MLO12_ARATH
ID MLO12_ARATH Reviewed; 576 AA.
AC O80961; Q94KB3;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=MLO-like protein 12;
DE Short=AtMlo12;
DE Short=AtMlo18;
GN Name=MLO12; OrderedLocusNames=At2g39200; ORFNames=T16B24.16;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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 -!- INTERACTION:
CC O80961; O80450: GT-3B; NbExp=3; IntAct=EBI-17061436, EBI-1571089;
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}.
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DR EMBL; AF369573; AAK53805.1; -; mRNA.
DR EMBL; AC004697; AAC28997.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC09645.1; -; Genomic_DNA.
DR PIR; T02582; T02582.
DR RefSeq; NP_565902.1; NM_129478.5.
DR AlphaFoldDB; O80961; -.
DR SMR; O80961; -.
DR BioGRID; 3843; 2.
DR IntAct; O80961; 2.
DR STRING; 3702.AT2G39200.1; -.
DR iPTMnet; O80961; -.
DR PaxDb; O80961; -.
DR PRIDE; O80961; -.
DR ProteomicsDB; 238341; -.
DR EnsemblPlants; AT2G39200.1; AT2G39200.1; AT2G39200.
DR GeneID; 818505; -.
DR Gramene; AT2G39200.1; AT2G39200.1; AT2G39200.
DR KEGG; ath:AT2G39200; -.
DR Araport; AT2G39200; -.
DR TAIR; locus:2056113; AT2G39200.
DR eggNOG; ENOG502QVKX; Eukaryota.
DR HOGENOM; CLU_024720_1_0_1; -.
DR InParanoid; O80961; -.
DR OMA; LIWCIAV; -.
DR OrthoDB; 387177at2759; -.
DR PhylomeDB; O80961; -.
DR PRO; PR:O80961; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80961; baseline and differential.
DR Genevisible; O80961; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:TAIR.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IMP:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0010150; P:leaf senescence; IMP:TAIR.
DR InterPro; IPR004326; Mlo.
DR PANTHER; PTHR31942; PTHR31942; 1.
DR Pfam; PF03094; Mlo; 1.
PE 1: Evidence at protein level;
KW Calmodulin-binding; Membrane; Pathogenesis-related protein; Phosphoprotein;
KW Plant defense; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..576
FT /note="MLO-like protein 12"
FT /id="PRO_0000209942"
FT TOPO_DOM 1..13
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..59
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..155
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..278
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..299
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..308
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 330..362
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..383
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 384..405
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 427..576
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 441..462
FT /note="Calmodulin-binding"
FT REGION 450..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 505
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9SXB6"
SQ SEQUENCE 576 AA; 66548 MW; 43DA9F6AED64D8E6 CRC64;
MAIKERSLEE TPTWAVAVVC FVLLFISIMI EYFLHFIGHW FKKKHKKALS EALEKVKAEL
MLLGFISLLL VVLQTPVSEI CIPRNIAATW HPCSNHQEIA KYGKDYIDDG RKILEDFDSN
DFYSPRRNLA TKGYDKCAEK GKVALVSAYG IHQLHIFIFV LAVFHVLYCI ITYALGKTKM
KKWKSWERET KTIEYQYAND PERFRFARDT SFGRRHLNIW SKSTFTLWIT CFFRQFFGSV
TKVDYLTLRH GFIMAHLPAG SAARFDFQKY IERSLEQDFT VVVGISPLIW CIAVLFILTN
THGWDSYLWL PFLPLIVILI VGAKLQMIIS KLGLRIQEKG DVVKGAPVVE PGDDLFWFGR
PRFILFLIHL VLFTNAFQLA FFVWSTYEFT LKNCFHHKTE DIAIRITMGV LIQVLCSYIT
LPLYALVTQM GTSMRPTIFN DRVANALKKW HHTAKKQTKH GHSGSNTPHS SRPTTPTHGM
SPVHLLHNYN NRSLDQQTSF TASPSPPRFS DYSGQGHGHQ HFFDPESQNH SYQREITDSE
FSNSHHPQVD MASPVREEKE IVEHVKVDLS EFTFKK
