MLO1_ARATH
ID MLO1_ARATH Reviewed; 526 AA.
AC O49621; O22766;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=MLO-like protein 1;
DE Short=AtMlo1;
DE AltName: Full=MLO protein homolog 1;
DE Short=AtMlo-H1;
GN Name=MLO1; Synonyms=MLO-H1; OrderedLocusNames=At4g02600;
GN ORFNames=T10P11.12;
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].
RA Panstruga R.;
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
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 INTERACTION WITH CALMODULIN, AND MUTAGENESIS OF LEU-453 AND TRP-456.
RX PubMed=11919636; DOI=10.1038/416447a;
RA Kim M.C., Panstruga R., Elliott C., Mueller J., Devoto A., Yoon H.W.,
RA Park H.C., Cho M.J., Schulze-Lefert P.;
RT "Calmodulin interacts with MLO protein to regulate defence against mildew
RT in barley.";
RL Nature 416:447-451(2002).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=15060130; DOI=10.1074/mcp.m400001-mcp200;
RA Marmagne A., Rouet M.-A., Ferro M., Rolland N., Alcon C., Joyard J.,
RA Garin J., Barbier-Brygoo H., Ephritikhine G.;
RT "Identification of new intrinsic proteins in Arabidopsis plasma membrane
RT proteome.";
RL Mol. Cell. Proteomics 3:675-691(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT phosphorylation site database.";
RL Plant Cell 16:2394-2405(2004).
CC -!- FUNCTION: May be involved in modulation of pathogen defense and leaf
CC cell death. Activity seems to be regulated by Ca(2+)-dependent
CC calmodulin binding and seems not to require heterotrimeric G proteins
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15060130};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- DOMAIN: The C-terminus contains a calmodulin-binding domain, which
CC binds calmodulin in a calcium-dependent fashion.
CC -!- SIMILARITY: Belongs to the MLO family. {ECO:0000305}.
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DR EMBL; Z95352; CAB08605.1; -; mRNA.
DR EMBL; AC002330; AAC78258.1; -; Genomic_DNA.
DR EMBL; AL161494; CAB80753.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82202.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82203.1; -; Genomic_DNA.
DR EMBL; AY072135; AAL59957.1; -; mRNA.
DR EMBL; AY113992; AAM45040.1; -; mRNA.
DR PIR; T01089; T01089.
DR RefSeq; NP_001031578.1; NM_001036501.2.
DR RefSeq; NP_192169.1; NM_116494.5.
DR AlphaFoldDB; O49621; -.
DR SMR; O49621; -.
DR BioGRID; 13518; 1.
DR STRING; 3702.AT4G02600.1; -.
DR iPTMnet; O49621; -.
DR PaxDb; O49621; -.
DR PRIDE; O49621; -.
DR ProteomicsDB; 238896; -.
DR EnsemblPlants; AT4G02600.1; AT4G02600.1; AT4G02600.
DR EnsemblPlants; AT4G02600.2; AT4G02600.2; AT4G02600.
DR GeneID; 828229; -.
DR Gramene; AT4G02600.1; AT4G02600.1; AT4G02600.
DR Gramene; AT4G02600.2; AT4G02600.2; AT4G02600.
DR KEGG; ath:AT4G02600; -.
DR Araport; AT4G02600; -.
DR TAIR; locus:2132313; AT4G02600.
DR eggNOG; KOG0017; Eukaryota.
DR HOGENOM; CLU_024720_3_0_1; -.
DR InParanoid; O49621; -.
DR OMA; PSVAIQM; -.
DR OrthoDB; 493070at2759; -.
DR PhylomeDB; O49621; -.
DR PRO; PR:O49621; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O49621; baseline and differential.
DR Genevisible; O49621; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009607; P:response to biotic stimulus; IEA:UniProtKB-KW.
DR InterPro; IPR004326; Mlo.
DR PANTHER; PTHR31942; PTHR31942; 1.
DR Pfam; PF03094; Mlo; 1.
PE 1: Evidence at protein level;
KW Calmodulin-binding; Cell membrane; Membrane; Pathogenesis-related protein;
KW Plant defense; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..526
FT /note="MLO-like protein 1"
FT /id="PRO_0000209931"
FT TOPO_DOM 1..11
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..61
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..160
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..287
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 330..372
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..393
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 394..412
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 413..433
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 434..526
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 447..468
FT /note="Calmodulin-binding"
FT REGION 471..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 453
FT /note="L->R: Disturbs binding to calmodulin; when
FT associated with R-456."
FT /evidence="ECO:0000269|PubMed:11919636"
FT MUTAGEN 456
FT /note="W->R: Disturbs binding to calmodulin; when
FT associated with R-453."
FT /evidence="ECO:0000269|PubMed:11919636"
SQ SEQUENCE 526 AA; 59126 MW; 8E63C276A71A9768 CRC64;
MGHGGEGMSL EFTPTWVVAG VCTVIVAISL AVERLLHYFG TVLKKKKQKP LYEALQKVKE
ELMLLGFISL LLTVFQGLIS KFCVKENVLM HMLPCSLDSR REAGASEHKN VTAKEHFQTF
LPIVGTTRRL LAEHAAVQVG YCSEKGKVPL LSLEALHHLH IFIFVLAISH VTFCVLTVIF
GSTRIHQWKK WEDSIADEKF DPETALRKRR VTHVHNHAFI KEHFLGIGKD SVILGWTQSF
LKQFYDSVTK SDYVTLRLGF IMTHCKGNPK LNFHKYMMRA LEDDFKQVVG ISWYLWIFVV
IFLLLNVNGW HTYFWIAFIP FALLLAVGTK LEHVIAQLAH EVAEKHVAIE GDLVVKPSDE
HFWFSKPQIV LYLIHFILFQ NAFEIAFFFW IWVTYGFDSC IMGQVRYIVP RLVIGVFIQV
LCSYSTLPLY AIVSQMGSSF KKAIFEENVQ VGLVGWAQKV KQKRDLKAAA SNGDEGSSQA
GPGPDSGSGS APAAGPGAGF AGIQLSRVTR NNAGDTNNEI TPDHNN
