LIMK2_RAT
ID LIMK2_RAT Reviewed; 638 AA.
AC P53670;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 170.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LIMK2A; LIMK2B; LIMK2C AND LIMK2D).
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=7651734;
RA Nunoue K., Ohashi K., Okano I., Mizuno K.;
RT "LIMK-1 and LIMK-2, two members of a LIM motif-containing protein kinase
RT family.";
RL Oncogene 11:701-710(1995).
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, directional trafficking of ciliary vesicles to
CC the ciliary base, and by facilitating YAP1 nuclear localization where
CC it acts as a transcriptional corepressor of the TEAD4 target genes
CC AURKA and PLK1 (By similarity). {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: [Isoform LIMK2A]: Cytoplasm
CC {ECO:0000250|UniProtKB:P53671}. Nucleus {ECO:0000250|UniProtKB:P53671}.
CC -!- SUBCELLULAR LOCATION: [Isoform LIMK2B]: Cytoplasm
CC {ECO:0000250|UniProtKB:P53671}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:P53671}. Nucleus {ECO:0000250|UniProtKB:P53671}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:P53671}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:P53671}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=LIMK2A;
CC IsoId=P53670-1; Sequence=Displayed;
CC Name=LIMK2B;
CC IsoId=P53670-2; Sequence=VSP_003128;
CC Name=LIMK2C;
CC IsoId=P53670-3; Sequence=VSP_003128, VSP_003129, VSP_003130;
CC Name=LIMK2D;
CC IsoId=P53670-4; Sequence=VSP_003128, VSP_003131;
CC -!- TISSUE SPECIFICITY: Found in various tissues at moderate levels, except
CC for testis, which shows very low expression.
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; D31874; BAA06673.1; -; mRNA.
DR EMBL; D31875; BAA06674.1; -; mRNA.
DR EMBL; D31876; BAA06675.1; -; mRNA.
DR EMBL; D31877; BAA06676.1; -; mRNA.
DR PIR; I78846; I78846.
DR PIR; I78847; I78847.
DR PIR; I78848; I78848.
DR RefSeq; NP_077049.2; NM_024135.2. [P53670-1]
DR RefSeq; XP_006251298.1; XM_006251236.3. [P53670-2]
DR AlphaFoldDB; P53670; -.
DR SMR; P53670; -.
DR IntAct; P53670; 1.
DR STRING; 10116.ENSRNOP00000026032; -.
DR iPTMnet; P53670; -.
DR PhosphoSitePlus; P53670; -.
DR PaxDb; P53670; -.
DR PRIDE; P53670; -.
DR Ensembl; ENSRNOT00000026032; ENSRNOP00000026032; ENSRNOG00000019000. [P53670-1]
DR GeneID; 29524; -.
DR KEGG; rno:29524; -.
DR UCSC; RGD:62056; rat. [P53670-1]
DR CTD; 3985; -.
DR RGD; 62056; Limk2.
DR eggNOG; KOG1187; Eukaryota.
DR GeneTree; ENSGT00940000159133; -.
DR HOGENOM; CLU_110071_0_0_1; -.
DR InParanoid; P53670; -.
DR OMA; NAGHSPT; -.
DR OrthoDB; 988822at2759; -.
DR PhylomeDB; P53670; -.
DR TreeFam; TF318014; -.
DR BRENDA; 2.7.10.2; 5301.
DR PRO; PR:P53670; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000019000; Expressed in esophagus and 20 other tissues.
DR ExpressionAtlas; P53670; baseline and differential.
DR Genevisible; P53670; RN.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005801; C:cis-Golgi network; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; ISO:RGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:RGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0030953; P:astral microtubule organization; ISS:UniProtKB.
DR GO; GO:0061303; P:cornea development in camera-type eye; ISO:RGD.
DR GO; GO:0051650; P:establishment of vesicle localization; ISS:UniProtKB.
DR GO; GO:0060322; P:head development; ISO:RGD.
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; IDA:RGD.
DR GO; GO:0007286; P:spermatid development; TAS:RGD.
DR GO; GO:0007283; P:spermatogenesis; ISO:RGD.
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 Alternative splicing; ATP-binding; Cytoplasm; Cytoskeleton; Kinase;
KW LIM domain; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase;
KW Zinc.
FT CHAIN 1..638
FT /note="LIM domain kinase 2"
FT /id="PRO_0000075811"
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 257..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..273
FT /note="Polar residues"
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 210
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P53671"
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"
FT VAR_SEQ 1..37
FT /note="MAALAGEEAWRCRGCGNYVPLSQRLYRTANEAWHSSC -> MGSYLSVPAYF
FT TSRDP (in isoform LIMK2B, isoform LIMK2C and isoform
FT LIMK2D)"
FT /evidence="ECO:0000303|PubMed:7651734"
FT /id="VSP_003128"
FT VAR_SEQ 185..638
FT /note="Missing (in isoform LIMK2D)"
FT /evidence="ECO:0000303|PubMed:7651734"
FT /id="VSP_003131"
FT VAR_SEQ 348..371
FT /note="VTHKATGKVMVMKELIRCDEETQK -> SWEGGSGDSQSHRQSDGHEGVNSL
FT (in isoform LIMK2C)"
FT /evidence="ECO:0000303|PubMed:7651734"
FT /id="VSP_003129"
FT VAR_SEQ 372..638
FT /note="Missing (in isoform LIMK2C)"
FT /evidence="ECO:0000303|PubMed:7651734"
FT /id="VSP_003130"
SQ SEQUENCE 638 AA; 72202 MW; A7E2D525751BE4F3 CRC64;
MAALAGEEAW RCRGCGNYVP LSQRLYRTAN EAWHSSCFRC SECQESLTNW YYEKDGKLYC
HKDYWAKFGE FCHGCSLLMT GPAMVAGEFK YHPECFACMS CKVIIEDGDA YALVQHATLY
CGKCHNEVVL APMFERLSTE SVQDQLPYSV TLISMPATTE CRRGFSVSVE SASSNYATTV
QVKEVNRMHI SPNNRNAIHP GDRILEINGT PVRTLRVEEV EDAINQTSQT LQLLIEHDPV
PQRLDQLRLD TRLSPHMQSS GHTLMLSTLD AKENQEGTLR RRSLRRSNSI SKSPGPSSPK
EPLLLSRDIS RSESLRCSSS YSQQIFRPCD LIHGEVLGKG FFGQAIKVTH KATGKVMVMK
ELIRCDEETQ KTFLTEVKVM RSLDHPNVLK FIGVLYKDKK LNLLTEYIEG GTLKDFLRNV
DPFPWQQKVR FAKGIASGMA YLHSMCIIHR DLNSHNCLIK LDKTVVVADF GLSRLIVEER
KRPPVEKAAT KKRTLRKSDR KKRYTVVGNP YWMAPEMLNG KSYDETVDVF SFGIVLCEII
GQVYADPDCL PRTLDFGLNV KLFWEKFVPT DCPPAFFPLA AICCKLEPES RPAFSKLEDS
FEALSLFLGE LAIPLPAELE ELDHTVSMEY GLTRDSPP
