PAK3_XENLA
ID PAK3_XENLA Reviewed; 564 AA.
AC Q8AXB4;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Serine/threonine-protein kinase PAK 3;
DE EC=2.7.11.1;
DE AltName: Full=p21-activated kinase 3;
DE Short=PAK-3;
GN Name=pak3;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=12456650; DOI=10.1093/emboj/cdf644;
RA Souopgui J., Solter M., Pieler T.;
RT "XPak3 promotes cell cycle withdrawal during primary neurogenesis in
RT Xenopus laevis.";
RL EMBO J. 21:6429-6439(2002).
RN [2]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=24095902; DOI=10.1016/j.ydbio.2013.09.028;
RA Martinez-De Luna R.I., Ku R.Y., Lyou Y., Zuber M.E.;
RT "Maturin is a novel protein required for differentiation during primary
RT neurogenesis.";
RL Dev. Biol. 384:26-40(2013).
CC -!- FUNCTION: Serine/threonine protein kinase that plays a role in a
CC variety of different signaling pathways. Involved in early neuronal
CC development; required for cell cycle exit and differentiation of
CC primary neurons. May be required for the formation of dendritic spines
CC and excitatory synapses (By similarity). Cooperates synergistically
CC with mturn to promote primary neural differentiation within the neural
CC plate. Involved in the cement gland formation.
CC {ECO:0000250|UniProtKB:Q61036, ECO:0000269|PubMed:12456650,
CC ECO:0000269|PubMed:24095902}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed from the egg to the tailbud stage
CC embryo. Expressed at late gastrula/early neurula stages of development
CC within the posterior neuroectoderm. Expressed in primary neurons as
CC they differentiate in the neural plate at stage 14.5 in the area of the
CC trigeminal placodes. Expressed in the cement gland at stage 17.
CC Expressed during later phases in the notochord in tissues derived from
CC dorsolateral cranial placodes. {ECO:0000269|PubMed:12456650,
CC ECO:0000269|PubMed:24095902}.
CC -!- INDUCTION: Up-regulated by the proneural transcription factors Neurog2,
CC Neurod1 and Ebf3. Down-regulated by the Notch pathway.
CC {ECO:0000269|PubMed:12456650}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein causes
CC inhibition of neuronal differentiation and an accumulation of neuronal
CC progenitor cells in the anterior neural plate.
CC {ECO:0000269|PubMed:24095902}.
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; AF485330; AAN52281.1; -; mRNA.
DR RefSeq; NP_001079232.1; NM_001085763.1.
DR AlphaFoldDB; Q8AXB4; -.
DR SMR; Q8AXB4; -.
DR MaxQB; Q8AXB4; -.
DR GeneID; 378493; -.
DR KEGG; xla:378493; -.
DR CTD; 378493; -.
DR Xenbase; XB-GENE-961767; pak3.L.
DR OrthoDB; 757766at2759; -.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 378493; Expressed in internal ear and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IEA:UniProtKB-KW.
DR GO; GO:0090017; P:anterior neural plate formation; IDA:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0071570; P:cement gland development; IMP:UniProtKB.
DR GO; GO:0007406; P:negative regulation of neuroblast proliferation; IMP:UniProtKB.
DR GO; GO:0021990; P:neural plate formation; IMP:UniProtKB.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0051726; P:regulation of cell cycle; IDA:UniProtKB.
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 ATP-binding; Cell cycle; Cytoplasm; Developmental protein; Differentiation;
KW Growth arrest; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..564
FT /note="Serine/threonine-protein kinase PAK 3"
FT /id="PRO_0000424910"
FT DOMAIN 70..83
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT DOMAIN 288..539
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..70
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..287
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 172..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..70
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 COMPBIAS 233..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 407
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 294..302
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 317
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 564 AA; 62767 MW; 2756B9DB4AB4A0D8 CRC64;
MSDSVDIEEK PPAPPLRMNS NNRDSSALNH CSKPLPMAPE EKNKKARLRS IFPGGGDKTN
KKKEKERPEI SLPSDFEHTI HVGFDAVTGE FTPDLCGSQM GTGKLPEGIP EQWARLLQTS
NITKLEQKKN PQAVLDVLKF YDSKETVNNQ KYMSFTSGDK SAHGYIAAHS LNAKTASEPP
LAPPVSEEED EEEEEEEDDN EPPPVIAPRP EHTKSIYTRS VIEPVALTAP AKEASTSPVT
PQPENSNSST STLYRNTDRQ RKKSKMTDEE ILEKLRSIVS VGDPKKKYTR FEKIGQGASG
TVYTAIDIAT GQEVAIKQMN LQQQPKKELI INEILVMREN KNPNIVNYLD SYLVGDELWV
VMEYLAGGSL TDVVTETCMD EGQIAAVCRE CLQALDFLHS NQVIHRDIKS DNILLGMDGS
VKLTDFGFCA QITPEQSKRS TMVGTPYWMA PEVVTRKAYG PKVDIWSLGI MAIEMVEGEP
PYLNENPLRA LYLIATNGTP ELQNPERLSA IFRDFLNRCL EMDVDRRGSA KELLQHPFLK
IAKPLSSLTP LIIAAKEAIK NSSR
