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Database: UniProt
Entry: A0A5N6Q794_9ASTR
LinkDB: A0A5N6Q794_9ASTR
Original site: A0A5N6Q794_9ASTR 
ID   A0A5N6Q794_9ASTR        Unreviewed;       574 AA.
AC   A0A5N6Q794;
DT   26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2020, sequence version 1.
DT   22-FEB-2023, entry version 8.
DE   RecName: Full=MLO-like protein {ECO:0000256|RuleBase:RU280816};
GN   Name=MLO {ECO:0000256|RuleBase:RU280816};
GN   ORFNames=E3N88_02864 {ECO:0000313|EMBL:KAD7479728.1};
OS   Mikania micrantha.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC   Heliantheae alliance; Eupatorieae; Mikania.
OX   NCBI_TaxID=192012 {ECO:0000313|EMBL:KAD7479728.1, ECO:0000313|Proteomes:UP000326396};
RN   [1] {ECO:0000313|EMBL:KAD7479728.1, ECO:0000313|Proteomes:UP000326396}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NLD-2019 {ECO:0000313|EMBL:KAD7479728.1};
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAD7479728.1};
RA   Liu B.;
RT   "Mikania micrantha, genome provides insights into the molecular mechanism
RT   of rapid growth.";
RL   Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases.
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KAD7479728.1}.
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DR   EMBL; SZYD01000001; KAD7479728.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5N6Q794; -.
DR   Proteomes; UP000326396; Miscellaneous, Linkage group lg1.
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:SF34; 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:UP000326396};
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..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        264..284
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        290..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        348..370
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        390..414
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          448..467
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        452..467
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   574 AA;  65601 MW;  587AC9F0997A3F21 CRC64;
     MGGASEGRSL EQTPTWAVAI VCFVLVAISI VIEQIIHKIE QWLKKKHNRG LYESLEKIKA
     ELMLLGFISL LLTVGTNPIT EICISKRAGS TWHPCSNQKL EQTSNEVAAS ILAGTNIGYN
     KCALKGKVSF MSYDGVHQLH IFIFVLAVSH VFYSVITMAL GRLKMGSWKH WETETKSAEY
     RFSHDSNRFR FTRDTSFGRR HMSFWSKSPI LLWIVCFYRQ FYRSVPKVDY LTLRHGFIMA
     HLTPHSHSGF DFQKYINRSL EEDFKVVVAI SPPIWLFVVA FLLFNTHGLY SYLWLPFIPL
     IIVLLVGTKL QVIITKMGLK IQERGEVVKG VPVVHPHDDL FWFNCPRLLL YFINFVLFQV
     TLFKFLFYFL MIQCQFGLKS CFHEHMEDVI IRITMGVLIQ ILCSYVTLPL YALVTQMGST
     MRPTIFNDRV ASALRKWHHT AKKKIKENKK SGQLTAMPSR PVTPTSSHNL SPVHLLGHYR
     NINIDSLDHT SLTRLNLNVM NWNVDGSPNP TNRMIGYSTC HHEIEIGYLD QGMDQVQEPS
     LSDVASCSDA ASKTEHEVMV GAPKDSCFEN KPGM
//
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