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Q9LM02

- SMT1_ARATH

UniProt

Q9LM02 - SMT1_ARATH

Protein

Cycloartenol-C-24-methyltransferase

Gene

SMT1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of cycloartenol to form 24-methylene cycloartenol.

    Catalytic activityi

    S-adenosyl-L-methionine + 5-alpha-cholesta-8,24-dien-3-beta-ol = S-adenosyl-L-homocysteine + 24-methylene-5-alpha-cholest-8-en-3-beta-ol.

    Pathwayi

    GO - Molecular functioni

    1. sterol 24-C-methyltransferase activity Source: TAIR

    GO - Biological processi

    1. embryo development ending in seed dormancy Source: TAIR
    2. sterol biosynthetic process Source: TAIR

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Biological processi

    Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Enzyme and pathway databases

    BioCyciARA:AT5G13710-MONOMER.
    ARA:GQT-948-MONOMER.
    MetaCyc:AT5G13710-MONOMER.
    UniPathwayiUPA00766.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cycloartenol-C-24-methyltransferase (EC:2.1.1.41)
    Alternative name(s):
    24-sterol C-methyltransferase 1
    Short name:
    Sterol C-methyltransferase 1
    Protein CEPHALOPOD
    Protein STEROL METHYLTRANSFERASE 1
    Gene namesi
    Name:SMT1
    Synonyms:CPH
    Ordered Locus Names:At5g13710
    ORF Names:MSH12.18
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 5

    Organism-specific databases

    TAIRiAT5G13710.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: TAIR
    2. plasmodesma Source: TAIR
    3. vacuole Source: TAIR

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 336336Cycloartenol-C-24-methyltransferasePRO_0000124800Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiQ9LM02.
    PRIDEiQ9LM02.

    Expressioni

    Tissue specificityi

    Highly expressed in vascular tissue, mature leaves and in regions undergoing cellular expansion.

    Gene expression databases

    GenevestigatoriQ9LM02.

    Interactioni

    Structurei

    3D structure databases

    ProteinModelPortaliQ9LM02.
    SMRiQ9LM02. Positions 62-202.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the class I-like SAM-binding methyltransferase superfamily. Erg6/SMT family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0500.
    HOGENOMiHOG000171097.
    InParanoidiQ9LM02.
    KOiK00559.
    OMAiFHFCRFS.
    PhylomeDBiQ9LM02.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    InterProiIPR025810. ERG6.
    IPR013216. Methyltransf_11.
    IPR029063. SAM-dependent_MTases-like.
    IPR013705. Sterol_MeTrfase_C.
    [Graphical view]
    PfamiPF08241. Methyltransf_11. 1 hit.
    PF08498. Sterol_MT_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF53335. SSF53335. 1 hit.
    PROSITEiPS51685. SAM_MT_ERG6_SMT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9LM02-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDLASNLGGK IDKSDVLTAV EKYEQYHVFH GGNEEERKAN YTDMVNKYYD    50
    LATSFYEYGW GESFHFAQRW KGESLRESIK RHEHFLALQL GIQPGQKVLD 100
    VGCGIGGPLR EIARFSNSVV TGLNNNEYQI TRGKELNRLA GVDKTCNFVK 150
    ADFMKMPFPE NSFDAVYAIE ATCHAPDAYG CYKEIYRVLK PGQCFAAYEW 200
    CMTDAFDPDN AEHQKIKGEI EIGDGLPDIR LTTKCLEALK QAGFEVIWEK 250
    DLAKDSPVPW YLPLDKNHFS LSSFRLTAVG RFITKNMVKI LEYIRLAPQG 300
    SQRVSNFLEQ AAEGLVDGGR REIFTPMYFF LARKPE 336
    Length:336
    Mass (Da):38,268
    Last modified:October 1, 2000 - v1
    Checksum:i4649BB3868DE1CE9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti119 – 1191V → A in AAM53553. (PubMed:12100483)Curated
    Sequence conflicti162 – 1621S → N in AAM53553. (PubMed:12100483)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF090372 mRNA. Translation: AAF78847.1.
    AF195648 mRNA. Translation: AAG28462.1.
    AF494289 mRNA. Translation: AAM53553.1.
    AB006704 Genomic DNA. Translation: BAB08698.1.
    CP002688 Genomic DNA. Translation: AED91930.1.
    CP002688 Genomic DNA. Translation: AED91931.1.
    AY120716 mRNA. Translation: AAM53274.1.
    BT000058 mRNA. Translation: AAN15377.1.
    RefSeqiNP_001078579.1. NM_001085110.1.
    NP_196875.1. NM_121374.3.
    UniGeneiAt.23211.

