ID I2CWB1_MACMU Unreviewed; 594 AA.
AC I2CWB1;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=PAK4 {ECO:0000313|EMBL:AFJ71246.1};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|EMBL:AFJ71246.1};
RN [1] {ECO:0000313|EMBL:AFJ71246.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Orbital {ECO:0000313|EMBL:AFJ71246.1};
RX PubMed=25319552; DOI=10.1186/1745-6150-9-20;
RA Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X., Pandey S.,
RA Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P., Tharp G.K.,
RA Marcais G., Roberts M., Ferguson B., Fox H.S., Treangen T., Salzberg S.L.,
RA Yorke J.A., Norgren R.B.Jr.;
RT "A new rhesus macaque assembly and annotation for next-generation
RT sequencing analyses.";
RL Biol. Direct 9:20-20(2014).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; JV635906; AFJ71246.1; -; mRNA.
DR AlphaFoldDB; I2CWB1; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01093; CRIB_PAK_like; 1.
DR Gene3D; 3.90.810.10; CRIB domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR036936; CRIB_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR033923; PAK_BD.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR PANTHER; PTHR48015; SERINE/THREONINE-PROTEIN KINASE TAO; 1.
DR PANTHER; PTHR48015:SF17; SERINE_THREONINE-PROTEIN KINASE PAK 4; 1.
DR Pfam; PF00786; PBD; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00285; PBD; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50108; CRIB; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Kinase {ECO:0000313|EMBL:AFJ71246.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Transferase {ECO:0000313|EMBL:AFJ71246.1}.
FT DOMAIN 11..24
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT DOMAIN 324..575
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 95..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..296
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 354
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 594 AA; 64360 MW; 6D28EE859AC3EA54 CRC64;
MFGKRKKRVE ISAPSNFEHR VHTGFDQHEQ KFTGLPRQWQ SLIEESARRP KPLIDPACIT
SIQPGAPKTI VRGSKGAKDG ALTLLLDEFE NMSVTRSNSL RRDSPPPPAR ARQENGMPEE
PATTARGGPG KAGSQGRIAS HSEAGGGSGD RRRVGPEKRP KSSREGSGGP QEPSRDKRPL
SGPDVGTPQP AGLASGAKLA AGRPFNTYPR ADTDHPSRGA QGEPHDVAPN GPSAGGLAVP
QSSSSSSRPP TRARGAPSPG VLGPHASEPQ LAPPAHTPAA PAAPAVPGPP GPRSPQREPQ
RVSHEQFRAA LQLVVDPGDP RSYLDNFIKI GEGSTGIVCI ATVRSSGKLV AVKKMDLRKQ
QRRELLFNEV VIMRDYQHEN VVEMYNSYLV GDELWVVMEF LEGGALTDIV THTRMNEEQI
AAVCLAVLQA LSVLHAQGVI HRDIKSDSIL LTHDGRVKLS DFGFCAQVSK EVPRRKSLVG
TPYWMAPELI SRLPYGPEVD IWSLGIMVIE MVDGEPPYFN EPPLKAMKMI RDNLPPRLKN
LHKVSPSLKG FLDRLLVRDP AHRATAAELL KHPFLAKAGP PASIVPLMRQ NRTR
//
