ID C9MT_CANAL Reviewed; 513 AA. AC Q5APD4; A0A1D8PES8; DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot. DT 26-APR-2005, sequence version 1. DT 10-APR-2019, entry version 98. DE RecName: Full=Sphingolipid C9-methyltransferase {ECO:0000303|PubMed:20019081}; DE Short=C-9-MT; DE EC=2.1.1.317 {ECO:0000269|PubMed:20019081}; DE AltName: Full=Cyclopropane fatty acyl phospholipid synthase homolog 1; DE AltName: Full=Methyltransferase for sphingolipid 1 {ECO:0000303|PubMed:20019081}; GN Name=MTS1 {ECO:0000303|PubMed:20019081}; Synonyms=CFA1; GN OrderedLocusNames=CAALFM_C109680WA; ORFNames=CaO19.12294, CaO19.4831; OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Debaryomycetaceae; OC Candida/Lodderomyces clade; Candida. OX NCBI_TaxID=237561; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=15123810; DOI=10.1073/pnas.0401648101; RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., RA Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., RA Davis R.W., Scherer S.; RT "The diploid genome sequence of Candida albicans."; RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004). RN [2] RP GENOME REANNOTATION. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52; RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D., RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M., RA Chibana H., Nantel A., Magee P.T.; RT "Assembly of the Candida albicans genome into sixteen supercontigs RT aligned on the eight chromosomes."; RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME RP REANNOTATION. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97; RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.; RT "Assembly of a phased diploid Candida albicans genome facilitates RT allele-specific measurements and provides a simple model for repeat RT and indel structure."; RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013). RN [4] RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE. RX PubMed=20019081; DOI=10.1099/mic.0.033985-0; RA Oura T., Kajiwara S.; RT "Candida albicans sphingolipid C9-methyltransferase is involved in RT hyphal elongation."; RL Microbiology 156:1234-1243(2010). CC -!- FUNCTION: Catalyzes methylation of the sphingoid base component of CC glucosylceramides (GluCers) at the C9-position. Sphingolipid C9- CC methylation requires 4,8-desaturated ceramides as substrates. CC Glucosylceramides play important roles in growth, differentiation CC and pathogenicity. The methyl group at the C9-position CC distinguishes fungal glucosylceramides from those of plants and CC animals, and may thus play a role in host-pathogen interactions CC enabling the host to recognize the fungal attack and initiate CC specific defense responses. Not necessary for vegetative growth at CC low temperatures, but plays a role in hyphal formation on solid CC medium. {ECO:0000269|PubMed:20019081}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a (4E,8E)-4-sphinga-4,8-dienine ceramide + S-adenosyl-L- CC methionine = a 9-methyl-(4E,8E)-sphinga-4,8-dienine ceramide + CC H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:46804, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:85953, ChEBI:CHEBI:87033; EC=2.1.1.317; CC Evidence={ECO:0000269|PubMed:20019081}; CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism. CC {ECO:0000305|PubMed:20019081}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:C4R7Z3}; CC Multi-pass membrane protein {ECO:0000255}. CC -!- DISRUPTION PHENOTYPE: Produces only non-methylated CC glucosylceramides. Has a decreased hyphal growth rate. CC {ECO:0000269|PubMed:20019081}. CC -!- SIMILARITY: Belongs to the CFA/CMAS family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP017623; AOW26600.1; -; Genomic_DNA. DR RefSeq; XP_723517.1; XM_718424.1. DR ProteinModelPortal; Q5APD4; -. DR SMR; Q5APD4; -. DR STRING; 5476.C4YD72; -. DR EnsemblFungi; KHC83715; KHC83715; W5Q_00934. DR EnsemblFungi; KHC89151; KHC89151; I503_00942. DR GeneID; 3634873; -. DR KEGG; cal:CAALFM_C109680WA; -. DR CGD; CAL0000177730; MTS1. DR EuPathDB; FungiDB:C1_09680W_A; -. DR HOGENOM; HOG000180107; -. DR InParanoid; Q5APD4; -. DR KO; K20238; -. DR OMA; IPMETFH; -. DR OrthoDB; 606410at2759; -. DR UniPathway; UPA00222; -. DR PRO; PR:Q5APD4; -. DR Proteomes; UP000000559; Chromosome 1. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IDA:CGD. DR GO; GO:0008168; F:methyltransferase activity; IMP:CGD. DR GO; GO:0030447; P:filamentous growth; IMP:CGD. DR GO; GO:0006679; P:glucosylceramide biosynthetic process; IMP:CGD. DR GO; GO:0009405; P:pathogenesis; IMP:CGD. DR InterPro; IPR003333; Mycolic_cyclopropane_synthase. DR InterPro; IPR029063; SAM-dependent_MTases. DR PIRSF; PIRSF003085; CMAS; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 1: Evidence at protein level; KW Complete proteome; Lipid biosynthesis; Lipid metabolism; Membrane; KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine; KW Sphingolipid metabolism; Transferase; Transmembrane; KW Transmembrane helix. FT CHAIN 1 513 Sphingolipid C9-methyltransferase. FT /FTId=PRO_0000434799. FT TRANSMEM 52 72 Helical. {ECO:0000255}. FT TRANSMEM 74 94 Helical. {ECO:0000255}. FT REGION 222 223 S-adenosyl-L-methionine binding. FT {ECO:0000250|UniProtKB:P9WPB7}. FT REGION 259 267 S-adenosyl-L-methionine binding. FT {ECO:0000250|UniProtKB:P9WPB7}. FT REGION 285 290 S-adenosyl-L-methionine binding. FT {ECO:0000250|UniProtKB:P9WPB7}. FT REGION 315 316 S-adenosyl-L-methionine binding. FT {ECO:0000250|UniProtKB:P9WPB7}. SQ SEQUENCE 513 AA; 58777 MW; 3CA020873BCD76B4 CRC64; MLDDVAFIKT PAAKKQPPAS NECGVWTTDS PAIHNAPLPA DGPGSTSFSN TILFSILALV PGYITYKLGL GFKTWVFFFL ILAIPILMAY WSIMSTFSPR INEKVKYPNR PISYYLEFHT PELKAKYETS NGGKGSKIPI ETFQELYFDG KVSFKGDCLD VLEYKHDWAS FRFTLGLFRF FLLGMIPEVI FHSQSQDEEQ VRDHYDRGDD FYTWFLGPRM IYTSGVISDI TREETLEELQ DNKLTVMADK IDLKKGDHVL DIGCGWGTWT TFASSKYGAN VTGITLGRNQ TKWGNTLLKE YGIPSDQSRI VCCDYRDAPK SSKPSGKYDK ITSVEMAEHV GIRRLTAYLE QCRDALEDDG LLFLQYSGLR KNWQYEDLEW GLFMNKYIFP GADASTPLSF FASCMESVGF EIVSVDNIGV HYSATLWRWY RNWIGNKDKV VNKYGVKWYR IWEFFLGSSV VASRNGTATC YQFICRKNIN SYRRIDYVPQ QKGLQGPVQE GTKWAKEFTN FYD //