ID A0A0E0F0H2_9ORYZ Unreviewed; 561 AA.
AC A0A0E0F0H2;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=MLO-like protein {ECO:0000256|RuleBase:RU280816};
GN Name=MLO {ECO:0000256|RuleBase:RU280816};
OS Oryza meridionalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40149 {ECO:0000313|EnsemblPlants:OMERI10G13730.1};
RN [1] {ECO:0000313|EnsemblPlants:OMERI10G13730.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=OR44 {ECO:0000313|EnsemblPlants:OMERI10G13730.1};
RA Wing R.A., Panaud O., Henry R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OMERI10G13730.1}
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; A0A0E0F0H2; -.
DR STRING; 40149.A0A0E0F0H2; -.
DR EnsemblPlants; OMERI10G13730.1; OMERI10G13730.1; OMERI10G13730.
DR Gramene; OMERI10G13730.1; OMERI10G13730.1; OMERI10G13730.
DR eggNOG; ENOG502QPZ5; Eukaryota.
DR HOGENOM; CLU_024720_1_0_1; -.
DR Proteomes; UP000008021; Chromosome 10.
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:SF112; MLO-LIKE PROTEIN; 1.
DR PANTHER; PTHR31942; MLO-LIKE PROTEIN 1; 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:UP000008021};
KW Transmembrane {ECO:0000256|RuleBase:RU280816, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|RuleBase:RU280816,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 25..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 69..88
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 150..171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 276..295
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 301..328
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 384..409
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 438..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 561 AA; 62590 MW; 012180C027CFE55D CRC64;
MSGGGGGGGG AGGDGARALD QTPTWAVAAV CAVIVAASIL LEGLLHHLGQ WFSKRRKKAL
FDALEKVKSE LMTLGFISLL LSVTGRYISR ICIPVGAADT MLPCSLRRSS SEQELHGGGH
GRRHLSGDPT NFKCAKGMVS LVSADGLHQL HIFVFFLAVF HVAFSAITMS LGRAKTRIWK
EWEKETCSLT YEFSYDPSKF RLTHQTSFVR QHASCWSKST ILLYFVSFFR QFFRSVRRTD
YLTLRHGFIA AHLSPGTRFN FRKYIKRSLE DDFKTVVGIS APLWASALAI MLFNVHGWHN
LFWFSTIPLV VTLAVGTKLQ AIIAMMAVEI KERHTVIQGM PVVKLSDEHF WFGKPRLVLH
LIHFASFQYE FGLRSCFHDN FELIIARVCL GVVVQFMCSY ITLPLYALVS QMGSQMKRTI
FDEQTAKALK KWHKAAVVKK KQQKGSSHEP GSETPGTETT TTTATEESQR ERDAAAVPVR
HLHRYKTIAH VGATGTLSDS DCSDTDTPFA SPTRLLIPPT KQRSLDAGRA EVRVDVDAMP
TTERHDSFSF PRLPAHNLQQ K
//
