ID ILKAP_BOVIN Reviewed; 370 AA. AC Q0IIF0; DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2006, sequence version 1. DT 27-MAR-2024, entry version 110. DE RecName: Full=Integrin-linked kinase-associated serine/threonine phosphatase 2C; DE Short=ILKAP; DE EC=3.1.3.16; GN Name=ILKAP; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Hereford; TISSUE=Hippocampus; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Protein phosphatase that may play a role in regulation of CC cell cycle progression via dephosphorylation of its substrates whose CC appropriate phosphorylation states might be crucial for cell CC proliferation. Selectively associates with integrin linked kinase CC (ILK), to modulate cell adhesion and growth factor signaling. Inhibits CC the ILK-GSK3B signaling axis and may play an important role in CC inhibiting oncogenic transformation (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:83421; EC=3.1.3.16; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:61977; EC=3.1.3.16; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250}; CC -!- SUBUNIT: Interacts with ILK. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC122677; AAI22678.1; -; mRNA. DR RefSeq; NP_001069123.1; NM_001075655.1. DR AlphaFoldDB; Q0IIF0; -. DR SMR; Q0IIF0; -. DR STRING; 9913.ENSBTAP00000062322; -. DR PaxDb; 9913-ENSBTAP00000013428; -. DR Ensembl; ENSBTAT00000013428.6; ENSBTAP00000013428.5; ENSBTAG00000010176.6. DR GeneID; 514223; -. DR KEGG; bta:514223; -. DR CTD; 80895; -. DR VEuPathDB; HostDB:ENSBTAG00000010176; -. DR VGNC; VGNC:30178; ILKAP. DR eggNOG; KOG0698; Eukaryota. DR GeneTree; ENSGT00940000157403; -. DR HOGENOM; CLU_013173_1_6_1; -. DR InParanoid; Q0IIF0; -. DR OrthoDB; 202023at2759; -. DR TreeFam; TF313513; -. DR Proteomes; UP000009136; Chromosome 3. DR Bgee; ENSBTAG00000010176; Expressed in retina and 109 other cell types or tissues. DR ExpressionAtlas; Q0IIF0; baseline. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC. DR CDD; cd00143; PP2Cc; 1. DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1. DR InterPro; IPR015655; PP2C. DR InterPro; IPR000222; PP2C_BS. DR InterPro; IPR036457; PPM-type-like_dom_sf. DR InterPro; IPR001932; PPM-type_phosphatase-like_dom. DR PANTHER; PTHR47992; PROTEIN PHOSPHATASE; 1. DR PANTHER; PTHR47992:SF105; PROTEIN PHOSPHATASE 1B; 1. DR Pfam; PF00481; PP2C; 1. DR SMART; SM00331; PP2C_SIG; 1. DR SMART; SM00332; PP2Cc; 1. DR SUPFAM; SSF81606; PP2C-like; 1. DR PROSITE; PS01032; PPM_1; 1. DR PROSITE; PS51746; PPM_2; 1. PE 2: Evidence at transcript level; KW Acetylation; Cytoplasm; Hydrolase; Magnesium; Manganese; Metal-binding; KW Phosphoprotein; Protein phosphatase; Reference proteome. FT CHAIN 1..370 FT /note="Integrin-linked kinase-associated serine/threonine FT phosphatase 2C" FT /id="PRO_0000272270" FT DOMAIN 86..368 FT /note="PPM-type phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082" FT REGION 1..69 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 46..69 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 130 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 130 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 131 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 304 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 359 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:Q9H0C8" FT MOD_RES 13 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9H0C8" FT MOD_RES 188 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9H0C8" SQ SEQUENCE 370 AA; 40622 MW; 3435602459B36030 CRC64; MDLFGDLPEP ERSPRPAAGS GGPLLFDDLP PASSGDSGSL DTSLSEEVKN EGKGAKRKAS DEEKNGSEEL VEKKVCKASS VIFSLKGYVA ERKGEREEMQ DAHVILNDIT AECQPPSALV TRVSYFAVFD GHGGIRASKF AAQNLHQNLI RKFPKGDGIS VEKTVKRCLL DTFKHTDEEF LKQASSQKPA WKDGSTATCV LAVDNTLYIA NLGDSRAILC RYNEESQKHA ALSLSKEHNP TQYEERMRIQ KAGGNVRDGR VLGVLEVSRS IGDGQYKRCG VTSVPDIRRC QLTPNDRFIL LACDGLFKVF TPEEAVNFIL SCLEDEKIQR REGKPTVDAR YEAACNRLAN KAVQRGSADN VTVMVVRIGL //