Q8VWZ8 (SMO22_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Methylsterol monooxygenase 2-2
EC=1.14.13.72

Alternative name(s):
Sterol 4-alpha-methyl-oxidase 1
Short name=AtSMO1
Sterol 4-alpha-methyl-oxidase 2-2

Gene names

Name:	SMO2-2
Synonyms:	SMO1
Ordered Locus Names:	At1g07420
ORF Names:	F22G5.23

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	266 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Non-heme iron oxygenase involved in sterols biosynthesis. 24-ethylidenelophenol and 24-ethyllophenol are the preferred substrates. Ref.1
Catalytic activity	4,4-dimethyl-5-alpha-cholest-7-en-3-beta-ol + NAD(P)H + O2 = 4-beta-hydroxymethyl-4-alpha-methyl-5-alpha-cholest-7-en-3-beta-ol + CA NAD(P)+ + H2O. 4-beta-hydroxymethyl-4-alpha-methyl-5-alpha-cholest-7-en-3-beta-ol + NAD(P)H + O2 = 3-beta-hydroxy-4-beta-methyl-5-alpha-cholest-7-ene-4-alpha-carbaldehyde + NAD(P)+ + 2 H2O. 3-beta-hydroxy-4-beta-methyl-5-alpha-cholest-7-ene-4-alpha-arbaldehyde + NAD(P)H + O2 = 3-beta-hydroxy-4-beta-methyl-5-alpha-cholest-7-ene-4-alpha-carboxylate + NAD(P)+ + H2O.
Cofactor	Iron By similarity.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.
Domain	The histidine box domains may contain the active site and/or be involved in metal ion binding.
Miscellaneous	Requires a membrane-bound cytochrome b5 as an obligatory electron carrier from NAD(P)H to SMO.
Sequence similarities	Belongs to the sterol desaturase family.
Sequence caution	The sequence AAF79571.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Lipid biosynthesis Lipid metabolism Steroid biosynthesis Steroid metabolism Sterol biosynthesis Sterol metabolism
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing
Domain	Transmembrane Transmembrane helix
Ligand	Iron NAD NADP
Molecular function	Monooxygenase Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid biosynthetic process Inferred from electronic annotation. Source: InterPro sterol biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	chloroplast envelope Inferred from direct assay PubMed 12938931. Source: TAIR endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	4-alpha-methyl-delta7-sterol-4alpha-methyl oxidase activity Inferred from genetic interaction Ref.2. Source: TAIR iron ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8VWZ8-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q8VWZ8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-55: MASFVESGWQYLVTHFSDFQLACIGSFLLHESVFFLSGLPFIFLERQGFLSKYKI → MLLLPFMVNTYFSFVPM

