SMSR1_CAEEL
ID SMSR1_CAEEL Reviewed; 483 AA.
AC Q20696;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Sphingomyelin synthase-related 1;
DE EC=2.7.8.-;
GN ORFNames=F53B1.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP IDENTIFICATION.
RX PubMed=14685263; DOI=10.1038/sj.emboj.7600034;
RA Huitema K., Van Den Dikkenberg J., Brouwers J.F.H.M., Holthuis J.C.;
RT "Identification of a family of animal sphingomyelin synthases.";
RL EMBO J. 23:33-44(2004).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the sphingomyelin synthase family.
CC {ECO:0000305}.
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DR EMBL; FO081052; CCD68826.1; -; Genomic_DNA.
DR PIR; T16443; T16443.
DR RefSeq; NP_508389.1; NM_075988.5.
DR AlphaFoldDB; Q20696; -.
DR SMR; Q20696; -.
DR STRING; 6239.F53B1.2; -.
DR EPD; Q20696; -.
DR PaxDb; Q20696; -.
DR PeptideAtlas; Q20696; -.
DR EnsemblMetazoa; F53B1.2.1; F53B1.2.1; WBGene00018735.
DR GeneID; 180524; -.
DR KEGG; cel:CELE_F53B1.2; -.
DR UCSC; F53B1.2; c. elegans.
DR CTD; 180524; -.
DR WormBase; F53B1.2; CE04642; WBGene00018735; -.
DR eggNOG; KOG3058; Eukaryota.
DR GeneTree; ENSGT00940000155540; -.
DR HOGENOM; CLU_027104_1_0_1; -.
DR InParanoid; Q20696; -.
DR OMA; WKTVLSC; -.
DR OrthoDB; 599210at2759; -.
DR PhylomeDB; Q20696; -.
DR Reactome; R-CEL-1660661; Sphingolipid de novo biosynthesis.
DR PRO; PR:Q20696; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00018735; Expressed in embryo and 4 other tissues.
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:0016021; C:integral component of membrane; NAS:UniProtKB.
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:0033188; F:sphingomyelin synthase activity; IBA:GO_Central.
DR GO; GO:0046513; P:ceramide biosynthetic process; IBA:GO_Central.
DR GO; GO:0006686; P:sphingomyelin biosynthetic process; NAS:UniProtKB.
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 Pfam; PF00536; SAM_1; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 3: Inferred from homology;
KW Lipid metabolism; Membrane; Reference proteome; Sphingolipid metabolism;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..483
FT /note="Sphingomyelin synthase-related 1"
FT /id="PRO_0000221077"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 397..483
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 450..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 330
FT /evidence="ECO:0000250"
FT ACT_SITE 373
FT /evidence="ECO:0000250"
FT ACT_SITE 377
FT /evidence="ECO:0000250"
SQ SEQUENCE 483 AA; 54988 MW; 41828EA82305FB6C CRC64;
MLDNRPIPAD PNEWRCEDVG NWLKKIGMAK YADLIAMKHK VDGKCLLALT DTDLKDPPVS
INCLGDIKKI LFAIEFLSQK VVEIGNSGVH HRSTPNGNGP SLKNSKDGLL VEYNEQNHLS
ISGEDVYTTT RRAEIVEDEE TLLDTLAKSS DGTSTVQLIS REEIIRQVER PDTYFKSVAK
LLIAFAYSSL SFLMTSFVMV LVHDRVPDTK TYPPLPDIVL DNVPHIPWAF DMCETIGLVL
AVVWFTVLFF HNQRVIVARR MFSLLGTVFL LRCFTMLITS LSVPGIHLQC EARPNTTMQE
KLHKAFHIWS NLGMSLHGVR SCGDYMFSGH TTVITMISHF ITEYTPADWT GLHTFTWVLN
CFAIFLILAA HEHYSIDVFI AFYISSRMFL YYHAYAYNHA GITATDYRMR TWFPLGWFFE
YGSQGKVENE FSLPINIRIP RRVFFAKSEE PKITPKSDSS RKRSSVVAAK QNGNSKNHTK
KHN