ID H2P439_PONAB Unreviewed; 685 AA.
AC H2P439; A0A2J8UVE6;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 14 {ECO:0000256|RuleBase:RU369059};
GN Name=LIMK2 {ECO:0000313|Ensembl:ENSPPYP00000013086.3};
GN ORFNames=CR201_G0024533 {ECO:0000313|EMBL:PNJ49234.1};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000013086.3, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000013086.3, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PNJ49234.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Susie {ECO:0000313|EMBL:PNJ49234.1};
RA Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT "High-resolution comparative analysis of great ape genomes.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSPPYP00000013086.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Inhibitor of PPP1CA. {ECO:0000256|RuleBase:RU369059}.
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: Membrane {ECO:0000256|RuleBase:RU369059};
CC Peripheral membrane protein {ECO:0000256|RuleBase:RU369059}.
CC -!- SIMILARITY: Belongs to the PP1 inhibitor family.
CC {ECO:0000256|ARBA:ARBA00005483, ECO:0000256|RuleBase:RU369059}.
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; NDHI03003442; PNJ49234.1; -; Genomic_DNA.
DR Ensembl; ENSPPYT00000013619.3; ENSPPYP00000013086.3; ENSPPYG00000011730.3.
DR GeneTree; ENSGT00940000159133; -.
DR HOGENOM; CLU_000288_7_23_1; -.
DR Proteomes; UP000001595; Chromosome 22.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005801; C:cis-Golgi network; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:0004864; F:protein phosphatase inhibitor activity; 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 Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 1.10.150.220; CPI-17; 1.
DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR008025; CPI-17.
DR InterPro; IPR036658; CPI-17_sf.
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; 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; PF00069; Pkinase; 1.
DR Pfam; PF05361; PP1_inhibitor; 1.
DR SMART; SM00132; LIM; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 2.
DR SUPFAM; SSF81790; Myosin phosphatase inhibitor 17kDa protein, CPI-17; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW LIM domain {ECO:0000256|ARBA:ARBA00023038, ECO:0000256|PROSITE-
KW ProRule:PRU00125}; Membrane {ECO:0000256|RuleBase:RU369059};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00125};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Phosphoprotein {ECO:0000256|RuleBase:RU369059};
KW Protein phosphatase inhibitor {ECO:0000256|ARBA:ARBA00023272,
KW ECO:0000256|RuleBase:RU369059};
KW Reference proteome {ECO:0000313|Proteomes:UP000001595};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 49..110
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 131..218
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 310..603
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 258..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 614..641
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 339
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 685 AA; 77707 MW; 27EA511B02A003A2 CRC64;
MGSYLSVPAY FTSRDPFRCS ECQDSLTNWY YEKDGKLYCP KDYWGKFGEF CHGCSLLMTG
PFMVAGEFKY HPECFACMSC KVIIEDGDAY ALVQHATLYC GKCHNEVVLA PMFERLSTES
VQEQLPYSVM LISMPATSEG RRGFSVSVES ACSNYATTVQ VKEVNRMHIS PNNRNAIHPG
DRILEINGTP VRTLRVEEVE DAISQTSQTL QLLIEHDPVS QRLDQLRLEA RLAPHIQNAG
HPHALSTLDT KENLEGTLKR RSLRRSNSIS KSPGPSSPKE PLLFSRDISR SESLRCSSSY
SQQIFRPCDL IHGEVLGKGF FGQAIKVTHK ATGKVMVMKE LIRCDEETQK TFLTEVKVMR
SLDHPNVLKF IGVLYKDKKL NLLTEYIEGG TLKDFLRSMD PFPWQQKVRF AKGIASGMAY
LHSMCIIHRD LNSHNCLIKL DKTVVVADFG LSRLIVEERK RPPMEKATTK KRTLRKNDRK
KRYTVVGNPY WMAPEMLNGK SYDETVDIFS FGIVLCEIIG QVYADPDCLP RTLDFGLNVK
LFWEKFVPTD CPPAFFPLAA ICCRLEPESR APGAAGEGPG GADDEGPVRR QGKVTIKYDH
KELRKRLNLE EWILEQLTRL YDCQEEEISE LEIDVDELLD MENDDARAAS VKELLIDCYK
PTEAFISGLL DKIRAMQKLS TPQKK
//
