ID A0A2P6PCY1_ROSCH Unreviewed; 562 AA.
AC A0A2P6PCY1;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=MLO-like protein {ECO:0000256|RuleBase:RU280816};
GN Name=MLO {ECO:0000256|RuleBase:RU280816};
GN ORFNames=RchiOBHm_Chr7g0221021 {ECO:0000313|EMBL:PRQ19781.1};
OS Rosa chinensis (China rose).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Rosoideae; Rosoideae incertae sedis;
OC Rosa.
OX NCBI_TaxID=74649 {ECO:0000313|EMBL:PRQ19781.1, ECO:0000313|Proteomes:UP000238479};
RN [1] {ECO:0000313|EMBL:PRQ19781.1, ECO:0000313|Proteomes:UP000238479}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Old Blush {ECO:0000313|Proteomes:UP000238479};
RA Bendahmane M.;
RT "The Rosa genome provides new insights in the design of modern roses.";
RL Nat. Genet. 0:0-0(2018).
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:PRQ19781.1}.
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DR EMBL; PDCK01000045; PRQ19781.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P6PCY1; -.
DR EnsemblPlants; PRQ19781; PRQ19781; RchiOBHm_Chr7g0221021.
DR Gramene; PRQ19781; PRQ19781; RchiOBHm_Chr7g0221021.
DR OMA; GVIVQFW; -.
DR OrthoDB; 368831at2759; -.
DR Proteomes; UP000238479; Chromosome 7.
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:SF9; MLO-LIKE PROTEIN 4; 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:UP000238479};
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..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 274..295
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 301..318
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 357..381
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 562 AA; 64173 MW; D461748C26CC4950 CRC64;
MEEVIQQQRS LAETPTYSVA SVVTVMVFVC LLVQRSIYRF GKWLKKTRRK ALFVSLEKIK
EELMLLGLIS LLLAQSARWI SEICVNSSLF TSKFYICSEK DYSNTNEKVK LESSFSSPNA
TDIPAGLINL SSHQCGEGHE PFVSYEGLEQ LHRFLFVLGI THVLYSCVAV GLAMSKIYSW
RKWENQAGLL ADANLQAKKN KVMRRQSTFV FQHTSHPWSR HRILIWMLCF LRQFKSSIQR
SDYLALRLGF ITKHRLPHSY NFHKYMVRSM EDEFQGILGI SWPLWGYAIV CIFVNVHGLN
IYFWLSFIPA ILVMLVGTKL QHVVSSLALE IVEQTGPAVG TEVKPRDDLF WFGKPVILLR
LIQFIIFQNA FEMATFLWSL WGLKERSCFM KNHVLIVIRL ASGVLVQFWC SHSTVPLNVI
VTQMGSRCKK ALVAESVRES LHSWCKRVKE RSKHSHAARS VCSLDTTIDE RDEITVASGT
LSRSSSLDSQ HQVTVAPMEQ PHAVLETTDL PQHEYSFQVA EYLADSVSIS ASQRPTTSEE
DDDSINGVEE KVDTLLELFQ KT
//