MLO13_ARATH
ID MLO13_ARATH Reviewed; 478 AA.
AC Q94KB2; Q9STW9;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=MLO-like protein 13;
DE Short=AtMlo13;
DE Short=AtMlo20;
GN Name=MLO13; OrderedLocusNames=At4g24250; ORFNames=T22A6.80;
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].
RX PubMed=12569425; DOI=10.1007/s00239-002-2382-5;
RA Devoto A., Hartmann H.A., Piffanelli P., Elliott C., Simmons C.,
RA Taramino G., Goh C.-S., Cohen F.E., Emerson B.C., Schulze-Lefert P.,
RA Panstruga R.;
RT "Molecular phylogeny and evolution of the plant-specific seven-
RT transmembrane MLO family.";
RL J. Mol. Evol. 56:77-88(2003).
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).
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: Membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- DOMAIN: The C-terminus contains a calmodulin-binding domain, which
CC binds calmodulin in a calcium-dependent fashion. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MLO family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB45060.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79335.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF369574; AAK53806.1; -; mRNA.
DR EMBL; AL078637; CAB45060.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161561; CAB79335.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84878.1; -; Genomic_DNA.
DR PIR; T09888; T09888.
DR RefSeq; NP_567697.1; NM_118558.4.
DR AlphaFoldDB; Q94KB2; -.
DR SMR; Q94KB2; -.
DR BioGRID; 13815; 3.
DR STRING; 3702.AT4G24250.1; -.
DR iPTMnet; Q94KB2; -.
DR PaxDb; Q94KB2; -.
DR PRIDE; Q94KB2; -.
DR ProteomicsDB; 238358; -.
DR EnsemblPlants; AT4G24250.1; AT4G24250.1; AT4G24250.
DR GeneID; 828526; -.
DR Gramene; AT4G24250.1; AT4G24250.1; AT4G24250.
DR KEGG; ath:AT4G24250; -.
DR Araport; AT4G24250; -.
DR TAIR; locus:2135982; AT4G24250.
DR eggNOG; ENOG502QSME; Eukaryota.
DR HOGENOM; CLU_024720_3_0_1; -.
DR InParanoid; Q94KB2; -.
DR OrthoDB; 493070at2759; -.
DR PhylomeDB; Q94KB2; -.
DR PRO; PR:Q94KB2; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q94KB2; baseline and differential.
DR Genevisible; Q94KB2; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Calmodulin-binding; Membrane; Pathogenesis-related protein; Plant defense;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..478
FT /note="MLO-like protein 13"
FT /id="PRO_0000209943"
FT TOPO_DOM 1..10
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..31
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..60
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..145
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..276
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..360
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 382..400
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 401..421
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 422..478
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 435..456
FT /note="Calmodulin-binding"
FT REGION 449..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 478 AA; 55068 MW; 82116BCE9D442CE7 CRC64;
MAEARSGSLE YTPTWVVAFI CFIIVLLSLL AERGLHHLGK CLKRRQQDAL FEALQKLKEE
LMLLGFISLM LTVSQAAIRH ICVPPALVNN MFPCKKPLEE HHAPKSSHSI INNARHLLST
GESPDHCAAK GQVPLVSVEA LHQLHIFIFV LAVFHVIFCA STMVLGGARI QQWKHWEDWF
KKRPSQKGTT RRGHHAHAHE LFSANHEFFE MHAGGFWRRS VVISWVRSFF KQFYGSVTKS
EYIALRQAFI MSHCRTNPSF DFHKYMLRTL EIDFKKVVSI SWYLWLFVVV FLLLNVGGWN
TYFWLSFLPL ILLLMVGAKL EYIISSLALD VSEKRSRAEE AVITPSDELF WFHRPGIVLQ
LIHFILFQNS FEIAFFFWIL FTYGIHSCIM EKLGYLIPRL VMGVLVQVLC SYSTLPLYAL
VTQMGSKFKK GIFDNVVQST LEGWLEDTRN RGESTSEAHR IEMQPTTPES YNVQSENP