MDIS1_ARATH
ID MDIS1_ARATH Reviewed; 695 AA.
AC C0LGU7; F4KEN6; Q9FJ52;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Protein MALE DISCOVERER 1 {ECO:0000303|PubMed:26863186};
DE Short=AtMDIS1 {ECO:0000303|PubMed:26863186};
DE AltName: Full=Probable LRR receptor-like serine/threonine-protein kinase At5g45840 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE Flags: Precursor;
GN Name=MDIS1 {ECO:0000303|PubMed:26863186}; OrderedLocusNames=At5g45840;
GN ORFNames=K15I22.4;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
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, DISRUPTION PHENOTYPE, INTERACTION WITH MIK1; MIK2 AND LURE1.2,
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-652, AND
RP SUBUNIT.
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 {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 -!- SUBUNIT: Homodimer. Interacts with MIK1, MIK2 and LURE1.2. LURE1.2
CC enhances the heterodimerization of MDIS1 with MIK1 or MIK2.
CC {ECO:0000269|PubMed:26863186}.
CC -!- INTERACTION:
CC C0LGU7; Q4VP08: LURE1.2; NbExp=5; IntAct=EBI-16196163, EBI-16196186;
CC C0LGU7; Q9M0G7: MIK1; NbExp=7; IntAct=EBI-16196163, EBI-16196224;
CC C0LGU7; Q8VZG8: MIK2; NbExp=5; IntAct=EBI-16196163, EBI-2270407;
CC C0LGU7; Q93ZS4: NIK3; NbExp=2; IntAct=EBI-16196163, EBI-17121474;
CC C0LGU7; Q9FZ59: PEPR2; NbExp=2; IntAct=EBI-16196163, EBI-20652612;
CC C0LGU7; P43298: TMK1; NbExp=2; IntAct=EBI-16196163, EBI-2023970;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26863186};
CC Single-pass type I membrane protein {ECO:0000305}. Endomembrane system
CC {ECO:0000269|PubMed:26863186}. Note=LURE1.2 binding triggers
CC endocytosis in the pollen tube tip. {ECO:0000269|PubMed:26863186}.
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=C0LGU7-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in pollen tubes and seedlings.
CC {ECO:0000269|PubMed:26863186}.
CC -!- PTM: Phosphorylated by MIK1. {ECO:0000269|PubMed:26863186}.
CC -!- DISRUPTION PHENOTYPE: Decreased micropylar guidance and fertilization
CC efficiency. {ECO:0000269|PubMed:26863186}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09312.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB016870; BAB09312.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; FJ708791; ACN59382.1; -; mRNA.
DR AlphaFoldDB; C0LGU7; -.
DR SMR; C0LGU7; -.
DR BioGRID; 19873; 25.
DR DIP; DIP-61968N; -.
DR IntAct; C0LGU7; 31.
DR STRING; 3702.AT5G45840.2; -.
DR iPTMnet; C0LGU7; -.
DR PaxDb; C0LGU7; -.
DR PRIDE; C0LGU7; -.
DR ProteomicsDB; 228868; -. [C0LGU7-1]
DR Araport; AT5G45840; -.
DR eggNOG; ENOG502QTJQ; Eukaryota.
DR InParanoid; C0LGU7; -.
DR OrthoDB; 464381at2759; -.
DR PhylomeDB; C0LGU7; -.
DR PRO; PR:C0LGU7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; C0LGU7; baseline and differential.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 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 Alternative splicing; ATP-binding; Cell membrane; Glycoprotein; Kinase;
KW Leucine-rich repeat; Membrane; Nucleotide-binding; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Serine/threonine-protein kinase;
KW Signal; Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..695
FT /note="Protein MALE DISCOVERER 1"
FT /id="PRO_0000387564"
FT TOPO_DOM 30..340
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 362..695
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 75..98
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 99..121
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 123..144
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 147..168
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT DOMAIN 363..668
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 302..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..318
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 652
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26863186"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 695 AA; 78476 MW; 9E3D930A2D2CD049 CRC64;
MGCRWNPIGF QFSCFMFLII TLQSRSSLSL ESEGFVLLKF RARVDSDPHG TLANWNVSDH
DHFCSWFGVT CVDNKVQMLN LSGCSLGGTL APELSQLSEL RSLILSKNKL SGDIPNEFAS
FAKLEFLDLR DNNLNGVVPP ELNKVLTPEN LLLSGNKFAG FMTVKFLRLQ SLYKVQMNKN
RELSSVSADV LDCVNRKLGY CVSRRSLITR NKAKAFVLRI RATSRHYMVR RESHGKNYVV
NYHPSENETS IFKRRELLEE TSNLAAMPAP DTPSPSPEII TIVFPRSSGS FPALTNAKKR
IPPLIPPSSP PPLPTNNTIA SDPPRKFEEK SKGFKDVWLY VVIGVAAFVA MLIIVAVIFF
FRKRAVKSIG PWKTGLSGQL QKAFVTGVPK LNRSELETAC EDFSNIIEAF DGYTVYKGTL
SSGVEIAVAS TAILETREWT RAMEMTYRRR IDTMSRVNHK NFINLIGYCE EDEPFNRMMV
FEYAPNGTLF EHLHDKEMEH LDWNARTRII MGTAYCLQYM HELNPPISHT KLVSSAIYLT
DDYAAKVGEV PFSGQTGSKP RKPMSGDLDQ SLLPLPPEPE TNVYSFGVLM LEIISGKLSD
SEEEGSILKW ASKYLENDNL RDMIDPTLTT YKEEELEAIC DVARHCLKLD ESQRPKMKYV
VQQLKEVINI SQEQATPRLS PLWWAELEIL SSEAT
