ID U3JLE4_FICAL Unreviewed; 389 AA.
AC U3JLE4;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Protein phosphatase 1A {ECO:0000256|ARBA:ARBA00040766};
DE AltName: Full=Protein phosphatase 2C isoform alpha {ECO:0000256|ARBA:ARBA00041227};
GN Name=PPM1A {ECO:0000313|Ensembl:ENSFALP00000003598.2};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000003598.2, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000003598.2, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000003598.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 Evidence={ECO:0000256|ARBA:ARBA00001482};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}. Membrane
CC {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004635}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000256|ARBA:ARBA00006702,
CC ECO:0000256|RuleBase:RU003465}.
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DR AlphaFoldDB; U3JLE4; -.
DR STRING; 59894.ENSFALP00000003598; -.
DR Ensembl; ENSFALT00000003612.2; ENSFALP00000003598.2; ENSFALG00000003457.2.
DR eggNOG; KOG0697; Eukaryota.
DR GeneTree; ENSGT00940000154832; -.
DR HOGENOM; CLU_013173_4_0_1; -.
DR OrthoDB; 11028at2759; -.
DR Proteomes; UP000016665; Chromosome 5.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0033192; F:calmodulin-dependent protein phosphatase activity; IEA:Ensembl.
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:0070412; F:R-SMAD binding; IEA:Ensembl.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
DR GO; GO:0016311; P:dephosphorylation; IEA:Ensembl.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IEA:Ensembl.
DR GO; GO:0043124; P:negative regulation of canonical NF-kappaB signal transduction; IEA:Ensembl.
DR GO; GO:1901223; P:negative regulation of non-canonical NF-kappaB signal transduction; IEA:Ensembl.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:Ensembl.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; IEA:Ensembl.
DR GO; GO:0006611; P:protein export from nucleus; IEA:Ensembl.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 1.10.10.430; Phosphatase 2C, C-terminal domain suprefamily; 1.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR000222; PP2C_BS.
DR InterPro; IPR012911; PP2C_C.
DR InterPro; IPR036580; PP2C_C_sf.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR PANTHER; PTHR47992; PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR47992:SF121; PROTEIN PHOSPHATASE 1A; 1.
DR Pfam; PF00481; PP2C; 1.
DR Pfam; PF07830; PP2C_C; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR SUPFAM; SSF81601; Protein serine/threonine phosphatase 2C, C-terminal domain; 1.
DR PROSITE; PS01032; PPM_1; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003465};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Myristate {ECO:0000256|ARBA:ARBA00022707};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912,
KW ECO:0000256|RuleBase:RU003465};
KW Reference proteome {ECO:0000313|Proteomes:UP000016665}.
FT DOMAIN 23..291
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
SQ SEQUENCE 389 AA; 43530 MW; 45FA63C928E1AE7D CRC64;
MGAFLDKPKM EKHNAQGQGN GLRYGLSSMQ GWRVEMEDAH TAVIGLPNGL DGWSFFAVYD
GHAGSQVAKY CCEHLLDHIT SNQDFKGPDG PPSVESVKCG IRTGFLQIDE HMRVISEKKH
GADRSGSTAV GVMISPQHTY FINCGDSRGL LCRNRKVHFF TQDHKPSNPL EKERIQNAGG
SVMIQRVNGS LAVSRALGDF DYKCVHGKGP TEQLVSPEPE VYEIERSEED DQFIILACDG
IWDVMGNEEL CDFVRSRLEV TDDLEKVCNE IVDTCLYKGS RDNMSVILIC FPNAPKVSPE
AVKREAELDK YLESRVEEII KKQGEGVPDL VHVMRTLATE SIPNLPPGGE LASKRSVIEA
VYNRLNPYRN DDALNKLRYA CRWWRLALE
//
