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PAK3_PANTR
ID   PAK3_PANTR              Reviewed;         559 AA.
AC   Q7YQL4;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Serine/threonine-protein kinase PAK 3;
DE            EC=2.7.11.1;
DE   AltName: Full=Beta-PAK;
DE   AltName: Full=p21-activated kinase 3;
DE            Short=PAK-3;
GN   Name=PAK3;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=12777533; DOI=10.1093/molbev/msg134;
RA   Kitano T., Schwarz C., Nickel B., Paeaebo S.;
RT   "Gene diversity patterns at 10 X-chromosomal loci in humans and
RT   chimpanzees.";
RL   Mol. Biol. Evol. 20:1281-1289(2003).
CC   -!- FUNCTION: Serine/threonine protein kinase that plays a role in a
CC       variety of different signaling pathways including cytoskeleton
CC       regulation, cell migration, or cell cycle regulation. Plays a role in
CC       dendrite spine morphogenesis as well as synapse formation and
CC       plasticity. Acts as downstream effector of the small GTPases CDC42 and
CC       RAC1. Activation by the binding of active CDC42 and RAC1 results in a
CC       conformational change and a subsequent autophosphorylation on several
CC       serine and/or threonine residues. Phosphorylates MAPK4 and MAPK6 and
CC       activates the downstream target MAPKAPK5, a regulator of F-actin
CC       polymerization and cell migration. Additionally, phosphorylates
CC       TNNI3/troponin I to modulate calcium sensitivity and relaxation
CC       kinetics of thin myofilaments. May also be involved in early neuronal
CC       development (By similarity). In hippocampal neurons, necessary for the
CC       formation of dendritic spines and excitatory synapses; this function is
CC       dependent on kinase activity and may be exerted by the regulation of
CC       actomyosin contractility through the phosphorylation of myosin II
CC       regulatory light chain (MLC) (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:Q61036}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Activated by binding small G proteins. Binding of
CC       GTP-bound CDC42 or RAC1 to the autoregulatory region releases monomers
CC       from the autoinhibited dimer, enables phosphorylation of Thr-436 and
CC       allows the kinase domain to adopt an active structure (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts tightly with GTP-bound but not GDP-bound CDC42/p21
CC       and RAC1. Shows highly specific binding to the SH3 domains of
CC       phospholipase C-gamma and of adapter protein NCK. Interacts with the C-
CC       terminal of APP. Interacts with ARHGEF6 and ARHGEF7 (By similarity).
CC       Interacts with GIT1 and GIT2 (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:O75914}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- PTM: Autophosphorylated when activated by CDC42/p21. {ECO:0000250}.
CC   -!- PTM: Neddylated. {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; AB102660; BAC81129.1; -; mRNA.
DR   RefSeq; NP_001009039.1; NM_001009039.1.
DR   RefSeq; XP_009437779.1; XM_009439504.2.
DR   RefSeq; XP_009437780.1; XM_009439505.2.
DR   RefSeq; XP_009437781.1; XM_009439506.2.
DR   RefSeq; XP_009437782.1; XM_009439507.2.
DR   RefSeq; XP_009437783.1; XM_009439508.2.
DR   RefSeq; XP_009437785.1; XM_009439510.2.
DR   RefSeq; XP_009437786.1; XM_009439511.2.
DR   RefSeq; XP_009437787.1; XM_009439512.2.
DR   RefSeq; XP_009437788.1; XM_009439513.2.
DR   RefSeq; XP_009437789.1; XM_009439514.2.
DR   RefSeq; XP_009437790.1; XM_009439515.2.
DR   RefSeq; XP_016798113.1; XM_016942624.1.
DR   RefSeq; XP_016798114.1; XM_016942625.1.
DR   AlphaFoldDB; Q7YQL4; -.
DR   SMR; Q7YQL4; -.
DR   STRING; 9598.ENSPTRP00000041645; -.
DR   PaxDb; Q7YQL4; -.
DR   Ensembl; ENSPTRT00000042397; ENSPTRP00000041645; ENSPTRG00000022187.
