -> V (in Ref. 2; AAH85803)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 365 AA; 42223 MW; A3BD73AFF11245D0 CRC64;
MDIIETAKLE GHLESQTNNS TNTYTSPTEA VEEEDKNGKG KPKTLSNGLR KGAKKYPDYI
QISMPNDSRN KLPLEWWKTG IAFVYALFNL ILTTVMITVV HERVPPKELS PPLPDKFFDY
VDRVKWAFSV SEINGMVLVG LWLTQWLFLR YKSIVGRRFF FIMGTLYLYR CITMYVTTLP
VPGMHFQCAP KLNGDSQAKI QRILRLLSGG GLSITGSHIL CGDFLFSGHT VVLTLTYLFI
KEYSPRHFWW YHLVCWLLSA AGIICILVAH EHYTVDVIIA YYITTRLFWW YHSMANEKNL
KVSSQTNFLS RAWWFPIFYF FEKNVQGSIP CCFSWPLSWP PGCFKSSCKK YSRVQKIGED
NEKST
