ID   PAK6_PONAB              Reviewed;         681 AA.
AC   Q5R8Z4;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Serine/threonine-protein kinase PAK 6;
DE            EC=2.7.11.1;
DE   AltName: Full=p21-activated kinase 6;
DE            Short=PAK-6;
GN   Name=PAK6;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Serine/threonine protein kinase that plays a role in the
CC       regulation of gene transcription. The kinase activity is induced by
CC       various effectors including AR or MAP2K6/MAPKK6. Phosphorylates the
CC       DNA-binding domain of androgen receptor/AR and thereby inhibits AR-
CC       mediated transcription. Inhibits also ESR1-mediated transcription. May
CC       play a role in cytoskeleton regulation by interacting with IQGAP1. May
CC       protect cells from apoptosis through phosphorylation of BAD (By
CC       similarity). {ECO:0000250}.
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   -!- SUBUNIT: Interacts tightly with GTP-bound but not GDP-bound CDC42/p21
CC       and RAC1. Interacts with the androgen receptor AR. Interacts with
CC       IQGAP1 and PPM1B (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC       Note=Cotranslocates into nucleus with AR in response to androgen
CC       induction. {ECO:0000250}.
CC   -!- PTM: Autophosphorylated. Phosphorylated by MAP2K6/MAPKK6, leading to
CC       PAK6 activation (By similarity). {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; CR859603; CAH91766.1; -; mRNA.
DR   RefSeq; NP_001126024.1; NM_001132552.1.
DR   RefSeq; XP_009247955.1; XM_009249680.1.
DR   RefSeq; XP_009247956.1; XM_009249681.1.
DR   RefSeq; XP_009247957.1; XM_009249682.1.
DR   RefSeq; XP_009247958.1; XM_009249683.1.
DR   AlphaFoldDB; Q5R8Z4; -.
DR   SMR; Q5R8Z4; -.
DR   STRING; 9601.ENSPPYP00000007186; -.
DR   Ensembl; ENSPPYT00000007485; ENSPPYP00000007186; ENSPPYG00000006346.
DR   GeneID; 100172971; -.
DR   KEGG; pon:100172971; -.
DR   CTD; 56924; -.
DR   eggNOG; KOG0578; Eukaryota.
DR   GeneTree; ENSGT00940000156528; -.
DR   HOGENOM; CLU_000288_26_6_1; -.
DR   InParanoid; Q5R8Z4; -.
DR   OMA; HRQMPWP; -.
DR   OrthoDB; 757766at2759; -.
DR   TreeFam; TF105352; -.
DR   Proteomes; UP000001595; Chromosome 15.
DR   GO; GO:0030054; C:cell junction; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP 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:0007612; P:learning; IEA:Ensembl.
DR   GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR   GO; GO:0007613; P:memory; IEA:Ensembl.
DR   GO; GO:0140058; P:neuron projection arborization; IEA:Ensembl.
DR   GO; GO:1990138; P:neuron projection extension; IEA:Ensembl.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   CDD; cd01093; CRIB_PAK_like; 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; IPR035066; PAK6.
DR   InterPro; IPR033923; PAK_BD.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   PANTHER; PTHR45832:SF3; PTHR45832:SF3; 1.
DR   Pfam; PF00786; PBD; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00285; PBD; 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.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN           1..681
FT                   /note="Serine/threonine-protein kinase PAK 6"
FT                   /id="PRO_0000278118"
FT   DOMAIN          12..25
FT                   /note="CRIB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT   DOMAIN          407..658
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          26..406
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          200..256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          268..355
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        275..289
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..355
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        526
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         413..421
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         436
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         560
FT                   /note="Phosphoserine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   681 AA;  74950 MW;  73655289ACEAD66F CRC64;
     MFRKKKKKRP EISAPQNFQH RVHTSFDPKE GKFVGLPPQW QNILDTLRRP KPVVDPSRIT
     RVQLQPMKTV VRGSTMPMDG YISGLLNDIQ KLSVISSNTL RGRSPTSRRR AQSLGLLGDE
     HWATDPDMYL QSPQSERTDP HGLYLSCNGG TPAGHKQMPW PEPQSPRVLP NGLAAKAQSL
     GPAEFQGASQ RCLQLGACLQ SSPPGASPPT GTNRRGMKAA KHGSEEARPQ SCLVGSATGR
     PGGEGSPSPK TRESSLKRRL FRSMFLSTAA TAPPSSSKPG PPPQSKPNSS FRPPQKDNPP
     SLVAKAQSLP SDQPVGTFSP LTTSDTSSPQ KSLRTAPATG QLPGRSSPAG SPRTWHAQIS
     TSNLYLPQDP TVAKGALAGE DTGVVTHEQF KAALRMVVDQ GDPRLLLDSY VKIGEGSTGI
     VCLAREKHSG RQVAVKMMDL RKQQRRELLF NEVVIMRDYQ HFNVVEMYKS YLVGEELWVL
     MEFLQGGALT DIVSQVRLNE EQIATVCEAV LQALAYLHAQ GVIHRDIKSD SILLTLDGRV
     KLSDFGFCAQ ISKDVPKRKS LVGTPYWMAP EVISRSLYAT EVDIWSLGIM VIEMVDGEPP
     YFSDSPVQAM KRLRDSPPPK LKNSHKVSPV LRDFLERMLV RDPQERATAQ ELLDHPFLLQ
     TGLPECLVPL IQLYRKQTST C