C9MT_CANAL
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 03-AUG-2022, entry version 110.
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; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; 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., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA 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 aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME 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 allele-
RT specific measurements and provides a simple model for repeat and indel
RT 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 hyphal
RT 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 and
CC pathogenicity. The methyl group at the C9-position distinguishes fungal
CC glucosylceramides from those of plants and animals, and may thus play a
CC role in host-pathogen interactions enabling the host to recognize the
CC fungal attack and initiate specific defense responses. Not necessary
CC for vegetative growth at low temperatures, but plays a role in hyphal
CC formation on solid 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 + H(+) +
CC S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:46804, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:85953,
CC 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}; Multi-
CC pass membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Produces only non-methylated glucosylceramides.
CC Has a decreased hyphal growth rate. {ECO:0000269|PubMed:20019081}.
CC -!- SIMILARITY: Belongs to the CFA/CMAS family. {ECO:0000305}.
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DR EMBL; CP017623; AOW26600.1; -; Genomic_DNA.
DR RefSeq; XP_723517.1; XM_718424.1.
DR AlphaFoldDB; Q5APD4; -.
DR SMR; Q5APD4; -.
DR STRING; 237561.Q5APD4; -.
DR PRIDE; Q5APD4; -.
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 VEuPathDB; FungiDB:C1_09680W_A; -.
DR eggNOG; ENOG502QS47; Eukaryota.
DR HOGENOM; CLU_026434_5_0_1; -.
DR InParanoid; Q5APD4; -.
DR OMA; HRVEGIP; -.
DR OrthoDB; 606410at2759; -.
DR UniPathway; UPA00222; -.
DR PRO; PR:Q5APD4; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:1903561; C:extracellular vesicle; IDA:CGD.
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:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Methyltransferase;
KW Reference proteome; S-adenosyl-L-methionine; Sphingolipid metabolism;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..513
FT /note="Sphingolipid C9-methyltransferase"
FT /id="PRO_0000434799"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 222..223
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P9WPB7"
FT BINDING 259..267
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P9WPB7"
FT BINDING 285..290
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P9WPB7"
FT BINDING 315..316
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="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
