ID   A0A287B700_PIG          Unreviewed;       506 AA.
AC   A0A287B700;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 2.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Protein phosphatase 1G {ECO:0000256|ARBA:ARBA00040767};
GN   Name=PPM1G {ECO:0000313|Ensembl:ENSSSCP00000052074.2,
GN   ECO:0000313|VGNC:VGNC:91707};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000052074.2, ECO:0000313|Proteomes:UP000008227};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000052074.2, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000052074.2,
RC   ECO:0000313|Proteomes:UP000008227};
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSSCP00000052074.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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   -!- SUBUNIT: Interacts with NOL3; may dephosphorylate NOL3.
CC       {ECO:0000256|ARBA:ARBA00038798}.
CC   -!- SIMILARITY: Belongs to the PP2C family.
CC       {ECO:0000256|RuleBase:RU003465}.
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DR   AlphaFoldDB; A0A287B700; -.
DR   Ensembl; ENSSSCT00000063374.3; ENSSSCP00000052074.2; ENSSSCG00000027135.4.
DR   VGNC; VGNC:91707; PPM1G.
DR   GeneTree; ENSGT00940000158427; -.
DR   Proteomes; UP000008227; Chromosome 3.
DR   Bgee; ENSSSCG00000027135; Expressed in testis and 44 other cell types or tissues.
DR   ExpressionAtlas; A0A287B700; baseline.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro.
DR   CDD; cd00143; PP2Cc; 2.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 2.
DR   InterPro; IPR015655; PP2C.
DR   InterPro; IPR000222; PP2C_BS.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   PANTHER; PTHR13832:SF876; PROTEIN PHOSPHATASE 1G; 1.
DR   PANTHER; PTHR13832; PROTEIN PHOSPHATASE 2C; 1.
DR   Pfam; PF00481; PP2C; 2.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   PROSITE; PS01032; PPM_1; 1.
DR   PROSITE; PS51746; PPM_2; 1.
PE   1: Evidence at protein level;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003465};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912,
KW   ECO:0000256|RuleBase:RU003465};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:A0A287B700};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008227}.
FT   DOMAIN          26..506
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   REGION          116..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          164..327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        201..223
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        261..314
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   506 AA;  54688 MW;  BE3C7AE859847823 CRC64;
     MGAYLSQPNT VKCSGDGVGA SRLPLPYGFS AMQGWRVSME DAHNCIPELD SETAMFSVYD
     GHGGEEVALY CAKYLPDIIK DQKAYKEGKL QKALEDAFLA IDAKLTTEEV IKELAQIAGR
     PTEDEDEKEK VADEDDVDNE EAALLHEEAT MTIEELLTRY GQNCHKGAPH SKSGAGTGEE
     AGSQGLNGEA GPEDPSRETS SEENGPTAKA HTGLSSNSER GTEAGQGGEP GTPTGEAGPS
     CSSASDKLPR VAKSKFFEDS EDESDEAEEE EEDSEECSEE EDGYSSEEAE NEEDEDDTEE
     AEEDEEEEEE MMVPGMEGKE EPGSDSGTTA VVALIRGKQL IVANAGDSRC VVSEAGKALD
     MSYDHKPEDE VELARIKNAG GKVTMDGRVN GGLNLSRAIG DHFYKRNKNL PPEEQMISAL
     PDIKVLTLTD DHEFMVIACD GIWNVMSSQE VIDFIQSKIS QRDENGELRL LSSIVEELLD
     QCLAPDTSGD GTGCDNIDNK KKAKRD
//