DR   Ensembl; ENSPTRT00000079025; ENSPTRP00000092335; ENSPTRG00000022187.
DR   GeneID; 450118; -.
DR   KEGG; ptr:450118; -.
DR   CTD; 5063; -.
DR   VGNC; VGNC:10463; PAK3.
DR   eggNOG; KOG0578; Eukaryota.
DR   GeneTree; ENSGT00950000182988; -.
DR   HOGENOM; CLU_000288_26_6_1; -.
DR   InParanoid; Q7YQL4; -.
DR   OrthoDB; 757766at2759; -.
DR   TreeFam; TF105351; -.
DR   Proteomes; UP000002277; Chromosome X.
DR   Bgee; ENSPTRG00000022187; Expressed in pituitary gland and 13 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004708; F:MAP kinase kinase activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   GO; GO:0007409; P:axonogenesis; ISS:UniProtKB.
DR   GO; GO:0016358; P:dendrite development; ISS:UniProtKB.
DR   GO; GO:0060997; P:dendritic spine morphogenesis; ISS:UniProtKB.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR   GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0030833; P:regulation of actin filament polymerization; ISS:UniProtKB.
DR   GO; GO:0050770; P:regulation of axonogenesis; IBA:GO_Central.
DR   GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
DR   CDD; cd01093; CRIB_PAK_like; 1.
DR   CDD; cd06656; STKc_PAK3; 1.
DR   Gene3D; 3.90.810.10; -; 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   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR035063; STK_PAK3.
DR   Pfam; PF00786; PBD; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00285; PBD; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50108; CRIB; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   Allosteric enzyme; ATP-binding; Cytoplasm; Developmental protein; Kinase;
KW   Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; SH3-binding;
KW   Transferase; Ubl conjugation.
FT   CHAIN           1..559
FT                   /note="Serine/threonine-protein kinase PAK 3"
FT                   /id="PRO_0000086471"
FT   DOMAIN          70..83
FT                   /note="CRIB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT   DOMAIN          283..534
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          65..150
FT                   /note="Autoregulatory region"
FT                   /evidence="ECO:0000250"
FT   REGION          65..123
FT                   /note="GTPase-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          84..282
FT                   /note="Linker"
FT   REGION          164..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          228..262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..72
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        184..201
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        402
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         289..297
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         312
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62829"
FT   MOD_RES         50
FT                   /note="Phosphoserine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:Q62829"
FT   MOD_RES         154
FT                   /note="Phosphoserine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:Q62829"
FT   MOD_RES         186
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61036"
FT   MOD_RES         436
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:Q62829"
SQ   SEQUENCE   559 AA;  62310 MW;  BC39AEC6F0A5478B CRC64;
     MSDGLDNEEK PPAPPLRMNS NNRDSSALNH SSKPLPMAPE EKNKKARLRS IFPGGGDKTN
     KKKEKERPEI SLPSDFEHTI HVGFDAVTGE FTPDLYGSQM CPGKLPEGIP EQWARLLQTS
     NITKLEQKKN PQAVLDVLKF YDSKETVNNQ KYMSFTSGDK SAHGYIAAHP SSTKTASEPP
     LAPPVSEEED EEEEEEEDEN EPPPVIAPRP EHTKSIYTRS VVESIASPAV PNKEVTPPSA
     ENANSSTLYR NTDRQRKKSK MTDEEILEKL RSIVSVGDPK KKYTRFEKIG QGASGTVYTA
     LDIATGQEVA IKQMNLQQQP KKELIINEIL VMRENKNPNI VNYLDSYLVG DELWVVMEYL
     AGGSLTDVVT ETCMDEGQIA AVCRECLQAL DFLHSNQVIH RDIKSDNILL GMDGSVKLTD
     FGFCAQITPE QSKRSTMVGT PYWMAPEVVT RKAYGPKVDI WSLGIMAIEM VEGEPPYLNE
     NPLRALYLIA TNGTPELQNP ERLSAVFRDF LNRCLEMDVD RRGSAKELLQ HPFLKLAKPL
     SSLTPLIIAA KEAIKNSSR
 
 
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