MEE39_ARATH
ID MEE39_ARATH Reviewed; 878 AA.
AC C0LGP2; Q0WNU0; Q9SNA4;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Probable LRR receptor-like serine/threonine-protein kinase MEE39;
DE EC=2.7.11.1;
DE AltName: Full=Protein MATERNAL EFFECT EMBRYO ARREST 39;
DE Flags: Precursor;
GN Name=MEE39; OrderedLocusNames=At3g46330; ORFNames=F18L15.50;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15634699; DOI=10.1242/dev.01595;
RA Pagnussat G.C., Yu H.-J., Ngo Q.A., Rajani S., Mayalagu S., Johnson C.S.,
RA Capron A., Xie L.-F., Ye D., Sundaresan V.;
RT "Genetic and molecular identification of genes required for female
RT gametophyte development and function in Arabidopsis.";
RL Development 132:603-614(2005).
CC -!- FUNCTION: Receptor-like serine/threonine-kinase required during the
CC endosperm development in seeds. {ECO:0000269|PubMed:15634699}.
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 -!- 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;
CC -!- INTERACTION:
CC C0LGP2; Q9M8T0: At3g02880; NbExp=2; IntAct=EBI-20663701, EBI-1238677;
CC C0LGP2; Q9C9Y8: At3g08680; NbExp=2; IntAct=EBI-20663701, EBI-16955024;
CC C0LGP2; Q8W4S5: At5g63710; NbExp=2; IntAct=EBI-20663701, EBI-16934827;
CC C0LGP2; Q9LVI6: RLK902; NbExp=2; IntAct=EBI-20663701, EBI-1626936;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Endosperm development arrested.
CC {ECO:0000269|PubMed:15634699}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB62024.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL133298; CAB62024.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE78147.1; -; Genomic_DNA.
DR EMBL; AK228880; BAF00771.1; -; mRNA.
DR EMBL; AK229346; BAF01209.1; -; mRNA.
DR EMBL; FJ708732; ACN59327.1; -; mRNA.
DR PIR; T45690; T45690.
DR RefSeq; NP_190217.2; NM_114500.5.
DR AlphaFoldDB; C0LGP2; -.
DR SMR; C0LGP2; -.
DR BioGRID; 9098; 26.
DR IntAct; C0LGP2; 30.
DR STRING; 3702.AT3G46330.1; -.
DR iPTMnet; C0LGP2; -.
DR PaxDb; C0LGP2; -.
DR PRIDE; C0LGP2; -.
DR ProteomicsDB; 228857; -.
DR EnsemblPlants; AT3G46330.1; AT3G46330.1; AT3G46330.
DR GeneID; 823778; -.
DR Gramene; AT3G46330.1; AT3G46330.1; AT3G46330.
DR KEGG; ath:AT3G46330; -.
DR Araport; AT3G46330; -.
DR TAIR; locus:2078176; AT3G46330.
DR eggNOG; ENOG502QQCZ; Eukaryota.
DR HOGENOM; CLU_000288_41_1_1; -.
DR InParanoid; C0LGP2; -.
DR OMA; DEHDRIW; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; C0LGP2; -.
DR PRO; PR:C0LGP2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; C0LGP2; baseline and differential.
DR Genevisible; C0LGP2; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0009960; P:endosperm development; IMP:UniProtKB.
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; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR024788; Malectin-like_Carb-bd_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF12819; Malectin_like; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Developmental protein; 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..25
FT /evidence="ECO:0000255"
FT CHAIN 26..878
FT /note="Probable LRR receptor-like serine/threonine-protein
FT kinase MEE39"
FT /id="PRO_0000387515"
FT TOPO_DOM 26..514
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 515..535
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 536..878
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 413..436
FT /note="LRR 1"
FT REPEAT 437..458
FT /note="LRR 2"
FT REPEAT 461..483
FT /note="LRR 3"
FT DOMAIN 566..840
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 849..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..869
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 691
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 572..580
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 594
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 557
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 639
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 726
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 727
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 732
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 740
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 404
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 768
FT /note="V -> M (in Ref. 3; BAF01209/BAF00771)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 878 AA; 98678 MW; 7EBD4F8B77F6EEAA CRC64;
MKNLCWVFLS LFWFGVFLII RFAEGQNQEG FISLDCGLPL NEPPYIESET GIQFSSDENF
IQSGKTGRIP KNLESENLKQ YATLRYFPDG IRNCYDLRVE EGRNYLIRAT FFYGNFDGLN
VSPEFDMHIG PNKWTTIDLQ IVPDGTVKEI IHIPRSNSLQ ICLVKTGATI PMISALELRP
LANDTYIAKS GSLKYYFRMY LSNATVLLRY PKDVYDRSWV PYIQPEWNQI STTSNVSNKN
HYDPPQVALK MAATPTNLDA ALTMVWRLEN PDDQIYLYMH FSEIQVLKAN DTREFDIILN
GETINTRGVT PKYLEIMTWL TTNPRQCNGG ICRMQLTKTQ KSTLPPLLNA FEVYSVLQLP
QSQTNEIEVV AIKNIRTTYG LSRISWQGDP CVPKQFLWDG LNCNITDISA PPRIISLNLS
SSGLSGTIVS NFQNLAHLES LDLSNNSLSG IVPEFLATMK SLLVINLSGN KLSGAIPQAL
RDREREGLKL NVLGNKELCL SSTCIDKPKK KVAVKVVAPV ASIAAIVVVI LLFVFKKKMS
SRNKPEPWIK TKKKRFTYSE VMEMTKNLQR PLGEGGFGVV YHGDLNGSEQ VAVKLLSQTS
AQGYKEFKAE VELLLRVHHI NLVNLVGYCD EQDHFALIYE YMSNGDLHQH LSGKHGGSVL
NWGTRLQIAI EAALGLEYLH TGCKPAMVHR DVKSTNILLD EEFKAKIADF GLSRSFQVGG
DQSQVSTVVA GTLGYLDPEY YLTSELSEKS DVYSFGILLL EIITNQRVID QTRENPNIAE
WVTFVIKKGD TSQIVDPKLH GNYDTHSVWR ALEVAMSCAN PSSVKRPNMS QVIINLKECL
ASENTRISRN NQNMDSGHSS DQLNVTVTFD TDVKPKAR
