SMO13_ARATH
ID SMO13_ARATH Reviewed; 291 AA.
AC F4JLZ6; F4JLZ3; Q5J909;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Methylsterol monooxygenase 1-3 {ECO:0000303|PubMed:14653780};
DE EC=1.14.18.11 {ECO:0000250|UniProtKB:Q8L7W5};
DE EC=1.14.18.9 {ECO:0000250|UniProtKB:Q8L7W5};
DE AltName: Full=Sterol 4-alpha-methyl-oxidase 1-3 {ECO:0000303|PubMed:14653780};
DE Short=AtSMO1-3 {ECO:0000303|PubMed:14653780};
GN Name=SMO1-3 {ECO:0000303|PubMed:14653780};
GN OrderedLocusNames=At4g22755 {ECO:0000312|Araport:AT4G22755};
GN ORFNames=T12H17.140 {ECO:0000312|EMBL:AL021635};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-273, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=14653780; DOI=10.1042/bj20031572;
RA Darnet S., Rahier A.;
RT "Plant sterol biosynthesis: identification of two distinct families of
RT sterol 4alpha-methyl oxidases.";
RL Biochem. J. 378:889-898(2004).
RN [4]
RP INTERACTION WITH ACBP1.
RC STRAIN=cv. Columbia;
RX PubMed=29288621; DOI=10.1111/nph.14965;
RA Lung S.-C., Liao P., Yeung E.C., Hsiao A.-S., Xue Y., Chye M.-L.;
RT "Arabidopsis ACYL-COA-BINDING PROTEIN1 interacts with STEROL C4-METHYL
RT OXIDASE1-2 to modulate gene expression of homeodomain-leucine zipper IV
RT transcription factors.";
RL New Phytol. 218:183-200(2018).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia, cv. Landsberg erecta, and cv. Wassilewskija;
RX PubMed=31341004; DOI=10.1104/pp.19.00144;
RA Song J., Sun S., Ren H., Grison M., Boutte Y., Bai W., Men S.;
RT "The SMO1 family of sterol 4alpha-methyl oxidases is essential for
RT auxin- and cytokinin-regulated embryogenesis.";
RL Plant Physiol. 181:578-594(2019).
CC -!- FUNCTION: Non-heme iron oxygenase involved in sterols biosynthesis by
CC catalyzing the removal of the first methyl group at the C-4 position
CC (By similarity). 4,4-dimethyl-9-beta,19-cyclopropylsterols such as 24-
CC methylenecycloartanol are the preferred substrates (By similarity).
CC {ECO:0000250|UniProtKB:Q8L7W5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4,4-dimethyl-5alpha-cholest-7-en-3beta-ol + 6 Fe(II)-
CC [cytochrome b5] + 5 H(+) + 3 O2 = 4alpha-carboxy-4beta-methyl-5alpha-
CC cholest-7-ene-3beta-ol + 6 Fe(III)-[cytochrome b5] + 4 H2O;
CC Xref=Rhea:RHEA:55220, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16455, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:58387; EC=1.14.18.9;
CC Evidence={ECO:0000250|UniProtKB:Q8L7W5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=24-methylidenelophenol + 6 Fe(II)-[cytochrome b5] + 5 H(+) + 3
CC O2 = 4alpha-carboxy-ergosta-7,24(24(1))-dien-3beta-ol + 6 Fe(III)-
CC [cytochrome b5] + 4 H2O; Xref=Rhea:RHEA:58868, Rhea:RHEA-COMP:10438,
CC Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:29107, ChEBI:CHEBI:142850; EC=1.14.18.11;
CC Evidence={ECO:0000250|UniProtKB:Q8L7W5};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000250|UniProtKB:P53045};
CC -!- SUBUNIT: Interacts with ACBP1. {ECO:0000269|PubMed:29288621}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:31341004}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in leaves, roots, siliques
CC and flowers. {ECO:0000269|PubMed:31341004}.
