SMO21_ARATH
ID SMO21_ARATH Reviewed; 272 AA.
AC Q9ZW22; A8MQF7; A8MRF1; F4IKN2; Q8W5A2; Q8W5B3;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Methylsterol monooxygenase 2-1 {ECO:0000303|PubMed:14653780};
DE EC=1.14.18.11 {ECO:0000269|PubMed:11707264};
DE EC=1.14.18.9 {ECO:0000269|PubMed:11707264};
DE AltName: Full=Sterol 4-alpha-methyl-oxidase 2 {ECO:0000303|PubMed:11707264, ECO:0000303|PubMed:14653780};
DE Short=AtSMO2 {ECO:0000303|PubMed:11707264, ECO:0000303|PubMed:14653780};
DE AltName: Full=Sterol 4-alpha-methyl-oxidase 2-1 {ECO:0000303|PubMed:14653780};
GN Name=SMO2-1 {ECO:0000303|PubMed:14653780};
GN Synonyms=SMO2 {ECO:0000303|PubMed:11707264, ECO:0000303|PubMed:14653780};
GN OrderedLocusNames=At2g29390 {ECO:0000312|Araport:AT2G29390};
GN ORFNames=F16P2.23 {ECO:0000312|EMBL:AAC95199.2};
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] (ISOFORM 2), FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=11707264; DOI=10.1016/s0014-5793(01)03002-2;
RA Darnet S., Bard M., Rahier A.;
RT "Functional identification of sterol-4alpha-methyl oxidase cDNAs from
RT Arabidopsis thaliana by complementation of a yeast erg25 mutant lacking
RT sterol-4alpha-methyl oxidation.";
RL FEBS Lett. 508:39-43(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [7]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=27006488; DOI=10.1104/pp.15.01814;
RA Zhang X., Sun S., Nie X., Boutte Y., Grison M., Li P., Kuang S., Men S.;
RT "Sterol methyl oxidases affect embryo development via auxin-associated
RT mechanisms.";
RL Plant Physiol. 171:468-482(2016).
CC -!- FUNCTION: Non-heme iron oxygenase involved in sterols biosynthesis by
CC catalyzing the removal of the second methyl group at the C-4 position
CC (PubMed:11707264). 24-ethylidenelophenol and 24-ethyllophenol are the
CC preferred substrates (PubMed:11707264). Together with SMO2-2, required
CC during embryogenesis, probably by maintaining sterols and auxin
CC homeostasis (PubMed:27006488). {ECO:0000269|PubMed:11707264,
CC ECO:0000269|PubMed:27006488}.
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:11707264};
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:0000269|PubMed:11707264};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000250|UniProtKB:P53045};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:27006488}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q9ZW22-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ZW22-2; Sequence=VSP_041864;
CC Name=3;
CC IsoId=Q9ZW22-3; Sequence=VSP_041862, VSP_041864;
CC Name=4;
CC IsoId=Q9ZW22-4; Sequence=VSP_041860, VSP_041864;
CC Name=5;
CC IsoId=Q9ZW22-5; Sequence=VSP_041861, VSP_041863, VSP_041864;
CC -!- TISSUE SPECIFICITY: Strongly expressed in leaves, flowers, siliques and
CC developing seeds. {ECO:0000269|PubMed:27006488}.
CC -!- DEVELOPMENTAL STAGE: In leaves, mostly expressed in vascular tissues
CC and trichomes (PubMed:27006488). In flowers, accumulates mainly in
CC sepals, stamen filaments, pollen grains and pistils, but barely
CC detectable in petals (PubMed:27006488). Present in siliques at all
CC stages of development (PubMed:27006488). During embroygenesis,
CC expressed in both embryos and endosperms throughout embryonic
CC development (PubMed:27006488). {ECO:0000269|PubMed:27006488}.
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: No obvious phenotype (PubMed:27006488). The smo2-
CC 1 smo2-2 double mutant accumulates the 4alpha-methylsterols 24-
CC ethylidene lophenol and 24-ethyl lophenol, and is embryonic lethal,
CC arrested in early stages with an altered endosperm development,
CC probably due to disturbed auxin flux and responses (PubMed:27006488).
CC {ECO:0000269|PubMed:27006488}.
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; AF327853; AAL32302.1; -; mRNA.
DR EMBL; AF222719; AAL32287.1; -; mRNA.
DR EMBL; AC004561; AAC95199.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC08245.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08246.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08247.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08248.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08249.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61554.1; -; Genomic_DNA.
DR EMBL; AY086287; AAM64359.1; -; mRNA.
DR EMBL; BT002780; AAO22608.1; -; mRNA.
DR EMBL; BT005125; AAO50658.1; -; mRNA.
DR PIR; G84695; G84695.
DR RefSeq; NP_001077974.1; NM_001084505.1. [Q9ZW22-4]
DR RefSeq; NP_001077975.1; NM_001084506.1. [Q9ZW22-5]
DR RefSeq; NP_001318311.1; NM_001336210.1. [Q9ZW22-4]
DR RefSeq; NP_565681.1; NM_128493.4. [Q9ZW22-1]
DR RefSeq; NP_850133.1; NM_179802.3. [Q9ZW22-2]
DR RefSeq; NP_973559.1; NM_201830.2. [Q9ZW22-3]
DR AlphaFoldDB; Q9ZW22; -.
