PERK3_ARATH
ID PERK3_ARATH Reviewed; 513 AA.
AC Q1PEM5; F4J7P4; Q9LV50;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Proline-rich receptor-like protein kinase PERK3;
DE EC=2.7.11.1;
DE AltName: Full=Proline-rich extensin-like receptor kinase 3;
DE Short=AtPERK3;
GN Name=PERK3; OrderedLocusNames=At3g24540; ORFNames=MOB24.4;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [4]
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 [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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q1PEM5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q1PEM5-2; Sequence=VSP_040357, VSP_040358;
CC -!- TISSUE SPECIFICITY: Expressed at low levels in inflorescence bolt,
CC flower buds, siliques, roots, seedlings and leaves.
CC {ECO:0000269|PubMed:15653807}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to two introns retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02005.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB020746; BAB02005.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DQ446692; ABE65962.1; -; mRNA.
DR AlphaFoldDB; Q1PEM5; -.
DR SMR; Q1PEM5; -.
DR STRING; 3702.AT3G24540.1; -.
DR PaxDb; Q1PEM5; -.
DR PRIDE; Q1PEM5; -.
DR ProteomicsDB; 236393; -. [Q1PEM5-1]
DR Araport; AT3G24540; -.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_106_6_1; -.
DR InParanoid; Q1PEM5; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q1PEM5; -.
DR PRO; PR:Q1PEM5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q1PEM5; baseline and differential.
DR Genevisible; Q1PEM5; 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 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 Alternative splicing; ATP-binding; Cell membrane; Glycoprotein; Kinase;
KW Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..513
FT /note="Proline-rich receptor-like protein kinase PERK3"
FT /id="PRO_0000400055"
FT TOPO_DOM 1..123
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..513
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 183..334
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 27..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..100
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 307
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 189..197
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 211
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 172
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 256
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 341
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 346
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 354
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 11
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 324..334
FT /note="ADFGLAKIALD -> RFIFLSFLSFH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17147637"
FT /id="VSP_040357"
FT VAR_SEQ 335..513
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17147637"
FT /id="VSP_040358"
SQ SEQUENCE 513 AA; 56081 MW; A11B735037C3C360 CRC64;
MARSNRCVPQ NSSIVQIPIE EVFKTQLKSR WQQITMSSAS SPPPPQVFVP EPLFSEPPPP
PKAPVNVSLS PPPPPRSPST STPPRLGNRN PPPPASPSGQ EPTTPTMTPG FSLSPPSPSR
LSTGAVVGIS IGGGVFVLTL IFFLCKKKRP RDDKALPAPI GLVLGIHQST FTYGELARAT
NKFSEANLLG EGGFGFVYKG ILNNGNEVAV KQLKVGSAQG EKEFQAEVNI ISQIHHRNLV
SLVGYCIAGA QRLLVYEFVP NNTLEFHLHG KGRPTMEWSL RLKIAVSSSK GLSYLHENCN
PKIIHRDIKA ANILIDFKFE AKVADFGLAK IALDTNTHVS TRVMGTFGYL APEYAASGKL
TEKSDVYSFG VVLLELITGR RPVDANNVYA DDSLVDWARP LLVQALEESN FEGLADIKLN
NEYDREEMAR MVACAAACVR YTARRRPRMD QVVRVLEGNI SPSDLNQGIT PGHSNTVSVR
LDARAVRVKP HGEMDSRWGR FKRTAQRYGG DSL
