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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//