LIMK1_XENLA
ID LIMK1_XENLA Reviewed; 615 AA.
AC O42565;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=LIM domain kinase 1;
DE Short=LIMK-1;
DE Short=xLIMK1;
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:P53667};
GN Name=limk1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=9186054;
RX DOI=10.1002/(sici)1097-0177(199706)209:2<196::aid-aja5>3.0.co;2-d;
RA Takahashi T., Aoki S., Nakamura T., Koshimizu U., Matsumoto K.,
RA Nakamura T.;
RT "Xenopus LIM motif-containing protein kinase, Xlimk1, is expressed in the
RT developing head structure of the embryo.";
RL Dev. Dyn. 209:196-205(1997).
RN [2]
RP FUNCTION.
RX PubMed=11150247; DOI=10.1006/dbio.2000.9999;
RA Takahashi T., Koshimizu U., Abe H., Obinata T., Nakamura T.;
RT "Functional involvement of Xenopus LIM kinases in progression of oocyte
RT maturation.";
RL Dev. Biol. 229:554-567(2001).
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.
CC {ECO:0000269|PubMed:11150247}.
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:0000250|UniProtKB:P53667}. Nucleus
CC {ECO:0000250|UniProtKB:P53667}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P53667}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the early cleavage stages of the
CC embryo. Expression decreases at the gastrula stage and subsequently
CC reappears at the neurula stage, and continues to increase from this
CC point on. In post neurula stages, expressed predominantly in the
CC anterior region of the embryo, including the developing brain and
CC sensory organs. {ECO:0000269|PubMed:9186054}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AB001469; BAA21488.1; -; mRNA.
DR RefSeq; NP_001081177.1; NM_001087708.1.
DR AlphaFoldDB; O42565; -.
DR SMR; O42565; -.
DR GeneID; 397696; -.
DR KEGG; xla:397696; -.
DR CTD; 397696; -.
DR Xenbase; XB-GENE-1011263; limk1.L.
DR OrthoDB; 988822at2759; -.
DR Proteomes; UP000186698; Chromosome 2L.
DR Bgee; 397696; Expressed in ovary and 12 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; 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:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; 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 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 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Cytoskeleton; Kinase; LIM domain; Metal-binding;
KW Nucleotide-binding; Nucleus; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase; Zinc.
FT CHAIN 1..615
FT /note="LIM domain kinase 1"
FT /id="PRO_0000075807"
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 161..247
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 314..572
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 435
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 320..328
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 343
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 615 AA; 69793 MW; 12089A05A4F72177 CRC64;
MRLMLLCCSW SEEHMGEEEG NVLPLCASCG QSIYDGCYLQ ALALDWHSDC FRCSDCGVSL
SHRYYEKDGR LFCKKHYWTR FGGMCQGCSE NITKGLVMVA GEHKYHPECF MCSRCKAYIG
DGETYALVER SKLYCGPCYY QFSVTPVIDS PGSRSPHTVT LVSLPASDGK RGLSVSITPS
CAEHSHTVRV TELDADFLGP DIQSSIHIGD RILEINGTPI RSVPLDEIDV LIQETSRLLQ
LTIEHDPHET PTMPSPCAEI AVRRQRPVMR SCSIDRSPGS SCVGSPSCSR RDMSRSESVR
TVTGVHRIFR PSDLIPGEVL GRGCFGQAIK VTHRVTGEVM VMKELIRFDE ETQRTFLKEV
KVMRCLEHPH VLKFIGVLYK DKRLNFITEY IPGGTLRRVI KSMDTHCPWN QRVSFARDIA
AGMTYLHSMN IIHRDLNSHN CLVREDGGLV VANFGLSRLI PEETRDLRKD RRKRYTVVGN
PYWMAPEMIN GRSYDESVDV FSFGIVICEI IGLVNADPDY LPRTMDFGLN VRAFLDRFCP
PNCPPGFFPS AVLCCDLDPE KRPRFSQLQL WLDSLLRHLN LQLPLSSHIE QLEQNFWENY
RRGDSTLHVH PEIPE
