ID YSD1_CAEEL Reviewed; 454 AA. AC P48459; G8JY37; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 07-APR-2021, sequence version 3. DT 27-MAR-2024, entry version 136. DE RecName: Full=Serine/threonine-protein phosphatase C23G10.1 {ECO:0000305}; DE EC=3.1.3.16 {ECO:0000250|UniProtKB:P36873}; GN ORFNames=C23G10.1 {ECO:0000312|WormBase:C23G10.1b}; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; 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). 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 Evidence={ECO:0000250|UniProtKB:P36873}; 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:0000250|UniProtKB:P36873}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000250|UniProtKB:P36873}; CC Note=Binds 2 manganese ions per subunit. CC {ECO:0000250|UniProtKB:P36873}; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=b {ECO:0000312|WormBase:C23G10.1b}; CC IsoId=P48459-1; Sequence=Displayed; CC Name=a {ECO:0000312|WormBase:C23G10.1a}; CC IsoId=P48459-2; Sequence=VSP_060920, VSP_060921; CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BX284603; CCD65292.2; -; Genomic_DNA. DR EMBL; BX284603; CCD65293.2; -; Genomic_DNA. DR RefSeq; NP_498351.1; NM_065950.3. DR RefSeq; NP_498352.1; NM_065951.3. DR AlphaFoldDB; P48459; -. DR SMR; P48459; -. DR STRING; 6239.C23G10.1b.1; -. DR PaxDb; 6239-C23G10-1b; -. DR EnsemblMetazoa; C23G10.1a.1; C23G10.1a.1; WBGene00016010. [P48459-2] DR EnsemblMetazoa; C23G10.1b.1; C23G10.1b.1; WBGene00016010. [P48459-1] DR UCSC; C23G10.1b; c. elegans. [P48459-1] DR AGR; WB:WBGene00016010; -. DR WormBase; C23G10.1a; CE54137; WBGene00016010; -. [P48459-2] DR WormBase; C23G10.1b; CE54185; WBGene00016010; -. [P48459-1] DR eggNOG; KOG0374; Eukaryota. DR GeneTree; ENSGT00970000196197; -. DR HOGENOM; CLU_600258_0_0_1; -. DR InParanoid; P48459; -. DR OrthoDB; 2878863at2759; -. DR PRO; PR:P48459; -. DR Proteomes; UP000001940; Chromosome III. DR Bgee; WBGene00016010; Expressed in adult organism and 1 other cell type or tissue. DR ExpressionAtlas; P48459; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. 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:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB. DR Gene3D; 3.60.21.10; -; 1. DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH. DR InterPro; IPR029052; Metallo-depent_PP-like. DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase. DR PANTHER; PTHR11668; SERINE/THREONINE PROTEIN PHOSPHATASE; 1. DR PANTHER; PTHR11668:SF211; SERINE_THREONINE-PROTEIN PHOSPHATASE C23G10.1; 1. DR Pfam; PF00149; Metallophos; 1. DR PRINTS; PR00114; STPHPHTASE. DR SMART; SM00156; PP2Ac; 1. DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1. DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1. PE 3: Inferred from homology; KW Alternative splicing; Hydrolase; Manganese; Metal-binding; KW Protein phosphatase; Reference proteome. FT CHAIN 1..454 FT /note="Serine/threonine-protein phosphatase C23G10.1" FT /id="PRO_0000058914" FT ACT_SITE 257 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:P36873" FT BINDING 196 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P36873" FT BINDING 198 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P36873" FT BINDING 224 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P36873" FT BINDING 224 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P36873" FT BINDING 256 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P36873" FT BINDING 308 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P36873" FT BINDING 382 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P36873" FT VAR_SEQ 5 FT /note="T -> P (in isoform a)" FT /evidence="ECO:0000305" FT /id="VSP_060920" FT VAR_SEQ 12..114 FT /note="DDCTKTVYPDPIPMPTCPQLINDGTSCFLNIILQMLKRANFHDHFKGDWQKG FT KQKMLMHKELQQIFNGKPGPKDVSRLREMFSNEALKDGPHPLLVALKCLIK -> E FT (in isoform a)" FT /evidence="ECO:0000305" FT /id="VSP_060921" SQ SEQUENCE 454 AA; 51755 MW; 226976410DDFCC46 CRC64; MSKKTRVPEV ADDCTKTVYP DPIPMPTCPQ LINDGTSCFL NIILQMLKRA NFHDHFKGDW QKGKQKMLMH KELQQIFNGK PGPKDVSRLR EMFSNEALKD GPHPLLVALK CLIKMSAVSD NDVIKEKGAR DKMFQKQSDE SNKMFAEHFI KTLLACKGMT KIRTMDIFRL IHICKKIFTV QKSMVEIDGP VRICGDLHGQ YPDLIRLFAQ GGFPPDSNYL FLGDYVDRGS FNLEVILLCL AYKARYPNNF MMLRGNHEVI HINEKYGFKD EVFNRKGEYH DELYPEFNEM MDMMPLVALV GGRILCMHGG LSQHIKSLDD LRNLRRPFHS EDECLENDIM WSDPAKVSGW TANPRGASVQ FGENEVKEMC KLLDIDLIVR GHQVVQDGYE FFAGKKLVTV FSAPHYMQSF TNSAAVCKVS AGLEVSFEVL KPEDIRVEEI KCSAESSCAS DMQQ //