ACCR1_ARATH
ID ACCR1_ARATH Reviewed; 775 AA.
AC Q9S7D9;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Serine/threonine-protein kinase-like protein CCR1;
DE EC=2.7.11.1;
DE AltName: Full=Protein CRINKLY 4 RELATED 1;
DE Short=AtCRR1;
DE Flags: Precursor;
GN Name=CCR1; Synonyms=CRR1; OrderedLocusNames=At3g09780;
GN ORFNames=F11F8.37, F8A24.17;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [4]
RP GENE FAMILY, CATALYTIC ACTIVITY, 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 [5]
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 [6]
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 with low activity.
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 Evidence={ECO:0000269|PubMed:15549374};
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; Evidence={ECO:0000269|PubMed:15549374};
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BX824605; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AC015985; AAF23257.1; -; Genomic_DNA.
DR EMBL; AC016661; AAF23306.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74812.1; -; Genomic_DNA.
DR EMBL; BX824605; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_187589.1; NM_111813.4.
DR AlphaFoldDB; Q9S7D9; -.
DR SMR; Q9S7D9; -.
DR STRING; 3702.AT3G09780.1; -.
DR PaxDb; Q9S7D9; -.
DR PRIDE; Q9S7D9; -.
DR ProteomicsDB; 244381; -.
DR EnsemblPlants; AT3G09780.1; AT3G09780.1; AT3G09780.
DR GeneID; 820136; -.
DR Gramene; AT3G09780.1; AT3G09780.1; AT3G09780.
DR KEGG; ath:AT3G09780; -.
DR Araport; AT3G09780; -.
DR TAIR; locus:2075074; AT3G09780.
DR eggNOG; ENOG502QUN0; Eukaryota.
DR HOGENOM; CLU_009948_0_0_1; -.
DR InParanoid; Q9S7D9; -.
DR OMA; LDCWMVN; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9S7D9; -.
DR PRO; PR:Q9S7D9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9S7D9; baseline and differential.
DR Genevisible; Q9S7D9; 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:0004672; F:protein kinase 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; 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 InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
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.
DR PROSITE; PS50050; TNFR_NGFR_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Disulfide bond; Glycoprotein; Kinase; Membrane;
KW Nucleotide-binding; Receptor; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..775
FT /note="Serine/threonine-protein kinase-like protein CCR1"
FT /id="PRO_0000382746"
FT TOPO_DOM 24..439
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 440..460
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 461..775
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 351..406
FT /note="TNFR-Cys"
FT DOMAIN 520..770
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 645
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 526..534
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 548
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 352..381
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 384..398
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 388..406
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
SQ SEQUENCE 775 AA; 84185 MW; A4615BFE756B74DA CRC64;
METRCSLLFL SLILLYLPKP GSGFGSSGPI AASFGGSAFF CAIDASGRQD VICWGKNYSS
PSSPSSSSSS SSIASSTSAS YNIPSMAVLS GGDGFLCGIL SNTSQAFCFS SLGSSSGMDL
VPLAYRTTAY SQIAAGNSHV CAVRGAYYSD HDSGTIDCWE ITRATNNNSL IAKENPNFYD
QIVSNLVFNN IVSGDGFSCG GIRDGGMLCF GPNSSNLGFN TTSDNFQVLA AGKNSVCAIL
NLSREVKCWG EDESFVNSPM NDSRFVSLTA GPRHFCGIRE DNHEVECWGN SNFSLIPKGS
GFKAIASSDF IVCGIREEDL VLDCWMVNGS STLAYDPPLE LCSPGMCRAG PCNEKEFAFN
ASILNEPDLT SLCVRKELMV CSPCGSDCSH GFFLSSSCTA NSDRICTPCS LCQNSSCSDI
CKLHNSNFPD KHWHQLQRLV LIIGSCASAL LIIIIGCCVV PRIVTSPNKE DGAANQFKSC
IGKPDLDTDQ PLENVSPAPS VTPFAQVFRL SELKDATNGF KEFNELGRGS YGFVYKAVLA
DGRQVAVKRA NAATIIHTNT REFETELEIL CNIRHCNIVN LLGYSTEMGE RLLVYEYMPH
GTLHDHLHSG FSPLSWSLRI KIAMQTAKGL EYLHNEAEPR IIHGDVKSSN VLLDSEWVAR
VADFGLVTSS NEKNLDIKRD VYDFGVVLLE ILTGRKRYDR DCDPPEIVEW TVPVIREGKA
AAIVDTYIAL PRNVEPLLKL ADVAELCVRE DPNQQPTMSE LANWLEHVAR DALIF
