ID A0A061DF10_THECC Unreviewed; 575 AA.
AC A0A061DF10;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=MLO-like protein {ECO:0000256|RuleBase:RU280816};
GN Name=MLO {ECO:0000256|RuleBase:RU280816};
GN ORFNames=TCM_000035 {ECO:0000313|EMBL:EOX90619.1};
OS Theobroma cacao (Cacao) (Cocoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOX90619.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOX90619.1, ECO:0000313|Proteomes:UP000026915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA Kuhn D.N.;
RT "The genome sequence of the most widely cultivated cacao type and its use
RT to identify candidate genes regulating pod color.";
RL Genome Biol. 14:R53.1-R53.24(2013).
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; CM001879; EOX90619.1; -; Genomic_DNA.
DR RefSeq; XP_007046462.1; XM_007046400.2.
DR RefSeq; XP_017983398.1; XM_018127909.1.
DR AlphaFoldDB; A0A061DF10; -.
DR STRING; 3641.A0A061DF10; -.
DR EnsemblPlants; EOX90619; EOX90619; TCM_000035.
DR EnsemblPlants; Tc01v2_t000250.1; Tc01v2_p000250.1; Tc01v2_g000250.
DR EnsemblPlants; Tc01v2_t000250.2; Tc01v2_p000250.2; Tc01v2_g000250.
DR GeneID; 18610625; -.
DR Gramene; EOX90619; EOX90619; TCM_000035.
DR Gramene; Tc01v2_t000250.1; Tc01v2_p000250.1; Tc01v2_g000250.
DR Gramene; Tc01v2_t000250.2; Tc01v2_p000250.2; Tc01v2_g000250.
DR KEGG; tcc:18610625; -.
DR eggNOG; ENOG502QPZ5; Eukaryota.
DR HOGENOM; CLU_024720_1_0_1; -.
DR InParanoid; A0A061DF10; -.
DR OMA; ALCLCSY; -.
DR OrthoDB; 368831at2759; -.
DR Proteomes; UP000026915; Chromosome 1.
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; MLO-LIKE PROTEIN 1; 1.
DR PANTHER; PTHR31942:SF49; MLO-LIKE PROTEIN 8; 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:UP000026915};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|RuleBase:RU280816, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|RuleBase:RU280816,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..575
FT /note="MLO-like protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001595780"
FT TRANSMEM 38..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 80..101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 170..191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 293..312
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 318..336
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 377..403
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 415..441
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 471..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..564
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 575 AA; 65533 MW; 1243FBDDDEC40DEC CRC64;
MRLLIWYFAW GWLMVGERVV MGATESSGER KLYQTPTWAV AGVCAVIIII SILLEKVLHK
LGTWFTERHK RALYEALDKV KAELMVLGFI SLLLTFGQSY IARICIPTNV ANTMLPCKAD
SEQDTSTSSE EEHRRRLLWF ERRFLAAVST ARKCKEGHEP LISTEGLHEL HILIFFLAVF
HVLYSFVTMM LGRLKIRGWK VWEQETLSHD YEFSNDPSRF RLTHETSFVK AHTSFWTRIP
FFFYIGCFFR QFFRSVGRVD YLTLRNGFIT VHLAPGSKFD FQKYIKRSLE DDFKIVVGVS
PVLWASFVIF LLLNVEGWQA LLWASIIPVI IILAVGTKLQ AILTKMALEI TERHAVVQGI
PLVQGSNKYF WFGRPQLVLY LIHFALFQNA FQITYFLWIL YSFGLDSCFH GNLKIAIIKV
SLGVGALCLC SYITLPLYAL VTQMGSNMKK SIFDEQTSKA LKKWHMAAKR KRGKAGRSPT
RTLGGTASPA STVHSTGHTL HRFKTTGHST RSSYAYEDHD MSDLEAEPLS PTPSTNLIIR
ADDEEQATEI SETHHVEGKN DDDFSFVKPA PVQGA
//
