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Database: UniProt
Entry: F7CCK6_HORSE
LinkDB: F7CCK6_HORSE
Original site: F7CCK6_HORSE 
ID   F7CCK6_HORSE            Unreviewed;       571 AA.
AC   F7CCK6;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2023, sequence version 3.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=dual-specificity kinase {ECO:0000256|ARBA:ARBA00013203};
DE            EC=2.7.12.1 {ECO:0000256|ARBA:ARBA00013203};
GN   Name=TESK1 {ECO:0000313|Ensembl:ENSECAP00000000156.3,
GN   ECO:0000313|VGNC:VGNC:24006};
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000000156.3, ECO:0000313|Proteomes:UP000002281};
RN   [1] {ECO:0000313|Ensembl:ENSECAP00000000156.3, ECO:0000313|Proteomes:UP000002281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000000156.3,
RC   ECO:0000313|Proteomes:UP000002281};
RX   PubMed=19892987; DOI=10.1126/science.1178158;
RG   Broad Institute Genome Sequencing Platform;
RG   Broad Institute Whole Genome Assembly Team;
RA   Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA   Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA   Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA   Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA   Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA   Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA   Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA   Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA   Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA   Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT   "Genome sequence, comparative analysis, and population genetics of the
RT   domestic horse.";
RL   Science 326:865-867(2009).
RN   [2] {ECO:0000313|Ensembl:ENSECAP00000000156.3}
RP   IDENTIFICATION.
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000000156.3};
RG   Ensembl;
RL   Submitted (NOV-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   AlphaFoldDB; F7CCK6; -.
DR   STRING; 9796.ENSECAP00000000156; -.
DR   PaxDb; 9796-ENSECAP00000000156; -.
DR   Ensembl; ENSECAT00000000214.3; ENSECAP00000000156.3; ENSECAG00000000204.3.
DR   VGNC; VGNC:24006; TESK1.
DR   GeneTree; ENSGT00940000157807; -.
DR   HOGENOM; CLU_018577_0_0_1; -.
DR   InParanoid; F7CCK6; -.
DR   OMA; SPPTWGD; -.
DR   OrthoDB; 5474815at2759; -.
DR   TreeFam; TF318014; -.
DR   Proteomes; UP000002281; Chromosome 25.
DR   Bgee; ENSECAG00000000204; Expressed in synovial membrane of synovial joint and 23 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:0051496; P:positive regulation of stress fiber assembly; IBA:GO_Central.
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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   PANTHER; PTHR46485:SF3; DUAL SPECIFICITY TESTIS-SPECIFIC PROTEIN KINASE 1; 1.
DR   PANTHER; PTHR46485; LIM DOMAIN KINASE 1; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   3: Inferred from homology;
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002281}.
FT   DOMAIN          1..257
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          267..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          368..464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          476..510
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..22
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        435..464
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   571 AA;  61189 MW;  D5B4330792D4A0FF CRC64;
     MAGERPPLRG PGPGPGEAPG DGPPGPGGAG GGPGRGRPSS YRALRSAVSS LARVDDFHCA
     EKIGAGFFSE VYKYMNGGTL EQLLSSPEPL SWPVRLRLAL DIARGLRYLH AKGVFHRDLT
     SKNCLIRRED RGFTAVVGDF GLAEKIPVYR EGARKEPLAV VGSPYWMAPE VLRGELYDEK
     ADVFAFGIVL CELIARVPAD PDYLPRTEDF GLDVPAFRSL VGDDCPLPFL LLAIHCCSME
     PSTRAPFTEI TQHLEWILEQ LPEPAPLPRA PLTHKQGSVP RGGPSATLPR PDPRLSRSRS
     DLFLPPSPES PPNWGDNLTR VNPFSLREDL RGGKIKLLDT PSKLVAPLPL VPPSPLPSTQ
     LPLVTTPETL VQPGTPARRC RSLPSSPELP RRMETALPGP GPPAVGPSVE ERMECEGSSP
     EPEPPGPAPQ PPLATATDNF ISTCSSASRP WSSRSGAPLN NNPPAVVVNS PQAWAGESWN
     RAQHSLPRAA ALERTEPSPP PSAPRESDEG LPCPGCCLGP FSFGFLSMCP RPTPAVARYR
     NLNCEAGSLL CHRGHHAKPP TPSLQLPGAR S
//
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