YSD1_CAEEL
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 03-AUG-2022, entry version 129.
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}.
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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; -.
DR PaxDb; P48459; -.
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 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; 766640at2759; -.
DR PRO; PR:P48459; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00016010; Expressed in adult organism and 1 other tissue.
DR ExpressionAtlas; P48459; baseline.
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 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 Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; SSF56300; 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
