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   24-JAN-2024, entry version 100.
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.C0LGQ4; -.
DR   GlyCosmos; C0LGQ4; 1 site, No reported glycans.
DR   iPTMnet; C0LGQ4; -.
DR   PaxDb; 3702-AT4G18640-1; -.
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; AT4G18640; MRH1.
DR   eggNOG; ENOG502QTJQ; Eukaryota.
DR   HOGENOM; CLU_000288_92_4_1; -.
DR   InParanoid; C0LGQ4; -.
DR   OMA; EQWASKY; -.
DR   OrthoDB; 1221012at2759; -.
DR   PhylomeDB; C0LGQ4; -.
DR   PRO; PR:C0LGQ4; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; C0LGQ4; baseline and differential.
DR   GO; GO:0012505; C:endomembrane system; IDA:TAIR.
DR   GO; GO:0016020; C: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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0048765; P:root hair cell differentiation; IMP:TAIR.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR001611; Leu-rich_rpt.
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   PANTHER; PTHR46084; PROTEIN MALE DISCOVERER 2; 1.
DR   PANTHER; PTHR46084:SF1; PROTEIN MALE DISCOVERER 2; 1.
DR   Pfam; PF00560; LRR_1; 2.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   Genevisible; C0LGQ4; AT.
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
//