MDIS2_ARATH
ID MDIS2_ARATH Reviewed; 678 AA.
AC C0LGQ4; Q9M0L9; Q9SN49;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Protein MALE DISCOVERER 2;
DE Short=AtMDIS2;
DE AltName: Full=Probable LRR receptor-like serine/threonine-protein kinase MRH1 {ECO:0000303|PubMed:16367956};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=Protein MORPHOGENESIS OF ROOT HAIR 1 {ECO:0000303|PubMed:16367956};
DE Flags: Precursor;
GN Name=MDIS2; Synonyms=MRH1 {ECO:0000303|PubMed:16367956};
GN OrderedLocusNames=At4g18640; ORFNames=F28A21.50;
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=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 [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 [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=20064227; DOI=10.1186/1471-2164-11-19;
RA Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.;
RT "Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-
RT like protein kinase genes in Arabidopsis thaliana.";
RL BMC Genomics 11:19-19(2010).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16367956; DOI=10.1111/j.1365-313x.2005.02609.x;
RA Jones M.A., Raymond M.J., Smirnoff N.;
RT "Analysis of the root-hair morphogenesis transcriptome reveals the
RT molecular identity of six genes with roles in root-hair development in
RT Arabidopsis.";
RL Plant J. 45:83-100(2006).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=26863186; DOI=10.1038/nature16975;
RA Wang T., Liang L., Xue Y., Jia P.F., Chen W., Zhang M.X., Wang Y.C.,
RA Li H.J., Yang W.C.;
RT "A receptor heteromer mediates the male perception of female attractants in
RT plants.";
RL Nature 531:241-244(2016).
CC -!- FUNCTION: Involved in the pollen tube perception of the female signal
CC by binding an unidentified female attractant (PubMed:26863186). May be
CC involved in the regulation of root hairs development (PubMed:16367956).
CC {ECO:0000269|PubMed:16367956, ECO:0000269|PubMed:26863186}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000305};
CC -!- INTERACTION:
CC C0LGQ4; Q9FL63: At5g24100; NbExp=2; IntAct=EBI-20665429, EBI-20657062;
CC -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000269|PubMed:26863186}; Single-pass type I membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in pollen tubes and seedlings.
CC {ECO:0000269|PubMed:26863186}.
CC -!- DISRUPTION PHENOTYPE: Short straight root hairs.
CC {ECO:0000269|PubMed:16367956}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB37449.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78866.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL035526; CAB37449.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161549; CAB78866.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84071.1; -; Genomic_DNA.
DR EMBL; FJ708745; ACN59339.1; -; mRNA.
DR PIR; T04856; T04856.
DR RefSeq; NP_193599.3; NM_117980.5.
DR AlphaFoldDB; C0LGQ4; -.
DR SMR; C0LGQ4; -.
DR BioGRID; 12891; 19.
DR IntAct; C0LGQ4; 20.
DR STRING; 3702.AT4G18640.1; -.
DR iPTMnet; C0LGQ4; -.
DR PaxDb; C0LGQ4; -.
DR PRIDE; C0LGQ4; -.
DR ProteomicsDB; 228869; -.
DR EnsemblPlants; AT4G18640.1; AT4G18640.1; AT4G18640.
DR GeneID; 827598; -.
DR Gramene; AT4G18640.1; AT4G18640.1; AT4G18640.
DR KEGG; ath:AT4G18640; -.
DR Araport; AT4G18640; -.
DR TAIR; locus:2124102; AT4G18640.
DR eggNOG; ENOG502QTJQ; Eukaryota.
DR HOGENOM; CLU_000288_92_4_1; -.
DR InParanoid; C0LGQ4; -.
DR OMA; RSENGFE; -.
DR OrthoDB; 464381at2759; -.
DR PhylomeDB; C0LGQ4; -.
DR PRO; PR:C0LGQ4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; C0LGQ4; baseline and differential.
DR Genevisible; C0LGQ4; AT.
DR GO; GO:0012505; C:endomembrane system; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0090406; C:pollen tube; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0048765; P:root hair cell differentiation; IMP:TAIR.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Glycoprotein; Kinase; Leucine-rich repeat; Membrane;
KW Nucleotide-binding; Receptor; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..678
FT /note="Protein MALE DISCOVERER 2"
FT /id="PRO_0000387516"
FT TOPO_DOM 26..323
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 345..678
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 71..94
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 95..117
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 119..141
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 143..164
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT DOMAIN 346..651
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 247..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 678 AA; 75820 MW; 4D792304B01F4C13 CRC64;
MMGCGFHFPW FFFLIIGLQA PLSLSLTSQG SALLKFRARV NSDPHGTLAN WNVSGINDLC
YWSGVTCVDG KVQILDLSGY SLEGTLAPEL SQLSDLRSLI LSRNHFSGGI PKEYGSFENL
EVLDLRENDL SGQIPPELSN GLSLKHLLLS GNKFSDDMRI KIVRLQSSYE VRLKKSPKLS
PLAVLGCINR KLGHCVSRNR IIQVKKVEAI VFRIKATSRR FLKAFPSFLE ETDIYKRREL
LEETSNLAAE PAPSAPSPSP GIITEASPRS SGSFPAVTNA KKRRPPLVPP VPSPDKGSTS
PDISKNQPQD NKQSKGSKHV WLYVVIAVAS FVGLLIIVAV IFFCRKRAVK SIGPWKTGLS
GQLQKAFVTG VPKLNRSELE TACEDFSNII ETFDGYTVYK GTLSSGVEIA VASTAIAESK
EWTRAMEMAY RRKIDTLSRI NHKNFVNLIG YCEEDDPFNR MMVFEYAPNG TLFEHLHDKE
TEHLDWSARM RIIMGTAYCL QHMHGMNPPM AHTDFNSSEI YLTDDYAAKV SEIPFNLEAR
LNPKKHVSGD LEQTSLLLPP EPEANVHSFG VLMLEIISGK LSFSDEYGSI EQWASKYLEK
DDLGEMIDPS LKTFKEEELE VICDVIRECL KTEQRQRPSM KDVAEQLKQV INITPEKATP
RSSPLWWAEL EILSSEAT
