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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//