MLO7_ARATH
ID MLO7_ARATH Reviewed; 542 AA.
AC O22752; Q94KB6;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2003, sequence version 3.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=MLO-like protein 7;
DE Short=AtMlo7;
DE AltName: Full=Protein NORTIA;
GN Name=MLO7; Synonyms=NTA; OrderedLocusNames=At2g17430; ORFNames=F5J6.19;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE OF 137-542.
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 [4]
RP TISSUE SPECIFICITY.
RX PubMed=16525893; DOI=10.1007/s11103-005-5082-x;
RA Chen Z., Hartmann H.A., Wu M.J., Friedman E.J., Chen J.G., Pulley M.,
RA Schulze-Lefert P., Panstruga R., Jones A.M.;
RT "Expression analysis of the AtMLO gene family encoding plant-specific
RT seven-transmembrane domain proteins.";
RL Plant Mol. Biol. 60:583-597(2006).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=21071669; DOI=10.1126/science.1195211;
RA Kessler S.A., Shimosato-Asano H., Keinath N.F., Wuest S.E., Ingram G.,
RA Panstruga R., Grossniklaus U.;
RT "Conserved molecular components for pollen tube reception and fungal
RT invasion.";
RL Science 330:968-971(2010).
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). Controls pollen tube reception in the female
CC gametophyte synergids. {ECO:0000250, ECO:0000269|PubMed:21071669}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21071669};
CC Multi-pass membrane protein {ECO:0000269|PubMed:21071669}. Endomembrane
CC system {ECO:0000269|PubMed:21071669}. Note=In synergids of unfertilized
CC mature female gametophytes, present in a punctate pattern of
CC endomembranes throughout the cytoplasm. Become polarly localized to the
CC basal half of the synergids, to the filiform apparatus, upon pollen
CC tube arrival at the micropyle. This relocalization upon fertilization
CC requires FER.
CC -!- TISSUE SPECIFICITY: Restricted to pollen, synergids, pistils and
CC immature anthers. Also detected in seedlings, leaves, stems and
CC inflorescens. {ECO:0000269|PubMed:16525893,
CC ECO:0000269|PubMed:21071669}.
CC -!- DOMAIN: The C-terminus contains a calmodulin-binding domain, which
CC binds calmodulin in a calcium-dependent fashion. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Impaired pollen tube reception in the female
CC gametophyte synergids; the pollen tube fails to arrest and continues to
CC grow inside the female gametophyte. {ECO:0000269|PubMed:21071669}.
CC -!- SIMILARITY: Belongs to the MLO family. {ECO:0000305}.
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DR EMBL; CP002685; AEC06624.1; -; Genomic_DNA.
DR EMBL; AF369568; AAK53800.1; -; mRNA.
DR PIR; B84552; B84552.
DR RefSeq; NP_179335.3; NM_127298.5.
DR AlphaFoldDB; O22752; -.
DR SMR; O22752; -.
DR BioGRID; 1606; 4.
DR IntAct; O22752; 3.
DR STRING; 3702.AT2G17430.1; -.
DR iPTMnet; O22752; -.
DR PaxDb; O22752; -.
DR PRIDE; O22752; -.
DR ProteomicsDB; 238378; -.
DR EnsemblPlants; AT2G17430.1; AT2G17430.1; AT2G17430.
DR GeneID; 816249; -.
DR Gramene; AT2G17430.1; AT2G17430.1; AT2G17430.
DR KEGG; ath:AT2G17430; -.
DR Araport; AT2G17430; -.
DR TAIR; locus:2827607; AT2G17430.
DR eggNOG; ENOG502QPZ5; Eukaryota.
DR HOGENOM; CLU_024720_1_0_1; -.
DR InParanoid; O22752; -.
DR OMA; LGNWLWK; -.
DR OrthoDB; 603362at2759; -.
DR PhylomeDB; O22752; -.
DR PRO; PR:O22752; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22752; baseline and differential.
DR Genevisible; O22752; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0012505; C:endomembrane system; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0010483; P:pollen tube reception; IMP:TAIR.
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 Calmodulin-binding; Cell membrane; Membrane; Pathogenesis-related protein;
KW Plant defense; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..542
FT /note="MLO-like protein 7"
FT /id="PRO_0000209937"
FT TOPO_DOM 1..38
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..59
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 60..82
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..165
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..288
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..315
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..336
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 337..374
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 396..414
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 436..542
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 449..470
FT /note="Calmodulin-binding"
SQ SEQUENCE 542 AA; 62112 MW; 203AE24F5D8E4C92 CRC64;
MITRSRCRRS LLWFLVFHGG ATATGAPSGG KELSQTPTWA VAVVCTFLIL ISHLLEKGLQ
RLANWLWKKH KNSLLEALEK IKAELMILGF ISLLLTFGEP YILKICVPRK AALSMLPCLS
EDTVLFQKLA PSSLSRHLLA AGDTSINCKQ GSEPLITLKG LHQLHILLFF LAIFHIVYSL
ITMMLSRLKI RGWKKWEQET LSNDYEFSID HSRLRLTHET SFVREHTSFW TTTPFFFYVG
CFFRQFFVSV ERTDYLTLRH GFISAHLAPG RKFNFQRYIK RSLEDDFKLV VGISPVLWAS
FVIFLLFNVN GWRTLFWASI PPLLIILAVG TKLQAIMATM ALEIVETHAV VQGMPLVQGS
DRYFWFDCPQ LLLHLIHFAL FQNAFQITHF FWIWYSFGLK SCFHKDFNLV VSKLFLCLGA
LILCSYITLP LYALVTQMGS HMKKAVFDEQ MAKALKKWHK DIKLKKGKAR KLPSKTLGVS
ESFSLSSSSS ATTLHRSKTT GHSSNIIYYK QEDEEDEMSD LEAGAEDAID RIQQQEMQFH
NS
