SMS1_CHICK
ID SMS1_CHICK Reviewed; 417 AA.
AC Q7T3T4; Q5ZI65;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Phosphatidylcholine:ceramide cholinephosphotransferase 1;
DE EC=2.7.8.27;
DE AltName: Full=Protein Mob;
DE AltName: Full=Sphingomyelin synthase 1;
GN Name=SGMS1; Synonyms=MOB; ORFNames=RCJMB04_29o9;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031 {ECO:0000312|EMBL:AAP37282.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Bone marrow;
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, chicken mob.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Sphingomyelin synthases synthesize the sphingolipid,
CC sphingomyelin, through transfer of the phosphatidyl head group,
CC phosphatidylcholine, on to the primary hydroxyl of ceramide. The
CC reaction is bidirectional depending on the respective levels of the
CC sphingolipid and ceramide. Golgi apparatus SMS1 directly and
CC specifically recognizes the choline head group on the substrate,
CC requiring two fatty chains on the choline-P donor molecule in order to
CC be recognized efficiently as a substrate. Major form in macrophages.
CC Required for cell growth in certain cell types. Suppresses BAX-mediated
CC apoptosis and also prevents cell death in response to stimuli such as
CC hydrogen peroxide, osmotic stress, elevated temperature and exogenously
CC supplied sphingolipids. May protect against cell death by reversing the
CC stress-inducible increase in levels of proapoptotic ceramide (By
CC 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 -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sphingomyelin synthase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP37282.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.; Evidence={ECO:0000305};
CC Sequence=CAG32578.1; 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; AY280962; AAP37282.1; ALT_SEQ; mRNA.
DR EMBL; AJ720919; CAG32578.1; ALT_SEQ; mRNA.
DR RefSeq; NP_989721.2; NM_204390.2.
DR RefSeq; XP_015134154.1; XM_015278668.1.
DR RefSeq; XP_015134155.1; XM_015278669.1.
DR RefSeq; XP_015134156.1; XM_015278670.1.
DR RefSeq; XP_015134157.1; XM_015278671.1.
DR RefSeq; XP_015134158.1; XM_015278672.1.
DR RefSeq; XP_015134159.1; XM_015278673.1.
DR RefSeq; XP_015134160.1; XM_015278674.1.
DR AlphaFoldDB; Q7T3T4; -.
DR SMR; Q7T3T4; -.
DR STRING; 9031.ENSGALP00000005856; -.
DR PaxDb; Q7T3T4; -.
DR GeneID; 378907; -.
DR KEGG; gga:378907; -.
DR CTD; 259230; -.
DR VEuPathDB; HostDB:geneid_378907; -.
DR eggNOG; KOG3058; Eukaryota.
DR HOGENOM; CLU_027104_1_0_1; -.
DR InParanoid; Q7T3T4; -.
DR OrthoDB; 599210at2759; -.
DR PhylomeDB; Q7T3T4; -.
DR BRENDA; 2.7.8.27; 1306.
DR PRO; PR:Q7T3T4; -.
DR Proteomes; UP000000539; 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; ISS:AgBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0047493; F:ceramide cholinephosphotransferase activity; ISS:AgBase.
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:0046513; P:ceramide biosynthetic process; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; ISS:AgBase.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:AgBase.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006686; P:sphingomyelin biosynthetic process; ISS:AgBase.
DR Gene3D; 1.10.150.50; -; 1.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR041418; SAM_3.
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 Pfam; PF18016; SAM_3; 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 Reference proteome; Sphingolipid metabolism; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..417
FT /note="Phosphatidylcholine:ceramide
FT cholinephosphotransferase 1"
FT /id="PRO_0000221071"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..417
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 11..74
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184,
FT ECO:0000305"
FT ACT_SITE 289
FT /evidence="ECO:0000250"
FT ACT_SITE 332
FT /evidence="ECO:0000250"
FT ACT_SITE 336
FT /evidence="ECO:0000250"
FT CONFLICT 224
FT /note="C -> G (in Ref. 2; CAG32578)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 417 AA; 49014 MW; 6370876619F1C0E6 CRC64;
MSGRMKEVVS WSPEEVTNWL MENAVPEYCE PLKSFTGQDL INLTEEDFKK TPLSRVSSDS
GQQLLHMIET LKMAHHIEAH KNGHVNGHIH VSVNNTAHEN GFSSKTKLNG VPNGYKKEMI
KIPMPEPERL QYPMEWGKTF LAFIYALFCF IFTTVTISVV HERVPPKEVQ PPLPDAFFDR
FDRVQWAFSI CEINGMILVG LWLVQWLLLK YKSIISRRFF CIVCTLYLYR CITMYVTTLP
VPGMHFKCSP KLFGDWESHL RRIMKLIAGG GLSITGSHNM CGDYLYSGHT VILTLTYLFI
KEYSPRRLWW YHWLCWTLSM VGMFCILLAH DHYTVDVVVA YYITTRLFWW YHTMANQQVL
KEASQTNLLA RVWWYKPFQY FEKNVQGIVP RSYHWPFPWP VLHRGRQVKY SRLVNDT
