ID A0A2Z7CVK5_9LAMI Unreviewed; 509 AA.
AC A0A2Z7CVK5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 22-FEB-2023, entry version 11.
DE RecName: Full=MLO-like protein {ECO:0000256|RuleBase:RU280816};
GN Name=MLO {ECO:0000256|RuleBase:RU280816};
GN ORFNames=F511_01904 {ECO:0000313|EMBL:KZV51112.1};
OS Dorcoceras hygrometricum.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Gesneriaceae; Didymocarpoideae; Trichosporeae;
OC Loxocarpinae; Dorcoceras.
OX NCBI_TaxID=472368 {ECO:0000313|EMBL:KZV51112.1, ECO:0000313|Proteomes:UP000250235};
RN [1] {ECO:0000313|EMBL:KZV51112.1, ECO:0000313|Proteomes:UP000250235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. XS01 {ECO:0000313|Proteomes:UP000250235};
RX PubMed=25902549; DOI=10.1073/pnas.1505811112;
RA Xiao L., Yang G., Zhang L., Yang X., Zhao S., Ji Z., Zhou Q., Hu M.,
RA Wang Y., Chen M., Xu Y., Jin H., Xiao X., Hu G., Bao F., Hu Y., Wan P.,
RA Li L., Deng X., Kuang T., Xiang C., Zhu J.K., Oliver M.J., He Y.;
RT "The resurrection genome of Boea hygrometrica: A blueprint for survival of
RT dehydration.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:5833-5837(2015).
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; KQ992022; KZV51112.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z7CVK5; -.
DR OrthoDB; 368831at2759; -.
DR Proteomes; UP000250235; Unassembled WGS sequence.
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:SF72; MLO-LIKE PROTEIN; 1.
DR PANTHER; PTHR31942; MLO-LIKE PROTEIN 1; 1.
DR Pfam; PF03094; Mlo; 2.
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:UP000250235};
KW Transmembrane {ECO:0000256|RuleBase:RU280816, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|RuleBase:RU280816,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 18..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 63..82
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 128..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 335..358
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 378..399
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 509 AA; 58369 MW; 072DF7E826037D91 CRC64;
MAGENSGESA TLETTPTWAV ATVCFVLISA SLLIEHGLHL LAKYLNRKRR NSLLQALNEV
KSDLLLLGFI SLFLTVLAKP IAGICIPEST AETFLPCGSI TIDDEREESK CQQQGKASLL
SRVGVQQLQM LIFFLAFFHV MSSFLTFSLG TAKMKRWERW EAETRTLEFQ FSHDPRRFQF
VHQTSFGKRH LKFWSEPRFL RLLGCFLRQF YGSVNKVDYF TLRHGFIAAH FSERTTFDFQ
KCIKRGLDKD FRVVVGMRLW IWVFSVLFIF LHANVFRSYF WLPFIPLVML LVVGTKLQGI
ITKMCLDTND VSRVVVGSLL VRPSDHFFWF DRPKFLLHLV HFIAFQNSFQ VAFFTWSWYK
FGLRTCFHRK TEDIVIKLAM GVVIPILSGY VTMPLYALVT QMGTSMGNSV FPEEVVGGLK
RWHAKAKRNL ARRNNYDLGR PSLEGSLDAS PSFATLDASM SLDLGHSSDD DSIELQIDIE
EGEIVDVTQL QECRKSESFE GFQSSRLKL
//