GenomeNet

Database: UniProt
Entry: A0A0S3RYT3_PHAAN
LinkDB: A0A0S3RYT3_PHAAN
Original site: A0A0S3RYT3_PHAAN 
ID   A0A0S3RYT3_PHAAN        Unreviewed;       493 AA.
AC   A0A0S3RYT3;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=MLO-like protein {ECO:0000256|RuleBase:RU280816};
GN   Name=Vigan.04G326900 {ECO:0000313|EMBL:BAT85697.1};
GN   Synonyms=MLO {ECO:0000256|RuleBase:RU280816};
GN   ORFNames=VIGAN_04326900 {ECO:0000313|EMBL:BAT85697.1};
OS   Vigna angularis var. angularis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX   NCBI_TaxID=157739 {ECO:0000313|EMBL:BAT85697.1, ECO:0000313|Proteomes:UP000291084};
RN   [1] {ECO:0000313|EMBL:BAT85697.1, ECO:0000313|Proteomes:UP000291084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX   PubMed=26616024; DOI=10.1038/srep16780;
RA   Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA   Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA   Tomooka N.;
RT   "The power of single molecule real-time sequencing technology in the de
RT   novo assembly of a eukaryotic genome.";
RL   Sci. Rep. 5:16780-16780(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; AP015037; BAT85697.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S3RYT3; -.
DR   Proteomes; UP000291084; Chromosome 4.
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:SF59; 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:UP000291084};
KW   Transmembrane {ECO:0000256|RuleBase:RU280816, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU280816,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        14..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        126..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        250..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        276..298
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        334..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        375..398
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          455..493
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        477..493
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   493 AA;  56711 MW;  F7F7620FCFCF01EB CRC64;
     MATPSYSLQH TPTWAIALVS FILISISIIL EHFIHLIIKW LRKHRKSDLV EAIERLKSEL
     MILGFMSLLL TVTQDAITEI CIPVRTADTM LPCRKRTTND TAILDSCSAK NTSEVALVSK
     HGIHQLHMFI FVLAVMQIVY SILTVSLARA KIRHWKAWDE ETQTMEYEIA NDPNRFRYTR
     QTTFGRRHIS TTTASPVSVW IKCFFRQFFH SVEKVDYLTL RHGFISAHFS ARNSNFDFQK
     YIEQSLEEDF RIIVSISPVM WFTVVIFLLV DVHGWHVYLW LSYIPLLLVL VVGAKLEVIV
     DEMALQMKDV NSVTKGTPLV SPSDEFFWFG HPGFVLTLLH YTLFVNAFEL AFFIWVSTQF
     GINSCYHEHR TFTVIRVVIA VAVQVLCSYV TLPLYALVAQ MGSQVKSKAL AKILRQWHVE
     VRERRRKQQK LVKSFSFSHM SSEWNQGNKS ALEFSSGLRE NTRSSSEGEI VQELEHPMKT
     QANSSSDPPP CVV
//
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