ID F6PHH1_HORSE Unreviewed; 764 AA.
AC F6PHH1;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 4.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=NEK4 {ECO:0000313|VGNC:VGNC:20671};
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:ENSECAP00000015599.4, ECO:0000313|Proteomes:UP000002281};
RN [1] {ECO:0000313|Ensembl:ENSECAP00000015599.4, ECO:0000313|Proteomes:UP000002281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000015599.4,
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:ENSECAP00000015599.4}
RP IDENTIFICATION.
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000015599.4};
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=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
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=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC protein kinase family. NIMA subfamily. {ECO:0000256|ARBA:ARBA00010886}.
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DR AlphaFoldDB; F6PHH1; -.
DR STRING; 9796.ENSECAP00000015599; -.
DR PaxDb; 9796-ENSECAP00000015599; -.
DR Ensembl; ENSECAT00000019076.4; ENSECAP00000015599.4; ENSECAG00000017761.4.
DR VGNC; VGNC:20671; NEK4.
DR GeneTree; ENSGT00940000157448; -.
DR HOGENOM; CLU_017439_0_0_1; -.
DR InParanoid; F6PHH1; -.
DR OMA; WQKKREL; -.
DR Proteomes; UP000002281; Chromosome 16.
DR Bgee; ENSECAG00000017761; Expressed in oviduct epithelium and 23 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; 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:0006974; P:DNA damage response; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd08223; STKc_Nek4; 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; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR44899; CAMK FAMILY PROTEIN KINASE; 1.
DR PANTHER; PTHR44899:SF3; SERINE_THREONINE PROTEIN KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
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; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F6PHH1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002281};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 6..261
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 377..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..571
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 764 AA; 85851 MW; 8D6D2318D41D3922 CRC64;
MPLAAYCYLR VVGRGSYGEV TLVRHRRDGR QYVIKKLNLR NASSRERRAA EQEAQLLSQL
KHPNIVTYKE SWEGGDGLLY IVMGFCEGGD LYRKLKEQKG QLLPESQVVE WFVQIAMALQ
YLHEKHILHR DLKTQNVFLT RTNIIKVGDL GIARVLENHC DMASTLIGTP YYMSPELFSN
KPYNYKSDVW ALGCCVYEMA TLKHAFNAKD MNSLVYRIIE GKLPPMPKDY SPELAELIRT
MLSKRPEERP SVRSILRQPY IKRQISLFLE ATKAKTCKNN TKNGDCKSKP VTTVVSGKAE
SNQEVVPFHP HSSEGSKTYV MGEDKCLSQE KLIVVGPLKT PTNLKGHTSK PDMNTTSESL
ATISRVNIDI LPAERRDSSN SLVQENQPRH LDASNELEGK CSISQVKESL QHNTKSSAQP
GNLISTCVSD SVTGEKNDPV KPLQPLNKDQ KPKDQDRVAG ECITEKQDRV YPGLQPHSSG
SEPSLSRQRR QKKREQTEHS GEKRQFQEAP PRLLPSLPTV GKVDDTLTQR DAENRSRVVT
GSVSSSRSSE MSSSKDRPLS ARERRRLKQS QEDIFPSGPS VRRASLSAAG PGKIQEEGQH
SAAGWLSSDC SVAQERKLTR CLSEDELSSS ASSTDKSDGD SREGKGHTNE MSDLLQLMTQ
TLKLDSKESC EDLPVPDPVS EFKLHRKYRD TLVLHGKVAE EAEELHCKEL PSAIMPGSEK
IRRIVEVLRA DVIRGLGIQL LEQVYDLLEE EDELEREINR KVEK
//
