ID A0A0D3DP31_BRAOL Unreviewed; 534 AA.
AC A0A0D3DP31;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=MLO-like protein {ECO:0000256|RuleBase:RU280816};
GN Name=MLO {ECO:0000256|RuleBase:RU280816};
GN Synonyms=106309471 {ECO:0000313|EnsemblPlants:Bo8g059990.1};
OS Brassica oleracea var. oleracea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo8g059990.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo8g059990.1, ECO:0000313|Proteomes:UP000032141}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA Chalhoub B., Sharpe A.G.;
RT "Transcriptome and methylome profiling reveals relics of genome dominance
RT in the mesopolyploid Brassica oleracea.";
RL Genome Biol. 15:R77-R77(2014).
RN [2] {ECO:0000313|EnsemblPlants:Bo8g059990.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-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 RefSeq; XP_013601952.1; XM_013746498.1.
DR AlphaFoldDB; A0A0D3DP31; -.
DR STRING; 109376.A0A0D3DP31; -.
DR EnsemblPlants; Bo8g059990.1; Bo8g059990.1; Bo8g059990.
DR GeneID; 106309471; -.
DR Gramene; Bo8g059990.1; Bo8g059990.1; Bo8g059990.
DR KEGG; boe:106309471; -.
DR eggNOG; ENOG502QVKX; Eukaryota.
DR HOGENOM; CLU_024720_1_0_1; -.
DR OMA; EFGISNC; -.
DR OrthoDB; 664386at2759; -.
DR Proteomes; UP000032141; Chromosome C8.
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:SF107; 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:UP000032141};
KW Transmembrane {ECO:0000256|RuleBase:RU280816, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|RuleBase:RU280816,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 138..159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 269..288
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 294..316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 350..371
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 391..414
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 437..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 534 AA; 61005 MW; 9D12A804D7CE9D27 CRC64;
MADKEYERTL EETSTWTVAV VCFVLILISL FIEHLIHKIG SWLKKKHKGN LYEALEKVKA
ELMLLGFISL LLTVAQTSIS SFCIPKSVAS SMRPCSAAEI AKKELDKKIP RRSLATKGYN
ECPKGKVPFV SAYGIHQLHI FIFVLAVVHV IYCIVTYALG KTKMRKWEQW EEETKTIEYQ
YSNDPGRFRF ARDTTFGRRH LNAWSKTSVT LWTVCFFRQF VGSVTKVDYL TLRHGFITAR
FAPGSGSEKM PYDFCNYIQR SLEKDFKTVV EISPVIWFVT VLFLLTNLDG LHSYLWLPFI
PLIVVLIVGT KLQVIITKLG LRIQEKGDVV RGAPLVKPGD DLFWFDKPSF MIFLIHLVLF
TNAFQLAFFA WSSYEFGISN CFHKEPQDIT IRIVVGLVVQ ILCSYVTLPL YALVTQMGTT
MKPTVFNGRV SKMLKKWHHK AQEETQHGRR SESNTPYPSR PTTPTHGSSP IHLLHNYNDR
SIESFPNPPS PNHHDHYQFY DPESQHKAAE SSTHHSTAHG SASMELPPLR PANA
//