ILKAP_RAT
ID ILKAP_RAT Reviewed; 392 AA.
AC Q9Z1Z6; Q6P6U8;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Integrin-linked kinase-associated serine/threonine phosphatase 2C;
DE Short=ILKAP;
DE EC=3.1.3.16;
DE AltName: Full=PP2Cdelta;
GN Name=Ilkap;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], COFACTOR, TISSUE SPECIFICITY, INDUCTION, AND
RP POSSIBLE FUNCTION.
RX PubMed=9857069; DOI=10.1074/jbc.273.52.35282;
RA Tong Y., Quirion R., Shen S.-H.;
RT "Cloning and characterization of a novel mammalian PP2C isozyme.";
RL J. Biol. Chem. 273:35282-35290(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 -!- TISSUE SPECIFICITY: Widely expressed. Highest expression observed in
CC kidney, liver and muscle. {ECO:0000269|PubMed:9857069}.
CC -!- INDUCTION: Activated in response to stress, such as the addition of
CC ethanol to the culture medium or UV irradiation of cells. Inhibited
CC rather than stimulated, by Magnesium. {ECO:0000269|PubMed:9857069}.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR EMBL; AF095927; AAC97497.1; -; mRNA.
DR EMBL; BC062010; AAH62010.1; -; mRNA.
DR RefSeq; NP_072128.1; NM_022606.1.
DR AlphaFoldDB; Q9Z1Z6; -.
DR SMR; Q9Z1Z6; -.
DR STRING; 10116.ENSRNOP00000027295; -.
DR iPTMnet; Q9Z1Z6; -.
DR PhosphoSitePlus; Q9Z1Z6; -.
DR jPOST; Q9Z1Z6; -.
DR PaxDb; Q9Z1Z6; -.
DR PRIDE; Q9Z1Z6; -.
DR GeneID; 64538; -.
DR KEGG; rno:64538; -.
DR UCSC; RGD:620128; rat.
DR CTD; 80895; -.
DR RGD; 620128; Ilkap.
DR eggNOG; KOG0698; Eukaryota.
DR InParanoid; Q9Z1Z6; -.
DR OrthoDB; 1044139at2759; -.
DR PhylomeDB; Q9Z1Z6; -.
DR TreeFam; TF313513; -.
DR PRO; PR:Q9Z1Z6; -.
DR Proteomes; UP000002494; Unplaced.
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:0004722; F:protein serine/threonine phosphatase activity; IDA:RGD.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:RGD.
DR GO; GO:0033262; P:regulation of nuclear cell cycle DNA replication; IDA:RGD.
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; 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 Protein phosphatase; Reference proteome.
FT CHAIN 1..392
FT /note="Integrin-linked kinase-associated serine/threonine
FT phosphatase 2C"
FT /id="PRO_0000272273"
FT DOMAIN 108..390
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT REGION 1..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 152
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 326
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 381
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 210
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0C8"
FT CONFLICT 13
FT /note="P -> A (in Ref. 2; AAH62010)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 392 AA; 42744 MW; 1468FDE0BA60D915 CRC64;
MDLFGDLPEP ERPPRPSAGK EAQEGPVLFE DLPPTSSTDS GSGGPLLFDG LPPAGSGNSG
SLATSGSQVV KNEGKGAKRK APEEEKNGGE ELVEKKVCKA SSVIFGLKGY VAERKGEREE
MQDAHVILND ITQECNPPSS LITRVSYFAV FDGHGGIRAS KFAAQNLHQN LIRKFPKGDV
ISVEKTVKRC LLDTFKHTDE EFLKQASSQK PAWKDGSTAT CVLAVDNILY IANLGDSRAI
LCRYNEESQK HAALSLSKEH NPTQYEERMR IQKAGGNVRD GRVLGVLEVS RSIGDGQYKR
CGVTSVPDIR RCQLTPNDRF ILLACDGLFK VFTPEEAVNF ILSCLEDEKI QTREGKPAVD
ARYEAACNRL ANKAVQRGSA DNVTVMVVRI GH
