ID M3WAV0_FELCA Unreviewed; 744 AA.
AC M3WAV0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 3.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Ribosomal protein S6 kinase {ECO:0000256|PIRNR:PIRNR000606};
DE EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR000606};
GN Name=RPS6KA6 {ECO:0000313|Ensembl:ENSFCAP00000008465.5,
GN ECO:0000313|VGNC:VGNC:64759};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000008465.5, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000008465.5, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000008465.5,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000008465.5, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000008465.5,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000008465.5}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000008465.5};
RG Ensembl;
RL Submitted (SEP-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|PIRNR:PIRNR000606};
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|PIRNR:PIRNR000606};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRNR:PIRNR000606};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. S6 kinase subfamily.
CC {ECO:0000256|ARBA:ARBA00009804, ECO:0000256|PIRNR:PIRNR000606}.
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DR EMBL; AANG04004376; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M3WAV0; -.
DR STRING; 9685.ENSFCAP00000008465; -.
DR PaxDb; 9685-ENSFCAP00000008465; -.
DR Ensembl; ENSFCAT00000009132.6; ENSFCAP00000008465.5; ENSFCAG00000009130.6.
DR VGNC; VGNC:64759; RPS6KA6.
DR eggNOG; KOG0603; Eukaryota.
DR GeneTree; ENSGT00940000159242; -.
DR HOGENOM; CLU_000288_58_3_1; -.
DR InParanoid; M3WAV0; -.
DR OMA; HSWITCK; -.
DR OrthoDB; 5489497at2759; -.
DR Proteomes; UP000011712; Chromosome X.
DR Bgee; ENSFCAG00000009130; Expressed in embryonic head and 7 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004711; F:ribosomal protein S6 kinase activity; IBA:GO_Central.
DR GO; GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05582; STKc_RSK_N; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR016239; Ribosomal_S6_kinase_II.
DR InterPro; IPR041906; RSK_N.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR PANTHER; PTHR24351:SF246; RIBOSOMAL PROTEIN S6 KINASE ALPHA-6; 1.
DR Pfam; PF00069; Pkinase; 2.
DR Pfam; PF00433; Pkinase_C; 1.
DR PIRSF; PIRSF000606; Ribsml_S6_kin_2; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000606};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000606};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000606};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000011712};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|PIRNR:PIRNR000606};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000606}.
FT DOMAIN 72..329
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 330..399
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 425..682
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT ACT_SITE 197
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000606-50"
FT ACT_SITE 542
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000606-50"
FT BINDING 78..86
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000606-51"
FT BINDING 104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000606-51,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 431..439
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000606-51"
FT BINDING 454
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000606-51,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 744 AA; 83917 MW; C253C6E2C332FE1E CRC64;
MLPFTPQEEL WNQEMEVFGG GASSGEVDGL KMVDEPMEEG EADSCQDEGI VKEIPITHHV
KEGYEKADPA QFELLKVLGQ GSFGKVFLVR KKTGPDAGQL YAMKVLKKAS LKVRDRVRTK
MERDILVEVN HPFIVKLHYA FQTEGKLYLI LDFLRGGDVF TRLSKEVLFT EEDVKFYLAE
LALALDHLHQ LGIVYRDLKP ENILLDEIGH IKLTDFGLSK ESVDQEKKAY SFCGTVEYMA
PEVVNRRGHS QSADWWSYGV LMFEMLTGTL PFQGKDRNET MNMILKAKLG MPQFLSAEAQ
SLLRMLFKRN PANRLGSEGV EEIKRHLFFA NVDWNKLYRR EVQPPFKPAS GKPDDTFCFD
PEFTAKTPKD SPGLPASANA HQLFKGFSFV ATSIAEEYKI TPVTSANVLP IVQINGNSGQ
FAELYELKED IGVGSYSVCK RCIHTATNME FAVKIIDKSK RDPSEEIEIL MRYGQHPNII
TLKDVYDDGR YVYLVTDLMK GGELLDHILK KKCFSEREAS DVLFVIIKTV DYLHCQGVVH
RDLKPSNILY MDESANADSI RICDFGFAKQ LRGENGLLLT PCYTANFVAP EVLMQQGYDA
ACDIWSLGVL FYTMLAGYTP FANGPNDTPE EILLRIGNGK FSLSGGNWDN ISDGAKDLLS
HMLHMDPHQR YTTEQVLKHS WITHRDQLLN DQPNRYDASH VIKGVVVTTC SALTHKTFQP
VLEPVAASNL AQRRSMKKRT STGL
//
