ID A0A6A3CVV9_HIBSY Unreviewed; 502 AA.
AC A0A6A3CVV9;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 24-JAN-2024, entry version 9.
DE RecName: Full=MLO-like protein {ECO:0000256|RuleBase:RU280816};
GN Name=MLO {ECO:0000256|RuleBase:RU280816};
GN ORFNames=F3Y22_tig00002840pilonHSYRG01341
GN {ECO:0000313|EMBL:KAE8731438.1};
OS Hibiscus syriacus (Rose of Sharon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Hibiscus.
OX NCBI_TaxID=106335 {ECO:0000313|EMBL:KAE8731438.1, ECO:0000313|Proteomes:UP000436088};
RN [1] {ECO:0000313|EMBL:KAE8731438.1, ECO:0000313|Proteomes:UP000436088}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Baekdansim {ECO:0000313|Proteomes:UP000436088};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAE8731438.1};
RA Kim Y.-M.;
RT "Draft genome information of white flower Hibiscus syriacus.";
RL Submitted (SEP-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:KAE8731438.1}.
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DR EMBL; VEPZ02000196; KAE8731438.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6A3CVV9; -.
DR Proteomes; UP000436088; 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:SF82; MLO PROTEIN HOMOLOG 1; 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:UP000436088};
KW Transmembrane {ECO:0000256|RuleBase:RU280816, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|RuleBase:RU280816,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 17..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 61..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 141..163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 331..354
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 384..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 502 AA; 56639 MW; 32AE1647373DEB44 CRC64;
MAGNYRKERS LEETPTWAVA VVCAIFVIIS ILIEHGIHSL GKWFQKRQKK AMMEALEKIK
AELMLLGFIS LLLTIGTYSI PAICIPEKIG YSMLPCERKS VYGGDGDKGS SKGMTLVTAA
GGSYFLMGKV ALISQSGMHD LHIFIFALAV FHVLYSVATI FLAKAKMKKW EAWESETKTL
EYQYTNGISS PIDLDFWINT SNFLRETSFW FLRNSRHQWI VAFFRQFFGS VSKVDYLTMR
NGFINAHFAA NTSFDFHKYI KRSMEDDFKV VVGIRMANSQ LAVTSPLDVG TKLEVIIMDM
AEEIQERSAV VRGAPVVEPN NKYFWFNRPQ WILFLIHYTL FQNAFQMAYF LWVWGSPWGV
PSNSMQLHYL PTLCFGDPDG VSHEINIRGA DSQGSKELAQ GCQEEKQEQS KREGSAGMNS
HASPSMSVDS TPSRGTSPLH LLHNHKHRST AACDQTDGVL NSPTHSNYSY PSDTEISDIE
AFSPRPRHAT PPLDHQHQTP TT
//