ID   A0A1D6M4G8_MAIZE        Unreviewed;       488 AA.
AC   A0A1D6M4G8;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=MLO-like protein {ECO:0000256|RuleBase:RU280816};
GN   Name=MLO {ECO:0000256|RuleBase:RU280816};
GN   ORFNames=ZEAMMB73_Zm00001d038199 {ECO:0000313|EMBL:AQK86025.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:AQK86025.1};
RN   [1] {ECO:0000313|EMBL:AQK86025.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Seedling {ECO:0000313|EMBL:AQK86025.1};
RG   Maize Genome Sequencing Project;
RA   Ware D.;
RT   "Update maize B73 reference genome by single molecule sequencing
RT   technologies.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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; CM000782; AQK86025.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D6M4G8; -.
DR   STRING; 4577.A0A1D6M4G8; -.
DR   PaxDb; 4577-GRMZM2G117608_P01; -.
DR   eggNOG; KOG0017; Eukaryota.
DR   InParanoid; A0A1D6M4G8; -.
DR   OMA; CEMEGKV; -.
DR   ExpressionAtlas; A0A1D6M4G8; baseline and differential.
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:SF132; 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};
KW   Pathogenesis-related protein {ECO:0000256|ARBA:ARBA00023265,
KW   ECO:0000256|RuleBase:RU280816};
KW   Plant defense {ECO:0000256|RuleBase:RU280816};
KW   Transmembrane {ECO:0000256|RuleBase:RU280816};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU280816}.
SQ   SEQUENCE   488 AA;  54974 MW;  832DF8EE1A8AD84C CRC64;
     MAEADETAAL QYTPTWIVAA VCSIIVLISL AAERGLHHLG KTLKKNHQRP LYEALLKVKE
     ELMLLGFISL LLTVLQGTIQ RTCIPPSWTD YMLPCQRPGH DEAPAAAASM AARFVAADIL
     GGISWARVLS EGEGAAAQAG LCEKEGKVPL LSLEALHQLH IFIFVLAVSH VFFCASTMLP
     GCAKIRKWKK WEEEIQKIAA ENGPKKVLPM HQVSFIRERY KGIGTDSKTL CWLHSFRKQF
     YGSVAKSDYA AMRLGFIMTH CRGNLKFDFH RYMVRVLESD FKKIVGTSWH LWIFVVIFLL
     LNVNASTVSH SFFTCLHAYF WIAFLPLVLL LAVGTKLEHV IAQLAYDVAE KQTAIEGDLV
     VTPSDQHFWF GRPRIILHLI HFILFQNAFE LAFFFWILMT YGLESCFMDH IGFLVPRLVL
     GVVIQLLCSY STLPLYAIVT QMGSYYKKEI FNEHVQQGVL GWAQKAKKRS GVKEVSSPSE
     PMHGEDAA
//