ILKAP_MOUSE
ID ILKAP_MOUSE Reviewed; 392 AA.
AC Q8R0F6; Q05CC3;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Integrin-linked kinase-associated serine/threonine phosphatase 2C;
DE Short=ILKAP;
DE EC=3.1.3.16;
GN Name=Ilkap;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N; TISSUE=Liver;
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).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R0F6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R0F6-2; Sequence=VSP_022384, VSP_022385;
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR EMBL; BC026953; AAH26953.1; -; mRNA.
DR EMBL; BC027439; AAH27439.1; -; mRNA.
DR CCDS; CCDS15162.1; -. [Q8R0F6-1]
DR RefSeq; NP_075832.1; NM_023343.2. [Q8R0F6-1]
DR RefSeq; XP_006529879.1; XM_006529816.3.
DR AlphaFoldDB; Q8R0F6; -.
DR SMR; Q8R0F6; -.
DR BioGRID; 212191; 4.
DR STRING; 10090.ENSMUSP00000027534; -.
DR iPTMnet; Q8R0F6; -.
DR PhosphoSitePlus; Q8R0F6; -.
DR EPD; Q8R0F6; -.
DR MaxQB; Q8R0F6; -.
DR PaxDb; Q8R0F6; -.
DR PeptideAtlas; Q8R0F6; -.
DR PRIDE; Q8R0F6; -.
DR ProteomicsDB; 269400; -. [Q8R0F6-1]
DR ProteomicsDB; 269401; -. [Q8R0F6-2]
DR Antibodypedia; 1494; 308 antibodies from 31 providers.
DR DNASU; 67444; -.
DR Ensembl; ENSMUST00000027534; ENSMUSP00000027534; ENSMUSG00000026309. [Q8R0F6-1]
DR GeneID; 67444; -.
DR KEGG; mmu:67444; -.
DR UCSC; uc007cak.1; mouse. [Q8R0F6-2]
DR UCSC; uc007cal.1; mouse. [Q8R0F6-1]
DR CTD; 80895; -.
DR MGI; MGI:1914694; Ilkap.
DR VEuPathDB; HostDB:ENSMUSG00000026309; -.
DR eggNOG; KOG0698; Eukaryota.
DR GeneTree; ENSGT00940000157403; -.
DR HOGENOM; CLU_013173_1_6_1; -.
DR InParanoid; Q8R0F6; -.
DR OMA; IIYCANI; -.
DR OrthoDB; 1044139at2759; -.
DR PhylomeDB; Q8R0F6; -.
DR TreeFam; TF313513; -.
DR BioGRID-ORCS; 67444; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Ilkap; mouse.
DR PRO; PR:Q8R0F6; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8R0F6; protein.
DR Bgee; ENSMUSG00000026309; Expressed in retinal neural layer and 263 other tissues.
DR ExpressionAtlas; Q8R0F6; baseline and differential.
DR Genevisible; Q8R0F6; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; ISO:MGI.
DR GO; GO:0033262; P:regulation of nuclear cell cycle DNA replication; ISO:MGI.
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 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Hydrolase; Magnesium;
KW Manganese; Metal-binding; Protein phosphatase; Reference proteome.
FT CHAIN 1..392
FT /note="Integrin-linked kinase-associated serine/threonine
FT phosphatase 2C"
FT /id="PRO_0000272272"
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 VAR_SEQ 1..120
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022384"
FT VAR_SEQ 347..392
FT /note="DDKIQTREGKPAVDARYEAACNRLANKAVQRGSADNVTVMVVRIGH -> VP
FT RQLHSSRSCFPEVSPERMTVVLAYTQLSISGVLGSLPEWMV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022385"
SQ SEQUENCE 392 AA; 42774 MW; 8DE1F77DAC9B7176 CRC64;
MDLFGDLPEP ERAPRPSAGK EAQGRPVLFE DLPPASSTDS GSGGPLLFDD LPPAASGNSG
SLATSGSQVV KTEGKGAKRK APEEEKNGGE ELVEKKVCKA SSVIFGLKGY VAERKGEREE
MQDAHVILND ITQECNPPSS LITRVSYFAV FDGHGGIRAS KFAAQNLHQN LIRKFPKGDI
ISVEKTVKRC LLDTFKHTDE EFLKQASSQK PAWKDGSTAT CVLAVDNILY IANLGDSRAI
LCRYNEESQK HAALSLSKEH NPTQYEERMR IQKAGGNVRD GRVLGVLEVS RSIGDGQYKR
CGVTSVPDIR RCQLTPNDRF ILLACDGLFK VFTPEEAVNF ILSCLEDDKI QTREGKPAVD
ARYEAACNRL ANKAVQRGSA DNVTVMVVRI GH
