SMO11_ARATH
ID SMO11_ARATH Reviewed; 298 AA.
AC Q8L7W5; Q71V05; Q8LB57; Q9SZ76;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Methylsterol monooxygenase 1-1 {ECO:0000303|PubMed:14653780};
DE EC=1.14.18.10 {ECO:0000269|PubMed:14653780};
DE EC=1.14.18.9 {ECO:0000269|PubMed:14653780};
DE AltName: Full=Sterol 4-alpha-methyl-oxidase 1-1 {ECO:0000303|PubMed:14653780};
DE Short=AtSMO1-1 {ECO:0000303|PubMed:14653780};
GN Name=SMO1-1 {ECO:0000303|PubMed:14653780};
GN OrderedLocusNames=At4g12110 {ECO:0000312|Araport:AT4G12110};
GN ORFNames=F16J13.180 {ECO:0000312|EMBL:CAB40952.1};
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, GENE FAMILY, AND
RP NOMENCLATURE.
RC STRAIN=cv. Columbia; TISSUE=Silique;
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 [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH ACBP1, DEVELOPMENTAL
RP STAGE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=28500265; DOI=10.1104/pp.17.00412;
RA Lung S.-C., Liao P., Yeung E.C., Hsiao A.-S., Xue Y., Chye M.-L.;
RT "Acyl-CoA-binding protein ACBP1 modulates sterol synthesis during
RT embryogenesis.";
RL Plant Physiol. 174:1420-1435(2017).
RN [7]
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 (PubMed:14653780). 4,4-dimethyl-9-beta,19-cyclopropylsterols such as
CC 24-methylenecycloartanol are the preferred substrates
CC (PubMed:14653780). Acts as a rate-limiting enzyme in the sterol pathway
CC via interaction with ACBP1; sterols serve as lipid modulators for gene
CC expression of homeodomain-leucine zipper IV transcription factors
CC (PubMed:28500265). Together with SMO1-2, involved in the maintenance of
CC sterol composition to balance auxin and cytokinin activities during
CC embryogenesis (PubMed:31341004). {ECO:0000269|PubMed:14653780,
CC ECO:0000269|PubMed:28500265, ECO:0000269|PubMed:31341004}.
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:0000269|PubMed:14653780};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=24-methylenecycloartanol + 6 Fe(II)-[cytochrome b5] + 5 H(+) +
CC 3 O2 = 4alpha-carboxy-4beta,14alpha-dimethyl-9beta,19-cyclo-5alpha-
CC ergost-24(24(1))-en-3beta-ol + 6 Fe(III)-[cytochrome b5] + 4 H2O;
CC Xref=Rhea:RHEA:58832, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:1307, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:142916; EC=1.14.18.10;
CC Evidence={ECO:0000269|PubMed:14653780};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000250|UniProtKB:P53045};
CC -!- SUBUNIT: Interacts with ACBP1. {ECO:0000269|PubMed:28500265}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:28500265, ECO:0000269|PubMed:31341004}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in rosettes, stems, roots, floral buds,
CC flowers and siliques. {ECO:0000269|PubMed:28500265,
CC ECO:0000269|PubMed:31341004}.
CC -!- DEVELOPMENTAL STAGE: Strongly expressed in developing ovules
CC (PubMed:28500265). During embryogenesis, expressed from the globular
CC stage to the mature stage in both the embryo and endosperm
CC (PubMed:31341004). From the torpedo to the mature embryo stages,
CC strongly expressed in the provascular cells of the developing hypocotyl
CC and in the shoot apical meristem (SAM) (PubMed:31341004). In leaves,
CC strongly expressed in vascular tissues and stomata (PubMed:31341004).
