ID   B5DF62_RAT              Unreviewed;       593 AA.
AC   B5DF62;
DT   14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2008, sequence version 1.
DT   02-SEP-2026, entry version 131.
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:ENSRNOP00000026966.5,
GN   ECO:0000313|RGD:1307705};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000026966.5, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0007829|PubMed:16641100}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA   Hoffert J.D., Pisitkun T., Wang G., Shen R.F., Knepper M.A.;
RT   "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT   regulation of aquaporin-2 phosphorylation at two sites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN   [2] {ECO:0007829|PubMed:22673903}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
RN   [3] {ECO:0000313|Ensembl:ENSRNOP00000026966.5}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000026966.5};
RA   Doris P.A., Kalbfleisch T., Li K., Howe K., Wood J.;
RT   "GRCr8: a new rat reference genome assembly contstructed from accurate long
RT   reads and long range scaffolding.";
RL   Submitted (JAN-2024) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|Ensembl:ENSRNOP00000026966.5}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000026966.5};
RG   Ensembl;
RL   Submitted (JAN-2026) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC         H(+); 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         Evidence={ECO:0000256|ARBA:ARBA00048679};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00047899};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. STE20 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008874}.
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DR   RefSeq; NP_001099708.1; NM_001106238.1.
DR   RefSeq; XP_063139397.1; XM_063283327.1.
DR   AlphaFoldDB; B5DF62; -.
DR   SMR; B5DF62; -.
DR   FunCoup; B5DF62; 2858.
DR   STRING; 10116.ENSRNOP00000076081; -.
DR   iPTMnet; B5DF62; -.
DR   PhosphoSitePlus; B5DF62; -.
DR   jPOST; B5DF62; -.
DR   PaxDb; 10116-ENSRNOP00000076081; -.
DR   PeptideAtlas; B5DF62; -.
DR   Ensembl; ENSRNOT00000026966.8; ENSRNOP00000026966.5; ENSRNOG00000019883.9.
DR   GeneID; 292756; -.
DR   KEGG; rno:292756; -.
DR   UCSC; RGD:1307705; rat.
DR   AGR; RGD:1307705; -.
DR   CTD; 10298; -.
DR   RGD; 1307705; Pak4.
DR   eggNOG; KOG0578; Eukaryota.
DR   GeneTree; ENSGT00940000159792; -.
DR   HOGENOM; CLU_000288_26_6_1; -.
DR   OMA; QRDQPGD; -.
DR   OrthoDB; 1022360at2759; -.
DR   Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR   Reactome; R-RNO-9013404; RAC2 GTPase cycle.
DR   Reactome; R-RNO-9013406; RHOQ GTPase cycle.
DR   Reactome; R-RNO-9013407; RHOH GTPase cycle.
DR   Reactome; R-RNO-9013408; RHOG GTPase cycle.
DR   Reactome; R-RNO-9013420; RHOU GTPase cycle.
DR   Reactome; R-RNO-9013423; RAC3 GTPase cycle.
DR   Reactome; R-RNO-9013424; RHOV GTPase cycle.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000019883; Expressed in stomach and 19 other cell types or tissues.
DR   ExpressionAtlas; B5DF62; baseline and differential.
DR   GO; GO:0030054; C:cell junction; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004672; F:protein kinase activity; ISO:RGD.
DR   GO; GO:0106310; F:protein serine kinase activity; ISO:RGD.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:RGD.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:RGD.
DR   GO; GO:0009267; P:cellular response to starvation; IBA:GO_Central.
DR   GO; GO:0060996; P:dendritic spine development; ISO:RGD.
DR   GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; ISO:RGD.
DR   GO; GO:0010897; P:negative regulation of triglyceride catabolic process; ISO:RGD.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; ISO:RGD.
DR   GO; GO:0120183; P:positive regulation of focal adhesion disassembly; ISO:RGD.
DR   GO; GO:0050821; P:protein stabilization; ISO:RGD.
DR   GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
DR   CDD; cd01093; CRIB_PAK_like; 1.
DR   FunFam; 1.10.510.10:FF:000073; Non-specific serine/threonine protein kinase; 1.
DR   FunFam; 3.30.200.20:FF:000141; Non-specific serine/threonine protein kinase; 1.
DR   FunFam; 3.90.810.10:FF:000002; Non-specific serine/threonine protein kinase; 1.
DR   Gene3D; 3.90.810.10; CRIB domain; 1.
DR   Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 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; IPR051931; PAK3-like.
DR   InterPro; IPR033923; PAK_BD.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   PANTHER; PTHR45832:SF9; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR   PANTHER; PTHR45832; SERINE/THREONINE-PROTEIN KINASE SAMKA-RELATED-RELATED; 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   1: Evidence at protein level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:B5DF62};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          11..24
FT                   /note="CRIB"
FT                   /evidence="ECO:0000259|PROSITE:PS50108"
FT   DOMAIN          323..574
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          95..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          128..303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..164
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        184..195
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..258
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        267..280
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        281..292
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..303
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         353
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   593 AA;  64750 MW;  705F68AE83264A87 CRC64;
     MFGKKKKRVE ISAPSNFEHR VHTGFDQHEQ KFTGLPRQWQ SLIEESARRP KPLIDPACIT
     SIQPGAPKTI VRGSKGAKDG ALTLLLDEFE NMSVTRSNSL RRESPPPPAR AHQENGMLEE
     RAALARMAPD KAGGRGRATG HSEAGSGSGD RRRVGPEKRP KSSREGPGGP QEVSRDKRPL
     SGPDVSTPQP GSLASETKLA AGRPFNTYPR ADTDHPPRGT QGEPHTMAPN GPSAIGLAAP
     QSSSSSRPPT RARGAPSPGV LGPHASEPQL APPARALAAP AVPPAPGPPG PRSPQREPQR
     VSHEQFRAAL QLVVDPGDPR SYLDNFIKIG EGSTGIVCIA TVRSSGKLVA VKKMDLRKQQ
     RRELLFNEVV IMRDYRHENV VEMYNSYLVG DELWVVMEFL EGGALTDIVT HTRMNEEQIA
     AVCLAVLQAL SVLHAQGVIH RDIKSDSILL THDGRVKLSD FGFCAQVSKE VPRRKSLVGT
     PYWMAPELIS RLPYGPEVDI WSLGVMVIEM VDGEPPYFNE PPLKAMKMIR DNLPPRLKNL
     HKASPSLKGF LDRLLVRDPA QRATAAELLK HPFLTKAGPP ASIVPLMRQH RNR
//