PAKB_DICDI
ID PAKB_DICDI Reviewed; 852 AA.
AC Q869N2; O00911; Q551M5; Q94488;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Serine/threonine-protein kinase pakB {ECO:0000303|PubMed:15509655};
DE Short=dPAKb;
DE EC=2.7.11.1;
DE AltName: Full=Myosin I heavy chain kinase {ECO:0000312|EMBL:AAC71063.1};
GN Name=pakB {ECO:0000312|EMBL:EAL69183.1};
GN Synonyms=Ddpak {ECO:0000312|EMBL:CAA71240.1},
GN mihck {ECO:0000312|EMBL:AAC71063.1}; ORFNames=DDB_G0276459;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC71063.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 242-250;
RP 353-358 AND 364-370, FUNCTION, AND AUTOPHOSPHORYLATION.
RC STRAIN=AX3;
RX PubMed=8900194; DOI=10.1074/jbc.271.43.27044;
RA Lee S.-F., Egelhoff T.T., Mahasneh A., Cote G.P.;
RT "Cloning and characterization of a Dictyostelium myosin I heavy chain
RT kinase activated by Cdc42 and Rac.";
RL J. Biol. Chem. 271:27044-27048(1996).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAC71063.1}
RP SEQUENCE REVISION TO N-TERMINUS, PROTEIN SEQUENCE OF 6-11 AND 740-745,
RP FUNCTION, PHOSPHOLIPID-BINDING ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS
RP OF SER-4, AND PHOSPHORYLATION AT SER-8.
RC STRAIN=AX3;
RX PubMed=9774403; DOI=10.1074/jbc.273.43.27911;
RA Lee S.-F., Mahasneh A., de la Roche M., Cote G.P.;
RT "Regulation of the p21-activated kinase-related Dictyostelium myosin I
RT heavy chain kinase by autophosphorylation, acidic phospholipids, and Ca2+-
RT calmodulin.";
RL J. Biol. Chem. 273:27911-27917(1998).
RN [3] {ECO:0000305, ECO:0000312|EMBL:CAA71240.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=AX2 {ECO:0000312|EMBL:CAA71240.1};
RA Strom M.;
RT "Cloning and characterization of a ste20 homolog from Dictyostelium
RT discoideum.";
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000312|EMBL:EAL69183.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4 {ECO:0000312|EMBL:EAL69183.1};
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [5] {ECO:0000312|EMBL:EAL69183.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4 {ECO:0000312|EMBL:EAL69183.1};
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [6] {ECO:0000305}
RP FUNCTION, INTERACTION WITH RAC1A; RAC1B; RAC1C; RACA; RACB; RACC AND RACF1,
RP AND SUBCELLULAR LOCATION.
RX PubMed=15509655; DOI=10.1091/mbc.e04-06-0534;
RA de la Roche M., Mahasneh A., Lee S.-F., Rivero F., Cote G.P.;
RT "Cellular distribution and functions of wild-type and constitutively
RT activated Dictyostelium PakB.";
RL Mol. Biol. Cell 16:238-247(2005).
CC -!- FUNCTION: Regulator of the myosin I component of the cytoskeleton:
CC required for regulation of cytokinesis, phagocytosis and pinocytosis.
CC {ECO:0000269|PubMed:15509655, ECO:0000269|PubMed:8900194,
CC ECO:0000269|PubMed:9774403}.
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:0000269|PubMed:15509655, ECO:0000269|PubMed:8900194,
CC ECO:0000269|PubMed:9774403};
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:0000269|PubMed:15509655,
CC ECO:0000269|PubMed:8900194, ECO:0000269|PubMed:9774403};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15509655, ECO:0000269|PubMed:8900194,
CC ECO:0000269|PubMed:9774403};
CC -!- SUBUNIT: Interacts with rac1A, rac1B, rac1C, racA, racB, racC and
CC racF1. {ECO:0000269|PubMed:15509655}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:15509655,
CC ECO:0000269|PubMed:9774403}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:15509655, ECO:0000269|PubMed:9774403}. Note=Mainly
CC cytosolic but enriched at the leading edge of migrating cells and at
CC macropinocytic and phagocytic cups, possibly due to binding to acidic
CC phospholipids.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:8900194, ECO:0000269|PubMed:9774403};
CC IsoId=Q869N2-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|Ref.3};
CC IsoId=Q869N2-2; Sequence=VSP_052996;
CC -!- PTM: Autophosphorylated at Ser-8. This may stimulate interaction with
CC GTP-bound Rac family members which then further stimulates
CC autophosphorylation and kinase activity. {ECO:0000269|PubMed:9774403}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000269|PubMed:15509655,
CC ECO:0000269|PubMed:8900194, ECO:0000269|PubMed:9774403}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA71240.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U67716; AAC71063.1; -; mRNA.
DR EMBL; Y10158; CAA71240.1; ALT_FRAME; mRNA.
DR EMBL; AAFI02000015; EAL69183.1; -; Genomic_DNA.
DR RefSeq; XP_643105.1; XM_638013.1.
DR AlphaFoldDB; Q869N2; -.
DR SMR; Q869N2; -.
DR IntAct; Q869N2; 11.
DR STRING; 44689.DDB0191345; -.
