ID   M1CN86_SOLTU            Unreviewed;       490 AA.
AC   M1CN86;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   22-FEB-2023, entry version 30.
DE   RecName: Full=MLO-like protein {ECO:0000256|RuleBase:RU280816};
GN   Name=MLO {ECO:0000256|RuleBase:RU280816};
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400071136, ECO:0000313|Proteomes:UP000011115};
RN   [1] {ECO:0000313|Proteomes:UP000011115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX   PubMed=21743474; DOI=10.1038/nature10158;
RG   The Potato Genome Sequencing Consortium;
RT   "Genome sequence and analysis of the tuber crop potato.";
RL   Nature 475:189-195(2011).
RN   [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400071136}
RP   IDENTIFICATION.
RC   STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400071136};
RG   EnsemblPlants;
RL   Submitted (JUN-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; M1CN86; -.
DR   EnsemblPlants; PGSC0003DMT400071136; PGSC0003DMT400071136; PGSC0003DMG400027665.
DR   Gramene; PGSC0003DMT400071136; PGSC0003DMT400071136; PGSC0003DMG400027665.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; M1CN86; baseline.
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:SF66; 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:UP000011115};
KW   Transmembrane {ECO:0000256|RuleBase:RU280816, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU280816,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        17..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        62..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        167..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        279..298
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        304..322
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        360..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        403..424
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          456..490
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        465..490
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   490 AA;  56480 MW;  E912CC66A6724594 CRC64;
     MDGGGEDEGS LEFTPTWVVA AVCTVIVSIS LAVERLIHYA GKRLKRKKQK HLYEALQKVK
     EELMLLGFIS LLLTVFQSRI VEICVPPRVV THLLPCALPL EHTSFSSPTP SPPPTHEEPH
     VNNQTVHYHA GPHHQRHLLA EETMTAEGYC HHKNKVPLLS LEALHHLHVF IFVLAIVHVT
     FSVLTIVFGG AKIRQWKQWE DAIVKDDYES EHAHLKPTVT HVYEHDFIRN RFQGMGRQSA
     ILGWVHSFFK QFYASVNESD YRALRLGFIM THCRGNPRFN FHSWYLWIFV ILFLLLNING
     WHTYFWIAFF PFILLLAVGT KLEHVILQLA HEIAEKHVAI EGELVVTPSD NHFWFDNPQI
     ILFLIHFILF QNAFEIAFFF WILFQYGFHS CIMGKYVFVI PRLVIGVIIQ VLCSYSTLPL
     YALVTQMGSH YKKSMFDNHV QACLMEWAEK VKKKKGHKYG RDSSTRSNEG SVLGSPMSIN
     DHKDLPQNGV
//