SMS1_RAT
ID SMS1_RAT Reviewed; 419 AA.
AC Q7TSX5;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Phosphatidylcholine:ceramide cholinephosphotransferase 1;
DE EC=2.7.8.27 {ECO:0000250|UniProtKB:Q86VZ5};
DE AltName: Full=Protein Mob;
DE AltName: Full=Sphingomyelin synthase 1;
DE AltName: Full=Transmembrane protein 23;
GN Name=Sgms1; Synonyms=Mob, Tmem23;
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 {ECO:0000312|EMBL:AAP37281.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Heart;
RA Yuan H.F., Wang X., Wang D.M., Li H.M., Feng K., Bai C.X., Zhang R.,
RA Chen L., Li Y.H., Gao Y.H., Zhen M., Yue W., Xie C., Xie X.Y., Niu L.L.,
RA Yue W., Zhang J., Cao H., Pei X.T.;
RT "Complete cDNA sequence of a novel gene, rat mob.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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: Major sphingomyelin synthase at the Golgi apparatus.
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 depends on the levels of CER and DAG in Golgi
CC membranes. Does not use free phosphorylcholine or CDP-choline as donor.
CC Regulates receptor-mediated signal transduction via mitogenic DAG and
CC proapoptotic CER, as well as via SM, a structural component of membrane
CC rafts that serve as platforms for signal transduction and protein
CC sorting (By similarity). Plays a role in secretory transport via
CC regulation of DAG pool at the Golgi apparatus and its downstream
CC effects on PRKD1 (PubMed:21980337). {ECO:0000250|UniProtKB:Q86VZ5,
CC 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:Q86VZ5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18766;
CC Evidence={ECO:0000250|UniProtKB:Q86VZ5};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18767;
CC Evidence={ECO:0000250|UniProtKB:Q86VZ5};
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:Q86VZ5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43321;
CC Evidence={ECO:0000250|UniProtKB:Q86VZ5};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:43322;
CC Evidence={ECO:0000250|UniProtKB:Q86VZ5};
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:Q86VZ5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41797;
CC Evidence={ECO:0000250|UniProtKB:Q86VZ5};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:41798;
CC Evidence={ECO:0000250|UniProtKB:Q86VZ5};
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:Q86VZ5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42141;
CC Evidence={ECO:0000250|UniProtKB:Q86VZ5};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42142;
CC Evidence={ECO:0000250|UniProtKB:Q86VZ5};
CC -!- PATHWAY: Sphingolipid metabolism. {ECO:0000250|UniProtKB:Q86VZ5}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q86VZ5}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the sphingomyelin synthase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP37281.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY280961; AAP37281.1; ALT_INIT; mRNA.
DR EMBL; BC081693; AAH81693.1; -; mRNA.
DR RefSeq; NP_852051.2; NM_181386.2.
DR AlphaFoldDB; Q7TSX5; -.
DR SMR; Q7TSX5; -.
DR STRING; 10116.ENSRNOP00000051643; -.
DR PaxDb; Q7TSX5; -.
DR Ensembl; ENSRNOT00000054761; ENSRNOP00000051643; ENSRNOG00000012536.
DR GeneID; 353229; -.
DR KEGG; rno:353229; -.
DR UCSC; RGD:727912; rat.
DR CTD; 259230; -.
DR RGD; 727912; Sgms1.
DR eggNOG; KOG3058; Eukaryota.
DR GeneTree; ENSGT00940000158306; -.
DR InParanoid; Q7TSX5; -.
DR OMA; WICWTLS; -.
DR OrthoDB; 599210at2759; -.
DR PhylomeDB; Q7TSX5; -.
DR TreeFam; TF314547; -.
DR Reactome; R-RNO-1660661; Sphingolipid de novo biosynthesis.
DR PRO; PR:Q7TSX5; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000012536; Expressed in testis and 19 other tissues.
DR ExpressionAtlas; Q7TSX5; baseline and differential.
DR Genevisible; Q7TSX5; RN.
DR GO; GO:0000138; C:Golgi trans cisterna; 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; 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: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; ISS:HGNC-UCL.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
DR GO; GO:0046513; P:ceramide biosynthetic process; ISO:RGD.
DR GO; GO:0006954; P:inflammatory response; IDA:RGD.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:RGD.
DR GO; GO:0006686; P:sphingomyelin biosynthetic process; ISS:HGNC-UCL.
DR Gene3D; 1.10.150.50; -; 1.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR045221; Sphingomyelin_synth-like.
DR InterPro; IPR025749; Sphingomyelin_synth-like_dom.
DR PANTHER; PTHR21290; PTHR21290; 1.
DR Pfam; PF14360; PAP2_C; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; Golgi apparatus; Kinase; Lipid metabolism; Membrane;
KW Phosphoprotein; Reference proteome; Sphingolipid metabolism; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..419
FT /note="Phosphatidylcholine:ceramide
FT cholinephosphotransferase 1"
FT /id="PRO_0000221070"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 331..419
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 13..76
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184,
FT ECO:0000305"
FT ACT_SITE 291
FT /evidence="ECO:0000250|UniProtKB:Q86VZ5"
FT ACT_SITE 334
FT /evidence="ECO:0000250|UniProtKB:Q86VZ5"
FT ACT_SITE 338
FT /evidence="ECO:0000250|UniProtKB:Q86VZ5"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86VZ5"
SQ SEQUENCE 419 AA; 49014 MW; CD1E73E61BA6F141 CRC64;
MLSASTMKEV VYWSPKKVAD WLLENAMPEY CEPLGHFTGQ DLINLTQEDF TKPPLCRVSS
DNGQRLLDMI ETLKMEHHIE AHKNGHANGH LSIGVDIPNP DGSFSIKIKP NGMPNGFRKE
MIKIPMPEPE RSQYPMEWGK TLLAFLYALS CFVLTTVMIS VVHERVPPKE VQPPLPDTFF
DHFNRVQWAF SICEINGMIL VGLWLFQWLL LKYKSIISRR FFCIVGTLYL YRCITMYVTT
LPVPGMHFNC SPKLFGDWEA QVRRIMKLIA GGGLSITGSH NMCGDYLYSG HTVMLTLTYL
FIKEYSPRRL WWYHWICWLL SVVGIFCILL AHDHYTVDVV VAYYITTRLF WWYHTMANQQ
VLKEASQMNL LARVWWYRPF QYFEKNVQGI VPRSYHWPLP WPVVHLSRQV KYSRLVNDT
