CLK3_BOVIN
ID CLK3_BOVIN Reviewed; 490 AA.
AC Q3SX21;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250}.
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; BC104550; AAI04551.1; -; mRNA.
DR RefSeq; NP_001029420.1; NM_001034248.1.
DR RefSeq; XP_005221975.1; XM_005221918.3.
DR AlphaFoldDB; Q3SX21; -.
DR SMR; Q3SX21; -.
DR STRING; 9913.ENSBTAP00000009609; -.
DR PaxDb; Q3SX21; -.
DR PRIDE; Q3SX21; -.
DR Ensembl; ENSBTAT00000009609; ENSBTAP00000009609; ENSBTAG00000007304.
DR GeneID; 505499; -.
DR KEGG; bta:505499; -.
DR CTD; 1198; -.
DR VEuPathDB; HostDB:ENSBTAG00000007304; -.
DR VGNC; VGNC:27450; CLK3.
DR eggNOG; KOG0671; Eukaryota.
DR GeneTree; ENSGT00940000160359; -.
DR HOGENOM; CLU_000288_5_16_1; -.
DR InParanoid; Q3SX21; -.
DR OMA; HTHHCHK; -.
DR OrthoDB; 915778at2759; -.
DR TreeFam; TF101041; -.
DR Proteomes; UP000009136; Chromosome 21.
DR Bgee; ENSBTAG00000007304; Expressed in saliva-secreting gland and 106 other tissues.
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; IEA:Ensembl.
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; IBA:GO_Central.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
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 2: Evidence at transcript 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_0000248283"
FT DOMAIN 156..472
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 22..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..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:0000250|UniProtKB:P49761"
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"
SQ SEQUENCE 490 AA; 58628 MW; 0BA34A089F25B697 CRC64;
MHHCKRYRSP EPDPYLSYRW KRRRSYSREH EGRLRYPSRR EPPPRRSRSR SHDRLPYQRR
YREHRDSDTY RCEDRSPSFG EDYYGSSRCH HRRRSREREP 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 LKSYMLQDTL EHVQLFDLMR RMLEFDPAQR ITLAEALLHP FFAGLTPEER
SFHTSRNPSR
