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Database: UniProt
Entry: Q9LY50
LinkDB: Q9LY50
Original site: Q9LY50 
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   27-MAR-2024, entry version 152.
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.Q9LY50; -.
DR   GlyCosmos; Q9LY50; 10 sites, No reported glycans.
DR   iPTMnet; Q9LY50; -.
DR   PaxDb; 3702-AT3G55950-1; -.
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; AT3G55950; CCR3.
DR   eggNOG; KOG1187; Eukaryota.
DR   HOGENOM; CLU_009948_1_1_1; -.
DR   InParanoid; Q9LY50; -.
DR   OMA; ATSWKLR; -.
DR   OrthoDB; 404991at2759; -.
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:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR044815; CCR1-4.
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; SERINE/THREONINE-PROTEIN KINASE-LIKE PROTEIN CCR4; 1.
DR   PANTHER; PTHR46146:SF3; SERINE_THREONINE-PROTEIN KINASE-LIKE PROTEIN CCR3-RELATED; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF13540; RCC1_2; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF50985; RCC1/BLIP-II; 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
//
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