ID   A0A1D6Q3D5_MAIZE        Unreviewed;       491 AA.
AC   A0A1D6Q3D5;
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_Zm00001d050805 {ECO:0000313|EMBL:AQK53076.1};
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:AQK53076.1};
RN   [1] {ECO:0000313|EMBL:AQK53076.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Seedling {ECO:0000313|EMBL:AQK53076.1};
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; CM000780; AQK53076.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D6Q3D5; -.
DR   OMA; SCIMGNK; -.
DR   ExpressionAtlas; A0A1D6Q3D5; 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:SF83; 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   491 AA;  55920 MW;  A39C52BCF452FF41 CRC64;
     MAGGDGADEI TLEHTPTWIV ASVCSIIVVI SLLFERLLHR LGKRLAKGRR KPLYEALLKV
     KEELMLLGFI SLLLTVFQGA TQKICVRESL MNHLLPCPRT TAKTSAHFVG TRRLLAGGGG
     VSSDYCLSKG KVPILSVDAI HQLHIFIFVL AVTHVVLSAV TVILGITQTR NWKYWEEKIQ
     QNDDSAPQMI KHVQEFKFIK SHFRGHGKRW GIFGWLRSFF KQFYGSVTEE DYTTLRLGFV
     MKHCRGHPKF NFYNYMDRAF EGDFKKVVGI SWYLWGMLMI FLLLNVHGWY VYIWISVIPF
     ILLLVLGSKM EHIITELALE VIQKHTAIEG VLVVTPSDEL FWFHRPKLVL LLIHIILFQN
     AFEIAFFFWL LVTYGFNSCI MGKPAYVITR VVISVISQVL CGYSTLPLYA LISQFDANIL
     SFSLIKMGSS FKKAIFDENV SEGLINWAEN ARRRNRMPTS VGDNSPVGEG IQMSNQTQRE
     SSMEQGTARL I
//