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PPM1A_BOVIN
ID   PPM1A_BOVIN             Reviewed;         382 AA.
AC   O62829;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=Protein phosphatase 1A;
DE            EC=3.1.3.16;
DE   AltName: Full=Protein phosphatase 2C isoform alpha;
DE            Short=PP2C-alpha;
GN   Name=PPM1A;
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 [MRNA].
RC   TISSUE=Retina;
RX   PubMed=9486768;
RX   DOI=10.1002/(sici)1097-4547(19980201)51:3<328::aid-jnr6>3.0.co;2-i;
RA   Klumpp S., Selke D., Fischer D., Baumann A., Mueller F., Thanos S.;
RT   "Protein phosphatase type-2C isozymes present in vertebrate retinae:
RT   purification, characterization, and localization in photoreceptors.";
RL   J. Neurosci. Res. 51:328-338(1998).
CC   -!- FUNCTION: Enzyme with a broad specificity. Negatively regulates TGF-
CC       beta signaling through dephosphorylating SMAD2 and SMAD3, resulting in
CC       their dissociation from SMAD4, nuclear export of the SMADs and
CC       termination of the TGF-beta-mediated signaling (By similarity).
CC       Dephosphorylates PRKAA1 and PRKAA2. Plays an important role in the
CC       termination of TNF-alpha-mediated NF-kappa-B activation through
CC       dephosphorylating and inactivating IKBKB/IKKB (By similarity).
CC       {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;
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC       Note=Binds 2 magnesium or manganese ions per subunit.;
CC   -!- SUBUNIT: Monomer. Interacts with SMAD2; the interaction
CC       dephosphorylates SMAD2 in its C-terminal SXS motif resulting in
CC       disruption of the SMAD2/SMAD4 complex, SMAD2 nuclear export and
CC       termination of the TGF-beta-mediated signaling. Interacts with SMAD2;
CC       the interaction dephosphorylates SMAD2 in its C-terminal SXS motif
CC       resulting in disruption of the SMAD2/SMAD4 complex, SMAD2 nuclear
CC       export and termination of the TGF-beta-mediated signaling (By
CC       similarity). Interacts with the phosphorylated form of IKBKB/IKKB (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P35813}.
CC       Cytoplasm, cytosol {ECO:0000250|UniProtKB:P35813}. Membrane
CC       {ECO:0000250|UniProtKB:P35813}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P35813}. Note=Weakly associates at the membrane
CC       and N-myristoylation mediates the membrane localization.
CC       {ECO:0000250|UniProtKB:P49443}.
CC   -!- PTM: N-myristoylation is essential for the recognition of its
CC       substrates for dephosphorylation. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR   EMBL; AJ005457; CAA06554.1; -; mRNA.
DR   RefSeq; NP_001289701.1; NM_001302772.1.
DR   RefSeq; NP_776854.1; NM_174429.3.
DR   RefSeq; XP_015328708.1; XM_015473222.1.
DR   AlphaFoldDB; O62829; -.
DR   SMR; O62829; -.
DR   STRING; 9913.ENSBTAP00000024128; -.
DR   PaxDb; O62829; -.
DR   PRIDE; O62829; -.
DR   Ensembl; ENSBTAT00000024128; ENSBTAP00000024128; ENSBTAG00000018127.
DR   GeneID; 281994; -.
DR   KEGG; bta:281994; -.
DR   CTD; 5494; -.
DR   VEuPathDB; HostDB:ENSBTAG00000018127; -.
DR   eggNOG; KOG0697; Eukaryota.
DR   GeneTree; ENSGT00940000154832; -.
DR   HOGENOM; CLU_013173_4_0_1; -.
DR   InParanoid; O62829; -.
DR   OrthoDB; 957254at2759; -.
DR   TreeFam; TF313590; -.
DR   Reactome; R-BTA-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR   Proteomes; UP000009136; Chromosome 10.
DR   Bgee; ENSBTAG00000018127; Expressed in longissimus thoracis muscle and 106 other tissues.
DR   ExpressionAtlas; O62829; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; ISS:AgBase.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR   GO; GO:0070412; F:R-SMAD binding; ISS:UniProtKB.
DR   GO; GO:0006499; P:N-terminal protein myristoylation; ISS:UniProtKB.
DR   GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR   GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; ISS:UniProtKB.
DR   GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IBA:GO_Central.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR   GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:AgBase.
DR   GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
DR   CDD; cd00143; PP2Cc; 1.
DR   Gene3D; 1.10.10.430; -; 1.
DR   Gene3D; 3.60.40.10; -; 1.
DR   InterPro; IPR000222; PP2C_BS.
DR   InterPro; IPR012911; PP2C_C.
DR   InterPro; IPR036580; PP2C_C_sf.
DR   InterPro; IPR036457; PPM-type_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase_dom.
DR   Pfam; PF00481; PP2C; 1.
DR   Pfam; PF07830; PP2C_C; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81601; SSF81601; 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   Cytoplasm; Hydrolase; Lipoprotein; Magnesium; Manganese; Membrane;
KW   Metal-binding; Myristate; Nucleus; Phosphoprotein; Protein phosphatase;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
FT   CHAIN           2..382
FT                   /note="Protein phosphatase 1A"
FT                   /id="PRO_0000057740"
FT   DOMAIN          23..291
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   BINDING         60
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         60
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         61
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         239
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         282
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         375
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
FT   MOD_RES         377
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P49443"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
SQ   SEQUENCE   382 AA;  42530 MW;  A716B3FA0E7E21C2 CRC64;
     MGAFLDKPKM EKHNAQGQGN GLRYGLSSMQ GWRVEMEDAH TAVIGLPSGL ETWSFFAVYD
     GHAGSQVAKY CCEHLLDHIT NNQDFKGSAG APSVENVKNG IRTGFLEIDE HMRVMSEKKH
     GADRSGSTAV GVLISPQHTY FINCGDSRGL LCRNRKVYFF TQDHKPSNPL EKERIQNAGG
     SVMIQRVNGS LAVSRALGDF DYKCVHGKGP TEQLVSPEPE VHDIERSEED DQFIILACDG
     IWDVMGNEEL CDFVRSRLEV TDDLEKVCNE VVDTCLYKGS RDNMSVILIC FPNAPKVSPE
     AVKKEEELDK YLESRVEEII KKQGEGVPDL VHVMRTLASE NIPSLPPGGE LASKRNVIEA
     VYNRLNPYKN DDTDSTSTDD MW
 
 
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