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Database: UniProt
Entry: A0A6A3CIT3_HIBSY
LinkDB: A0A6A3CIT3_HIBSY
Original site: A0A6A3CIT3_HIBSY 
ID   A0A6A3CIT3_HIBSY        Unreviewed;       513 AA.
AC   A0A6A3CIT3;
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_tig00004004pilonHSYRG00072
GN   {ECO:0000313|EMBL:KAE8729063.1};
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:KAE8729063.1, ECO:0000313|Proteomes:UP000436088};
RN   [1] {ECO:0000313|EMBL:KAE8729063.1, 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:KAE8729063.1};
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:KAE8729063.1}.
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DR   EMBL; VEPZ02000240; KAE8729063.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A6A3CIT3; -.
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; MLO-LIKE PROTEIN 1; 1.
DR   PANTHER; PTHR31942:SF53; MLO-LIKE PROTEIN 5-RELATED; 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: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..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        58..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        167..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        290..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        315..333
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        378..398
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        410..438
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          98..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          469..513
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..126
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        469..507
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   513 AA;  58611 MW;  02F4107BD1F56FD5 CRC64;
     MSGGGVSGRE LDQTPTWAVA VVVALIILIS IALEKILHTV FEHKKKEALL EALEKVKGEL
     MVLGFISLLL TFGQSYISKI CIPEEVADTM LFCPKRHAES AHGQGGHGDH KEEGHGDHHE
     EGARGEEHHR RLLFYDDARR FLSGHDNTAA CDKGYVPLIS VHALHQLHIF IFFLAVFHVA
     YSATTMMLGR LKTRGWKEWE RECINSLNEL NDPSRFRLTH ETSFVRDHTR GAWTKTKFSF
     YFVCMWRQFF RSVTKADYST MRHGFVSVHL TPGSKFDFQK YIKKSLEDDF KVVVGITPAL
     WGLAVLFLLF DVHGWHIMTF MSMLPLVLTL AVGTKLQAII ARMALEIVEK HAVIQGMPLV
     QVSDKHFWFA YPPLCLHLIH YVLFQNAFEI TYFFWIWYEF GLKSCFHEDF TLITIRVCLG
     VVVQFICSYI TLPLYALVTQ MGSTMKRSIF DEQTSKALKQ WHKKAAQKTD LGHGHENGHG
     HDHRHGHDHG KKESSHHEEK GEEHGAEGAT PAH
//
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