ID F1MGL9_BOVIN Unreviewed; 640 AA.
AC F1MGL9;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 2.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=LIM domain kinase 2 {ECO:0000256|ARBA:ARBA00040666};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=LIMK2 {ECO:0000313|Ensembl:ENSBTAP00000041788.2,
GN ECO:0000313|VGNC:VGNC:52793};
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 {ECO:0000313|Ensembl:ENSBTAP00000041788.2, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000041788.2, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000041788.2,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000041788.2}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000041788.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001127};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000256|ARBA:ARBA00001127};
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:0000256|ARBA:ARBA00001416};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000256|ARBA:ARBA00001416};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC {ECO:0000256|ARBA:ARBA00004186}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00005843}.
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DR AlphaFoldDB; F1MGL9; -.
DR Ensembl; ENSBTAT00000044280.2; ENSBTAP00000041788.2; ENSBTAG00000010662.6.
DR VEuPathDB; HostDB:ENSBTAG00000010662; -.
DR VGNC; VGNC:52793; LIMK2.
DR GeneTree; ENSGT00940000159133; -.
DR HOGENOM; CLU_000288_7_23_1; -.
DR TreeFam; TF318014; -.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000010662; Expressed in esophagus and 107 other cell types or tissues.
DR ExpressionAtlas; F1MGL9; baseline and differential.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005801; C:cis-Golgi network; IEA:Ensembl.
DR GO; GO:0072686; C:mitotic spindle; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0030953; P:astral microtubule organization; IEA:Ensembl.
DR GO; GO:0061303; P:cornea development in camera-type eye; IEA:Ensembl.
DR GO; GO:0051650; P:establishment of vesicle localization; IEA:Ensembl.
DR GO; GO:0060322; P:head development; IEA:Ensembl.
DR GO; GO:1902018; P:negative regulation of cilium assembly; IEA:Ensembl.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IEA:Ensembl.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR CDD; cd09465; LIM2_LIMK2; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd14222; STKc_LIMK2; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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 PANTHER; PTHR46485; LIM DOMAIN KINASE 1; 1.
DR PANTHER; PTHR46485:SF1; LIM DOMAIN KINASE 2; 1.
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; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 2.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW LIM domain {ECO:0000256|ARBA:ARBA00023038, ECO:0000256|PROSITE-
KW ProRule:PRU00125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00125};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 12..72
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 73..133
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 154..241
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 333..603
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 282..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 362
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 640 AA; 72468 MW; 1EF8F6FB4512A571 CRC64;
MIAQKGSCDD AWRCQGCGDY VAPNQRLYRT VSEAWPTSCF RCSECQDSLT NWYYEKDGKL
YCHKDYWGKF GEFCHGCSLL MTGPVMVAGE FKYHPECFAC MSCKVIIEDG DAYALVQHAT
LYCGKCHNEV VLAPMFERLS TESVQDQLPY SVTHISMPAT TEGRRGFSVS VESACSNYAT
TVQVREVNRM HISPNNRNAI HPGDRILEIN GAPVRTLRVE EVEDAISQTT QTLQLLIEHD
PVSQRLDQLQ LDARLSPCAQ NDRHAHTLSP LDTKENLEGT LRRRSLRRSN SISKSPGPSS
PKEPLLLSRD ISRSESLRCS SSCSQQIFRP CDLIHGEVLG KGFFGQAIKV THKATGKVMV
MKELIRCDEE TQKTFLTEVK VMRSLDHPNV LKFIGVLYKD KKLNLLTEYI EGGTLKDFLR
NVDPFPWQQK VRFAKGIASG MAYLHSMCII HRDLNSHNCL IKLDKTVVVA DFGLSRLIVE
ERKKPPVEKA TTKKRTLRKS DRKKRYTVVG NPYWMAPEML NGKSYDETVD VFSFGIVLCE
IIGQVYADPD CLPRTLDFGL NVKLFWEKFV PEECPPAFFP LAAICCRLEP ESRPAFSKLE
DFFEALSLYL GELGIPLPTE LEDLDHTVSM EYGLIRNPPP
//
