MLO3_ARATH
ID MLO3_ARATH Reviewed; 508 AA.
AC Q94KB9; Q9M3E8;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=MLO-like protein 3;
DE Short=AtMlo3;
GN Name=MLO3; OrderedLocusNames=At3g45290; ORFNames=F18N11.50;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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=CAB72478.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF369564; AAK53796.1; -; mRNA.
DR EMBL; AL132953; CAB72478.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE78019.1; -; Genomic_DNA.
DR PIR; T47469; T47469.
DR RefSeq; NP_566879.1; NM_114398.2.
DR AlphaFoldDB; Q94KB9; -.
DR SMR; Q94KB9; -.
DR BioGRID; 8987; 23.
DR IntAct; Q94KB9; 22.
DR STRING; 3702.AT3G45290.1; -.
DR PaxDb; Q94KB9; -.
DR PRIDE; Q94KB9; -.
DR ProteomicsDB; 238711; -.
DR EnsemblPlants; AT3G45290.1; AT3G45290.1; AT3G45290.
DR GeneID; 823667; -.
DR Gramene; AT3G45290.1; AT3G45290.1; AT3G45290.
DR KEGG; ath:AT3G45290; -.
DR Araport; AT3G45290; -.
DR TAIR; locus:2078292; AT3G45290.
DR eggNOG; ENOG502QW1A; Eukaryota.
DR HOGENOM; CLU_024720_1_0_1; -.
DR InParanoid; Q94KB9; -.
DR OMA; WVTLQFG; -.
DR OrthoDB; 448417at2759; -.
DR PhylomeDB; Q94KB9; -.
DR PRO; PR:Q94KB9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q94KB9; baseline and differential.
DR Genevisible; Q94KB9; 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; Phosphoprotein;
KW Plant defense; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..508
FT /note="MLO-like protein 3"
FT /id="PRO_0000209933"
FT TOPO_DOM 1..21
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..42
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..68
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..153
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..275
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..304
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 326..357
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 358..378
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 379..401
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..422
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 423..508
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 436..457
FT /note="Calmodulin-binding"
FT REGION 453..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 494
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9SXB6"
SQ SEQUENCE 508 AA; 58563 MW; 5A3D0246B05DFFB6 CRC64;
MTDKEESNHS SEVGAVRSLQ ETPTWALATV CFFFIAVSIC LERLINLLST RLKKNRKTSL
LEAVEKLKSV LMVLGFMSLM LNVTEGEVSK ICIPIKYANR MLPCRKTIKS HNDVSEDDDD
DDGDNHDNSF FHQCSSKGKT SLISEEGLTQ LSYFFFVLAC MHILCNLAIL LLGMAKMRKW
NSWEKETQTV EYLAANDPNR FRITRDTTFA RRHLSSWTET SFQLWIKCFF RQFYNSVAKV
DYLTLRHGFI FAHVSSNNAF NFQNYIQRSL HEDFKTVVGI SPLMWLTVVI FMLLDVSGWR
VYFYMSFVPL IIVLVIGTKL EMIVAKMAVT IKENNSVIRG TPLVESNDTH FWFSNPRFLL
SILHYTLFLN TFEMAFIVWI TWQFGINSCY HDNQGIIITR LVLAVTVQFL SSYITLPLYA
IVTQMGSSYK RAILEEQLAN VLRHWQGMVR DKKKTIQTPD TDNNSNNNNG DIDSGESPVQ
TEVASEFRFS GRQSPILQEI QIQEKTER