DR BioGRID; 2838; 2.
DR IntAct; Q9ZW22; 2.
DR STRING; 3702.AT2G29390.1; -.
DR PaxDb; Q9ZW22; -.
DR PRIDE; Q9ZW22; -.
DR ProteomicsDB; 232541; -. [Q9ZW22-1]
DR EnsemblPlants; AT2G29390.1; AT2G29390.1; AT2G29390. [Q9ZW22-1]
DR EnsemblPlants; AT2G29390.2; AT2G29390.2; AT2G29390. [Q9ZW22-2]
DR EnsemblPlants; AT2G29390.3; AT2G29390.3; AT2G29390. [Q9ZW22-3]
DR EnsemblPlants; AT2G29390.4; AT2G29390.4; AT2G29390. [Q9ZW22-4]
DR EnsemblPlants; AT2G29390.5; AT2G29390.5; AT2G29390. [Q9ZW22-5]
DR EnsemblPlants; AT2G29390.6; AT2G29390.6; AT2G29390. [Q9ZW22-4]
DR GeneID; 817488; -.
DR Gramene; AT2G29390.1; AT2G29390.1; AT2G29390. [Q9ZW22-1]
DR Gramene; AT2G29390.2; AT2G29390.2; AT2G29390. [Q9ZW22-2]
DR Gramene; AT2G29390.3; AT2G29390.3; AT2G29390. [Q9ZW22-3]
DR Gramene; AT2G29390.4; AT2G29390.4; AT2G29390. [Q9ZW22-4]
DR Gramene; AT2G29390.5; AT2G29390.5; AT2G29390. [Q9ZW22-5]
DR Gramene; AT2G29390.6; AT2G29390.6; AT2G29390. [Q9ZW22-4]
DR KEGG; ath:AT2G29390; -.
DR Araport; AT2G29390; -.
DR TAIR; locus:2043132; AT2G29390.
DR eggNOG; KOG0873; Eukaryota.
DR InParanoid; Q9ZW22; -.
DR OMA; WCAFTGN; -.
DR OrthoDB; 1493916at2759; -.
DR PhylomeDB; Q9ZW22; -.
DR BioCyc; ARA:AT2G29390-MON; -.
DR BioCyc; MetaCyc:AT2G29390-MON; -.
DR BRENDA; 1.14.18.10; 399.
DR BRENDA; 1.14.18.11; 399.
DR PRO; PR:Q9ZW22; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZW22; baseline and differential.
DR Genevisible; Q9ZW22; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
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; IGI:TAIR.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0080065; P:4-alpha-methyl-delta7-sterol oxidation; IGI:TAIR.
DR GO; GO:0016126; P:sterol biosynthetic process; IGI:TAIR.
DR InterPro; IPR006694; Fatty_acid_hydroxylase.
DR Pfam; PF04116; FA_hydroxylase; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Iron; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Monooxygenase; Oxidoreductase;
KW Reference proteome; Steroid biosynthesis; Steroid metabolism;
KW Sterol biosynthesis; Sterol metabolism; Transmembrane; Transmembrane helix.
FT CHAIN 1..272
FT /note="Methylsterol monooxygenase 2-1"
FT /id="PRO_0000413164"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 113..259
FT /note="Fatty acid hydroxylase"
FT /evidence="ECO:0000255"
FT MOTIF 127..131
FT /note="Histidine box-1"
FT /evidence="ECO:0000250|UniProtKB:P53045"
FT MOTIF 140..144
FT /note="Histidine box-2"
FT /evidence="ECO:0000250|UniProtKB:P53045"
FT MOTIF 231..237
FT /note="Histidine box-3"
FT /evidence="ECO:0000250|UniProtKB:P53045"
FT VAR_SEQ 1..83
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_041860"
FT VAR_SEQ 1..41
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_041861"
FT VAR_SEQ 1..10
FT /note="MDSLVESGWK -> MMQ (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_041862"
FT VAR_SEQ 42..56
FT /note="IFLERTGFLSNYKIQ -> MERYHQVVSVLISPM (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_041863"
FT VAR_SEQ 217..228
FT /note="Missing (in isoform 2, isoform 3, isoform 4 and
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:11707264,
FT ECO:0000303|PubMed:14593172, ECO:0000303|PubMed:14653780"
FT /id="VSP_041864"
SQ SEQUENCE 272 AA; 31649 MW; F147E4D4712D5B04 CRC64;
MDSLVESGWK YLVTHFSDFQ LACIGSFILH ESVFFLSGLP YIFLERTGFL SNYKIQTKSN
TPEAQGKCIA RLLLYHCCVN LPLMMASYPV FRFMGMESSF PLPSWKVVSA QILFYFIIED
FVFYWGHRIL HTKWLYKNVH SVHHEYATPF GLTSEYAHPA EILFLGFATI VGPALTGPHL
ITLWLWMMLR VIETVEAHCG YHFPWSPSNF LPLYGGSLIL MWESFAYSAD FHDYHHRLLY
TKSGNYSSTF VYMDWIFGTD KGYRKLKALK ET
