ID   A0A178VNS1_ARATH        Unreviewed;       576 AA.
AC   A0A178VNS1;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   18-JAN-2017, entry version 5.
DE   RecName: Full=MLO-like protein {ECO:0000256|RuleBase:RU280816};
GN   Name=MLO {ECO:0000256|RuleBase:RU280816};
GN   OrderedLocusNames=AXX17_At2g36100 {ECO:0000313|EMBL:OAP07466.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702 {ECO:0000313|EMBL:OAP07466.1};
RN   [1] {ECO:0000313|EMBL:OAP07466.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Leaf {ECO:0000313|EMBL:OAP07466.1};
RA   Zapata L., Schneeberger K., Ossowski S.;
RT   "Full-length assembly of Arabidopsis thaliana Ler reveals the
RT   complement of translocations and inversions.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved in modulation of pathogen defense and
CC       leaf cell death. {ECO:0000256|RuleBase:RU280816}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU280816};
CC       Multi-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.
CC       {ECO:0000256|RuleBase:RU280816}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OAP07466.1}.
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DR   EMBL; LUHQ01000002; OAP07466.1; -; Genomic_DNA.
DR   RefSeq; NP_565902.1; NM_129478.5.
DR   UniGene; At.12809; -.
DR   EnsemblPlants; AT2G39200.1; AT2G39200.1; AT2G39200.
DR   GeneID; 818505; -.
DR   Gramene; AT2G39200.1; AT2G39200.1; AT2G39200.
DR   KEGG; ath:AT2G39200; -.
DR   KO; K08472; -.
DR   PhylomeDB; A0A178VNS1; -.
DR   GO; GO:0016021; C:integral component of membrane; 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   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|RuleBase:RU280816};
KW   Plant defense {ECO:0000256|RuleBase:RU280816};
KW   Transmembrane {ECO:0000256|RuleBase:RU280816,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU280816,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     14     37       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     58     77       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    154    175       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    279    300       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    306    325       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    363    384       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    404    427       Helical. {ECO:0000256|SAM:Phobius}.
SQ   SEQUENCE   576 AA;  66548 MW;  43DA9F6AED64D8E6 CRC64;
     MAIKERSLEE TPTWAVAVVC FVLLFISIMI EYFLHFIGHW FKKKHKKALS EALEKVKAEL
     MLLGFISLLL VVLQTPVSEI CIPRNIAATW HPCSNHQEIA KYGKDYIDDG RKILEDFDSN
     DFYSPRRNLA TKGYDKCAEK GKVALVSAYG IHQLHIFIFV LAVFHVLYCI ITYALGKTKM
     KKWKSWERET KTIEYQYAND PERFRFARDT SFGRRHLNIW SKSTFTLWIT CFFRQFFGSV
     TKVDYLTLRH GFIMAHLPAG SAARFDFQKY IERSLEQDFT VVVGISPLIW CIAVLFILTN
     THGWDSYLWL PFLPLIVILI VGAKLQMIIS KLGLRIQEKG DVVKGAPVVE PGDDLFWFGR
     PRFILFLIHL VLFTNAFQLA FFVWSTYEFT LKNCFHHKTE DIAIRITMGV LIQVLCSYIT
     LPLYALVTQM GTSMRPTIFN DRVANALKKW HHTAKKQTKH GHSGSNTPHS SRPTTPTHGM
     SPVHLLHNYN NRSLDQQTSF TASPSPPRFS DYSGQGHGHQ HFFDPESQNH SYQREITDSE
     FSNSHHPQVD MASPVREEKE IVEHVKVDLS EFTFKK
//