LIMK2_BOVIN
ID LIMK2_BOVIN Reviewed; 638 AA.
AC Q32L23;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=LIM domain kinase 2;
DE Short=LIMK-2;
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:P53671};
GN Name=LIMK2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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. Displays
CC serine/threonine-specific phosphorylation of myelin basic protein and
CC histone (MBP) in vitro. Suppresses ciliogenesis via multiple pathways;
CC phosphorylation of CFL1, suppression of directional trafficking of
CC ciliary vesicles to the ciliary base, and by facilitating YAP1 nuclear
CC localization where it acts as a transcriptional corepressor of the
CC TEAD4 target genes AURKA and PLK1 (By similarity).
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 MARF1 (By similarity). Interacts with NISCH
CC (By similarity). {ECO:0000250|UniProtKB:P53671,
CC ECO:0000250|UniProtKB:Q8BJ34}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:P53671}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:P53671}.
CC -!- PTM: Phosphorylated on serine and/or threonine residues by ROCK1.
CC {ECO:0000250|UniProtKB:P53671}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; BC109802; AAI09803.1; -; mRNA.
DR RefSeq; NP_001033187.1; NM_001038098.1.
DR AlphaFoldDB; Q32L23; -.
DR SMR; Q32L23; -.
DR STRING; 9913.ENSBTAP00000041788; -.
DR PaxDb; Q32L23; -.
DR PRIDE; Q32L23; -.
DR GeneID; 513539; -.
DR KEGG; bta:513539; -.
DR CTD; 3985; -.
DR eggNOG; KOG1187; Eukaryota.
DR InParanoid; Q32L23; -.
DR OrthoDB; 988822at2759; -.
DR Proteomes; UP000009136; Unplaced.
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:0051650; P:establishment of vesicle localization; ISS:UniProtKB.
DR GO; GO:1902018; P:negative regulation of cilium assembly; ISS:UniProtKB.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; ISS:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; 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; 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; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 2.
DR PROSITE; PS50106; PDZ; 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..638
FT /note="LIM domain kinase 2"
FT /id="PRO_0000291380"
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 280..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 293
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53671"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53671"
FT MOD_RES 505
FT /note="Phosphothreonine; by ROCK1 and CDC42BP"
FT /evidence="ECO:0000250|UniProtKB:P53671"
SQ SEQUENCE 638 AA; 72165 MW; 11F6BDBD26B69EC7 CRC64;
MAAQAGDDAW RCQGCGDYVA PNQRLYRTVS EAWPTSCFRC SECQDSLTNW YYEKDGKLYC
HKDYWGKFGE FCHGCSLLMT GPVMVAGEFK YHPECFACMS CKVIIEDGDA YALVQHATLY
CGKCHNEVVL APMFERLSTE SVQDQLPYSV THISMPATTE GRRGFSVSVE SACSNYATTV
QVREVNRMHI SPNNRNAIHP GDRILEINGA PVRTLRVEEV EDAISQTTQT LQLLIEHDPV
SQRLDQLQLD ARLSPCAQND RHAHTLSPLD TKENLEGTLR RRSLRRSNSI SKSPGPSSPK
EPLLLSRDIS RSESLRCSSS CSQQIFRPCD LIHGEVLGKG FFGQAIKVTH KATGKVMVMN
ELIRCDEETQ KTFLTEVKVM RSLDHPNVLK FIGVLYKDKK LNLLTEYIEG GTLKDFLRNV
DPFPWQQKVR FAKGIASGMA YLHSMCIIHR DLNSHNCLIK LDKTVVVADF GLSRLIVEER
KKPPVEKATT KKRTLRKSDR KKRYTVVGNP YWMAPEMLNG KSYDETVDVF SFGIVLCEII
GQVYADPDCL PRTLDFGLNV KLFWEKFVPE ECPPAFFPLA AICCRLEPES RPAFSKLEDF
FEALSLYLGE LGIPLPTELE DLDHTVSMEY GLIRNPPP
