ACCR2_ARATH
ID ACCR2_ARATH Reviewed; 776 AA.
AC O80963;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Serine/threonine-protein kinase-like protein CCR2;
DE EC=2.7.11.1;
DE AltName: Full=Protein CRINKLY 4 RELATED 2;
DE Short=AtCRR2;
DE Flags: Precursor;
GN Name=CCR2; Synonyms=CRR2; OrderedLocusNames=At2g39180; ORFNames=T16B24.18;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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=AK228187; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AC004697; AAC28989.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09642.1; -; Genomic_DNA.
DR EMBL; AK228187; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T02584; T02584.
DR RefSeq; NP_181451.1; NM_129475.4.
DR AlphaFoldDB; O80963; -.
DR SMR; O80963; -.
DR BioGRID; 3841; 5.
DR IntAct; O80963; 5.
DR STRING; 3702.AT2G39180.1; -.
DR PaxDb; O80963; -.
DR PRIDE; O80963; -.
DR ProteomicsDB; 244514; -.
DR EnsemblPlants; AT2G39180.1; AT2G39180.1; AT2G39180.
DR GeneID; 818503; -.
DR Gramene; AT2G39180.1; AT2G39180.1; AT2G39180.
DR KEGG; ath:AT2G39180; -.
DR Araport; AT2G39180; -.
DR TAIR; locus:2056033; AT2G39180.
DR eggNOG; ENOG502QUN0; Eukaryota.
DR HOGENOM; CLU_009948_0_0_1; -.
DR InParanoid; O80963; -.
DR OMA; CAITSNT; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; O80963; -.
DR PRO; PR:O80963; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80963; baseline and differential.
DR Genevisible; O80963; 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; -; 1.
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; 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; SSF50985; SSF50985; 2.
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 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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..776
FT /note="Serine/threonine-protein kinase-like protein CCR2"
FT /id="PRO_0000382747"
FT TOPO_DOM 23..432
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 433..453
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 454..776
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 341..396
FT /note="TNFR-Cys"
FT DOMAIN 519..776
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 644
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 525..533
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 547
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 404
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 342..371
FT /evidence="ECO:0000250"
FT DISULFID 374..388
FT /evidence="ECO:0000250"
FT DISULFID 378..396
FT /evidence="ECO:0000250"
SQ SEQUENCE 776 AA; 85303 MW; 8A150033797C69C9 CRC64;
MQPNSHIFVI ITISSLIITV SAYGSTGTIA AAFGENGFFC AIDASGKQEV ICWDRGNTNR
SLNRPPGEIS GYSPPMTSLS GGEGFLCAIT SNTSRAFCWN LEDPSENLVP RAFQYNSYLQ
IASGNNHVCA ISGLYYSGPD YGPVHCWEYS DNTNFTSGLL WNSSFHNPYI DSLMFRKIVS
GDGFSCGVTK DGDLVCWGPK SNLLNFSNNE EFEVLASGRN SVCGVSKDSG QLHCFGDETE
FGSLPNRPRF IALSAGANHY CGIREDDHGV ECWGRNLNSS SSSSAPNTSG FVAISSSDST
TCGVRELDLV LDCWRVHDSS KADYSPPLEL CSPGMCSPRG NCGDGWFAFN ASILKESELT
SLCSFHNLNI CLRCGISCLE GYFPSSTCNP NADRVCTPCS LCQNSSCYGI CKIRATKSKE
HEQKEQREVR RLVIIIGCSV LGFLVMLIGL SFIPKMTKGS KRDDEERSKM TCCFCFDKNS
VEADPDPVPH QSVLLPTAVS LGETKIFRLS ELKDATHGFK EFNELGRGSF GFVYKAVLSD
GIHVAVKRAN AATIIHSNNR GFESELEILC KIRHNNIVNL LGYCSEMGER LLVYEYMPHG
TLHDHLHGDL SQLDWSMRLK IMLQAARGLD YLHNEVDPPI IHRDVKTSNI LLDGEMCARI
ADFGLVSSNE RDSSNSDREG DVYDFGIVLL EILSGRKAID RESDPAGIAE WAVPLIRKGK
AAAIIDRNIC LPRNVEPLLK LAELAELAVR ENSNERPNIR NILCFLDLIV KSGLTF
