PEK12_ARATH
ID PEK12_ARATH Reviewed; 720 AA.
AC Q9ZUE0; Q9LQC5;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Proline-rich receptor-like protein kinase PERK12;
DE EC=2.7.11.1;
DE AltName: Full=Proline-rich extensin-like receptor kinase 12;
DE Short=AtPERK12;
DE AltName: Full=Protein INFLORESCENCE GROWTH INHIBITOR 1;
GN Name=PERK12; Synonyms=IGI1; OrderedLocusNames=At1g23540;
GN ORFNames=F28C11.17, F5O8.10;
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 GENE FAMILY.
RX PubMed=12374299; DOI=10.1023/a:1019951120788;
RA Silva N.F., Goring D.R.;
RT "The proline-rich, extensin-like receptor kinase-1 (PERK1) gene is rapidly
RT induced by wounding.";
RL Plant Mol. Biol. 50:667-685(2002).
RN [4]
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).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY AUXIN.
RX PubMed=20473553; DOI=10.1007/s11103-010-9645-0;
RA Hwang I., Kim S.Y., Kim C.S., Park Y., Tripathi G.R., Kim S.-K., Cheong H.;
RT "Over-expression of the IGI1 leading to altered shoot-branching development
RT related to MAX pathway in Arabidopsis.";
RL Plant Mol. Biol. 73:629-641(2010).
CC -!- FUNCTION: Regulates the auxin-related MAX (More Axillary Growth)
CC pathway during the shoot branching. {ECO:0000269|PubMed:20473553}.
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 apical parts, including flower
CC buds, and particularly in anthers. Also present in root hairs.
CC {ECO:0000269|PubMed:15653807, ECO:0000269|PubMed:20473553}.
CC -!- INDUCTION: Repressed by auxin (IAA) treatment.
CC {ECO:0000269|PubMed:20473553}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC98010.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF79592.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC005990; AAC98010.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC007945; AAF79592.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30401.1; -; Genomic_DNA.
DR PIR; B86369; B86369.
DR RefSeq; NP_173768.2; NM_102203.3.
DR AlphaFoldDB; Q9ZUE0; -.
DR SMR; Q9ZUE0; -.
DR STRING; 3702.AT1G23540.1; -.
DR PaxDb; Q9ZUE0; -.
DR PRIDE; Q9ZUE0; -.
DR ProteomicsDB; 236445; -.
DR EnsemblPlants; AT1G23540.1; AT1G23540.1; AT1G23540.
DR GeneID; 838963; -.
DR Gramene; AT1G23540.1; AT1G23540.1; AT1G23540.
DR KEGG; ath:AT1G23540; -.
DR Araport; AT1G23540; -.
DR TAIR; locus:2028911; AT1G23540.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_106_3_1; -.
DR InParanoid; Q9ZUE0; -.
DR OMA; NWSPPPQ; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9ZUE0; -.
DR PRO; PR:Q9ZUE0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9ZUE0; baseline and differential.
DR Genevisible; Q9ZUE0; 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:0032502; P:developmental process; IMP:TAIR.
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 InterPro; IPR008271; Ser/Thr_kinase_AS.
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.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Glycoprotein; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..720
FT /note="Proline-rich receptor-like protein kinase PERK12"
FT /id="PRO_0000400064"
FT TOPO_DOM 1..246
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..720
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 371..624
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 698..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..211
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 495
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 377..385
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 399
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 444
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 529
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 534
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 542
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 720 AA; 76302 MW; 482D0AA292B6913E CRC64;
MSDLGESPSS SPPAPPADTA PPPETPSENS ALPPVDSSPP SPPADSSSTP PLSEPSTPPP
DSQLPPLPSI LPPLTDSPPP PSDSSPPVDS TPSPPPPTSN ESPSPPEDSE TPPAPPNESN
DNNPPPSQDL QSPPPSSPSP NVGPTNPESP PLQSPPAPPA SDPTNSPPAS PLDPTNPPPI
QPSGPATSPP ANPNAPPSPF PTVPPKTPSS GPVVSPSLTS PSKGTPTPNQ GNGDGGGGGG
GYQGKTMVGM AVAGFAIMAL IGVVFLVRRK KKRNIDSYNH SQYLPHPNFS VKSDGFLYGQ
DPGKGYSSGP NGSMYNNSQQ QQSSMGNSYG TAGGGYPHHQ MQSSGTPDSA ILGSGQTHFS
YEELAEITQG FARKNILGEG GFGCVYKGTL QDGKVVAVKQ LKAGSGQGDR EFKAEVEIIS
RVHHRHLVSL VGYCISDQHR LLIYEYVSNQ TLEHHLHGKG LPVLEWSKRV RIAIGSAKGL
AYLHEDCHPK IIHRDIKSAN ILLDDEYEAQ VADFGLARLN DTTQTHVSTR VMGTFGYLAP
EYASSGKLTD RSDVFSFGVV LLELVTGRKP VDQTQPLGEE SLVEWARPLL LKAIETGDLS
ELIDTRLEKR YVEHEVFRMI ETAAACVRHS GPKRPRMVQV VRALDCDGDS GDISNGIKIG
QSTTYDSGQY NEDIMKFRKM AFGGDNSVES GLYSGNYSAK SSSDFSGNES ETRPFNNRRF
