MLO15_ARATH
ID MLO15_ARATH Reviewed; 496 AA.
AC O80580;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=MLO-like protein 15;
DE Short=AtMlo15;
GN Name=MLO15; OrderedLocusNames=At2g44110; ORFNames=F6E13.24;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12569425; DOI=10.1007/s00239-002-2382-5;
RA Devoto A., Hartmann H.A., Piffanelli P., Elliott C., Simmons C.,
RA Taramino G., Goh C.-S., Cohen F.E., Emerson B.C., Schulze-Lefert P.,
RA Panstruga R.;
RT "Molecular phylogeny and evolution of the plant-specific seven-
RT transmembrane MLO family.";
RL J. Mol. Evol. 56:77-88(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
CC -!- FUNCTION: May be involved in modulation of pathogen defense and leaf
CC cell death. Activity seems to be regulated by Ca(2+)-dependent
CC calmodulin binding and seems not to require heterotrimeric G proteins
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O80580-1; Sequence=Displayed;
CC -!- DOMAIN: The C-terminus contains a calmodulin-binding domain, which
CC binds calmodulin in a calcium-dependent fashion. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MLO family. {ECO:0000305}.
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DR EMBL; AF369576; AAK53808.1; -; mRNA.
DR EMBL; AC004005; AAC23431.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10376.1; -; Genomic_DNA.
DR PIR; T00691; T00691.
DR RefSeq; NP_181939.1; NM_129974.1. [O80580-1]
DR AlphaFoldDB; O80580; -.
DR SMR; O80580; -.
DR BioGRID; 4353; 7.
DR IntAct; O80580; 7.
DR STRING; 3702.AT2G44110.2; -.
DR PaxDb; O80580; -.
DR PRIDE; O80580; -.
DR EnsemblPlants; AT2G44110.1; AT2G44110.1; AT2G44110. [O80580-1]
DR GeneID; 819017; -.
DR Gramene; AT2G44110.1; AT2G44110.1; AT2G44110. [O80580-1]
DR KEGG; ath:AT2G44110; -.
DR Araport; AT2G44110; -.
DR eggNOG; KOG0017; Eukaryota.
DR HOGENOM; CLU_024720_3_0_1; -.
DR InParanoid; O80580; -.
DR PhylomeDB; O80580; -.
DR PRO; PR:O80580; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80580; baseline and differential.
DR Genevisible; O80580; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; PTHR31942; 1.
DR Pfam; PF03094; Mlo; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calmodulin-binding; Membrane;
KW Pathogenesis-related protein; Plant defense; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..496
FT /note="MLO-like protein 15"
FT /id="PRO_0000209945"
FT TOPO_DOM 1..9
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..30
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..59
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..147
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..269
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..290
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313..355
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 377..397
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..418
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 419..496
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 432..453
FT /note="Calmodulin-binding"
FT REGION 454..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 496 AA; 56151 MW; 1B5FBE2DD33DFC3C CRC64;
MAGGGTTLEY TPTWVVALVC SVIVSISFAV ERLIHRAGKH FKNNDQKQLF GALQKIKEEL
MLVGFISLLL SVGQSKIAKI CISKELSEKF LPCTKPAGAE KSLKDSSHFQ FSFTGRHLLA
GDAPAGDYCS LKGKVPIMSL SALHELHIFI FVLAVAHIIF CLLTIVFGTM KIKQWKKWED
KVLEKDFDTD QSIKKFTHVQ EHEFIRSRFL GVGKADASLG WVQSFMKQFL ASVNESDYIT
MRLGFVTTHC KTNPKFNFHK YLMRALNSDF KKVVGISWYL WVFVVLFLLL NIVAWHVYFW
LAFIPLILLL AVGTKLEHII TDLAHEVAEK HIAVEGDLVV RPSDDLFWFQ SPRLVLFLIH
FILFQNSFEI AYFFFILFQF GWDSCIMDHV KFVIPRLVIG VIIQLLCSYS TLPLYALVTQ
MGSSFKGAIF NEQTQEHLVG WAKMAKRGVK KGATQVGTSH DATSPRPSIQ LNSLLGKGSS
QQNQNPKEKS EIAHHD