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 266	266	Methylsterol monooxygenase 2-2		PRO_0000413165
Regions
	Transmembrane	24 – 44	21	Helical; Potential
	Transmembrane	71 – 91	21	Helical; Potential
	Transmembrane	107 – 127	21	Helical; Potential
	Transmembrane	162 – 182	21	Helical; Potential
	Motif	127 – 131	5	Histidine box-1
	Motif	140 – 144	5	Histidine box-2
	Motif	219 – 225	7	Histidine box-3
Natural variations
	Alternative sequence	1 – 55	55	MASFV…SKYKI → MLLLPFMVNTYFSFVPM in isoform 2.		VSP_041865
Experimental info
	Sequence conflict	29	1	L → F in AAM64821. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: A7A7FF6BF5F01380	FASTA	266	30,927
	10 20 30 40 50 60 MASFVESGWQ YLVTHFSDFQ LACIGSFLLH ESVFFLSGLP FIFLERQGFL SKYKIQTKNN 70 80 90 100 110 120 TPAAQGKCIT RLLLYHFSVN LPLMLASYPV FRAMGMRSSF PLPSWKEVSA QILFYFIIED 130 140 150 160 170 180 FVFYWGHRIL HSKWLYKNVH SVHHEYATPF GLTSEYAHPA EILFLGFATI VGPALTGPHL 190 200 210 220 230 240 ITLWLWMVLR VLETVEAHCG YHFPWSLSNF LPLYGGADFH DYHHRLLYTK SGNYSSTFVY 250 260 MDWIFGTDKG YRRLKTLKEN GDMKQT
	Isoform 2 [UniParc]. Checksum: 124DC5510BCB1A6F	FASTA	228	26,594
	10 20 30 40 50 60 MLLLPFMVNT YFSFVPMQTK NNTPAAQGKC ITRLLLYHFS VNLPLMLASY PVFRAMGMRS 70 80 90 100 110 120 SFPLPSWKEV SAQILFYFII EDFVFYWGHR ILHSKWLYKN VHSVHHEYAT PFGLTSEYAH 130 140 150 160 170 180 PAEILFLGFA TIVGPALTGP HLITLWLWMV LRVLETVEAH CGYHFPWSLS NFLPLYGGAD 190 200 210 220 FHDYHHRLLY TKSGNYSSTF VYMDWIFGTD KGYRRLKTLK ENGDMKQT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Functional identification of sterol-4alpha-methyl oxidase cDNAs from Arabidopsis thaliana by complementation of a yeast erg25 mutant lacking sterol-4alpha-methyl oxidation." Darnet S., Bard M., Rahier A. FEBS Lett. 508:39-43(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION. Strain: cv. Columbia. Tissue: Silique.
[2]	"Plant sterol biosynthesis: identification of two distinct families of sterol 4alpha-methyl oxidases." Darnet S., Rahier A. Biochem. J. 378:889-898(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), GENE FAMILY, NOMENCLATURE. Strain: cv. Columbia. Tissue: Silique.
[3]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[5]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]	"Arabidopsis ORF clones." de los Reyes C., Quan R., Chen H., Bautista V., Kim C.J., Ecker J.R. Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[7]	"Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs." Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K. DNA Res. 16:155-164(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Strain: cv. Columbia. Tissue: Rosette leaf.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF346734 mRNA. Translation: AAL32303.1. AC022464 Genomic DNA. Translation: AAF79571.1. Sequence problems. CP002684 Genomic DNA. Translation: AEE28122.1. CP002684 Genomic DNA. Translation: AEE28123.1. AY087267 mRNA. Translation: AAM64821.1. BT044610 mRNA. Translation: ACI31310.1. AK316820 mRNA. Translation: BAH19532.1.
IPI	IPI00528164.
RefSeq	NP_563789.1. NM_100616.2. NP_973777.1. NM_202048.2.
UniGene	At.27344. At.67216.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT1G07420.1-P.
Protocols and materials databases
DNASU	837254.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G07420.1; AT1G07420.1; AT1G07420.
GeneID	837254.
KEGG	ath:AT1G07420.
Organism-specific databases
TAIR	At1g07420.
Phylogenomic databases
eggNOG	COG3000.
HOGENOM	HOG000162289.
InParanoid	Q8VWZ8.
KO	K14424.
OMA	KNNTPAA.
PhylomeDB	Q8VWZ8.
ProtClustDB	CLSN2916981.
Enzyme and pathway databases
BioCyc	ARA:AT1G07420-MONOMER. MetaCyc:AT1G07420-MONOMER.
BRENDA	1.14.13.72. 302.
Gene expression databases
ArrayExpress	Q8VWZ8.
Genevestigator	Q8VWZ8.
Family and domain databases
InterPro	IPR006694. Fatty_acid_hydroxylase. [Graphical view]
Pfam	PF04116. FA_hydroxylase. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SMO22_ARATH

Accession

Primary (citable) accession number: Q8VWZ8
Secondary accession number(s): B9DFL5, Q8LBE1, Q9LNW2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 19, 2011
Last sequence update:	March 1, 2002
Last modified:	April 3, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program