MLOH1_ORYSJ
ID MLOH1_ORYSJ Reviewed; 540 AA.
AC Q0DC45; O49914; Q67W42; Q84TU0;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=MLO protein homolog 1;
DE AltName: Full=OsMLO1;
GN Name=MLO1; Synonyms=MLO-H1; OrderedLocusNames=Os06g0486300, LOC_Os06g29110;
GN ORFNames=OJ1568_D07.18, P0008F02.13;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 128-241.
RC STRAIN=cv. LTH;
RX PubMed=12561471;
RA Liu W.D., Wang S.P.;
RT "Analysis and mapping of homologous sequences of barley disease resistance
RT gene Mlo and maize disease resistance gene Hm1 in rice.";
RL Yi Chuan Xue Bao 29:875-879(2002).
CC -!- FUNCTION: May be involved in modulation of pathogen defense and leaf
CC cell death. Activity seems to be regulated by Ca(2+)-dependent
CC calmodulin binding and seems not to require heterotrimeric G proteins
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- DOMAIN: The C-terminus contains a calmodulin-binding domain, which
CC binds calmodulin in a calcium-dependent fashion. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MLO family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO61753.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD37345.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAD37627.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAF19578.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP003518; BAD37345.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP004012; BAD37627.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008212; BAF19578.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014962; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF490386; AAO61753.1; ALT_FRAME; Genomic_DNA.
DR RefSeq; XP_015642002.1; XM_015786516.1.
DR AlphaFoldDB; Q0DC45; -.
DR SMR; Q0DC45; -.
DR STRING; 4530.OS06T0486300-00; -.
DR PaxDb; Q0DC45; -.
DR PRIDE; Q0DC45; -.
DR GeneID; 4341067; -.
DR KEGG; osa:4341067; -.
DR eggNOG; ENOG502QVKX; Eukaryota.
DR HOGENOM; CLU_024720_1_0_1; -.
DR InParanoid; Q0DC45; -.
DR OrthoDB; 541654at2759; -.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR Genevisible; Q0DC45; OS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; PTHR31942; 1.
DR Pfam; PF03094; Mlo; 1.
PE 3: Inferred from homology;
KW Calmodulin-binding; Membrane; Pathogenesis-related protein; Plant defense;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..540
FT /note="MLO protein homolog 1"
FT /id="PRO_0000209930"
FT TOPO_DOM 1..16
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..37
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..60
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..142
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 164..265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..347
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 348..368
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 369..383
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 384..404
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 405..540
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 426..447
FT /note="Calmodulin-binding"
FT REGION 468..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 540 AA; 60728 MW; BA809A89FA45BAF6 CRC64;
MAGGRSGSRE LPETPTWAVA VVCAVLVLVS VAMEHGLHNL SHWFRRRQKK AMGDALDKIK
AELMLLGFIS LLLTVAQAPI SKICIPKSAA NILLPCKAGQ DAIEEEAASD RRSLAGAGGG
DYCSKFDGKV ALMSAKSMHQ LHIFIFVLAV FHVTYCVITM GLGRLKMKKW KKWESQTNSL
EYQFAIDPSR FRFTHQTSFV KRHLGSFSST PGLRWIVAFF RQFFGSVTKV DYLTMRQGFI
NAHLSQNSKF DFHKYIKRSL EDDFKVVVGI SLPLWFVGIL VLFLDIHGLG TLIWISFVPL
IIVLLVGTKL EMVIMQMAQE IQDRATVIQG APVVEPSNKY FWFNRPDWVL FFIHLTLFHN
AFQMAHFVWT MATPGLKKCF HENIWLSIVE VIVGISLQVL CSYITFPLYA LVTQMGSNMK
KTIFEEQTMK ALMNWRKKAM EKKKVRDADA FLAQMSVDFA TPASSRSASP VHLLQDHRAR
SDDPPSPITV ASPPAPEEDI YPVPAAAASR QLLDDPPDRR WMASSSADIA DSDFSFSAQR
