ID Q8QHM0_XENLA Unreviewed; 606 AA.
AC Q8QHM0;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 128.
DE RecName: Full=LIM domain kinase 2 {ECO:0000256|ARBA:ARBA00040666};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=limk2.L {ECO:0000313|RefSeq:NP_001082219.1,
GN ECO:0000313|Xenbase:XB-GENE-976148};
GN Synonyms=limk2 {ECO:0000313|RefSeq:NP_001082219.1,
GN ECO:0000313|Xenbase:XB-GENE-976148}, Xlimk2
GN {ECO:0000313|EMBL:BAB85114.1}, xlimk2
GN {ECO:0000313|RefSeq:NP_001082219.1};
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 {ECO:0000313|EMBL:BAB85114.1};
RN [1] {ECO:0000313|EMBL:BAB85114.1, ECO:0000313|RefSeq:NP_001082219.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Ovary {ECO:0000313|EMBL:BAB85114.1};
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).
RN [2] {ECO:0000313|RefSeq:NP_001082219.1}
RP IDENTIFICATION.
RG RefSeq;
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 EMBL; AB038517; BAB85114.1; -; mRNA.
DR RefSeq; NP_001082219.1; NM_001088750.1.
DR IntAct; Q8QHM0; 1.
DR GeneID; 398298; -.
DR KEGG; xla:398298; -.
DR AGR; Xenbase:XB-GENE-976148; -.
DR CTD; 398298; -.
DR Xenbase; XB-GENE-976148; limk2.L.
DR OrthoDB; 5474815at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 398298; Expressed in ovary and 19 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd09365; LIM2_LIMK; 1.
DR CDD; cd14222; STKc_LIMK2; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 1.
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; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00132; LIM; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
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; 1.
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 {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Kinase {ECO:0000313|EMBL:BAB85114.1, ECO:0000313|RefSeq:NP_001082219.1};
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:UP000186698};
KW Transferase {ECO:0000313|EMBL:BAB85114.1,
KW ECO:0000313|RefSeq:NP_001082219.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 60..121
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 142..216
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 293..562
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 322
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 606 AA; 67476 MW; A40BDFBF0E47E457 CRC64;
MMSSAVGSRL DLRQDNRANG APDGTFLVKR TFTQDIQMRA SDSRDGLSPQ VLSPADTWTE
QCLSCSLCLT GPAMVVSHYK FHPECFSCSG CKAMIGEGES FSLVQGTALY CGPCQKLLLL
QPKFEGLCSE SAQEQDPHML TLLRLPPQAG GKRGFSVSAK NMQVTQVSAK NWNLLHLGDR
ILEINGSPVG TLNSNEADDL LCSTNRTLQL LIEHNPPSNL PVDNAPPKSP SFRYTEGKGS
TEGTMKRSSI RRSNSNTRSS GICSPKDPRS VSRSESLRCG VGGIQQIFRP CELLHGEELG
KGFFGRAIKV THRATGRVMV MKELIQFDEQ TQKNFLTEVK VMRSLDHPNV LRFIGVLYKD
SRLNLLTEFI ECGTLKDYLR ADYCTWQKKV SFAKDIACGM AYLHSMSIIH RDLNSHNCLI
KLDGTAVVAD FGLSRLIVEE KPLPPPDRPP TKKRTLGKNN RKKRYTVVGN PYWMAPEMLN
GKDYDEKVDI FSFGIVLCEI IGQVYADPDC LPRTLDFGLN VRLFWDKFVP KDCPPGFFPL
ATSCCHLEPD RRPDFPHLHD ALTALSLFLG ELGIPLPSEL EYMEHSVQLQ YGLTRECSKL
EEGASV
//
