LIMK1_CHICK
ID LIMK1_CHICK Reviewed; 662 AA.
AC Q8QFP8;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=LIM domain kinase 1;
DE Short=LIMK-1;
DE Short=chLIMK1;
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:P53667};
GN Name=LIMK1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF ASP-467.
RC TISSUE=Embryo;
RX PubMed=12684437; DOI=10.1523/jneurosci.23-07-02527.2003;
RA Endo M., Ohashi K., Sasaki Y., Goshima Y., Niwa R., Uemura T., Mizuno K.;
RT "Control of growth cone motility and morphology by LIM kinase and Slingshot
RT via phosphorylation and dephosphorylation of cofilin.";
RL J. Neurosci. 23:2527-2537(2003).
CC -!- FUNCTION: Protein kinase which regulates actin filament dynamics.
CC Phosphorylates and inactivates the actin binding/depolymerizing factor
CC cofilin, thereby stabilizing the actin cytoskeleton. Required for
CC motility of the axon growth cone. {ECO:0000269|PubMed:12684437}.
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:P53667};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000250|UniProtKB:P53667};
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:P53667};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000250|UniProtKB:P53667};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12684437}. Nucleus
CC {ECO:0000250|UniProtKB:P53667}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P53667}. Cell projection, growth cone
CC {ECO:0000269|PubMed:12684437}. Note=Recruited to axon growth cones.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in the brain.
CC {ECO:0000269|PubMed:12684437}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AB073752; BAB88398.1; -; mRNA.
DR RefSeq; NP_989462.1; NM_204131.1.
DR AlphaFoldDB; Q8QFP8; -.
DR SMR; Q8QFP8; -.
DR STRING; 9031.ENSGALP00000039786; -.
DR PaxDb; Q8QFP8; -.
DR Ensembl; ENSGALT00000040584; ENSGALP00000039786; ENSGALG00000001076.
DR GeneID; 373922; -.
DR KEGG; gga:373922; -.
DR CTD; 3984; -.
DR VEuPathDB; HostDB:geneid_373922; -.
DR eggNOG; KOG1187; Eukaryota.
DR GeneTree; ENSGT00940000156345; -.
DR HOGENOM; CLU_000288_7_23_1; -.
DR InParanoid; Q8QFP8; -.
DR OMA; FDGQYLQ; -.
DR OrthoDB; 988822at2759; -.
DR PhylomeDB; Q8QFP8; -.
DR Reactome; R-GGA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-GGA-399954; Sema3A PAK dependent Axon repulsion.
DR Reactome; R-GGA-5627123; RHO GTPases activate PAKs.
DR PRO; PR:Q8QFP8; -.
DR Proteomes; UP000000539; Chromosome 19.
DR Bgee; ENSGALG00000001076; Expressed in cerebellum and 11 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; 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; ISS:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00412; LIM; 2.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00132; LIM; 2.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 2.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell projection; Cytoplasm; Cytoskeleton; Kinase; LIM domain;
KW Metal-binding; Nucleotide-binding; Nucleus; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase; Zinc.
FT CHAIN 1..662
FT /note="LIM domain kinase 1"
FT /id="PRO_0000075806"
FT DOMAIN 24..83
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 84..145
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 166..259
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 346..611
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 262..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..284
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 467
FT /evidence="ECO:0000305"
FT BINDING 352..360
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 375
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 467
FT /note="D->A: Abrogates kinase activity."
FT /evidence="ECO:0000269|PubMed:12684437"
SQ SEQUENCE 662 AA; 74445 MW; DD9FED2466C8E623 CRC64;
MRLMLLCCTW RDEPMGEEEG TDLPVCASCG QGIFDGQYLQ ALNADWHADC FRCGECGASL
SHQYYEKDGR LYCKKDYWAR FGELCHGCAE QITKGLVMVA GEQKYHPECF SCLNCRAFIG
DGDTYALVER SKLYCGHCYY QMVVTPVIEQ ILPDSPGSRI PHTVTLVSIP ACSDGKRGFS
VSIDPHCGAQ GCGAEHSRTV RVREVDPDCI SPDVKNSIHV GDRILEINGT PIGHVPLDEI
DLLIQETSRL LQLTIEHDPH EPLPRDLALP CSPLPDPHSP LRSPVPAPHG DLGTMRQRAV
MRSCSTDKSP GSSSVGSPAS QRKDIGRSES LRVVSRAHRI FRPSDLIHGE VLGKGCFGQA
IKVTHRETGE VMVMKELIRF DEETQRTFLK EVKVMRCLEH PNVLKFIGVL YKEKRLNFIT
EYIKGGTLRG LIKSMDSHYP WSQRVSFAKD IAAGMAYLHS MNIIHRDLNS HNCLVRENKS
VVVADFGLAR LMVDEKNQPE HLQNLKKPDR KKRYTVVGNP YWMAPEMING RSYDEKVDIF
SFGIVLCEII GRVSADPDYL PRTTDFGLNV RGFLERYCPP ACPPSFFPIA ACCCDLDPEK
RPSFSKLEQW LETLRMHLDI RLPLSSQLEQ LTCAFWETHR RGEGGLPPHP ELPDTAPHLH
PL
