ID D7KVJ7_ARALL Unreviewed; 586 AA.
AC D7KVJ7;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=MLO-like protein {ECO:0000256|RuleBase:RU280816};
GN Name=MLO {ECO:0000256|RuleBase:RU280816};
GN ORFNames=ARALYDRAFT_315221 {ECO:0000313|EMBL:EFH62793.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
CC -!- FUNCTION: May be involved in modulation of pathogen defense and leaf
CC cell death. {ECO:0000256|RuleBase:RU280816}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU280816}; Multi-
CC pass membrane protein {ECO:0000256|RuleBase:RU280816}.
CC -!- DOMAIN: The C-terminus contains a calmodulin-binding domain, which
CC binds calmodulin in a calcium-dependent fashion.
CC {ECO:0000256|RuleBase:RU280816}.
CC -!- SIMILARITY: Belongs to the MLO family. {ECO:0000256|ARBA:ARBA00006574,
CC ECO:0000256|RuleBase:RU280816}.
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DR EMBL; GL348714; EFH62793.1; -; Genomic_DNA.
DR RefSeq; XP_002886534.1; XM_002886488.1.
DR AlphaFoldDB; D7KVJ7; -.
DR STRING; 81972.D7KVJ7; -.
DR EnsemblPlants; fgenesh1_pm.C_scaffold_2000254; fgenesh1_pm.C_scaffold_2000254; fgenesh1_pm.C_scaffold_2000254.
DR GeneID; 9322600; -.
DR Gramene; fgenesh1_pm.C_scaffold_2000254; fgenesh1_pm.C_scaffold_2000254; fgenesh1_pm.C_scaffold_2000254.
DR KEGG; aly:9322600; -.
DR eggNOG; ENOG502QVKX; Eukaryota.
DR HOGENOM; CLU_024720_1_0_1; -.
DR OrthoDB; 368831at2759; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IEA:EnsemblPlants.
DR InterPro; IPR004326; Mlo.
DR PANTHER; PTHR31942; MLO-LIKE PROTEIN 1; 1.
DR PANTHER; PTHR31942:SF80; MLO-LIKE PROTEIN 6; 1.
DR Pfam; PF03094; Mlo; 1.
PE 3: Inferred from homology;
KW Calmodulin-binding {ECO:0000256|RuleBase:RU280816};
KW Membrane {ECO:0000256|RuleBase:RU280816, ECO:0000256|SAM:Phobius};
KW Pathogenesis-related protein {ECO:0000256|ARBA:ARBA00023265,
KW ECO:0000256|RuleBase:RU280816};
KW Plant defense {ECO:0000256|RuleBase:RU280816};
KW Reference proteome {ECO:0000313|Proteomes:UP000008694};
KW Transmembrane {ECO:0000256|RuleBase:RU280816, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|RuleBase:RU280816,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 16..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 58..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 162..183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 290..309
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 315..337
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 371..392
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 412..435
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 463..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..554
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 586 AA; 67293 MW; 7D68D51D711EAE74 CRC64;
MADQVKEKTL EETSTWAVAV VCFVLLLISI VIEKLIHKLG SWFKSKNKKA LYEALEKVKA
ELMLMGFISL LLTIGQGYIS NICIPKNIAA SMHPCSASEE ARKYGKKDAA KKDGEDGENS
RRKLLQLVDS LIPRRSLATK GYDKCAEKGK VAFVSAYGMH QLHIFIFVLA VCHVIYCIVT
YALGKTKMRR WKRWEEETKT IEYQYSHDPE RFRFARDTSF GRRHLNFWSK STITLWIVCF
FRQFFRSVTK VDYLTLRHGF IMAHLAPGSD ARFDFRKYIQ RSLEEDFKTI VEINPVIWFI
AVLFLLTNTH GLNSYLWLPF IPFVVILIVG TKLQVIITKL GLRIQEKGDV VKGTPLVQPG
DHFFWFGRPR FILFLIHLVL FTNAFQLAFF AWSTYEFGLK NCFHESRVDV IIRISIGLIV
QILCSYVTLP LYALVTQMGS KMKPTVFNER VATALKSWHH TAKKQIKHGR TSESTTPFSS
RPTTPTHGSS PIHLLRNAPH KRSRSVDESF ANSMSPRNSD FDSWDPESQH EAAETSNSNH
CSRVREEESE KKFVSSSSVE LPPGPGQIRT QHEISTISLR DFSFKR
//
