IPP2C_MACFA
ID IPP2C_MACFA Reviewed; 205 AA.
AC Q4R615; G7P816;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Protein phosphatase inhibitor 2 family member C;
DE AltName: Full=Protein phosphatase 1, regulatory subunit 2 pseudogene 9;
DE AltName: Full=Type-1 protein phosphatase inhibitor 4;
DE Short=I-4;
GN Name=PPP1R2C; Synonyms=PPP1R2P9; ORFNames=QtsA-19341;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22002653; DOI=10.1038/nbt.1992;
RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT "Genome sequencing and comparison of two nonhuman primate animal models,
RT the cynomolgus and Chinese rhesus macaques.";
RL Nat. Biotechnol. 29:1019-1023(2011).
CC -!- FUNCTION: Functions as a protein phosphatase inhibitor. It inhibits
CC activity of the catalytic subunit of PP1 and weakly inhibits the
CC activity of myosin-associated phosphates (By similarity).
CC {ECO:0000250|UniProtKB:O14990}.
CC -!- SIMILARITY: Belongs to the protein phosphatase inhibitor 2 family.
CC {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; AB169376; BAE01460.1; -; mRNA.
DR EMBL; CM001281; EHH54437.1; -; Genomic_DNA.
DR RefSeq; NP_001270534.1; NM_001283605.1.
DR AlphaFoldDB; Q4R615; -.
DR STRING; 9541.XP_005593398.1; -.
DR Ensembl; ENSMFAT00000086578; ENSMFAP00000046357; ENSMFAG00000064193.
DR GeneID; 101925705; -.
DR CTD; 80316; -.
DR eggNOG; KOG4041; Eukaryota.
DR GeneTree; ENSGT00940000164483; -.
DR OrthoDB; 1321970at2759; -.
DR Proteomes; UP000009130; Chromosome 6.
DR Proteomes; UP000233100; Chromosome X.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; IEA:InterPro.
DR GO; GO:0009966; P:regulation of signal transduction; IEA:InterPro.
DR InterPro; IPR007062; PPI-2.
DR PANTHER; PTHR12398; PTHR12398; 1.
DR Pfam; PF04979; IPP-2; 1.
PE 2: Evidence at transcript level;
KW Protein phosphatase inhibitor; Reference proteome.
FT CHAIN 1..205
FT /note="Protein phosphatase inhibitor 2 family member C"
FT /id="PRO_0000286139"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 12..17
FT /note="Required for binding PPP1CC"
FT /evidence="ECO:0000250"
FT REGION 43..55
FT /note="Required for binding PPP1CC"
FT /evidence="ECO:0000250"
FT REGION 70..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..150
FT /note="Required for binding PPP1CC catalytic center,
FT displacing metal ions and inhibition of PPP1CC catalytic
FT activity"
FT /evidence="ECO:0000250"
FT REGION 165..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 205 AA; 23070 MW; 4EEF2006B0854099 CRC64;
MSASTSSHRP IKGILKNKSS SGSSVATSGQ QSGGNIQDVK RKKSQKWDES SILATHRATY
RDYDLMKANE PGTSYMNLQD DGEDSVRDVE GEDSVRGVEG KEAMAATDAS DHSCEVEEEE
SNEAYMRKLL LHKQEKKRQF EIRRRLHYNE ELNIKLARQL MWNDLQSEDD ENEERPQATN
EEKTAAEESE EAPLSGGLQT QSCDP