SMS1_PIG
ID SMS1_PIG Reviewed; 418 AA.
AC A0AAS4;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Phosphatidylcholine:ceramide cholinephosphotransferase 1;
DE EC=2.7.8.27 {ECO:0000250|UniProtKB:Q86VZ5};
DE AltName: Full=Sphingomyelin synthase 1;
GN Name=SGMS1; Synonyms=SMS1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=17156943; DOI=10.1016/j.gene.2006.10.013;
RA Guillen N., Navarro M.A., Surra J.C., Arnal C., Fernandez-Juan M.,
RA Cebrian-Perez J.A., Osada J.;
RT "Cloning, characterization, expression and comparative analysis of pig
RT Golgi membrane sphingomyelin synthase 1.";
RL Gene 388:117-124(2007).
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. Plays a role in secretory transport via regulation of DAG pool
CC at the Golgi apparatus and its downstream effects on PRKD1.
CC {ECO:0000250|UniProtKB:Q86VZ5}.
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 -!- TISSUE SPECIFICITY: Widely expressed. Highest expression in the
CC cardiovascular system. {ECO:0000269|PubMed:17156943}.
CC -!- SIMILARITY: Belongs to the sphingomyelin synthase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAJ81057.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.; Evidence={ECO:0000305};
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DR EMBL; AM233751; CAJ81057.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001090907.1; NM_001097438.2.
DR RefSeq; XP_013838963.1; XM_013983509.1.
DR AlphaFoldDB; A0AAS4; -.
DR SMR; A0AAS4; -.
DR STRING; 9823.ENSSSCP00000011122; -.
DR PaxDb; A0AAS4; -.
DR GeneID; 100037303; -.
DR KEGG; ssc:100037303; -.
DR CTD; 259230; -.
DR eggNOG; KOG3058; Eukaryota.
DR InParanoid; A0AAS4; -.
DR OrthoDB; 599210at2759; -.
DR BRENDA; 2.7.8.27; 6170.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
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:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0047493; F:ceramide cholinephosphotransferase activity; IBA:GO_Central.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0033188; F:sphingomyelin synthase activity; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0046513; P:ceramide biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006686; P:sphingomyelin biosynthetic process; IBA:GO_Central.
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..418
FT /note="Phosphatidylcholine:ceramide
FT cholinephosphotransferase 1"
FT /id="PRO_0000290121"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 12..75
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT ACT_SITE 290
FT /evidence="ECO:0000250|UniProtKB:Q86VZ5"
FT ACT_SITE 333
FT /evidence="ECO:0000250|UniProtKB:Q86VZ5"
FT ACT_SITE 337
FT /evidence="ECO:0000250|UniProtKB:Q86VZ5"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86VZ5"
SQ SEQUENCE 418 AA; 48984 MW; A783E4D04DBAAD4F CRC64;
MSASTMKEVV YWSPKKVADW LLENAMPEYC EPLEHFTGRD LINLTQEDFT KPPLCRVSSD
NGQRLLDMIE TLKMEHHMEA HKNGHANGHL SIGTDVPAPD GSFSIKVKPN GMPNGYRKEM
IKIPMPEPER SQYPMEWGKT FLAFLYALSC FVLTTVMISV VHERVPPKEV QPPLPDTFFD
HFNRVQWAFS ICEINGMILV GLWLIQWLLL KYKSIISRRF FCIVGTLYLY RCITMYVTTL
PVPGMHFNCS PKLFGDWEAQ LRRIMKLIAG GGLSITGSHN MCGDYLYSGH TVMLTLTYLF
IKEYSPRRLW WYHWICWLLS VVGIFCILLA HDHYTVDVVV AYYITTRLFW WYHTMANQQV
LKEASQMNLL ARVWWYRPFQ YFEKNVQGIV PRSYHWPFPW PVVHLGRQVK YSRLVNDT
