ID A0A0E0MD57_ORYPU Unreviewed; 464 AA.
AC A0A0E0MD57;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=MLO-like protein {ECO:0000256|RuleBase:RU280816};
GN Name=MLO {ECO:0000256|RuleBase:RU280816};
OS Oryza punctata (Red rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC11G04780.1};
RN [1] {ECO:0000313|EnsemblPlants:OPUNC11G04780.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OPUNC11G04780.1}
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; A0A0E0MD57; -.
DR STRING; 4537.A0A0E0MD57; -.
DR EnsemblPlants; OPUNC11G04780.1; OPUNC11G04780.1; OPUNC11G04780.
DR Gramene; OPUNC11G04780.1; OPUNC11G04780.1; OPUNC11G04780.
DR eggNOG; ENOG502QQK2; Eukaryota.
DR HOGENOM; CLU_024720_2_1_1; -.
DR OMA; GVIVQFW; -.
DR Proteomes; UP000026962; Chromosome 11.
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:SF9; MLO-LIKE PROTEIN 4; 1.
DR Pfam; PF03094; Mlo; 2.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000026962};
KW Transmembrane {ECO:0000256|RuleBase:RU280816, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|RuleBase:RU280816,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 56..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 150..171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 239..262
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 302..326
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 464 AA; 52862 MW; 9DD71987A520DD56 CRC64;
MVEEGRSLAE TPTWSVATVT TLMVAACFLV ERGLSRFAKW LRKTKRKAML AALEKIREEL
MLLGVISLLL SQTARWISEI CVPSSLFTSR FYICSETDYE DLVVGGKRST MEMNQTVVPN
GLFGIRSQNV CSEGHEPFVS YEGLEQLHRF LFILGITHVL YTFVTVVLSM IKIYSWRKFE
TQACQLPTEQ LQAMLSASIQ AFHQEVRLYG IEIGTISCHT RIISTNTWYG AWKMIIMEVL
ASGLNIYFWI SFVPAILVLL VGTELQHVIA QLALEVVGAT APYVGTQLKL RDDLFWFGKP
RVLWWLIQFI SFQNAFEMAT FVWSLLELSA QSCFMKNHYM IVLRLTSGIL VQFWCSYNTL
PLNVIITQMG SKFKKSLVSE SVRESLHSWC KRVKDKNRHN LASRSVCSLD TTYEETDHET
ATVGTLSRTV SATSLDEELT VATVDDNDDQ EMSRIDQDHI DRSL
//
