IKU2_ARATH
ID IKU2_ARATH Reviewed; 991 AA.
AC Q9LJM4;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Receptor-like protein kinase HAIKU2;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN Name=IKU2; OrderedLocusNames=At3g19700; ORFNames=MMB12.19;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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 FUNCTION.
RX PubMed=12692325; DOI=10.1104/pp.102.018762;
RA Garcia D., Saingery V., Chambrier P., Mayer U., Juergens G., Berger F.;
RT "Arabidopsis haiku mutants reveal new controls of seed size by endosperm.";
RL Plant Physiol. 131:1661-1670(2003).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF ARG-953.
RX PubMed=16293693; DOI=10.1073/pnas.0508418102;
RA Luo M., Dennis E.S., Berger F., Peacock W.J., Chaudhury A.;
RT "MINISEED3 (MINI3), a WRKY family gene, and HAIKU2 (IKU2), a leucine-rich
RT repeat (LRR) KINASE gene, are regulators of seed size in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:17531-17536(2005).
CC -!- FUNCTION: Modulates the seed size by negatively regulating the
CC cellularization of syncytial endosperm. {ECO:0000269|PubMed:12692325,
CC ECO:0000269|PubMed:16293693}.
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 Q9LJM4; C0LGR6: At4g29180; NbExp=2; IntAct=EBI-20664220, EBI-20654480;
CC Q9LJM4; Q9LVI6: RLK902; NbExp=2; IntAct=EBI-20664220, EBI-1626936;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the endosperm of fertilized ovules.
CC {ECO:0000269|PubMed:16293693}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AP000417; BAB02557.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76277.1; -; Genomic_DNA.
DR PIR; T52400; T52400.
DR RefSeq; NP_188604.1; NM_112860.1.
DR AlphaFoldDB; Q9LJM4; -.
DR SMR; Q9LJM4; -.
DR BioGRID; 6840; 13.
DR IntAct; Q9LJM4; 15.
DR STRING; 3702.AT3G19700.1; -.
DR PaxDb; Q9LJM4; -.
DR PRIDE; Q9LJM4; -.
DR ProteomicsDB; 228876; -.
DR EnsemblPlants; AT3G19700.1; AT3G19700.1; AT3G19700.
DR GeneID; 821507; -.
DR Gramene; AT3G19700.1; AT3G19700.1; AT3G19700.
DR KEGG; ath:AT3G19700; -.
DR Araport; AT3G19700; -.
DR TAIR; locus:2091206; AT3G19700.
DR eggNOG; ENOG502QVPY; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; Q9LJM4; -.
DR OMA; DIVMWVW; -.
DR OrthoDB; 121113at2759; -.
DR PhylomeDB; Q9LJM4; -.
DR PRO; PR:Q9LJM4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LJM4; differential.
DR Genevisible; Q9LJM4; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0009960; P:endosperm development; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
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 InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00369; LRR_TYP; 6.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Glycoprotein; Kinase; Leucine-rich repeat; Membrane;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..991
FT /note="Receptor-like protein kinase HAIKU2"
FT /id="PRO_0000240278"
FT TOPO_DOM 20..616
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 617..637
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 638..991
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 66..90
FT /note="LRR 1"
FT REPEAT 99..123
FT /note="LRR 2"
FT REPEAT 125..148
FT /note="LRR 3"
FT REPEAT 150..170
FT /note="LRR 4"
FT REPEAT 171..196
FT /note="LRR 5"
FT REPEAT 197..220
FT /note="LRR 6"
FT REPEAT 221..244
FT /note="LRR 7"
FT REPEAT 246..267
FT /note="LRR 8"
FT REPEAT 269..291
FT /note="LRR 9"
FT REPEAT 292..314
FT /note="LRR 10"
FT REPEAT 315..339
FT /note="LRR 11"
FT REPEAT 341..363
FT /note="LRR 12"
FT REPEAT 365..387
FT /note="LRR 13"
FT REPEAT 388..411
FT /note="LRR 14"
FT REPEAT 413..435
FT /note="LRR 15"
FT REPEAT 436..459
FT /note="LRR 16"
FT REPEAT 461..482
FT /note="LRR 17"
FT REPEAT 483..508
FT /note="LRR 18"
FT REPEAT 510..531
FT /note="LRR 19"
FT REPEAT 532..554
FT /note="LRR 20"
FT REPEAT 555..578
FT /note="LRR 21"
FT DOMAIN 671..970
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 972..991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 814
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 677..685
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 699
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 762
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 801
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 859
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 866
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT MOD_RES 867
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT CARBOHYD 22
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 495
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 538
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 953
FT /note="R->K: In iku2-3; reduced seed size and earlier
FT endosperm cellularization."
FT /evidence="ECO:0000269|PubMed:16293693"
SQ SEQUENCE 991 AA; 110475 MW; DDA49AF2F2CFE8D6 CRC64;
MLRLLFIVRL LFLMPLASSR SNHSEEVENL LKLKSTFGET KSDDVFKTWT HRNSACEFAG
IVCNSDGNVV EINLGSRSLI NRDDDGRFTD LPFDSICDLK LLEKLVLGNN SLRGQIGTNL
GKCNRLRYLD LGINNFSGEF PAIDSLQLLE FLSLNASGIS GIFPWSSLKD LKRLSFLSVG
DNRFGSHPFP REILNLTALQ WVYLSNSSIT GKIPEGIKNL VRLQNLELSD NQISGEIPKE
IVQLKNLRQL EIYSNDLTGK LPLGFRNLTN LRNFDASNNS LEGDLSELRF LKNLVSLGMF
ENRLTGEIPK EFGDFKSLAA LSLYRNQLTG KLPRRLGSWT AFKYIDVSEN FLEGQIPPYM
CKKGVMTHLL MLQNRFTGQF PESYAKCKTL IRLRVSNNSL SGMIPSGIWG LPNLQFLDLA
SNYFEGNLTG DIGNAKSLGS LDLSNNRFSG SLPFQISGAN SLVSVNLRMN KFSGIVPESF
GKLKELSSLI LDQNNLSGAI PKSLGLCTSL VDLNFAGNSL SEEIPESLGS LKLLNSLNLS
GNKLSGMIPV GLSALKLSLL DLSNNQLTGS VPESLVSGSF EGNSGLCSSK IRYLRPCPLG
KPHSQGKRKH LSKVDMCFIV AAILALFFLF SYVIFKIRRD KLNKTVQKKN DWQVSSFRLL
NFNEMEIIDE IKSENIIGRG GQGNVYKVSL RSGETLAVKH IWCPESSHES FRSSTAMLSD
GNNRSNNGEF EAEVATLSNI KHINVVKLFC SITCEDSKLL VYEYMPNGSL WEQLHERRGE
QEIGWRVRQA LALGAAKGLE YLHHGLDRPV IHRDVKSSNI LLDEEWRPRI ADFGLAKIIQ
ADSVQRDFSA PLVKGTLGYI APEYAYTTKV NEKSDVYSFG VVLMELVTGK KPLETDFGEN
NDIVMWVWSV SKETNREMMM KLIDTSIEDE YKEDALKVLT IALLCTDKSP QARPFMKSVV
SMLEKIEPSY NKNSGEASYG ESANDEITKV V
