ID H9GI94_ANOCA Unreviewed; 693 AA.
AC H9GI94;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 3.
DT 27-MAR-2024, entry version 73.
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|Ensembl:ENSACAP00000011679.4};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000011679.4, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000011679.4}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000011679.4};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000011679.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_003228952.1; XM_003228904.3.
DR RefSeq; XP_008120994.1; XM_008122787.2.
DR RefSeq; XP_008120995.1; XM_008122788.2.
DR AlphaFoldDB; H9GI94; -.
DR STRING; 28377.ENSACAP00000011679; -.
DR Ensembl; ENSACAT00000011920.4; ENSACAP00000011679.4; ENSACAG00000011848.4.
DR GeneID; 100563762; -.
DR KEGG; acs:100563762; -.
DR CTD; 10298; -.
DR eggNOG; KOG0578; Eukaryota.
DR GeneTree; ENSGT00940000159792; -.
DR HOGENOM; CLU_000288_26_6_1; -.
DR InParanoid; H9GI94; -.
DR OrthoDB; 460351at2759; -.
DR TreeFam; TF105352; -.
DR Proteomes; UP000001646; Unplaced.
DR Bgee; ENSACAG00000011848; Expressed in ovary and 11 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:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0060996; P:dendritic spine development; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IEA:Ensembl.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
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 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000001646}.
FT DOMAIN 11..24
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT DOMAIN 423..674
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 128..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..388
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 453
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 693 AA; 77912 MW; EDB8B266E1669886 CRC64;
MFSKKKKRIE ISAPSNFEHR VHTGYDQQEQ KFTGLPRQWQ GIIEESAKRP KPLIDPVCIT
AVQSGSQKTI VRGNKASKDG SLAWLLDEFE NMSVSRSNSL RRDSPPFPPR HDHLYQENGL
IEARPHHYHH HQEDAGGGRG KEPKERNRHV AKSEPPEQSK EPRSKDDRTP GKSHQPSGHH
RPPPPEYHNK PAPDHHHHRH RAHDRDGRKE PPDRVVRRER PDVPDKRPKS SYTGEASPQS
PREKRPLSGP NIRTPNIPVS EGVMKTAQQT GRPFNTYPRA DTDPVRGAQG EHRPGKPQET
ASNGPLSGNI SSSRVPPSVP PRSRIPEVPH AGLSQHASDP HLTHIPGHPP SYSPPQPPSG
PPPQHLPPQP QQQPPPLGPS PPAPQQQQHQ PRSPQREPQR VSHEQFRAAL QMVVDPGDPR
TYLDNFIKIG EGSTGIVCIA TVKSTGKLVA VKKMDLRKQQ RRELLFNEVV IMRDYQHENV
VEMYNSYLVG DELWVVMEFL EGGALTDIVT HTRMNEEQIA AVCLSVLKAL SVLHAQGVIH
RDIKSDSILL THDGRVKLSD FGFCAQVNKE VPRRKSLVGT PYWMAPELIS RLPYGPEVDI
WSLGVMVIEM VDGEPPYFNE PPLKAMKMIR DNLPPKLKNL HKVSPSLKGF LDRLLVRDPA
QRATANELLK HPFLGKAGPP SCIVPLMRQN RMR
//
