ACCR3_ARATH
ID ACCR3_ARATH Reviewed; 814 AA.
AC Q9LY50;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Putative serine/threonine-protein kinase-like protein CCR3;
DE EC=2.7.11.1;
DE AltName: Full=Protein CRINKLY 4 RELATED 3;
DE Short=AtCRR3;
DE Flags: Precursor;
GN Name=CCR3; Synonyms=CRR3; OrderedLocusNames=At3g55950; ORFNames=F27K19.130;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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, AND TISSUE SPECIFICITY.
RX PubMed=15549374; DOI=10.1007/s00425-004-1378-3;
RA Cao X., Li K., Suh S.-G., Guo T., Becraft P.W.;
RT "Molecular analysis of the CRINKLY4 gene family in Arabidopsis thaliana.";
RL Planta 220:645-657(2005).
RN [4]
RP HOMODIMERIZATION.
RX PubMed=18539132; DOI=10.1016/j.abb.2008.05.010;
RA Stokes K.D., Gururaj Rao A.;
RT "Dimerization properties of the transmembrane domains of Arabidopsis
RT CRINKLY4 receptor-like kinase and homologs.";
RL Arch. Biochem. Biophys. 477:219-226(2008).
RN [5]
RP GENE FAMILY.
RX PubMed=19529822; DOI=10.1093/mp/ssn083;
RA Chae L., Sudat S., Dudoit S., Zhu T., Luan S.;
RT "Diverse transcriptional programs associated with environmental stress and
RT hormones in the Arabidopsis receptor-like kinase gene family.";
RL Mol. Plant 2:84-107(2009).
CC -!- FUNCTION: Serine/threonine-protein kinase.
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 -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, shoot apical meristems
CC (SAM), and floral buds. {ECO:0000269|PubMed:15549374}.
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; AL163832; CAB87849.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79460.1; -; Genomic_DNA.
DR PIR; T49207; T49207.
DR RefSeq; NP_191154.1; NM_115453.3.
DR AlphaFoldDB; Q9LY50; -.
DR SMR; Q9LY50; -.
DR BioGRID; 10077; 1.
DR IntAct; Q9LY50; 1.
DR STRING; 3702.AT3G55950.1; -.
DR iPTMnet; Q9LY50; -.
DR PaxDb; Q9LY50; -.
DR PRIDE; Q9LY50; -.
DR ProteomicsDB; 243303; -.
DR EnsemblPlants; AT3G55950.1; AT3G55950.1; AT3G55950.
DR GeneID; 824761; -.
DR Gramene; AT3G55950.1; AT3G55950.1; AT3G55950.
DR KEGG; ath:AT3G55950; -.
DR Araport; AT3G55950; -.
DR TAIR; locus:2082033; AT3G55950.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_009948_1_1_1; -.
DR InParanoid; Q9LY50; -.
DR OMA; AEHSCAI; -.
DR OrthoDB; 242765at2759; -.
DR PhylomeDB; Q9LY50; -.
DR PRO; PR:Q9LY50; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LY50; baseline and differential.
DR Genevisible; Q9LY50; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
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 Gene3D; 2.130.10.30; -; 2.
DR InterPro; IPR044815; CCR3/4.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR46146; PTHR46146; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF50985; SSF50985; 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; Glycoprotein; Kinase; Membrane; Nucleotide-binding; Receptor;
KW Reference proteome; Serine/threonine-protein kinase; Signal; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..814
FT /note="Putative serine/threonine-protein kinase-like
FT protein CCR3"
FT /id="PRO_0000382748"
FT TOPO_DOM 31..393
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 394..414
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 415..814
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 496..794
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 366..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..385
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 631
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 502..510
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 524
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 6
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 814 AA; 87682 MW; 5FEF08B231D0262A CRC64;
MKRFINSTVT FSVTVTIAVI IFFLLSPVTS LGSGSTYAVV YGSDTVCALI SGQPTQRILC
YDTRLNINVT LNPGVSFSSI AAGDNFLCGI RSGGYSLLCW DNIGSYSPNR KRIYQNDNVL
LETLSVGDKQ ICATVNGTNS LKCWRGSVSD QSKPPNERFR SISSGVGFSC GVSIRNNRIL
CWGTDPVKSN QIQTGFGNTP MVTISAGKSH ACGLNTTGNL ICIGNNDSGQ LNVIAPDQPN
LYSSSLSLGS NFTCAMRISN NSVVCWGGGA ERFNNVTDSI SFESISSGPG LICGLISSNL
SIMCWNPTNF SRIFLPFPEV LPGPCVESSS SSLCSCGVYP QSDKLCSGTG SICKSCPIQF
PASPPSQFPL PPPPPPPPPS PSTSSPPSKA LTRGLLAFAI VGSVGAFAGI CSVVYCLWTG
VCLGKKKVHN SVQPTITRGG SNSRSNSSNS RSLSIRRQGS RMLSMRRQRS GTSSMKHADK
AEEFSFSELA SATGNFSLEN KIGSGSFGVV YRGKLNDGRE VAIKRGEVNA KMKKFQEKET
AFDSEIAFLS RLHHKHLVRL VGYCEEREEK LLVYDYMKNG ALYDHLHDKN NVEKHSSLIN
SWKMRIKIAL DAARGIEYLH NYAVPPIIHR DIKSSNILLD SNWVARVSDF GLSLMGPVLG
KDHNPYQRPT KAAGTVGYID PEYYSLNVLT DKSDVYGLGV VLLELLTGKR AIFRNNGDVE
EEEGCVPVHL VDYSVPAITA DELSTILDPR VGSPELGEGD AVELVAYTAM HCVNAEGRNR
PTMTDIVGNL ERALDLCGDS HGSISSGICS IVSD
