CLK3_RAT
ID CLK3_RAT Reviewed; 490 AA.
AC Q63117; Q6IRK2;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Dual specificity protein kinase CLK3;
DE EC=2.7.12.1;
DE AltName: Full=CDC-like kinase 3;
GN Name=Clk3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=8679717; DOI=10.1016/0167-4889(96)00036-5;
RA Becker W., Kentrup H., Heukelbach J., Joost H.G.;
RT "cDNA cloning and characterization of rat Clk3, a LAMMER kinase
RT predominately expressed in testis.";
RL Biochim. Biophys. Acta 1312:63-67(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Dual specificity kinase acting on both serine/threonine and
CC tyrosine-containing substrates. Phosphorylates serine- and arginine-
CC rich (SR) proteins of the spliceosomal complex. May be a constituent of
CC a network of regulatory mechanisms that enable SR proteins to control
CC RNA splicing and can cause redistribution of SR proteins from speckles
CC to a diffuse nucleoplasmic distribution. Phosphorylates SRSF1 and
CC SRSF3. Regulates the alternative splicing of tissue factor (F3) pre-
CC mRNA in endothelial cells (By similarity). {ECO:0000250}.
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=2.7.12.1;
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=2.7.12.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.1;
CC -!- ACTIVITY REGULATION: Leucettine L41 inhibits its kinase activity and
CC affects the regulation of alternative splicing mediated by
CC phosphorylation of SR proteins. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250}.
CC -!- PTM: Autophosphorylates on all three types of residues.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. Lammer subfamily. {ECO:0000305}.
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DR EMBL; X94351; CAA64076.1; -; mRNA.
DR EMBL; BC070891; AAH70891.1; -; mRNA.
DR PIR; S70352; S70352.
DR RefSeq; NP_599167.1; NM_134340.1.
DR AlphaFoldDB; Q63117; -.
DR SMR; Q63117; -.
DR STRING; 10116.ENSRNOP00000061691; -.
DR iPTMnet; Q63117; -.
DR PhosphoSitePlus; Q63117; -.
DR PaxDb; Q63117; -.
DR PRIDE; Q63117; -.
DR GeneID; 171305; -.
DR KEGG; rno:171305; -.
DR UCSC; RGD:621259; rat.
DR CTD; 1198; -.
DR RGD; 621259; Clk3.
DR VEuPathDB; HostDB:ENSRNOG00000030126; -.
DR eggNOG; KOG0671; Eukaryota.
DR HOGENOM; CLU_000288_5_16_1; -.
DR InParanoid; Q63117; -.
DR OMA; HTHHCHK; -.
DR OrthoDB; 915778at2759; -.
DR PhylomeDB; Q63117; -.
DR BRENDA; 2.7.12.1; 5301.
DR PRO; PR:Q63117; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000030126; Expressed in thymus and 20 other tissues.
DR Genevisible; Q63117; RN.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0016301; F:kinase activity; IDA:RGD.
DR GO; GO:0004672; F:protein kinase activity; IDA:RGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004713; F:protein tyrosine kinase activity; ISO:RGD.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISO:RGD.
DR GO; GO:0046777; P:protein autophosphorylation; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR GO; GO:0043484; P:regulation of RNA splicing; ISS:UniProtKB.
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 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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Cytoplasmic vesicle; Kinase; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase.
FT CHAIN 1..490
FT /note="Dual specificity protein kinase CLK3"
FT /id="PRO_0000085872"
FT DOMAIN 156..472
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..118
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 283
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 162..170
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 7
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P49761"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49761"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49761"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49761"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49761"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49761"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49761"
FT CONFLICT 458
FT /note="A -> S (in Ref. 1; CAA64076)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 490 AA; 58485 MW; 6B10CA96A64AB19A CRC64;
MHHCKRYRSP EPDPYLSYRW KRRRSYSREH EGRLRYPSRR EPPPRRSRSR SHDRIPYQRR
YREHRDSDTY RCEERSPSFG EDCYGSSRSR HRRRSRERGP YRTRKHAHHC HKRRTRSCSS
ASSRSQQSSK RSSRSVEDDK EGHLVCRIGD WLQERYEIVG NLGEGTFGKV VECLDHARGK
SQVALKIIRN VGKYREAARL EINVLKKIKE KDKENKFLCV LMSDWFNFHG HMCIAFELLG
KNTFEFLKEN NFQPYPLPHV RHMAYQLCHA LRFLHENQLT HTDLKPENIL FVNSEFETLY
NEHKSCEEKS VKNTSIRVAD FGSATFDHEH HTTIVATRHY RPPEVILELG WAQPCDVWSI
GCILFEYYRG FTLFQTHENR EHLVMMEKIL GPIPSHMIHR TRKQKYFYKG GLVWDENSSD
GRYVKENCKP LKSYMLQDSL EHVQLFDLMR RMLEFDPAQR ITLAEALLHP FFAGLTPEER
SFHSSRNPSR
