PEK15_ARATH
ID PEK15_ARATH Reviewed; 509 AA.
AC Q9C821;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Proline-rich receptor-like protein kinase PERK15;
DE EC=2.7.11.1;
DE AltName: Full=Proline-rich extensin-like receptor kinase 15;
DE Short=AtPERK15;
GN Name=PERK15; OrderedLocusNames=At1g52290; ORFNames=F19K6.9;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 Cheuk R.F., Chen H., Kim C.J., Shinn P., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15653807; DOI=10.1093/pcp/pch206;
RA Nakhamchik A., Zhao Z., Provart N.J., Shiu S.-H., Keatley S.K.,
RA Cameron R.K., Goring D.R.;
RT "A comprehensive expression analysis of the Arabidopsis proline-rich
RT extensin-like receptor kinase gene family using bioinformatic and
RT experimental approaches.";
RL Plant Cell Physiol. 45:1875-1881(2004).
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in inflorescence bolts, and, to a
CC lower extent, in flower buds and siliques.
CC {ECO:0000269|PubMed:15653807}.
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; AC037424; AAG51550.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32778.1; -; Genomic_DNA.
DR EMBL; BT011757; AAS49120.1; -; mRNA.
DR EMBL; AK221628; BAD95250.1; -; mRNA.
DR PIR; A96563; A96563.
DR RefSeq; NP_175639.1; NM_104108.4.
DR AlphaFoldDB; Q9C821; -.
DR SMR; Q9C821; -.
DR BioGRID; 26884; 23.
DR IntAct; Q9C821; 23.
DR STRING; 3702.AT1G52290.1; -.
DR iPTMnet; Q9C821; -.
DR PaxDb; Q9C821; -.
DR PRIDE; Q9C821; -.
DR ProteomicsDB; 236679; -.
DR EnsemblPlants; AT1G52290.1; AT1G52290.1; AT1G52290.
DR GeneID; 841659; -.
DR Gramene; AT1G52290.1; AT1G52290.1; AT1G52290.
DR KEGG; ath:AT1G52290; -.
DR Araport; AT1G52290; -.
DR TAIR; locus:2018209; AT1G52290.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_106_3_1; -.
DR InParanoid; Q9C821; -.
DR OMA; MTRVVAC; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9C821; -.
DR PRO; PR:Q9C821; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C821; baseline and differential.
DR Genevisible; Q9C821; 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: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 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 Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..509
FT /note="Proline-rich receptor-like protein kinase PERK15"
FT /id="PRO_0000400067"
FT TOPO_DOM 1..61
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..509
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 143..423
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 267
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 149..157
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 132
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 216
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 301
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 306
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 314
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
SQ SEQUENCE 509 AA; 55659 MW; 1BEFAC6862E264C2 CRC64;
MSTDTIPSLS SPPAPEFPST TPDTATSPAP SQPSIIGPSS LAPFPETTTN IDGGSRNVAL
TGLITGVVLG ATFVLLGVCI FVCFYKRKKR KLKKKKKEDI EASINRDSLD PKDDSNNLQQ
WSSSEIGQNL FTYEDLSKAT SNFSNTNLLG QGGFGYVHRG VLVDGTLVAI KQLKSGSGQG
EREFQAEIQT ISRVHHRHLV SLLGYCITGA QRLLVYEFVP NKTLEFHLHE KERPVMEWSK
RMKIALGAAK GLAYLHEDCN PKTIHRDVKA ANILIDDSYE AKLADFGLAR SSLDTDTHVS
TRIMGTFGYL APEYASSGKL TEKSDVFSIG VVLLELITGR RPVDKSQPFA DDDSIVDWAK
PLMIQALNDG NFDGLVDPRL ENDFDINEMT RMVACAAASV RHSAKRRPKM SQIVRAFEGN
ISIDDLTEGA APGQSTIYSL DGSSDYSSTQ YKEDLKKFKK MAFESKTFGS SECSGLTSDN
GQNPSGSSSI TEGQRTTQEI EPEKNTKDT
