PPM1A_CAEEL
ID PPM1A_CAEEL Reviewed; 468 AA.
AC Q19775; A8WHR6; Q7JLJ3;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Protein phosphatase ppm-1.A {ECO:0000305};
DE EC=3.1.3.16 {ECO:0000255|PROSITE-ProRule:PRU01082};
DE AltName: Full=Protein phosphatase 2C 1 {ECO:0000305};
DE AltName: Full=Protein phosphatase Mg2+/Mn2+ dependent 1 {ECO:0000312|WormBase:F25D1.1a};
GN Name=ppm-1.A {ECO:0000312|WormBase:F25D1.1a};
GN ORFNames=F25D1.1 {ECO:0000312|WormBase:F25D1.1a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF ASP-329.
RX PubMed=21968191; DOI=10.1534/genetics.111.134791;
RA Tulgren E.D., Baker S.T., Rapp L., Gurney A.M., Grill B.;
RT "PPM-1, a PP2Calpha/beta phosphatase, regulates axon termination and
RT synapse formation in Caenorhabditis elegans.";
RL Genetics 189:1297-1307(2011).
CC -!- FUNCTION: Probable phosphatase which regulates axon termination in ALM
CC and PLM neurons, and synaptic branch extension and/or stabilization in
CC PLM neurons. Plays a role in synapse formation in GABAergic DD motor
CC neurons probably by dephosphorylating pmk-3 thereby negatively
CC regulating a MAP kinase pathway that includes dlk-1, mkk-4 and pmk-3.
CC {ECO:0000269|PubMed:21968191}.
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; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU01082};
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; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU01082};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01082};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01082};
CC Note=Binds 2 magnesium or manganese ions per subunit.
CC {ECO:0000255|PROSITE-ProRule:PRU01082};
CC -!- SUBCELLULAR LOCATION: Synapse {ECO:0000269|PubMed:21968191}.
CC Note=Localizes to presynaptic terminals of motor neurons in the dorsal
CC nerve cord. {ECO:0000269|PubMed:21968191}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a {ECO:0000312|WormBase:F25D1.1a};
CC IsoId=Q19775-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:F25D1.1b};
CC IsoId=Q19775-4; Sequence=VSP_058263;
CC Name=c {ECO:0000312|WormBase:F25D1.1c};
CC IsoId=Q19775-5; Sequence=VSP_058264;
CC -!- TISSUE SPECIFICITY: Expressed in neurons of the nerve ring and motor
CC neurons of the ventral nerve cord. {ECO:0000269|PubMed:21968191}.
CC -!- DISRUPTION PHENOTYPE: Approximately 15 percent of mutants have an
CC overextension of the axon of ALM neurons which terminates with a small
CC hook. Approximately 30 percent of mutants have an overextension of the
CC axon of PLM neurons. Approximately 10 percent of mutants lack synaptic
CC branch extension in PLM neurons. {ECO:0000269|PubMed:21968191}.
CC -!- SIMILARITY: Belongs to the PP2C family.
CC {ECO:0000255|RuleBase:RU003465}.
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DR EMBL; BX284605; CAA98265.1; -; Genomic_DNA.
DR EMBL; BX284605; CAE54908.1; -; Genomic_DNA.
DR EMBL; BX284605; CAP16273.1; -; Genomic_DNA.
DR PIR; T21331; T21331.
DR RefSeq; NP_001023842.1; NM_001028671.3. [Q19775-1]
DR RefSeq; NP_001023843.1; NM_001028672.4. [Q19775-4]
DR RefSeq; NP_001122929.1; NM_001129457.2. [Q19775-5]
DR AlphaFoldDB; Q19775; -.
DR SMR; Q19775; -.
DR DIP; DIP-25616N; -.
DR STRING; 6239.F25D1.1a; -.
DR EPD; Q19775; -.
DR PaxDb; Q19775; -.
DR PeptideAtlas; Q19775; -.