    Genome annotation databases

    EnsemblPlantsiAT5G13710.1; AT5G13710.1; AT5G13710.
    AT5G13710.2; AT5G13710.2; AT5G13710.
    GeneIDi831216.
    KEGGiath:AT5G13710.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF090372 mRNA. Translation: AAF78847.1 .
    AF195648 mRNA. Translation: AAG28462.1 .
    AF494289 mRNA. Translation: AAM53553.1 .
    AB006704 Genomic DNA. Translation: BAB08698.1 .
    CP002688 Genomic DNA. Translation: AED91930.1 .
    CP002688 Genomic DNA. Translation: AED91931.1 .
    AY120716 mRNA. Translation: AAM53274.1 .
    BT000058 mRNA. Translation: AAN15377.1 .
    RefSeqi NP_001078579.1. NM_001085110.1.
    NP_196875.1. NM_121374.3.
    UniGenei At.23211.

    3D structure databases

    ProteinModelPortali Q9LM02.
    SMRi Q9LM02. Positions 62-202.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi Q9LM02.
    ChEMBLi CHEMBL4264.

    Proteomic databases

    PaxDbi Q9LM02.
    PRIDEi Q9LM02.

    Protocols and materials databases

    DNASUi 831216.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT5G13710.1 ; AT5G13710.1 ; AT5G13710 .
    AT5G13710.2 ; AT5G13710.2 ; AT5G13710 .
    GeneIDi 831216.
    KEGGi ath:AT5G13710.

    Organism-specific databases

    TAIRi AT5G13710.

    Phylogenomic databases

    eggNOGi COG0500.
    HOGENOMi HOG000171097.
    InParanoidi Q9LM02.
    KOi K00559.
    OMAi FHFCRFS.
    PhylomeDBi Q9LM02.

    Enzyme and pathway databases

    UniPathwayi UPA00766 .
    BioCyci ARA:AT5G13710-MONOMER.
    ARA:GQT-948-MONOMER.
    MetaCyc:AT5G13710-MONOMER.

    Gene expression databases

    Genevestigatori Q9LM02.

    Family and domain databases

    Gene3Di 3.40.50.150. 1 hit.
    InterProi IPR025810. ERG6.
    IPR013216. Methyltransf_11.
    IPR029063. SAM-dependent_MTases-like.
    IPR013705. Sterol_MeTrfase_C.
    [Graphical view ]
    Pfami PF08241. Methyltransf_11. 1 hit.
    PF08498. Sterol_MT_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53335. SSF53335. 1 hit.
    PROSITEi PS51685. SAM_MT_ERG6_SMT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Schaeffer A., Schaller H., Benveniste P.
      Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Columbia.
    2. "Sterol methyltransferase 1 controls the level of cholesterol in plants."
      Diener A.C., Li H., Zhou W.-X., Whoriskey W.J., Nes W.D., Fink G.R.
      Plant Cell 12:853-870(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Columbia.
    3. "Interactions between sterol biosynthesis genes in embryonic development of Arabidopsis."
      Schrick K., Mayer U., Martin G., Bellini C., Kuhnt C., Schmidt J., Juergens G.
      Plant J. 31:61-73(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Landsberg erecta.
    4. "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence features of the regions of 1,044,062 bp covered by thirteen physically assigned P1 clones."
      Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N., Tabata S.
      DNA Res. 4:291-300(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    5. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    6. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    7. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSMT1_ARATH
    AccessioniPrimary (citable) accession number: Q9LM02
    Secondary accession number(s): Q8LKW1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2005
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 95 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3