CCR12_ARATH
ID CCR12_ARATH Reviewed; 470 AA.
AC Q9SGN7;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Serine/threonine-protein kinase-like protein At1g28390;
DE EC=2.7.11.1;
DE AltName: Full=CRINKLY 4-related kinase;
GN OrderedLocusNames=At1g28390; ORFNames=F3M18.17;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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=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.
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 -!- 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9SGN7-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC010155; AAF16755.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30966.1; -; Genomic_DNA.
DR EMBL; AY075610; AAL91624.1; -; mRNA.
DR RefSeq; NP_174161.1; NM_102606.4. [Q9SGN7-1]
DR AlphaFoldDB; Q9SGN7; -.
DR SMR; Q9SGN7; -.
DR BioGRID; 24971; 6.
DR IntAct; Q9SGN7; 6.
DR STRING; 3702.AT1G28390.2; -.
DR PaxDb; Q9SGN7; -.
DR PRIDE; Q9SGN7; -.
DR EnsemblPlants; AT1G28390.1; AT1G28390.1; AT1G28390. [Q9SGN7-1]
DR GeneID; 839736; -.
DR Gramene; AT1G28390.1; AT1G28390.1; AT1G28390. [Q9SGN7-1]
DR KEGG; ath:AT1G28390; -.
DR Araport; AT1G28390; -.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_21_4_1; -.
DR InParanoid; Q9SGN7; -.
DR OMA; NCNPRRS; -.
DR PhylomeDB; Q9SGN7; -.
DR PRO; PR:Q9SGN7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SGN7; baseline and differential.
DR Genevisible; Q9SGN7; AT.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045271; SRF-like.
DR PANTHER; PTHR27001; PTHR27001; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 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 Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW Phosphoprotein; Receptor; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..470
FT /note="Serine/threonine-protein kinase-like protein
FT At1g28390"
FT /id="PRO_0000382751"
FT DOMAIN 52..333
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 186
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 58..66
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 221
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 226
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 234
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
SQ SEQUENCE 470 AA; 53076 MW; 91345428A7E4AE3B CRC64;
MGYLSCNGES AVAICDTYNW NPRRRSKVPE KRHPPKLRVF NYDELAVATN GFSANNFLGK
GSHGRVYKAV LDDGKLLAAV KRTTITTTVG NNNNNVSQVD NEIEILSRVR HRWMVNLIGY
CVDHRRKTKL LVVEYMPNGT LHDQLHSRSS LDSRLSSWNR RIKHALQIAI AVHALHTAET
QVIHRDIKSC NVLIDGDGNA RLADFGLALI GNVDDERLKY TPPAGTLGYL DPSYLAPADL
TAKSDVFSFG ILLLEIISGR EAIDLNYSPS CIVDWAVPLI KRGDYDAICD LKIKNRPYYA
VIRKLAVMAA RCVRSTAKKR PDMLEVVECL KTVRQLSPAW NKLRRRSEER SENVLAVEEE
KEEIHVRIVR GGSRKNRKVS NVTTSVDDVY ERLVPEETLP FRRRNFVLRS RSVGAKVGPD
PYDGFGDETV VTMRLLIEKE RPVTTAAMRL SKSRSVGIVR SHKTASRKRY
