STRM1_CAEEL
ID STRM1_CAEEL Reviewed; 334 AA.
AC Q9TYP1;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Sterol 4-C-methyltransferase strm-1;
DE Short=STRM-1 {ECO:0000303|PubMed:19531354};
DE EC=2.1.1.- {ECO:0000269|PubMed:19531354};
DE AltName: Full=Sterol A-ring methylase-1 {ECO:0000303|PubMed:19531354};
GN Name=strm-1; ORFNames=H14E04.1;
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]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND
RP PATHWAY.
RX PubMed=19531354; DOI=10.1016/j.devcel.2009.04.012;
RA Hannich J.T., Entchev E.V., Mende F., Boytchev H., Martin R., Zagoriy V.,
RA Theumer G., Riezman I., Riezman H., Knolker H.J., Kurzchalia T.V.;
RT "Methylation of the sterol nucleus by STRM-1 regulates dauer larva
RT formation in Caenorhabditis elegans.";
RL Dev. Cell 16:833-843(2009).
RN [3]
RP FUNCTION, AND PATHWAY.
RX PubMed=24411940; DOI=10.1016/j.cmet.2013.11.024;
RA Mahanti P., Bose N., Bethke A., Judkins J.C., Wollam J., Dumas K.J.,
RA Zimmerman A.M., Campbell S.L., Hu P.J., Antebi A., Schroeder F.C.;
RT "Comparative metabolomics reveals endogenous ligands of DAF-12, a nuclear
RT hormone receptor, regulating C. elegans development and lifespan.";
RL Cell Metab. 19:73-83(2014).
CC -!- FUNCTION: Catalyzes the methyl transfer from S-adenosyl-methionine to
CC the C-4 of the A-ring sterols such as lathosterone (5alpha-cholest-7-
CC en-3-one) thereby rendering them unsuitable as ligand precursors. May
CC irreversibly shunt sterols away from hormone dafachronic acid
CC production. Dafachronic acids act as ligands and bind directly to the
CC nuclear hormone receptor (NHR) daf-12 suppressing dauer formation and
CC inducing reproductive growth. By reducing the biosynthesis of
CC dafachronic acids, this methyltransferase can regulate dauer larva
CC formation. {ECO:0000269|PubMed:19531354, ECO:0000269|PubMed:24411940}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5alpha-cholest-7-en-3-one + S-adenosyl-L-methionine = 4alpha-
CC methyl-5alpha-cholest-7-en-3-one + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:35483, ChEBI:CHEBI:15378, ChEBI:CHEBI:16495,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:71550;
CC Evidence={ECO:0000269|PubMed:19531354};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35484;
CC Evidence={ECO:0000269|PubMed:19531354};
CC -!- PATHWAY: Steroid hormone biosynthesis; dafachronic acid biosynthesis.
CC {ECO:0000269|PubMed:19531354, ECO:0000269|PubMed:24411940}.
CC -!- TISSUE SPECIFICITY: Expressed in the pharynx and hypodermal syncytium.
CC {ECO:0000269|PubMed:19531354}.
CC -!- DISRUPTION PHENOTYPE: Mutants show impaired dauer larvae production.
CC {ECO:0000269|PubMed:19531354}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Erg6/SMT family. {ECO:0000255|PROSITE-ProRule:PRU01022}.
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DR EMBL; FO081521; CCD72180.1; -; Genomic_DNA.
DR PIR; T33885; T33885.
DR RefSeq; NP_497549.2; NM_065148.4.
DR AlphaFoldDB; Q9TYP1; -.
DR SMR; Q9TYP1; -.
DR STRING; 6239.H14E04.1; -.
DR SwissLipids; SLP:000000039; -.
DR SwissLipids; SLP:000000218; -.
DR EPD; Q9TYP1; -.
DR PaxDb; Q9TYP1; -.
DR PeptideAtlas; Q9TYP1; -.
DR EnsemblMetazoa; H14E04.1.1; H14E04.1.1; WBGene00019198.
DR GeneID; 175358; -.
DR KEGG; cel:CELE_H14E04.1; -.
DR UCSC; H14E04.1; c. elegans.
DR CTD; 175358; -.
DR WormBase; H14E04.1; CE29973; WBGene00019198; strm-1.
DR eggNOG; KOG1269; Eukaryota.
DR HOGENOM; CLU_840216_0_0_1; -.
DR InParanoid; Q9TYP1; -.
DR OMA; ISNMCKV; -.
DR OrthoDB; 661953at2759; -.
DR PhylomeDB; Q9TYP1; -.
DR BRENDA; 2.1.1.B118; 1045.
DR UniPathway; UPA01020; -.
DR PRO; PR:Q9TYP1; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00019198; Expressed in embryo and 4 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IMP:WormBase.
DR GO; GO:0003838; F:sterol 24-C-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0043414; P:macromolecule methylation; IMP:WormBase.
DR GO; GO:0061065; P:regulation of dauer larval development; IMP:WormBase.
DR GO; GO:0016126; P:sterol biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR013216; Methyltransf_11.
DR InterPro; IPR030384; MeTrfase_SMT.
DR InterPro; IPR020803; PKS_MeTfrase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF08241; Methyltransf_11; 1.
DR SMART; SM00828; PKS_MT; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51685; SAM_MT_ERG6_SMT; 1.
PE 1: Evidence at protein level;
KW Cholesterol metabolism; Lipid metabolism; Methyltransferase;
KW Reference proteome; S-adenosyl-L-methionine; Steroid metabolism;
KW Sterol metabolism; Transferase.
FT CHAIN 1..334
FT /note="Sterol 4-C-methyltransferase strm-1"
FT /id="PRO_0000421681"
SQ SEQUENCE 334 AA; 37825 MW; 7B2364B30F7E01E9 CRC64;
MSINMNANFL KLLTHFRRHD LTNFKSEHDT LYEKALETGD HLEVTSHYYS VMSTVIDEYF
GGNFHFVPPK FEGQKLEEAL KSLHCHIAEK LELSENVHCL DIGCGIGGVM LDIADFGAKL
TGVTIAPNEA EIGNEKFANM GISDRCKIVA ADCQKMPFED STFDVAYAIY SLKYIPNLDK
VMKEIQRVLK PGGKFIVYDL IKTNDYDKDN KEHYKTLHHL EYACGMPSLH TQSEVEAAAE
KWEMPVVERE NLEETYGNRA FHYCFSASPM FMWLVSSPVI DHTIRMAEIL RILPAGFKQF
NRTFLCGTVN SIVGGGRMGI LSGADILLFE KKKI
