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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}.
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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
 
 
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