ILKAP_BOVIN
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 03-AUG-2022, entry version 102.
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}.
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DR EMBL; BC122677; AAI22678.1; -; mRNA.
DR RefSeq; NP_001069123.1; NM_001075655.1.
DR AlphaFoldDB; Q0IIF0; -.
DR SMR; Q0IIF0; -.
DR STRING; 9913.ENSBTAP00000013428; -.
DR PaxDb; Q0IIF0; -.
DR Ensembl; ENSBTAT00000013428; ENSBTAP00000013428; ENSBTAG00000010176.
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; 1044139at2759; -.
DR TreeFam; TF313513; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000010176; Expressed in retina and 109 other tissues.
DR ExpressionAtlas; Q0IIF0; baseline.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR000222; PP2C_BS.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR PANTHER; PTHR13832; PTHR13832; 1.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00331; PP2C_SIG; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 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
