ACCR4_ARATH
ID ACCR4_ARATH Reviewed; 751 AA.
AC Q9FIJ6;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Serine/threonine-protein kinase-like protein CCR4;
DE EC=2.7.11.1;
DE AltName: Full=CRINKLY 4-related kinase 1;
DE Short=AtCRK1;
DE AltName: Full=Protein CRINKLY 4 RELATED 4;
DE Short=AtCCR4;
DE Flags: Precursor;
GN Name=CCR4; Synonyms=CRK1; OrderedLocusNames=At5g47850; ORFNames=MCA23.19;
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=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
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=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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 -!- 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, especially in
CC trichomes, shoot apical meristems (SAM), and, to a lower extent, in
CC 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; AB016886; BAB11332.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95580.1; -; Genomic_DNA.
DR EMBL; AY078947; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_199596.1; NM_124159.3.
DR AlphaFoldDB; Q9FIJ6; -.
DR SMR; Q9FIJ6; -.
DR STRING; 3702.AT5G47850.1; -.
DR PaxDb; Q9FIJ6; -.
DR PRIDE; Q9FIJ6; -.
DR EnsemblPlants; AT5G47850.1; AT5G47850.1; AT5G47850.
DR GeneID; 834836; -.
DR Gramene; AT5G47850.1; AT5G47850.1; AT5G47850.
DR KEGG; ath:AT5G47850; -.
DR Araport; AT5G47850; -.
DR TAIR; locus:2160952; AT5G47850.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_009948_1_1_1; -.
DR InParanoid; Q9FIJ6; -.
DR OMA; GENRSCA; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9FIJ6; -.
DR PRO; PR:Q9FIJ6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FIJ6; baseline and differential.
DR Genevisible; Q9FIJ6; 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; 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 1: Evidence at protein 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..31
FT /evidence="ECO:0000255"
FT CHAIN 32..751
FT /note="Serine/threonine-protein kinase-like protein CCR4"
FT /id="PRO_0000382749"
FT TOPO_DOM 32..366
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 388..751
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 443..733
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 579
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 449..457
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 471
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 327
FT /note="Missing (in Ref. 3; AY078947)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 751 AA; 83774 MW; 16666D2630E9DAD8 CRC64;
MALTISISCF SSYFVSLLLL VLSSFSFVCF SLSTVSISHI SNQTLVCALN NHSYLQCSSF
PLNSIPFSLT GNLRNRRFSG VVSGNGFVCG LISRLDSNTS TLLCWRFSVD GTNMLHKRIY
HGPELEELEA GNFRICGVER VSRRLRCWQP YYLPRPDNYR SIALGDNFFC GLSQPPGMIS
CEGIAKVPSG DHYIAIAAGS RQACAITVDN DVECWGQTQS LPREKFLALA VGEDRGCGVR
WSNGTVVCWG NNNNFSLPQT LKDIHFTSIY AKGPMFCGVA TRNYTLICWG NENFKSGVFT
PFQGLISQVV MPGPCRRECP YRPLSGSQSL CGNELMICDL KRNDGEFPDT RAQNSKNKTW
SRRNIAFLVV GCVGTFSLLL VISFLIFKSH CRCRVHDSGR LDDTRTIDIP KLEKRLCTLA
SLGNPGQLME FSIDELALAT DGFSVRFHLG IGSFGSVYQG VLSDGRHVAI KRAELTNPTL
SGTTMRHRRA DKDSAFVNEL ESMSRLNHKN LVRLLGFYED TEERILVYEY MKNGSLADHL
HNPQFDPLSW QTRLMIALDA ARGIQYLHEF IVPPVIHRDI KSSNILLDAT WTAKVSDFGL
SQMGPTEEDD VSHLSLHAAG TLGYIDPEYY KFQQLTTKSD VYSFGVVLLE LLSGHKAIHN
NEDENPRNLV EYVVPYILLD EAHRILDQRI PPPTPYEIEA VAHVGYLAAE CLMPCSRKRP
SMVEVVSKLE SALAACLTAP KTETVSRSNT Y
