ID A0A2U9CMQ7_SCOMX Unreviewed; 480 AA.
AC A0A2U9CMQ7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Protein phosphatase, Mg2+/Mn2+ dependent, 1Bb {ECO:0000313|Ensembl:ENSSMAP00000007711.2};
GN Name=ppm1bb {ECO:0000313|Ensembl:ENSSMAP00000007711.2};
GN ORFNames=F2P81_022490 {ECO:0000313|EMBL:KAF0025609.1}, SMAX5B_017255
GN {ECO:0000313|EMBL:AWP17924.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP17924.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP17924.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAF0025609.1, ECO:0000313|Proteomes:UP000438429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ysfricsl-2016a {ECO:0000313|EMBL:KAF0025609.1};
RC TISSUE=Blood {ECO:0000313|EMBL:KAF0025609.1};
RA Xu H., Xu X.-W., Shao C., Chen S.;
RT "Draft genomes of female and male turbot (Scophthalmus maximus).";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSSMAP00000007711.2}
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}.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000256|ARBA:ARBA00006702,
CC ECO:0000256|RuleBase:RU003465}.
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DR EMBL; CP026260; AWP17924.1; -; Genomic_DNA.
DR EMBL; VEVO01000020; KAF0025609.1; -; Genomic_DNA.
DR STRING; 52904.ENSSMAP00000007724; -.
DR Ensembl; ENSSMAT00000007809.2; ENSSMAP00000007711.2; ENSSMAG00000004769.2.
DR GeneTree; ENSGT00940000156070; -.
DR OrthoDB; 11028at2759; -.
DR Proteomes; UP000246464; Chromosome 18.
DR Proteomes; UP000438429; Unassembled WGS sequence.
DR Proteomes; UP000694558; Chromosome 18.
DR Bgee; ENSSMAG00000004769; Expressed in muscle tissue and 6 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; 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:SF105; PROTEIN PHOSPHATASE 1B; 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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912,
KW ECO:0000256|RuleBase:RU003465};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464}.
FT DOMAIN 23..290
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 368..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..462
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 480 AA; 51475 MW; 2006556AFFEFDDF5 CRC64;
MGAFLDKPKT EKHSAHGEGN GLLYGLSSMQ GWRVEMEDAH TAAVGLPHGL TDWSFFAVYD
GHAGSRVANY CSGHLLEHIL TGGVDFGSGA GSVDGVKDGI RLGFLNIDEY MRSFTDLRQG
LDRSGSTAVC VLLSPTHLYF INCGDSRAVL SRDGKVGFST QDHKPCNPRE KERIQNAGGS
VMIQRVNGSL AVSRALGDYD YKCVDGKGPT EQLVSPEPEV CVLERAAEGD EFVVLACDGI
WDVMSNEELC EFVRSRLLVC DDLEKVCNSV VDTCLHKGSR DNMSVVLVCL PGAPKISEEA
VKKEEELDKY LETRVEELLG NCGDAGVPDL VSVLRSIATE NIPNLPPGGG LASKRSVIEA
MYNKLNPHRE EEGASAGGEE ESEEGGGSTA AHLLEALRQF RLHHRGQYRT VLEESLVAYH
LRGESAAEGT GESPRTSDNN DGQEQPASPP SPPSPPPSPA TAEPEASQDA PTPESDPSSD
//
