ID A0A0E0ABS7_9ORYZ Unreviewed; 444 AA.
AC A0A0E0ABS7;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=MLO-like protein {ECO:0000256|RuleBase:RU280816};
GN Name=MLO {ECO:0000256|RuleBase:RU280816};
OS Oryza glumipatula.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM06G21870.1};
RN [1] {ECO:0000313|EnsemblPlants:OGLUM06G21870.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A., Panaud O., Oliveira A.C.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OGLUM06G21870.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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 AlphaFoldDB; A0A0E0ABS7; -.
DR STRING; 40148.A0A0E0ABS7; -.
DR EnsemblPlants; OGLUM06G21870.1; OGLUM06G21870.1; OGLUM06G21870.
DR Gramene; OGLUM06G21870.1; OGLUM06G21870.1; OGLUM06G21870.
DR eggNOG; ENOG502QPZ5; Eukaryota.
DR HOGENOM; CLU_024720_3_1_1; -.
DR Proteomes; UP000026961; 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: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; MLO-LIKE PROTEIN 1; 1.
DR PANTHER; PTHR31942:SF54; MLO-LIKE PROTEIN 13; 1.
DR Pfam; PF03094; Mlo; 3.
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:UP000026961};
KW Transmembrane {ECO:0000256|RuleBase:RU280816, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|RuleBase:RU280816,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 108..129
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 240..258
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 299..323
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 379..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 444 AA; 49836 MW; 4BF50823CB2FCF4F CRC64;
MEESSITHTP TWVVAVVCFA IVSFLKHKDQ KALFSALERL KEELMLLGFI SFVLSLSEGF
IVGICVSENA MHLMLPCKKE SYQLSEGVKL CKKKGEVPLL SVEALHQLHI FIFILGLVHV
VFCATTILLG GAKIRKWKLW ETEIQQEMQQ KLQQRDATPG RIAHNQQGEF VSERTKGLWM
KLAVVSWIIA FFKQFHDSVS KSDYKALRSA FGLKHFPSHP SFNFYKYLIR ALEHDFKRVV
GIRMAYILLL LLVVGAKLEH IITRLAQEAA AVASLSHGTE RTPYVKPSKE HFWFGRPEIV
LNLIHFILFQ NSFEIGFFIW VLVTFGFDSC IMEKKVYAIS RLVIGALIQV ICSYMDGGIK
LQGIGSGLHE SVAGWALDAR RKKEEQQSSH GGATTGATEG SNYRSDHFGA SPRSALAPPP
PPSPDLVEIV SVAAADDDDS RHRR
//
