LIMK2_CHICK
ID LIMK2_CHICK Reviewed; 642 AA.
AC P53666;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=LIM domain kinase 2;
DE Short=LIMK-2;
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:P53671};
GN Name=LIMK2; Synonyms=LIMK;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Lung;
RX PubMed=7852284; DOI=10.1093/oxfordjournals.jbchem.a124573;
RA Ohashi K., Toshima J., Tajinda K., Nakamura T., Mizuno K.;
RT "Molecular cloning of a chicken lung cDNA encoding a novel protein kinase
RT with N-terminal two LIM/double zinc finger motifs.";
RL J. Biochem. 116:636-642(1994).
CC -!- FUNCTION: Serine/threonine-protein kinase that plays an essential role
CC in the regulation of actin filament dynamics. Acts downstream of
CC several Rho family GTPase signal transduction pathways. Involved in
CC astral microtubule organization and mitotic spindle orientation during
CC early stages of mitosis by mediating phosphorylation of TPPP.
CC {ECO:0000250|UniProtKB:P53671}.
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:P53671};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000250|UniProtKB:P53671};
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:P53671};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000250|UniProtKB:P53671};
CC -!- SUBUNIT: Binds ROCK1 and LKAP. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:P53671}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:P53671}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in the lung, and faintly in
CC the kidney, liver, brain, spleen, gizzard, and intestine.
CC {ECO:0000269|PubMed:7852284}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D26310; BAA05372.1; -; mRNA.
DR PIR; JP0079; JP0079.
DR RefSeq; NP_990446.1; NM_205115.1.
DR AlphaFoldDB; P53666; -.
DR SMR; P53666; -.
DR STRING; 9031.ENSGALP00000011249; -.
DR PaxDb; P53666; -.
DR Ensembl; ENSGALT00000011263; ENSGALP00000011249; ENSGALG00000006950.
DR GeneID; 396010; -.
DR KEGG; gga:396010; -.
DR CTD; 3985; -.
DR VEuPathDB; HostDB:geneid_396010; -.
DR eggNOG; KOG1187; Eukaryota.
DR GeneTree; ENSGT00940000159133; -.
DR HOGENOM; CLU_000288_7_23_1; -.
DR InParanoid; P53666; -.
DR OMA; NAGHSPT; -.
DR OrthoDB; 988822at2759; -.
DR PhylomeDB; P53666; -.
DR TreeFam; TF318014; -.
DR BRENDA; 2.7.10.2; 1306.
DR PRO; PR:P53666; -.
DR Proteomes; UP000000539; Chromosome 15.
DR Bgee; ENSGALG00000006950; Expressed in ovary and 12 other tissues.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
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:0030953; P:astral microtubule organization; ISS:UniProtKB.
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 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 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Cytoskeleton; Kinase; LIM domain; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase; Zinc.
FT CHAIN 1..642
FT /note="LIM domain kinase 2"
FT /id="PRO_0000075812"
FT DOMAIN 12..63
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 72..124
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 152..239
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 331..608
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 282..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 451
FT /evidence="ECO:0000250|UniProtKB:P53671"
FT BINDING 337..345
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 360
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 505
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 642 AA; 72468 MW; 6D3E500B8C3A8277 CRC64;
MAGPPGEEVW RCLGCGDLIA AGQRLYRMVN EAWHISCFRC SECQDPLTNW YYEKDGKLYC
HKDYWGKFGE SCHGCSLLMT GPVMVAGEYK YHPECFACMS CKVIIEDGDT YALVQHSTLY
CGKCHNQIVL TPMIEKHSTE SLREQLPYTL TLISMPAATD GKRGFSVSVE GGCSSYATGV
QVKEVNRMHI SPDVRNAIHP ADRILEINGA PIRTLQVEEV EDLIRKTSQT LQLLIEHDPV
SQRLDRLRLD SRLPTHIKSP ISPHSISPLD IKENLEGTLR RRSLRRSNSI SKSPGPSSPK
EPLLLSRDIS RSESLRSSSS CSQQIFRPCD LIHGEVLGKG FFGQAIKVTH KATGKVMVMK
ELIRCDEETQ KTFLTEVKVM RSLDHPNVLK FIGVLYKDKK LNLLTEYIEG GTLKDFLRNA
DPFPWQQKVS FAKGIASGMA YLHSMCIIHR DLNSHNCLIK LDKTVVVADF GLSRLIVEER
KKPTLEKPSA KKRTLRKSDR KKRYTVVGNP YWMAPEMLNG QSYDETVDIF SFGIVLCEII
GQVYADPDCL PRTLDFGLNV KLFWEKFVPA DCPPAFFPLA AICCRLEPES RPPFSKLEDS
FEALSLYLGE LAIPLPSELE ELDHNVSVQY GLNRDKLPEN TT
