PK2_CAEEL
ID PK2_CAEEL Reviewed; 522 AA.
AC G5EFU0; Q9U3M1;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Serine/threonine-protein kinase pak-2 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q17850};
DE AltName: Full=p21-activated kinase 2 {ECO:0000303|PubMed:17050621};
GN Name=pak-2 {ECO:0000312|WormBase:C45B11.1a};
GN ORFNames=C45B11.1 {ECO:0000312|WormBase:C45B11.1a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:ABF71876.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=17050621; DOI=10.1242/dev.02648;
RA Lucanic M., Kiley M., Ashcroft N., L'Etoile N., Cheng H.J.;
RT "The Caenorhabditis elegans P21-activated kinases are differentially
RT required for UNC-6/netrin-mediated commissural motor axon guidance.";
RL Development 133:4549-4559(2006).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19797046; DOI=10.1534/genetics.109.106880;
RA Locke C.J., Kautu B.B., Berry K.P., Lee S.K., Caldwell K.A., Caldwell G.A.;
RT "Pharmacogenetic analysis reveals a post-developmental role for Rac GTPases
RT in Caenorhabditis elegans GABAergic neurotransmission.";
RL Genetics 183:1357-1372(2009).
CC -!- FUNCTION: Serine/threonine-protein kinase which plays a redundant role
CC with pak-1 in embryogenesis but, in contrast to pak-1, is not involved
CC in commissural axon guidance of ventral cord motoneurons or in distal
CC tip cell (DTC) migration. {ECO:0000269|PubMed:17050621,
CC ECO:0000269|PubMed:19797046}.
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 Evidence={ECO:0000250|UniProtKB:Q17850};
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; Evidence={ECO:0000250|UniProtKB:Q17850};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q17850};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q17850};
CC Note=Divalent cations such as magnesium or manganese.
CC {ECO:0000250|UniProtKB:Q17850};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:C45B11.1a};
CC IsoId=G5EFU0-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:C45B11.1b};
CC IsoId=G5EFU0-2; Sequence=VSP_057792;
CC -!- TISSUE SPECIFICITY: Expressed in pharynx, vulva and spermatheca. Unlike
CC other p21-activated kinases, expression is not detected in neurons.
CC {ECO:0000269|PubMed:17050621}.
CC -!- DISRUPTION PHENOTYPE: Low level of embryonic lethality (< 15 percent)
CC which is suppressed by simultaneous RNAi-mediated knockdown of max-2
CC (PubMed:19797046). In pak-1 and pak-2 double mutants, defects in
CC embryogenesis and L1 stage lethality. The few animals reaching
CC adulthood are smaller but have normal ventral cord commissural
CC motoneuron axonal guidance and are relatively coordinated
CC (PubMed:17050621, PubMed:19797046). {ECO:0000269|PubMed:17050621,
CC ECO:0000269|PubMed:19797046}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
CC -!- CAUTION: Despite the gene name, this is not the ortholog of vertebrate
CC PAK2. {ECO:0000305}.
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DR EMBL; DQ523831; ABF71876.1; -; mRNA.
DR EMBL; BX284605; CAA98429.2; -; Genomic_DNA.
DR EMBL; BX284605; CAA98433.2; -; Genomic_DNA.
DR PIR; T19952; T19952.
DR PIR; T19956; T19956.
DR RefSeq; NP_505809.2; NM_073408.3. [G5EFU0-1]
DR RefSeq; NP_505810.2; NM_073409.4. [G5EFU0-2]
DR AlphaFoldDB; G5EFU0; -.
DR SMR; G5EFU0; -.
DR STRING; 6239.C45B11.1a; -.
DR EPD; G5EFU0; -.
DR PaxDb; G5EFU0; -.
DR PeptideAtlas; G5EFU0; -.
DR EnsemblMetazoa; C45B11.1a.1; C45B11.1a.1; WBGene00006443. [G5EFU0-1]
DR EnsemblMetazoa; C45B11.1b.1; C45B11.1b.1; WBGene00006443. [G5EFU0-2]
DR GeneID; 179527; -.
DR KEGG; cel:CELE_C45B11.1; -.
DR UCSC; C45B11.1b; c. elegans.
DR CTD; 179527; -.
DR WormBase; C45B11.1a; CE40445; WBGene00006443; pak-2. [G5EFU0-1]
DR WormBase; C45B11.1b; CE40446; WBGene00006443; pak-2. [G5EFU0-2]
DR eggNOG; KOG0578; Eukaryota.
DR GeneTree; ENSGT00940000169130; -.
DR InParanoid; G5EFU0; -.
DR OMA; CLKPLAY; -.
DR OrthoDB; 757766at2759; -.
DR PhylomeDB; G5EFU0; -.
DR Reactome; R-CEL-9013149; RAC1 GTPase cycle.
DR Reactome; R-CEL-9013405; RHOD GTPase cycle.
DR Reactome; R-CEL-9013407; RHOH GTPase cycle.
DR Reactome; R-CEL-9013420; RHOU GTPase cycle.
DR Reactome; R-CEL-9013424; RHOV GTPase cycle.
DR PRO; PR:G5EFU0; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00006443; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0002119; P:nematode larval development; IGI:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
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; -; 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 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 Alternative splicing; ATP-binding; Kinase; Magnesium; Manganese;
KW Metal-binding; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..522
FT /note="Serine/threonine-protein kinase pak-2"
FT /evidence="ECO:0000305"
FT /id="PRO_0000433490"
FT DOMAIN 16..29
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT DOMAIN 231..482
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 183..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 350
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 237..245
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 260
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 84..85
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_057792"
SQ SEQUENCE 522 AA; 58837 MW; CF21D2118EF7381C CRC64;
MNRTFSLRRK VKKSEISTPS NFEHRIHAGF DARSGTYTGL PKQWQALLGP PRSISRPKPM
VDPSCITPVD VAELKTVIRG PSSSFRYNSP LPFGMTNSPM PSVARSNSLR ISATASPVVN
VSSARHSFRP TLPPVSQRGY PFNDPSYAPL PLRNQKPPMS TTFGVEKPHQ YQQIITIVAP
SRTTTPQLQP KSPSTPQAMR QQPKCTEGVS DEEFRNALKF VVDGTDPRSD LTDYKQIGEG
STGVVEAAYK ISTKQIVAVK RMNLRKQQRR ELLFNEVSIL RQYQHPNIVR FFSSHLVDDE
LWVVMEFMEG GSLTDIVTAT RMTEPQIATI SRQVLGALDF LHARKVIHRD IKSDSILLKR
DGTVKLTDFG FCGQLSEEVP RRRSLVGTPY WTAAEVIARE PYDTRADIWS FGIMLIEMVE
GEPPFFNDQP FQAMKRIRDE HEARFSRHAK VSVELSELLS HCIVKDVNKR WPAKDLLRHP
FFAKAQHSSS IAPLLLQLQG NTINGNNPPT HHHSSQITTV IQ
