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Database: UniProt
Entry: F1S370_PIG
LinkDB: F1S370_PIG
Original site: F1S370_PIG 
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
//
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