DR PRIDE; Q19775; -.
DR EnsemblMetazoa; F25D1.1a.1; F25D1.1a.1; WBGene00006460. [Q19775-1]
DR EnsemblMetazoa; F25D1.1b.1; F25D1.1b.1; WBGene00006460. [Q19775-4]
DR EnsemblMetazoa; F25D1.1c.1; F25D1.1c.1; WBGene00006460. [Q19775-5]
DR GeneID; 179469; -.
DR KEGG; cel:CELE_F25D1.1; -.
DR UCSC; F25D1.1a; c. elegans.
DR CTD; 179469; -.
DR WormBase; F25D1.1a; CE05722; WBGene00006460; ppm-1.A. [Q19775-1]
DR WormBase; F25D1.1b; CE36134; WBGene00006460; ppm-1.A. [Q19775-4]
DR WormBase; F25D1.1c; CE41642; WBGene00006460; ppm-1.A. [Q19775-5]
DR eggNOG; KOG0697; Eukaryota.
DR GeneTree; ENSGT00940000165923; -.
DR InParanoid; Q19775; -.
DR OMA; KRMAINI; -.
DR OrthoDB; 957254at2759; -.
DR PhylomeDB; Q19775; -.
DR Reactome; R-CEL-1169408; ISG15 antiviral mechanism.
DR Reactome; R-CEL-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR Reactome; R-CEL-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR PRO; PR:Q19775; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00006460; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0032873; P:negative regulation of stress-activated MAPK cascade; IBA:GO_Central.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IBA:GO_Central.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR000222; PP2C_BS.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS01032; PPM_1; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Protein phosphatase; Reference proteome; Synapse.
FT CHAIN 1..468
FT /note="Protein phosphatase ppm-1.A"
FT /evidence="ECO:0000305"
FT /id="PRO_0000436100"
FT DOMAIN 106..381
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 145
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9CAJ0"
FT BINDING 145
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O75688"
FT BINDING 146
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9CAJ0"
FT BINDING 329
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O75688"
FT BINDING 372
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O75688"
FT VAR_SEQ 1..106
FT /note="MTISRADLQIASSAEPKTHGNLNESFAPEIRQTASTIASLSIFGTPSDQECQ
FT PIPVVPRSSSSDELRVWRVTSAGLVEVDAKTMGAFLDKPKTDKTNVHGEGNGIR -> M
FT EKEI (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_058263"
FT VAR_SEQ 1..83
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_058264"
FT MUTAGEN 329
FT /note="D->N: Probable loss of phosphatase activity. No
FT rescue of abnormal axon termination in a fsn-1 mutant
FT background."
FT /evidence="ECO:0000269|PubMed:21968191"
SQ SEQUENCE 468 AA; 51899 MW; 7E76592F4DE8BC0E CRC64;
MTISRADLQI ASSAEPKTHG NLNESFAPEI RQTASTIASL SIFGTPSDQE CQPIPVVPRS
SSSDELRVWR VTSAGLVEVD AKTMGAFLDK PKTDKTNVHG EGNGIRYGMS SMQGWRICME
DSHIAEAIMS QSSPYKDWSF FAVFDGHAGH HIANRASSQL LEHLISSEEF REMTKTLEEN
NGVLTDSTLK LLEKGIKKGF LSFDEISKTS NDISKSGCTA VCAIVTPTHF IIGNLGDSRA
VVAGKNEIFG TEDHKPYLEK ERKRIEGAGG SVMIQRINGS LAVSRAFGDY EYKDDPRLPA
DQQLVSPEPD VYIRERNLEN DQFMVVACDG IYDVMTNEEL AEFVKDRLSV HSDLREVCDD
VLDECLVKGS RDNMTMVVVC FPAAPEVNIH RKEAEEAWVS RVKTVINQFL DEAVAAEDFK
QEEDMVTLKS ILDKVTANGL LPTDLRVPEH TVTTLAQKIL TQRDIKHV
