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Database: UniProt
Entry: A0A2C9VGM9_MANES
LinkDB: A0A2C9VGM9_MANES
Original site: A0A2C9VGM9_MANES 
ID   A0A2C9VGM9_MANES        Unreviewed;       518 AA.
AC   A0A2C9VGM9;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=MLO-like protein {ECO:0000256|RuleBase:RU280816};
GN   Name=MLO {ECO:0000256|RuleBase:RU280816};
GN   ORFNames=MANES_08G155900 {ECO:0000313|EMBL:OAY44505.1};
OS   Manihot esculenta (Cassava) (Jatropha manihot).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC   Manihot.
OX   NCBI_TaxID=3983 {ECO:0000313|EMBL:OAY44505.1, ECO:0000313|Proteomes:UP000091857};
RN   [1] {ECO:0000313|EMBL:OAY44505.1, ECO:0000313|Proteomes:UP000091857}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. AM560-2 {ECO:0000313|Proteomes:UP000091857};
RC   TISSUE=Leaf {ECO:0000313|EMBL:OAY44505.1};
RA   Bredeson J.V., Prochnik S.E., Lyons J.B., Schmutz J., Grimwood J.,
RA   Vrebalov J., Bart R.S., Amuge T., Ferguson M.E., Green R., Putnam N.,
RA   Stites J., Rounsley S., Rokhsar D.S.;
RT   "WGS assembly of Manihot esculenta.";
RL   Submitted (FEB-2016) 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}.
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DR   EMBL; CM004394; OAY44505.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C9VGM9; -.
DR   STRING; 3983.A0A2C9VGM9; -.
DR   EnsemblPlants; OAY44505; OAY44505; MANES_08G155900.
DR   Gramene; OAY44505; OAY44505; MANES_08G155900.
DR   OMA; APNHESH; -.
DR   OrthoDB; 368831at2759; -.
DR   Proteomes; UP000091857; Chromosome lg8.
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:SF52; 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:UP000091857};
KW   Transmembrane {ECO:0000256|RuleBase:RU280816, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU280816,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        18..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        64..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        162..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        287..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        371..394
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        414..435
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          476..518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        504..518
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   518 AA;  58333 MW;  45D5847B1D4AB24E CRC64;
     MSGGGSEEGD SLEFTPTWVV AAVCTVIVAI SLAAERFLHY GGKYLKMKNQ KPLFEALQKV
     KEELMLLGFI SLLLTVSQGT ISKICVPEHV ITNMLPCDLS EKRKGGEESN TTATTEHFQR
     FFTTGISGTA RRLLAESTES QIGYCAKKGK VPLLSIEALH HLHIFIFVLA IVHVTFSVLT
     IVFGGARIRQ WQHWENSIAK DRYDTDELLK KKVTHVHQHT FIQEHFLGIG KESALLGWVH
     SFFKQFYACV TKSDYVTLRL GFITTHCRGN PKFNFHRYMV RALEDDFKTV VGISWYLWIF
     VVVFLLLNVN GWHTYFWIAF IPFILLLAVG TKLEHVITQL ARDVAEKHVA IEGDLVVKPS
     DEHFWFNRPD IVLFLIHFIL FQNAFEIAFF FWIWVQYGFD SCIMGQVRYI VPRLIIGVII
     QVLCSYSTLP LYAIVTQMGS SYKKAIFEEH VQAGLVGWAE KVKRKKGLKA AAAAAAAKEG
     PNQSSSHDSS LGIQLGRIGR NGSAPQEIQP SAGSEGQT
//
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