STK10_BOVIN
ID STK10_BOVIN Reviewed; 966 AA.
AC E1BK52;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 3.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Serine/threonine-protein kinase 10;
DE EC=2.7.11.1;
GN Name=STK10;
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 GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
CC -!- FUNCTION: Serine/threonine-protein kinase involved in regulation of
CC lymphocyte migration. Phosphorylates MSN, and possibly PLK1. Involved
CC in regulation of lymphocyte migration by mediating phosphorylation of
CC ERM proteins such as MSN. Acts as a negative regulator of MAP3K1/MEKK1.
CC May also act as a cell cycle regulator by acting as a polo kinase
CC kinase: mediates phosphorylation of PLK1 in vitro; however such data
CC require additional evidences in vivo (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=2.7.11.1;
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=2.7.11.1;
CC -!- ACTIVITY REGULATION: Inhibited by the pyrrole-indolinone inhibitor
CC SU11274 (K00593): intercalates between the ATP-binding Lys-65 and
CC alpha-C glutamate (Glu-81), resulting in a partial disordering of the
CC lysine side chain. Also specifically inhibited by erlotinib. Slightly
CC inhibited by gefitinib (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; homodimerization is required for activation segment
CC autophosphorylation. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
CC -!- PTM: Autophosphorylates following homodimerization, leading to
CC activation of the protein. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
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DR EMBL; AAFC03041244; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03048417; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03048418; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03048420; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; E1BK52; -.
DR SMR; E1BK52; -.
DR STRING; 9913.ENSBTAP00000023199; -.
DR PaxDb; E1BK52; -.
DR PRIDE; E1BK52; -.
DR eggNOG; KOG0579; Eukaryota.
DR HOGENOM; CLU_001965_3_0_1; -.
DR InParanoid; E1BK52; -.
DR OMA; CHMLVEN; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:2000401; P:regulation of lymphocyte migration; ISS:UniProtKB.
DR CDD; cd06644; STKc_STK10; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR022165; PKK.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR042743; STK10_STKc.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF12474; PKK; 2.
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 3: Inferred from homology;
KW ATP-binding; Cell cycle; Cell membrane; Coiled coil; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..966
FT /note="Serine/threonine-protein kinase 10"
FT /id="PRO_0000414710"
FT DOMAIN 36..294
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 175..224
FT /note="Activation segment"
FT /evidence="ECO:0000250"
FT REGION 318..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 941..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 571..945
FT /evidence="ECO:0000255"
FT COMPBIAS 361..375
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..860
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..957
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 157
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 42..50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94804"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9PTG8"
FT MOD_RES 185
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 191
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:O94804"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94804"
FT MOD_RES 449
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94804"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94804"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94804"
FT MOD_RES 512
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94804"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94804"
SQ SEQUENCE 966 AA; 111615 MW; B43C96AE39E1B9AA CRC64;
MAFANFRRIL RLSTFEKRKS REYEHVRRDL DPNEVWEIVG ELGDGAFGKV YKAKNKETGA
LAAAKVIETN SEEELEDYIV EIEILATCDH PYIVKLLGAY YYDGKLWIMI EFCPGGAVDA
IMLELDRGLT EPQIQVVCRQ MLEALTFLHG KKIIHRDLKA GNVLMTLEGD IRLADFGVSA
KNLKTLQKRD SFIGTPYWMA PEVVMCETMK DTPYDYKADI WSLGITLIEM AQIEPPHHEL
NPMRVLLKIA KSDPPTLLSP SKWSAEFRDF LKTALDKNPE TRPSAAQLLE HPFVSSVTSN
KALRELVAEA KAEVMEEIED GRDEGDEEDA VEAASPLENH TRDSSEVSQL SIDADKLLKE
SPFTPPPPSQ PQDGANGPSE PPGHGALPAT SPLDVAPGNE NGQAVPVPLR KFRPVSMGAR
IQVSEEKQAA DQGGDLSPAA SRSQKASQSR PNSSALETLR SELTNGSLEL PTPGAQSLSK
RDSDCGSVST SGSTDFGTSL SADMSVNKES GSLSIKDSRL HNKTLKRTRK FVVDGVEVSI
TTSKIISEDE KKDEEMRFLR RQELRELRLL QKEEHRNQTQ LSSKHELQLE QMHKRFEQEI
NAKKKFFDIE LENLERQQKQ QVEKMEQDHA VRRREEAKRI RLEQERDYAK FQEQLKLMKK
EVKNEVEKLP RQQRKESMKQ KMEEHTQKKQ LLDRDFLAKQ KEDLELAMKR ITADNRREIC
DKERECLTRK QELLRDREAA LWEMEEHHLQ ERHQLVKQQL KDQYFLQRHE LLRKHEKERE
QMQRYNQRMI EQLKVRQQQE KARLPKIQRS EGKTRMAMYK KSLHINGGGS AAEQREKIKQ
FSQQEEKRQK AERLQQQQKH ENQMRDMLAQ CESNMSELQQ LQNEKCHLLI EHETQKLKAL
DESHNQNLKE WRDKLRPRKK ALEEDLNQKK REQEMFFKMN EESECANPTS PNKVTKFFPY
SSADAA
