O49621 (MLO1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
MLO-like protein 1
Short name=AtMlo1

Alternative name(s):
MLO protein homolog 1
Short name=AtMlo-H1

Gene names

Name:	MLO1
Synonyms:	MLO-H1
Ordered Locus Names:	At4g02600
ORF Names:	T10P11.12

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	526 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May be involved in modulation of pathogen defense and leaf cell death. Activity seems to be regulated by Ca2+-dependent calmodulin binding and seems not to require heterotrimeric G proteins By similarity.
Subcellular location	Membrane; Multi-pass membrane protein By similarity.
Domain	The C-terminus contains a calmodulin-binding domain, which binds calmodulin in a calcium-dependent fashion.
Sequence similarities	Belongs to the MLO family.

Ontologies

Keywords
Biological process	Plant defense
Cellular component	Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Calmodulin-binding
Molecular function	Pathogenesis-related protein
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell death Inferred from electronic annotation. Source: InterPro defense response Inferred from electronic annotation. Source: UniProtKB-KW response to biotic stimulus Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from direct assay Ref.6. Source: TAIR
Molecular function	calmodulin binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 526	526	MLO-like protein 1		PRO_0000209931
Regions
	Topological domain	1 – 11	11	Extracellular Potential
	Transmembrane	12 – 32	21	Helical; Name=1; Potential
	Topological domain	33 – 61	29	Cytoplasmic Potential
	Transmembrane	62 – 82	21	Helical; Name=2; Potential
	Topological domain	83 – 160	78	Extracellular Potential
	Transmembrane	161 – 181	21	Helical; Name=3; Potential
	Topological domain	182 – 287	106	Cytoplasmic Potential
	Transmembrane	288 – 308	21	Helical; Name=4; Potential
	Transmembrane	309 – 329	21	Helical; Name=5; Potential
	Topological domain	330 – 372	43	Cytoplasmic Potential
	Transmembrane	373 – 393	21	Helical; Name=6; Potential
	Topological domain	394 – 412	19	Extracellular Potential
	Transmembrane	413 – 433	21	Helical; Name=7; Potential
	Topological domain	434 – 526	93	Cytoplasmic Potential
	Region	447 – 468	22	Calmodulin-binding
Amino acid modifications
	Modified residue	486	1	Phosphoserine Ref.6
	Modified residue	506	1	Phosphoserine Ref.7
Experimental info
	Mutagenesis	453	1	L → R: Disturbs binding to calmodulin; when associated with R-456. Ref.5
	Mutagenesis	456	1	W → R: Disturbs binding to calmodulin; when associated with R-453. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	O49621 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 8E63C276A71A9768	FASTA	526	59,126
	10 20 30 40 50 60 MGHGGEGMSL EFTPTWVVAG VCTVIVAISL AVERLLHYFG TVLKKKKQKP LYEALQKVKE 70 80 90 100 110 120 ELMLLGFISL LLTVFQGLIS KFCVKENVLM HMLPCSLDSR REAGASEHKN VTAKEHFQTF 130 140 150 160 170 180 LPIVGTTRRL LAEHAAVQVG YCSEKGKVPL LSLEALHHLH IFIFVLAISH VTFCVLTVIF 190 200 210 220 230 240 GSTRIHQWKK WEDSIADEKF DPETALRKRR VTHVHNHAFI KEHFLGIGKD SVILGWTQSF 250 260 270 280 290 300 LKQFYDSVTK SDYVTLRLGF IMTHCKGNPK LNFHKYMMRA LEDDFKQVVG ISWYLWIFVV 310 320 330 340 350 360 IFLLLNVNGW HTYFWIAFIP FALLLAVGTK LEHVIAQLAH EVAEKHVAIE GDLVVKPSDE 370 380 390 400 410 420 HFWFSKPQIV LYLIHFILFQ NAFEIAFFFW IWVTYGFDSC IMGQVRYIVP RLVIGVFIQV 430 440 450 460 470 480 LCSYSTLPLY AIVSQMGSSF KKAIFEENVQ VGLVGWAQKV KQKRDLKAAA SNGDEGSSQA 490 500 510 520 GPGPDSGSGS APAAGPGAGF AGIQLSRVTR NNAGDTNNEI TPDHNN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Panstruga R. Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Calmodulin interacts with MLO protein to regulate defence against mildew in barley." Kim M.C., Panstruga R., Elliott C., Mueller J., Devoto A., Yoon H.W., Park H.C., Cho M.J., Schulze-Lefert P. Nature 416:447-451(2002) [PubMed: 11919636] [Abstract] Cited for: INTERACTION WITH CALMODULIN, MUTAGENESIS OF LEU-453 AND TRP-456.
[6]	"Large-scale analysis of in vivo phosphorylated membrane proteins by immobilized metal ion affinity chromatography and mass spectrometry." Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C. Mol. Cell. Proteomics 2:1234-1243(2003) [PubMed: 14506206] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486, MASS SPECTROMETRY. Strain: cv. La-0.
[7]	"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks." Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S. Plant Physiol. 150:889-903(2009) [PubMed: 19376835] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-506, MASS SPECTROMETRY. Strain: cv. Columbia. Tissue: Seedling.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z95352 mRNA. Translation: CAB08605.1. AC002330 Genomic DNA. Translation: AAC78258.1. AL161494 Genomic DNA. Translation: CAB80753.1. CP002687 Genomic DNA. Translation: AEE82202.1. CP002687 Genomic DNA. Translation: AEE82203.1. AY072135 mRNA. Translation: AAL59957.1. AY113992 mRNA. Translation: AAM45040.1.
IPI	IPI00519393.
PIR	T01089.
RefSeq	NP_001031578.1. NM_001036501.1. NP_192169.1. NM_116494.4.
UniGene	At.20439.
3D structure databases
ModBase	Search...
Proteomic databases
PRIDE	O49621.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G02600.1; AT4G02600.1; AT4G02600. AT4G02600.2; AT4G02600.2; AT4G02600.
GeneID	828229.
GenomeReviews	Gene locus AT4G02600 in contig CT486007_GR.
KEGG	ath:AT4G02600.
NMPDR	fig|3702.1.peg.18075.
Organism-specific databases
TAIR	At4g02600.
Phylogenomic databases
GeneTree	EPGT00050000013153.
HOGENOM	HBG319688.
InParanoid	O49621.
OMA	GWAQKVK.
PhylomeDB	O49621.
ProtClustDB	CLSN2685759.
Gene expression databases
ArrayExpress	O49621.
Genevestigator	O49621.
GermOnline	AT4G02600. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR004326. Mlo. [Graphical view]
KO	K08472.
Pfam	PF03094. Mlo. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MLO1_ARATH

Accession

Primary (citable) accession number: O49621
Secondary accession number(s): O22766

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	June 1, 1998
Last modified:	December 14, 2011
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program