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MLO13_ARATH
ID   MLO13_ARATH             Reviewed;         478 AA.
AC   Q94KB2; Q9STW9;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 110.
DE   RecName: Full=MLO-like protein 13;
DE            Short=AtMlo13;
DE            Short=AtMlo20;
GN   Name=MLO13; OrderedLocusNames=At4g24250; ORFNames=T22A6.80;
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(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   -!- 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB45060.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB79335.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF369574; AAK53806.1; -; mRNA.
DR   EMBL; AL078637; CAB45060.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161561; CAB79335.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE84878.1; -; Genomic_DNA.
DR   PIR; T09888; T09888.
DR   RefSeq; NP_567697.1; NM_118558.4.
DR   AlphaFoldDB; Q94KB2; -.
DR   SMR; Q94KB2; -.
DR   BioGRID; 13815; 3.
DR   STRING; 3702.AT4G24250.1; -.
DR   iPTMnet; Q94KB2; -.
DR   PaxDb; Q94KB2; -.
DR   PRIDE; Q94KB2; -.
DR   ProteomicsDB; 238358; -.
DR   EnsemblPlants; AT4G24250.1; AT4G24250.1; AT4G24250.
DR   GeneID; 828526; -.
DR   Gramene; AT4G24250.1; AT4G24250.1; AT4G24250.
DR   KEGG; ath:AT4G24250; -.
DR   Araport; AT4G24250; -.
DR   TAIR; locus:2135982; AT4G24250.
DR   eggNOG; ENOG502QSME; Eukaryota.
DR   HOGENOM; CLU_024720_3_0_1; -.
DR   InParanoid; Q94KB2; -.
DR   OrthoDB; 493070at2759; -.
DR   PhylomeDB; Q94KB2; -.
DR   PRO; PR:Q94KB2; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q94KB2; baseline and differential.
DR   Genevisible; Q94KB2; 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   Calmodulin-binding; Membrane; Pathogenesis-related protein; Plant defense;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..478
FT                   /note="MLO-like protein 13"
FT                   /id="PRO_0000209943"
FT   TOPO_DOM        1..10
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        11..31
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        32..60
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        61..81
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        82..145
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        146..166
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        167..276
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        277..297
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        298..318
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        319..360
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        361..381
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        382..400
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        401..421
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        422..478
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          435..456
FT                   /note="Calmodulin-binding"
FT   REGION          449..478
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..478
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   478 AA;  55068 MW;  82116BCE9D442CE7 CRC64;
     MAEARSGSLE YTPTWVVAFI CFIIVLLSLL AERGLHHLGK CLKRRQQDAL FEALQKLKEE
     LMLLGFISLM LTVSQAAIRH ICVPPALVNN MFPCKKPLEE HHAPKSSHSI INNARHLLST
     GESPDHCAAK GQVPLVSVEA LHQLHIFIFV LAVFHVIFCA STMVLGGARI QQWKHWEDWF
     KKRPSQKGTT RRGHHAHAHE LFSANHEFFE MHAGGFWRRS VVISWVRSFF KQFYGSVTKS
     EYIALRQAFI MSHCRTNPSF DFHKYMLRTL EIDFKKVVSI SWYLWLFVVV FLLLNVGGWN
     TYFWLSFLPL ILLLMVGAKL EYIISSLALD VSEKRSRAEE AVITPSDELF WFHRPGIVLQ
     LIHFILFQNS FEIAFFFWIL FTYGIHSCIM EKLGYLIPRL VMGVLVQVLC SYSTLPLYAL
     VTQMGSKFKK GIFDNVVQST LEGWLEDTRN RGESTSEAHR IEMQPTTPES YNVQSENP
 
 
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