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Database: UniProt
Entry: A0A068TZS2_COFCA
LinkDB: A0A068TZS2_COFCA
Original site: A0A068TZS2_COFCA 
ID   A0A068TZS2_COFCA        Unreviewed;       540 AA.
AC   A0A068TZS2;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=MLO-like protein {ECO:0000256|RuleBase:RU280816};
GN   Name=MLO {ECO:0000256|RuleBase:RU280816};
GN   ORFNames=GSCOC_T00036928001 {ECO:0000313|EMBL:CDP01770.1};
OS   Coffea canephora (Robusta coffee).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Gentianales; Rubiaceae; Ixoroideae; Gardenieae complex;
OC   Bertiereae - Coffeeae clade; Coffeeae; Coffea.
OX   NCBI_TaxID=49390 {ECO:0000313|EMBL:CDP01770.1, ECO:0000313|Proteomes:UP000295252};
RN   [1] {ECO:0000313|Proteomes:UP000295252}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DH200-94 {ECO:0000313|Proteomes:UP000295252};
RX   PubMed=25190796; DOI=10.1126/science.1255274;
RA   Denoeud F., Carretero-Paulet L., Dereeper A., Droc G., Guyot R.,
RA   Pietrella M., Zheng C., Alberti A., Anthony F., Aprea G., Aury J.M.,
RA   Bento P., Bernard M., Bocs S., Campa C., Cenci A., Combes M.C.,
RA   Crouzillat D., Da Silva C., Daddiego L., De Bellis F., Dussert S.,
RA   Garsmeur O., Gayraud T., Guignon V., Jahn K., Jamilloux V., Joet T.,
RA   Labadie K., Lan T., Leclercq J., Lepelley M., Leroy T., Li L.T.,
RA   Librado P., Lopez L., Munoz A., Noel B., Pallavicini A., Perrotta G.,
RA   Poncet V., Pot D., Priyono X., Rigoreau M., Rouard M., Rozas J.,
RA   Tranchant-Dubreuil C., VanBuren R., Zhang Q., Andrade A.C., Argout X.,
RA   Bertrand B., de Kochko A., Graziosi G., Henry R.J., Jayarama X., Ming R.,
RA   Nagai C., Rounsley S., Sankoff D., Giuliano G., Albert V.A., Wincker P.,
RA   Lashermes P.;
RT   "The coffee genome provides insight into the convergent evolution of
RT   caffeine biosynthesis.";
RL   Science 345:1181-1184(2014).
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; HG739091; CDP01770.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A068TZS2; -.
DR   STRING; 49390.A0A068TZS2; -.
DR   EnsemblPlants; CDP01770; CDP01770; GSCOC_T00036928001.
DR   Gramene; CDP01770; CDP01770; GSCOC_T00036928001.
DR   InParanoid; A0A068TZS2; -.
DR   OMA; LMNWRKK; -.
DR   PhylomeDB; A0A068TZS2; -.
DR   Proteomes; UP000295252; Chromosome 7.
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:SF82; MLO PROTEIN HOMOLOG 1; 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:UP000295252};
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..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        58..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        139..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        261..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        286..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        345..368
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        388..409
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          440..540
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        476..491
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        514..528
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   540 AA;  61304 MW;  4FFA372A8168F0B6 CRC64;
     MAGGPGDRSL KETPTWAVAA VCAVFVIISV LIEHGIHSLA KWFQKSQKKA LLEALEKIKA
     ELMLLGFISL LITVGQKPIS KICISKGAGD TMLPCKKLLW YAGDALARRF LAAAGGDDTD
     HCSKYKKVPL ISQSGIHQLH IFIFVLAVFH VLYSVLTIVL ARAKVKKWKS WEQETASLNY
     QLTNDPSRFR FVHQTSFIRQ YSGFSTKPGI RWIVTFFRQF FCSVTKTDYL TLRHGFINAH
     FAANSKFDFH KYIKRSMEDD FKVVVGISIP LWTFAILFLA LNVYRWYSLF AISLVPPIML
     VIIGAKLQII IMDMALHIQD RTTVVTGVPI VEPSNKYFWF NRPHFILGLI HFTSFENAFQ
     MAYFLWTWYQ FGLTSCFHEN LPVILAKVFL GVAVQVLGSY ITFPLYALVT QMGSHMKKAI
     FEEQTAKALM KWQKAAKERR KLRKAGGDMS PDLMSGNTTP SRGSSPIHLL HKYKTNSDIE
     NSINNPTPRP YHSDADYSET EGPALNSSDD QNARNHNTPK KEIVGKEPET YNWDFSFSKS
//
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