SMO22_ARATH
ID SMO22_ARATH Reviewed; 266 AA.
AC Q8VWZ8; B9DFL5; Q8LBE1; Q9LNW2;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Methylsterol monooxygenase 2-2 {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 1 {ECO:0000303|PubMed:11707264, ECO:0000303|PubMed:14653780};
DE Short=AtSMO1 {ECO:0000303|PubMed:11707264, ECO:0000303|PubMed:14653780};
DE AltName: Full=Sterol 4-alpha-methyl-oxidase 2-2 {ECO:0000303|PubMed:14653780};
GN Name=SMO2-2 {ECO:0000303|PubMed:14653780};
GN Synonyms=SMO1 {ECO:0000303|PubMed:11707264, ECO:0000303|PubMed:14653780};
GN OrderedLocusNames=At1g07420 {ECO:0000312|Araport:AT1G07420};
GN ORFNames=F22G5.23 {ECO:0000312|EMBL:AAF79571.1};
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] (ISOFORM 1), FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Columbia; TISSUE=Silique;
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 1), GENE FAMILY, AND 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 1).
RA de los Reyes C., Quan R., Chen H., Bautista V., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [8]
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 SMO2-1, 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=2;
CC Name=1;
CC IsoId=Q8VWZ8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VWZ8-2; Sequence=VSP_041865;
CC -!- TISSUE SPECIFICITY: Expressed in shoots, roots, siliques and flowers,
CC and, slightly, in developing seeds. {ECO:0000269|PubMed:27006488}.
CC -!- DEVELOPMENTAL STAGE: In shoots, restricted to the apical meristem (SAM)
CC (PubMed:27006488). In roots, detected only in adventitious root
CC primordia, lateral root primordia, and the root tip meristem
CC (PubMed:27006488). In flowers, expressed in vascular tissues of sepals
CC and petals as well as in stamen filaments and pollen (PubMed:27006488).
CC In young siliques, confined to the style and silique funiculus
CC (PubMed:27006488). In mature siliques, restricted to the abscission
CC zone (PubMed:27006488). During embroygenesis, first expressed at very
CC low levels in seeds at the early developmental stages; accumulates
CC slightly in the late stages (PubMed:27006488).
CC {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79571.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF346734; AAL32303.1; -; mRNA.
DR EMBL; AC022464; AAF79571.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28122.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28123.1; -; Genomic_DNA.
DR EMBL; AY087267; AAM64821.1; -; mRNA.
DR EMBL; BT044610; ACI31310.1; -; mRNA.
DR EMBL; AK316820; BAH19532.1; -; mRNA.
DR RefSeq; NP_563789.1; NM_100616.3. [Q8VWZ8-1]
DR RefSeq; NP_973777.1; NM_202048.2. [Q8VWZ8-2]
DR AlphaFoldDB; Q8VWZ8; -.
DR STRING; 3702.AT1G07420.1; -.
DR PaxDb; Q8VWZ8; -.
DR PRIDE; Q8VWZ8; -.
DR ProteomicsDB; 228446; -. [Q8VWZ8-1]
DR DNASU; 837254; -.
DR EnsemblPlants; AT1G07420.1; AT1G07420.1; AT1G07420. [Q8VWZ8-1]
DR EnsemblPlants; AT1G07420.2; AT1G07420.2; AT1G07420. [Q8VWZ8-2]
DR GeneID; 837254; -.
DR Gramene; AT1G07420.1; AT1G07420.1; AT1G07420. [Q8VWZ8-1]
DR Gramene; AT1G07420.2; AT1G07420.2; AT1G07420. [Q8VWZ8-2]
DR KEGG; ath:AT1G07420; -.
DR Araport; AT1G07420; -.
DR TAIR; locus:2024982; AT1G07420.
DR eggNOG; KOG0873; Eukaryota.
DR InParanoid; Q8VWZ8; -.
DR OMA; IVHEFIY; -.
DR PhylomeDB; Q8VWZ8; -.
DR BioCyc; ARA:AT1G07420-MON; -.
DR BioCyc; MetaCyc:AT1G07420-MON; -.
DR BRENDA; 1.14.18.10; 399.
DR BRENDA; 1.14.18.11; 399.
DR PRO; PR:Q8VWZ8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8VWZ8; baseline and differential.
DR Genevisible; Q8VWZ8; AT.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
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:0009793; P:embryo development ending in seed dormancy; IGI:TAIR.
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 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..266
FT /note="Methylsterol monooxygenase 2-2"
FT /id="PRO_0000413165"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
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 DOMAIN 113..247
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 219..225
FT /note="Histidine box-3"
FT /evidence="ECO:0000250|UniProtKB:P53045"
FT VAR_SEQ 1..55
FT /note="MASFVESGWQYLVTHFSDFQLACIGSFLLHESVFFLSGLPFIFLERQGFLSK
FT YKI -> MLLLPFMVNTYFSFVPM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_041865"
FT CONFLICT 29
FT /note="L -> F (in Ref. 5; AAM64821)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 266 AA; 30927 MW; A7A7FF6BF5F01380 CRC64;
MASFVESGWQ YLVTHFSDFQ LACIGSFLLH ESVFFLSGLP FIFLERQGFL SKYKIQTKNN
TPAAQGKCIT RLLLYHFSVN LPLMLASYPV FRAMGMRSSF PLPSWKEVSA QILFYFIIED
FVFYWGHRIL HSKWLYKNVH SVHHEYATPF GLTSEYAHPA EILFLGFATI VGPALTGPHL
ITLWLWMVLR VLETVEAHCG YHFPWSLSNF LPLYGGADFH DYHHRLLYTK SGNYSSTFVY
MDWIFGTDKG YRRLKTLKEN GDMKQT
