ID F1S370_PIG Unreviewed; 568 AA.
AC F1S370;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 24-JAN-2024, entry version 73.
DE RecName: Full=dual-specificity kinase {ECO:0000256|ARBA:ARBA00013203};
DE EC=2.7.12.1 {ECO:0000256|ARBA:ARBA00013203};
GN Name=TESK2 {ECO:0000313|Ensembl:ENSSSCP00000004232.3,
GN ECO:0000313|VGNC:VGNC:93886};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000004232.3, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000004232.3, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000004232.3,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:HDB78317.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30723633; DOI=.7717/peerj.6374;
RA Gilbert D.G.;
RT "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL PeerJ 7:E6374-E6374(2019).
RN [3] {ECO:0000313|Ensembl:ENSSSCP00000004232.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
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 Evidence={ECO:0000256|ARBA:ARBA00000972};
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; Evidence={ECO:0000256|ARBA:ARBA00001076};
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 Evidence={ECO:0000256|ARBA:ARBA00001687};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00005843}.
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DR EMBL; DQIR01222840; HDB78317.1; -; Transcribed_RNA.
DR RefSeq; XP_003128092.3; XM_003128044.5.
DR RefSeq; XP_005665531.1; XM_005665474.2.
DR RefSeq; XP_005665532.1; XM_005665475.2.
DR RefSeq; XP_005665533.1; XM_005665476.2.
DR RefSeq; XP_005665534.1; XM_005665477.2.
DR PaxDb; 9823-ENSSSCP00000004232; -.
DR Ensembl; ENSSSCT00000004332.3; ENSSSCP00000004232.3; ENSSSCG00000003917.5.
DR GeneID; 100513361; -.
DR KEGG; ssc:100513361; -.
DR CTD; 10420; -.
DR VGNC; VGNC:93886; TESK2.
DR eggNOG; ENOG502QTCP; Eukaryota.
DR GeneTree; ENSGT00940000158765; -.
DR HOGENOM; CLU_018577_1_0_1; -.
DR OMA; ISYLHYK; -.
DR OrthoDB; 5474815at2759; -.
DR TreeFam; TF318014; -.
DR Proteomes; UP000008227; Chromosome 6.
DR Bgee; ENSSSCG00000003917; Expressed in testis and 43 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14155; PKc_TESK; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR PANTHER; PTHR46485:SF6; DUAL SPECIFICITY TESTIS-SPECIFIC PROTEIN KINASE 2; 1.
DR PANTHER; PTHR46485; LIM DOMAIN KINASE 1; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Kinase {ECO:0000313|EMBL:HDB78317.1};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Transferase {ECO:0000313|EMBL:HDB78317.1}.
FT DOMAIN 59..314
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 509..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 568 AA; 63027 MW; B918A3FB39C2C3B0 CRC64;
MDRSKRNSIA GFPPRVERLE DFEGGGGGGD GSLSHVGRVW PSSYRALISA FSRLTRLDDF
TCEKIGSGFF SEVFKVRHRA SGQVMALKMN TLSSNRANML KEVQLMNRLS HPNILRFMGV
CVHQGQLHAL TEYINSGNLE QLLDSNLHLP WTVRVKLAYD IAVGLSYLHF KGIFHRDLTS
KNCLIKRDES GYSAVVADFG LAEKIPDGSM GSEKLAVVGS PFWMAPEVLR DEPYNEKADV
FSYGIILCEI IARIQADPDY LPRTENFGLD YDAFQHMVGD CPPDFLQLTF NCCNMDPKLR
PSFAEIGKTL EEILSRLQEE ELERDRKLQP AAKGLLEKGP GLKRLSLQDN KIPPKSPRPR
RTIWLSRSQS DIFSSKPPRT VNVLDPYYQP QRGGAARAPK INPFSARQDL KGGKIKFFDL
PSKSVISLVF DLDAPGPGST PVAEWQEPLA PPARRWRSLP GSPEFLHQEA CPFVGREESL
SDGPPPRLSS HKYRVREIPP FRAPALPAAP AHEAMDCSGP QEENGFGPRP PGPGLCLAGA
LEEMEVEERP RDLAVSGTGL KTQGEQDG
//