MLO8_ARATH
ID MLO8_ARATH Reviewed; 593 AA.
AC O22757; Q94KB5; Q9SHM0;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2003, sequence version 2.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=MLO-like protein 8;
DE Short=AtMlo8;
GN Name=MLO8; OrderedLocusNames=At2g17480; ORFNames=F5J6.21, MJB20.4;
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT phosphorylation site database.";
RL Plant Cell 16:2394-2405(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
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 -!- 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; AF369569; AAK53801.1; -; mRNA.
DR EMBL; AC007584; AAD32905.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC06633.1; -; Genomic_DNA.
DR EMBL; BT002918; AAO22734.1; -; mRNA.
DR EMBL; BT004356; AAO42350.1; -; mRNA.
DR PIR; F84552; F84552.
DR RefSeq; NP_565416.1; NM_127302.3.
DR AlphaFoldDB; O22757; -.
DR STRING; 3702.AT2G17480.1; -.
DR iPTMnet; O22757; -.
DR PaxDb; O22757; -.
DR PRIDE; O22757; -.
DR ProteomicsDB; 238343; -.
DR EnsemblPlants; AT2G17480.1; AT2G17480.1; AT2G17480.
DR GeneID; 816254; -.
DR Gramene; AT2G17480.1; AT2G17480.1; AT2G17480.
DR KEGG; ath:AT2G17480; -.
DR Araport; AT2G17480; -.
DR TAIR; locus:2053888; AT2G17480.
DR eggNOG; ENOG502QPZ5; Eukaryota.
DR HOGENOM; CLU_024720_1_0_1; -.
DR InParanoid; O22757; -.
DR OMA; VLWDRHK; -.
DR OrthoDB; 603362at2759; -.
DR PhylomeDB; O22757; -.
DR PRO; PR:O22757; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22757; baseline and differential.
DR Genevisible; O22757; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
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 1: Evidence at protein level;
KW Calmodulin-binding; Membrane; Pathogenesis-related protein; Plant defense;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..593
FT /note="MLO-like protein 8"
FT /id="PRO_0000209938"
FT TOPO_DOM 1..46
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..67
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..181
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 203..304
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 326
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 348..393
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 394..414
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 415..430
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 431..451
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 452..593
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 465..486
FT /note="Calmodulin-binding"
FT REGION 481..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..577
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 593 AA; 67212 MW; 522E0445655931F6 CRC64;
MGIIDGSLLR RLICLCLWCL LGGGVTVVTA EDEKKVVHKQ LNQTPTWAVA AVCTFFIVVS
VLLEKLLHKV GKVLWDRHKT ALLDALEKIK AELMVLGFIS LLLTFGQTYI LDICIPSHVA
RTMLPCPAPN LKKEDDDNGE SHRRLLSFEH RFLSGGEASP TKCTKEGYVE LISAEALHQL
HILIFFLAIF HVLYSFLTMM LGRLKIRGWK HWENETSSHN YEFSTDTSRF RLTHETSFVR
AHTSFWTRIP FFFYVGCFFR QFFRSVGRTD YLTLRNGFIA VHLAPGSQFN FQKYIKRSLE
DDFKVVVGVS PVLWGSFVLF LLLNIDGFKM MFIGTAIPVI IILAVGTKLQ AIMTRMALGI
TDRHAVVQGM PLVQGNDEYF WFGRPHLILH LMHFALFQNA FQITYFFWIW YSFGSDSCYH
PNFKIALVKV AIALGVLCLC SYITLPLYAL VTQMGSRMKK SVFDEQTSKA LKKWRMAVKK
KKGVKATTKR LGGDGSASPT ASTVRSTSSV RSLQRYKTTP HSMRYEGLDP ETSDLDTDNE
ALTPPKSPPS FELVVKVEPN KTNTGETSRD TETDSKEFSF VKPAPSNESS QDR