CC In roots, accumulates in the stele and at lateral root formation sites
CC (PubMed:31341004). In flowers, observed in anthers and pistils
CC (PubMed:31341004). In siliques, high levels in seedpods
CC (PubMed:31341004). {ECO:0000269|PubMed:28500265,
CC 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: Proembryo abortion in the double mutant lacking
CC both SMO1-1 and ACBP1 associated with altered fatty acids (FAs) and
CC sterols profiles (PubMed:28500265). The double mutant smo1-1 smo1-3
CC shows no obvious phenotype (PubMed:31341004). The double mutant smo1-1
CC smo1-2, which accumulates dramatically 4,4-dimethylsterols, is embryo
CC lethal, with embryo exhibiting severe defects, including no cotyledon
CC or shoot apical meristem formation, abnormal division of suspensor
CC cells, and twin embryos, and is associated with altered auxin and
CC cytokinin homeostasis (PubMed:31341004). {ECO:0000269|PubMed:28500265,
CC 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB40952.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78254.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF039199; AAQ13424.1; -; mRNA.
DR EMBL; AL049638; CAB40952.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161533; CAB78254.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83097.1; -; Genomic_DNA.
DR EMBL; AY125499; AAM78091.1; -; mRNA.
DR EMBL; BT000546; AAN18115.1; -; mRNA.
DR EMBL; AY087412; AAM64961.1; -; mRNA.
DR PIR; T06618; T06618.
DR RefSeq; NP_192948.1; NM_117281.3.
DR AlphaFoldDB; Q8L7W5; -.
DR STRING; 3702.AT4G12110.1; -.
DR PaxDb; Q8L7W5; -.
DR PRIDE; Q8L7W5; -.
DR ProteomicsDB; 228445; -.
DR EnsemblPlants; AT4G12110.1; AT4G12110.1; AT4G12110.
DR GeneID; 826819; -.
DR Gramene; AT4G12110.1; AT4G12110.1; AT4G12110.
DR KEGG; ath:AT4G12110; -.
DR Araport; AT4G12110; -.
DR TAIR; locus:2118121; AT4G12110.
DR eggNOG; KOG0873; Eukaryota.
DR HOGENOM; CLU_047036_5_3_1; -.
DR InParanoid; Q8L7W5; -.
DR OMA; YGGVAHH; -.
DR OrthoDB; 1493916at2759; -.
DR BioCyc; ARA:AT4G12110-MON; -.
DR BioCyc; MetaCyc:AT4G12110-MON; -.
DR BRENDA; 1.14.18.10; 399.
DR PRO; PR:Q8L7W5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8L7W5; baseline and differential.
DR Genevisible; Q8L7W5; 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; IMP:TAIR.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0080064; P:4,4-dimethyl-9beta,19-cyclopropylsterol oxidation; NAS:TAIR.
DR GO; GO:0055089; P:fatty acid homeostasis; IMP:UniProtKB.
DR GO; GO:0016126; P:sterol biosynthetic process; IMP:TAIR.
DR GO; GO:0055092; P:sterol homeostasis; IMP:UniProtKB.
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..298
FT /note="Methylsterol monooxygenase 1-1"
FT /id="PRO_0000413161"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 132..267
FT /note="Fatty acid hydroxylase"
FT /evidence="ECO:0000255"
FT MOTIF 147..151
FT /note="Histidine box-1"
FT /evidence="ECO:0000250|UniProtKB:P53045"
FT MOTIF 160..164
FT /note="Histidine box-2"
FT /evidence="ECO:0000250|UniProtKB:P53045"
FT MOTIF 239..245
FT /note="Histidine box-3"
FT /evidence="ECO:0000250|UniProtKB:P53045"
FT CONFLICT 59
FT /note="V -> I (in Ref. 5; AAM64961)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="D -> E (in Ref. 1; AAQ13424)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 298 AA; 34647 MW; 81240E5E23BF8B4E CRC64;
MIPYATVEEA SIALGRNLTR LETLWFDYSA TKSDYYLYCH NILFLFLVFS LVPLPLVFVE
LARSASGLFN RYKIQPKVNY SLSDMFKCYK DVMTMFILVV GPLQLVSYPS IQMIEIRSGL
PLPTITEMLS QLVVYFLIED YTNYWVHRFF HSKWGYDKIH RVHHEYTAPI GYAAPYAHWA
EVLLLGIPTF MGPAIAPGHM ITFWLWIALR QMEAIETHSG YDFPWSPTKY IPFYGGAEYH
DYHHYVGGQS QSNFASVFTY CDYIYGTDKG YRFQKKLLEQ IKESSKKSNK HNGGIKSD