DR iPTMnet; Q869N2; -.
DR PaxDb; Q869N2; -.
DR EnsemblProtists; EAL69183; EAL69183; DDB_G0276459.
DR GeneID; 8620509; -.
DR KEGG; ddi:DDB_G0276459; -.
DR dictyBase; DDB_G0276459; pakB.
DR eggNOG; KOG0578; Eukaryota.
DR HOGENOM; CLU_335071_0_0_1; -.
DR InParanoid; Q869N2; -.
DR OMA; APPIDNS; -.
DR PhylomeDB; Q869N2; -.
DR BRENDA; 2.7.11.7; 1939.
DR Reactome; R-DDI-389359; CD28 dependent Vav1 pathway.
DR Reactome; R-DDI-5621575; CD209 (DC-SIGN) signaling.
DR Reactome; R-DDI-5627123; RHO GTPases activate PAKs.
DR Reactome; R-DDI-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-DDI-9013149; RAC1 GTPase cycle.
DR Reactome; R-DDI-9013404; RAC2 GTPase cycle.
DR Reactome; R-DDI-9013406; RHOQ GTPase cycle.
DR Reactome; R-DDI-9013407; RHOH GTPase cycle.
DR Reactome; R-DDI-9013420; RHOU GTPase cycle.
DR Reactome; R-DDI-9013423; RAC3 GTPase cycle.
DR Reactome; R-DDI-9013424; RHOV GTPase cycle.
DR PRO; PR:Q869N2; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005938; C:cell cortex; IDA:dictyBase.
DR GO; GO:0031252; C:cell leading edge; IDA:dictyBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:dictyBase.
DR GO; GO:0016020; C:membrane; IDA:dictyBase.
DR GO; GO:0001891; C:phagocytic cup; IDA:dictyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
DR GO; GO:0051015; F:actin filament binding; IDA:dictyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IPI:dictyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016905; F:myosin heavy chain kinase activity; IDA:dictyBase.
DR GO; GO:0005543; F:phospholipid binding; IDA:dictyBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:dictyBase.
DR GO; GO:0031267; F:small GTPase binding; IPI:dictyBase.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IGI:dictyBase.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IGI:dictyBase.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:dictyBase.
DR GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR GO; GO:0006907; P:pinocytosis; IMP:dictyBase.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; IDA:dictyBase.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IMP:dictyBase.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:dictyBase.
DR GO; GO:1902463; P:protein localization to cell leading edge; IDA:dictyBase.
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 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; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Kinase; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Phagocytosis; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..852
FT /note="Serine/threonine-protein kinase pakB"
FT /id="PRO_0000361051"
FT DOMAIN 356..369
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT DOMAIN 570..823
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..106
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..193
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 691
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 576..584
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 599
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 8
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:9774403"
FT VAR_SEQ 413..440
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_052996"
FT MUTAGEN 4
FT /note="S->A: No effect on autophosphorylation."
FT /evidence="ECO:0000269|PubMed:9774403"
FT CONFLICT 310
FT /note="Missing (in Ref. 1; AAC71063)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 852 AA; 93123 MW; 49C134B3DC077C1E CRC64;
MEQSKRVSMM REKFEAQSNE AESSPPPNRK PPPPNKRVQT NGTSSLNSSG SSFVSPSPSP
SPSPQQPVKR PLPSPGVNKQ APPALPTQPR PQQQQPEIPV RPTTPTRTPP NLINSNGTSG
GSGFSSSSGN SGYSSSNNNN SNSNSSINMN GNHSNGLNGG SSNPVPMRKV SSPINIANGT
TPPPPPQPTP SQQPQQSPSS ASHNNTQHNI PSPPPLPNNK PKKLAPTAVP AGLGSIIGGP
KTPAISPGST SPSLGSSNGN IPISTTSTPI TPTPPISVPL ATSPNNSHKD SISNSNSNNN
NNNNNNNNNN SSNATTSPPS PPVSNVGNKQ DEEKKGFLSI FTNKKKNKDK KKEFSVGSPF
NVKHNIHVNY HSVTGFEGLP KEWEVILQSS GITREDVVEH SEVVIDVLDF HMQQQQQQAQ
QEQQALMQKQ MQQSGIPAHM LNNPKPPTIP IRDANKQPHN QLQPTPHQPP QHHHQQQPPQ
QHHHQQQQQQ HNNNNNNNNN NNNNNNNQQS AQQQSAGILS QQQEQQLEEM MCGGAYDDEQ
YDLNNQPLPD ETNVSLYDLV SQEDPTKLFG EGSTKIGEGA AGEVFVVTQL KTNNKVAIKK
MPLNQQNMKL IVTEIGIMKS CRHQNIIDYI DSYLVGDSLW VAMEFMGGGC LTEILEQFNS
VKLVEAQIAY VCAETLKGLA YIHSQHRIHR DIKSDNILLG SDGSVKLADF GYAAQLTKSK
QKRVTIVGTP YWMAPELIRG QNYDRKVDIW SLGIMAMEMA ESEPPYMSFP PLRALFLITT
KGIPDLKDQN KWSDDFKDFV KKCLDKDVEN RPEAKVLLNH PFLKTACNSN GLVPAIMEAK
KAKEAHSKFS IH
