GenomeNet

Database: UniProt
Entry: A0A0E0MA87_ORYPU
LinkDB: A0A0E0MA87_ORYPU
Original site: A0A0E0MA87_ORYPU 
ID   A0A0E0MA87_ORYPU        Unreviewed;       571 AA.
AC   A0A0E0MA87;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=MLO-like protein {ECO:0000256|RuleBase:RU280816};
GN   Name=MLO {ECO:0000256|RuleBase:RU280816};
OS   Oryza punctata (Red rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC10G15530.1};
RN   [1] {ECO:0000313|EnsemblPlants:OPUNC10G15530.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OPUNC10G15530.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
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   AlphaFoldDB; A0A0E0MA87; -.
DR   STRING; 4537.A0A0E0MA87; -.
DR   EnsemblPlants; OPUNC10G15530.1; OPUNC10G15530.1; OPUNC10G15530.
DR   Gramene; OPUNC10G15530.1; OPUNC10G15530.1; OPUNC10G15530.
DR   eggNOG; ENOG502QPZ5; Eukaryota.
DR   HOGENOM; CLU_024720_1_0_1; -.
DR   OMA; EWEKETC; -.
DR   Proteomes; UP000026962; Chromosome 10.
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:SF112; MLO-LIKE PROTEIN; 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:UP000026962};
KW   Transmembrane {ECO:0000256|RuleBase:RU280816, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU280816,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        65..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        146..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        272..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        297..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        353..377
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        392..417
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          104..124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          447..482
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          504..571
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        109..124
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        456..472
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        504..518
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        534..552
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   571 AA;  64258 MW;  5C4F3F1E3615190B CRC64;
     MSGGGGGGGD GARALDQTPT WAVAAVCAVI VAASILLEGL LHHLGQWFSK RRKKALFDAL
     EKVKSELMTL GFISLLLSVT GRYISRICIP VGAADTMLPC SLRRSSSEQE EPGGGHGRRH
     LSGDPTNFKC AKGMVSLVSA DGLHQLHIFV FFLAVFHVAF SAITMSLGRA KTRIWKEWEK
     ETCSLTYEFS YDPSKFRLTH QTSFVRQHAS CWSKSTILLY FVSFFRQFFR SVRRTDYLTL
     RHGFIAAHLS PGTRFNFRKY IKRSLEDDFK TVVGISAPLW ASALAVMLFN VHGWHNLFWF
     STIPLVVTLA VGTKLQAIIA MMAVEIKERH TVIQGMPVVK LSDEHFWFGK PRLVLHLIHF
     ASFQNAFEIT YFFWIWYEFG LRSCFHDNFE LIIARVCLGV IVQFMCSYIT LPLYALVSQM
     GSQMKRTIFD EQTAKALKKW HKAAVVKKKQ QKGSSHEPGS ETPGTETTMT TATEESQRKR
     DTAAVPVRHL HRYKTIAHVG ATGTLSDSDY SDTDTPFASP TRLLIPPTKQ RSLDSGRAEV
     RVDVDVDATP TPERHDSFSF PRLPAHNLQQ K
//
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