ID A0A2K6QYZ8_RHIRO Unreviewed; 677 AA.
AC A0A2K6QYZ8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=LIM domain kinase 1 {ECO:0000256|ARBA:ARBA00040667};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=LIMK1 {ECO:0000313|Ensembl:ENSRROP00000034025.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000034025.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000034025.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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
CC {ECO:0000256|ARBA:ARBA00004245}.
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; A0A2K6QYZ8; -.
DR STRING; 61622.ENSRROP00000034025; -.
DR Ensembl; ENSRROT00000058467.1; ENSRROP00000034025.1; ENSRROG00000040573.1.
DR GeneTree; ENSGT00940000156345; -.
DR Proteomes; UP000233200; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:Ensembl.
DR GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0031072; F:heat shock protein binding; IEA:Ensembl.
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:0048675; P:axon extension; IEA:Ensembl.
DR GO; GO:0045773; P:positive regulation of axon extension; IEA:Ensembl.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl.
DR GO; GO:0043149; P:stress fiber assembly; IEA:Ensembl.
DR CDD; cd09462; LIM1_LIMK1; 1.
DR CDD; cd09464; LIM2_LIMK1; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd14221; STKc_LIMK1; 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:SF7; LIM DOMAIN KINASE 1; 1.
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; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 3.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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:UP000233200};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 53..112
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 113..174
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 195..288
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 369..634
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 290..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 398
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 677 AA; 75525 MW; 1EECBE536FE6E360 CRC64;
MSSILELSTS RQGVPPSVLD WTTQFLWPLD SAQTRAPSRT LGRAAPAPGS ELPVCASCGQ
RIYDGQYLQA LNADWHADCF RCCDCSASLS HQYYEKDGQL FCKKDYWARY GESCHGCSEQ
ITKGLVMVAG ELKYHPECFI CLTCGTFIGD GDTYTLVEHS KLYCGHCYYQ TVVTPVIEQI
LPDSPGSHLP HTVTLVSIPA SSHGKRGLSV SIDPPHGPPG CGTEHAHTVR VQGVDPGCMS
PDVKNSIHIG DRILEINGTP IRNVPLDEID LLIQETSRLL QLTLEHDPHD TLGHGLGPET
SPLSSPVHTP SGEAGGSARQ KPVLRSCSID RSPGAGSLGS PASQRKDLGR SESLRVVCRP
HRIFRPSDLI HGEVLGKGCF GQAIKVTHRE TGEVMVMKEL IRFDEETQRT FLKEVKVMRC
LEHPNVLKFI GVLYKDKRLN FITEYIKGGT LRGIIKSMDS QYPWSQRVSF AKDIASGMAY
LHSMNIIHRD LNSHNCLVRE NKNVVVADFG LARLMVDEKT QPEDLRSLKK PDRKKRYTVV
GNPYWMAPEM INGRSYDEKV DVFSFGIVLC EIIGRVNADP DYLPRTMDFG LNVRGFLDRY
CPANCPPSFF PITVRCCDLD PEKRPSFVKL EHWLETLRMH LAGHLPLGPQ LEQLDRGFWE
TYRRGESGLP AHPEVPD
//