CC -!- DEVELOPMENTAL STAGE: In vegetative organs, confined to vascular tissues
CC of leaves and roots (PubMed:31341004). In flowers, detected in petal
CC vascular tissues, anther filaments and styles (PubMed:31341004). In
CC siliques, present in funiculi (PubMed:31341004). During embryogenesis,
CC expressed from the globular stage to the mature stage in the embryo but
CC not in the endosperm (PubMed:31341004). {ECO:0000269|PubMed:31341004}.
CC -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC involved in metal ion binding. {ECO:0000250|UniProtKB:P53045}.
CC -!- DISRUPTION PHENOTYPE: The double mutant smo1-1 smo1-3 shows no obvious
CC phenotype. {ECO:0000269|PubMed:31341004}.
CC -!- MISCELLANEOUS: Requires a membrane-bound cytochrome b5 as an obligatory
CC electron carrier from NAD(P)H to SMO. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the sterol desaturase family. {ECO:0000305}.
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DR EMBL; AL021635; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002687; ANM66182.1; -; Genomic_DNA.
DR EMBL; AY323213; AAQ94118.1; -; mRNA.
DR RefSeq; NP_567669.1; NM_118403.2.
DR AlphaFoldDB; F4JLZ6; -.
DR STRING; 3702.AT4G22753.2; -.
DR PRIDE; F4JLZ6; -.
DR EnsemblPlants; AT4G22755.1; AT4G22755.1; AT4G22755.
DR GeneID; 28720173; -.
DR Gramene; AT4G22755.1; AT4G22755.1; AT4G22755.
DR KEGG; ath:AT4G22755; -.
DR Araport; AT4G22755; -.
DR TAIR; locus:505006514; AT4G22753.
DR eggNOG; KOG0873; Eukaryota.
DR eggNOG; KOG1315; Eukaryota.
DR HOGENOM; CLU_047036_5_3_1; -.
DR OMA; GYRIHKK; -.
DR OrthoDB; 1321777at2759; -.
DR BioCyc; ARA:AT4G22755-MON; -.
DR BioCyc; MetaCyc:GQT-5411-MON; -.
DR BRENDA; 1.14.18.10; 399.
DR PRO; PR:F4JLZ6; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JLZ6; baseline and differential.
DR Genevisible; F4JLZ6; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0000254; F:C-4 methylsterol oxidase activity; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016126; P:sterol biosynthetic process; IBA:GO_Central.
DR InterPro; IPR006694; Fatty_acid_hydroxylase.
DR Pfam; PF04116; FA_hydroxylase; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Iron; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Monooxygenase; Oxidoreductase; Reference proteome;
KW Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
KW Sterol metabolism; Transmembrane; Transmembrane helix.
FT CHAIN 1..291
FT /note="Methylsterol monooxygenase 1-3"
FT /id="PRO_0000413163"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 128..263
FT /note="Fatty acid hydroxylase"
FT /evidence="ECO:0000255"
FT MOTIF 143..147
FT /note="Histidine box-1"
FT /evidence="ECO:0000250|UniProtKB:P53045"
FT MOTIF 156..160
FT /note="Histidine box-2"
FT /evidence="ECO:0000250|UniProtKB:P53045"
FT MOTIF 235..241
FT /note="Histidine box-3"
FT /evidence="ECO:0000250|UniProtKB:P53045"
FT CONFLICT 260
FT /note="I -> IS (in Ref. 3; AAQ94118)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 291 AA; 34284 MW; EDEDA085DFB4978A CRC64;
MIPYPTVEDA SVALGRNLTW FETVWFDYSA TKSNFHVYCH TILVLFLVFS LAPFPLVIVE
WTGWFDQFKI QKKVKYSLSD MFQCYKEVMK LFLLVVGTLQ IVSYPSIQMV GIRSGLPLPS
LMEIVAQLVV YFLIEDYTNY WIHRWMHCKW GYEKIHRIHH EYTSPIGYAS PYAHWAEILI
LGIPTFLGPA IAPGHIMTFW LWISLRQFEA IETHSGYDFP WSVTKLIPFY GGPEYHDYHH
YVGGQSQSNF ASVFTYCDYI YGTDKGYRIH KKLLHHQIKE EAEEKRVRKH D
