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MLO2_ARATH
ID   MLO2_ARATH              Reviewed;         573 AA.
AC   Q9SXB6;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 129.
DE   RecName: Full=MLO-like protein 2;
DE            Short=AtMlo2;
GN   Name=MLO2; OrderedLocusNames=At1g11310; ORFNames=T28P6.4;
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
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].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   INTERACTION WITH CALMODULIN.
RX   PubMed=11919636; DOI=10.1038/416447a;
RA   Kim M.C., Panstruga R., Elliott C., Mueller J., Devoto A., Yoon H.W.,
RA   Park H.C., Cho M.J., Schulze-Lefert P.;
RT   "Calmodulin interacts with MLO protein to regulate defence against mildew
RT   in barley.";
RL   Nature 416:447-451(2002).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512, AND IDENTIFICATION BY
RP   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   -!- 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=Q9SXB6-1; Sequence=Displayed;
CC   -!- DOMAIN: The C-terminus contains a calmodulin-binding domain, which
CC       binds calmodulin in a calcium-dependent fashion.
CC   -!- SIMILARITY: Belongs to the MLO family. {ECO:0000305}.
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DR   EMBL; AF369563; AAK53795.1; -; mRNA.
DR   EMBL; AC007259; AAD49991.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE28715.1; -; Genomic_DNA.
DR   EMBL; AY086586; AAM63648.1; -; mRNA.
DR   PIR; B86247; B86247.
DR   RefSeq; NP_172598.1; NM_101004.4. [Q9SXB6-1]
DR   AlphaFoldDB; Q9SXB6; -.
DR   SMR; Q9SXB6; -.
DR   BioGRID; 22913; 13.
DR   IntAct; Q9SXB6; 2.
DR   STRING; 3702.AT1G11310.1; -.
DR   iPTMnet; Q9SXB6; -.
DR   PaxDb; Q9SXB6; -.
DR   PRIDE; Q9SXB6; -.
DR   ProteomicsDB; 251413; -. [Q9SXB6-1]
DR   EnsemblPlants; AT1G11310.1; AT1G11310.1; AT1G11310. [Q9SXB6-1]
DR   GeneID; 837673; -.
DR   Gramene; AT1G11310.1; AT1G11310.1; AT1G11310. [Q9SXB6-1]
DR   KEGG; ath:AT1G11310; -.
DR   Araport; AT1G11310; -.
DR   TAIR; locus:2202064; AT1G11310.
DR   eggNOG; ENOG502QVKX; Eukaryota.
DR   InParanoid; Q9SXB6; -.
DR   PhylomeDB; Q9SXB6; -.
DR   PRO; PR:Q9SXB6; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9SXB6; baseline and differential.
DR   Genevisible; Q9SXB6; AT.
DR   GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; ISS:TAIR.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR   GO; GO:0031348; P:negative regulation of defense response; IMP:TAIR.
DR   GO; GO:0009620; P:response to fungus; IMP:TAIR.
DR   InterPro; IPR004326; Mlo.
DR   PANTHER; PTHR31942; PTHR31942; 1.
DR   Pfam; PF03094; Mlo; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calmodulin-binding; Membrane;
KW   Pathogenesis-related protein; Phosphoprotein; Plant defense;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..573
FT                   /note="MLO-like protein 2"
FT                   /id="PRO_0000209932"
FT   TOPO_DOM        1..15
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        16..36
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        37..61
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        62..82
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        83..164
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        165..185
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        186..287
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        288..308
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        309..317
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        318..338
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        339..371
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        372..392
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        393..415
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        416..436
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        437..573
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          450..471
FT                   /note="Calmodulin-binding"
FT   REGION          462..573
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        472..513
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        516..543
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         512
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19376835"
SQ   SEQUENCE   573 AA;  65544 MW;  36FA911F8B1D94A6 CRC64;
     MADQVKERTL EETSTWAVAV VCFVLLFISI VLEHSIHKIG TWFKKKHKQA LFEALEKVKA
     ELMLLGFISL LLTIGQTPIS NICISQKVAS TMHPCSAAEE AKKYGKKDAG KKDDGDGDKP
     GRRLLLELAE SYIHRRSLAT KGYDKCAEKG KVAFVSAYGI HQLHIFIFVL AVVHVVYCIV
     TYAFGKIKMR TWKSWEEETK TIEYQYSNDP ERFRFARDTS FGRRHLNFWS KTRVTLWIVC
     FFRQFFGSVT KVDYLALRHG FIMAHFAPGN ESRFDFRKYI QRSLEKDFKT VVEISPVIWF
     VAVLFLLTNS YGLRSYLWLP FIPLVVILIV GTKLEVIITK LGLRIQEKGD VVRGAPVVQP
     GDDLFWFGKP RFILFLIHLV LFTNAFQLAF FAWSTYEFNL NNCFHESTAD VVIRLVVGAV
     VQILCSYVTL PLYALVTQMG SKMKPTVFND RVATALKKWH HTAKNETKHG RHSGSNTPFS
     SRPTTPTHGS SPIHLLHNFN NRSVENYPSS PSPRYSGHGH HEHQFWDPES QHQEAETSTH
     HSLAHESSEP VLASVELPPI RTSKSLRDFS FKK
 
 
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