ALE2_ARATH
ID ALE2_ARATH Reviewed; 744 AA.
AC Q8RWW0; Q9SK72;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Receptor-like serine/threonine-protein kinase ALE2;
DE EC=2.7.11.1;
DE AltName: Full=Protein ABNORMAL LEAF SHAPE 2;
DE Flags: Precursor;
GN Name=ALE2; OrderedLocusNames=At2g20300; ORFNames=F11A3.15;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
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 [5]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF LYS-377,
RP AUTOPHOSPHORYLATION, PHOSPHORYLATION BY ACR4, AND CATALYTIC ACTIVITY.
RX PubMed=17376810; DOI=10.1242/dev.003533;
RA Tanaka H., Watanabe M., Sasabe M., Hiroe T., Tanaka T., Tsukaya H.,
RA Ikezaki M., Machida C., Machida Y.;
RT "Novel receptor-like kinase ALE2 controls shoot development by specifying
RT epidermis in Arabidopsis.";
RL Development 134:1643-1652(2007).
CC -!- FUNCTION: Required during the differentiation of the protoderm into
CC shoots epidermis and cuticle. {ECO:0000269|PubMed:17376810}.
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:0000269|PubMed:17376810};
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:0000269|PubMed:17376810};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- PTM: Autophosphorylated and phosphorylated by ACR4.
CC {ECO:0000269|PubMed:17376810}.
CC -!- DISRUPTION PHENOTYPE: Various epidermal defects, including
CC disorganization of epidermis-related tissues, defects in the leaf
CC cuticle and the fusion of organs. {ECO:0000269|PubMed:17376810}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD21758.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC006569; AAD21758.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC06991.1; -; Genomic_DNA.
DR EMBL; AY091071; AAM13891.1; -; mRNA.
DR EMBL; AY133858; AAM91792.1; -; mRNA.
DR EMBL; AK226880; BAE98959.1; -; mRNA.
DR PIR; E84587; E84587.
DR RefSeq; NP_849998.1; NM_179667.3.
DR AlphaFoldDB; Q8RWW0; -.
DR SMR; Q8RWW0; -.
DR BioGRID; 1902; 28.
DR IntAct; Q8RWW0; 28.
DR STRING; 3702.AT2G20300.1; -.
DR iPTMnet; Q8RWW0; -.
DR MetOSite; Q8RWW0; -.
DR PaxDb; Q8RWW0; -.
DR PRIDE; Q8RWW0; -.
DR ProteomicsDB; 245046; -.
DR EnsemblPlants; AT2G20300.1; AT2G20300.1; AT2G20300.
DR GeneID; 816549; -.
DR Gramene; AT2G20300.1; AT2G20300.1; AT2G20300.
DR KEGG; ath:AT2G20300; -.
DR Araport; AT2G20300; -.
DR TAIR; locus:2038992; AT2G20300.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_24_3_1; -.
DR InParanoid; Q8RWW0; -.
DR OMA; VVYITYP; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q8RWW0; -.
DR PRO; PR:Q8RWW0; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8RWW0; baseline and differential.
DR Genevisible; Q8RWW0; AT.
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:0016301; F:kinase activity; IDA:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; HDA:TAIR.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0090558; P:plant epidermis development; IMP:TAIR.
DR GO; GO:1905393; P:plant organ formation; IMP:TAIR.
DR GO; GO:0046777; P:protein autophosphorylation; HDA:TAIR.
DR GO; GO:0010068; P:protoderm histogenesis; IMP:TAIR.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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; PF07714; PK_Tyr_Ser-Thr; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
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; Cell membrane; Developmental protein; Differentiation;
KW Glycoprotein; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
KW Receptor; Reference proteome; Serine/threonine-protein kinase; Signal;
KW Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..744
FT /note="Receptor-like serine/threonine-protein kinase ALE2"
FT /id="PRO_0000403337"
FT TOPO_DOM 20..260
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 282..744
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 349..619
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 59..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 470
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 355..363
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 377
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 377
FT /note="K->W: Impaired kinase activity."
FT /evidence="ECO:0000269|PubMed:17376810"
SQ SEQUENCE 744 AA; 81633 MW; 85E330F0BBA8A2E0 CRC64;
MRNFAMLLLL ILLLHSLASF PICFARLFPM SLPFTRSKAH QMHFFHPYLN PSVAPTPSPA
FSPNPSRIPP LRHKGHHRHR RWHLRRNATA VSPSSHDCQQ TCVEPLTSTP FGSPCGCVFP
MKVQLLLSVA PFSIFPVTNE LEIEVAAGTY LEQSQVKIMG ASADSENQGK TVVDINLVPL
GEKFDNTTAT LIYQRFRHKK VPLNETVFGD YEVTHISYPG IPSSSPNGDV TGDAPGGLPI
PINATTFANK SQGIGFRTIA IIALSGFVLI LVLVGAISII VKWKKIGKSS NAVGPALAPS
INKRPGAGSM FSSSARSSGS DSLMSSMATC ALSVKTFTLS ELEKATDRFS AKRVLGEGGF
GRVYQGSMED GTEVAVKLLT RDNQNRDREF IAEVEMLSRL HHRNLVKLIG ICIEGRTRCL
IYELVHNGSV ESHLHEGTLD WDARLKIALG AARGLAYLHE DSNPRVIHRD FKASNVLLED
DFTPKVSDFG LAREATEGSQ HISTRVMGTF GYVAPEYAMT GHLLVKSDVY SYGVVLLELL
TGRRPVDMSQ PSGEENLVTW ARPLLANREG LEQLVDPALA GTYNFDDMAK VAAIASMCVH
QEVSHRPFMG EVVQALKLIY NDADETCGDY CSQKDSSVPD SADFKGDLAP SDSSWWNLTP
RLRYGQASSF ITMDYSSGPL EDMENRPHSA SSIPRVGGLI LPNRSGPLRP MRSRRNFFRL
RGSMSEHGGP SSSRHLWSGN GDWL
