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Database: UniProt
Entry: A0A287B9M7_PIG
LinkDB: A0A287B9M7_PIG
Original site: A0A287B9M7_PIG 
ID   A0A287B9M7_PIG          Unreviewed;       735 AA.
AC   A0A287B9M7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2022, sequence version 3.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Ribosomal protein S6 kinase {ECO:0000256|PIRNR:PIRNR000606};
DE            EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR000606};
GN   Name=RPS6KA2 {ECO:0000313|Ensembl:ENSSSCP00000053197.3,
GN   ECO:0000313|VGNC:VGNC:92441};
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:ENSSSCP00000053197.3, ECO:0000313|Proteomes:UP000008227};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000053197.3, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000053197.3,
RC   ECO:0000313|Proteomes:UP000008227};
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSSCP00000053197.3}
RP   IDENTIFICATION.
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|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   AlphaFoldDB; A0A287B9M7; -.
DR   Ensembl; ENSSSCT00000041914.3; ENSSSCP00000053197.3; ENSSSCG00000004022.5.
DR   VGNC; VGNC:92441; RPS6KA2.
DR   GeneTree; ENSGT00940000159956; -.
DR   Proteomes; UP000008227; Chromosome 1.
DR   Bgee; ENSSSCG00000004022; Expressed in prefrontal cortex and 38 other cell types or tissues.
DR   ExpressionAtlas; A0A287B9M7; baseline and differential.
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:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
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:SF213; RIBOSOMAL PROTEIN S6 KINASE ALPHA-2; 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:UP000008227};
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          75..334
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          332..401
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   DOMAIN          428..674
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        200
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000606-50"
FT   ACT_SITE        539
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000606-50"
FT   BINDING         81..89
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000606-51"
FT   BINDING         107
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000606-51,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         434..442
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000606-51"
FT   BINDING         457
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000606-51,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   735 AA;  82141 MW;  F0DF6D184040CFDF CRC64;
     MEENRGGTHG NRGRRGGPGP GRGAQHRRHG GRGQGGRHLA GGQGLSRLEE EGVVKEVDIS
     HHVKAGFEKA DPSQFELLKV LGQGSYGKVF LVRKVKGSDA GQLYAMKVLK KATLKVRDRV
     RSKMERDILA EVNHPFIVKL HYAFQTEGKL YLILDFLRGG DLFTRLSKEV MFTEEDVKFY
     LAELALALDH LHGLGIIYRD LKPENILLDE EGHIKITDFG LSKEAIDHDK RAYSFCGTIE
     YMAPEVVNRR GHTQSADWWS FGVLMFEMLT GSLPFQGKDR KETMALVLKA KLGMPQFLSA
     EAQSLLRALF KRNPCNRLGG ADAVPPRAPQ RPSASPQKLY RKEIKPPFKP AVGRPEDTFH
     FDPEFTTRTP TDSPGVPPSA NAHHLFRGFS FVASSLVQEP SQQDLHKATV HPIVQQLHGN
     NIHFTDGYEI KEDIGVGSYS VCKRCVHKAT DAEYAVKIID KSKRDPSEEI EILLRYGQHP
     NIITLKDVYD DGKCVYLVME LMRGGELLDR ILRQRCFSER EASDVLCVTP LPLQVVHRDL
     KPSNILYMDE SGNPESIRIC DFGFAKQLRA ENGLLMTPCY TANFVAPEVL KRQGYDAACD
     IWSLGILLYT MLSAAGITHG CFPAGTNDTP GSLRALGGNW DSISDAAKDV VSKMLHVDPH
     QRLTAVQVLK HPWIVNREYL SQNQLSRQDV HLVKGAMAAT YFALNRTPQA PRLEPVLSSS
     LAQRRGMKRL TSTRL
//
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