ID GLC7C_CAEEL Reviewed; 305 AA.
AC O02658;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 27-MAR-2024, entry version 156.
DE RecName: Full=Serine/threonine-protein phosphatase PP1-gamma {ECO:0000305};
DE EC=3.1.3.16 {ECO:0000255|RuleBase:RU004273};
DE AltName: Full=CeGLC-7-gamma {ECO:0000305};
DE AltName: Full=Glc seven-like phosphatase 3 {ECO:0000312|WormBase:W09C3.6};
GN Name=gsp-3 {ECO:0000312|WormBase:W09C3.6};
GN ORFNames=W09C3.6 {ECO:0000312|WormBase:W09C3.6};
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, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=16943775; DOI=10.1038/nature05050;
RA Chu D.S., Liu H., Nix P., Wu T.F., Ralston E.J., Yates J.R. III,
RA Meyer B.J.;
RT "Sperm chromatin proteomics identifies evolutionarily conserved fertility
RT factors.";
RL Nature 443:101-105(2006).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=22042574; DOI=10.1534/genetics.111.135376;
RA Wu J.C., Go A.C., Samson M., Cintra T., Mirsoian S., Wu T.F., Jow M.M.,
RA Routman E.J., Chu D.S.;
RT "Sperm development and motility are regulated by PP1 phosphatases in
RT Caenorhabditis elegans.";
RL Genetics 190:143-157(2012).
CC -!- FUNCTION: Probable phosphatase which plays a redundant role with gsp-4
CC in spermatogenesis by regulating sister chromatid segregation during
CC meiosis (PubMed:16943775, PubMed:22042574). In addition, involved in
CC sperm motility by controlling the dynamic disassembly of major sperm
CC proteins (MSP) in the spermatozoan pseudopodium (PubMed:22042574).
CC {ECO:0000269|PubMed:16943775, ECO:0000269|PubMed:22042574}.
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:0000255|RuleBase:RU004273};
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:0000255|RuleBase:RU004273};
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:16943775}. Cell
CC projection, pseudopodium {ECO:0000269|PubMed:22042574}. Cytoplasm
CC {ECO:0000269|PubMed:22042574}. Note=Co-localizes with MSP in oblong
CC stripes in the cytoplasm of inactive sperm and in the pseudopodium in
CC activated sperm. {ECO:0000269|PubMed:22042574}.
CC -!- TISSUE SPECIFICITY: Expressed in male germline including spermatocytes,
CC spermatids and spermatozoa. {ECO:0000269|PubMed:16943775,
CC ECO:0000269|PubMed:22042574}.
CC -!- DEVELOPMENTAL STAGE: Expressed at all stages of spermatocyte meiosis.
CC {ECO:0000269|PubMed:16943775, ECO:0000269|PubMed:22042574}.
CC -!- DISRUPTION PHENOTYPE: No obvious phenotype (PubMed:22042574).
CC Simultaneous RNAi-mediated knockdown of gsp-3 and gsp-4 results in male
CC sterility due to chromosome segregation defects during sperm meiosis
CC (PubMed:16943775). gsp-3 and gsp-4 double mutant hermaphrodites have
CC egg laying defects and no viable progeny. gsp-3, gsp-4 and him-8 triple
CC mutants have incomplete separation of sister chromatids during the
CC second meiotic segregation. Mislocalization of MSP in activated sperm.
CC In addition, have partial reduction in mpk-1 phosphorylation and air-2
CC association with bivalent chromosomes in the most proximal oocyte in
CC response to MSP (PubMed:22042574). {ECO:0000269|PubMed:16943775,
CC ECO:0000269|PubMed:22042574}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family.
CC {ECO:0000255|RuleBase:RU004273}.
CC -!- CAUTION: Due to the high similarity between gsp-3 and gsp-4, the
CC antibody used to study expression does not distinguish between the two
CC proteins. {ECO:0000303|PubMed:16943775, ECO:0000303|PubMed:22042574}.
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DR EMBL; BX284601; CCD64235.1; -; Genomic_DNA.
DR PIR; T34462; T34462.
DR RefSeq; NP_491429.1; NM_059028.3.
DR AlphaFoldDB; O02658; -.
DR SMR; O02658; -.
DR DIP; DIP-27281N; -.
DR STRING; 6239.W09C3.6.1; -.
DR EPD; O02658; -.
DR PaxDb; 6239-W09C3-6; -.
DR PeptideAtlas; O02658; -.
DR EnsemblMetazoa; W09C3.6.1; W09C3.6.1; WBGene00021113.
DR EnsemblMetazoa; W09C3.6.2; W09C3.6.2; WBGene00021113.
DR GeneID; 172082; -.
DR KEGG; cel:CELE_W09C3.6; -.
DR UCSC; W09C3.6; c. elegans.
DR AGR; WB:WBGene00021113; -.
DR WormBase; W09C3.6; CE14754; WBGene00021113; gsp-3.
DR eggNOG; KOG0374; Eukaryota.
DR GeneTree; ENSGT00940000169571; -.
DR HOGENOM; CLU_004962_0_0_1; -.
DR InParanoid; O02658; -.
DR OMA; CCTVAKS; -.
DR OrthoDB; 2871629at2759; -.
DR PhylomeDB; O02658; -.
DR SignaLink; O02658; -.
DR PRO; PR:O02658; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00021113; Expressed in adult organism and 2 other cell types or tissues.
DR GO; GO:0000785; C:chromatin; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031143; C:pseudopodium; IDA:WormBase.
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:0097723; P:amoeboid sperm motility; IGI:WormBase.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0018991; P:egg-laying behavior; IGI:WormBase.
DR GO; GO:0007060; P:male meiosis chromosome segregation; IGI:WormBase.
DR GO; GO:0031272; P:regulation of pseudopodium assembly; IGI:WormBase.
DR GO; GO:0000003; P:reproduction; IMP:WormBase.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
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 InterPro; IPR031675; STPPase_N.
DR PANTHER; PTHR11668; SERINE/THREONINE PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR11668:SF492; SERINE_THREONINE-PROTEIN PHOSPHATASE PP1-DELTA-RELATED; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF16891; STPPase_N; 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 2: Evidence at transcript level;
KW Cell projection; Chromosome; Cytoplasm; Differentiation; Hydrolase;
KW Manganese; Metal-binding; Protein phosphatase; Reference proteome;
KW Spermatogenesis.
FT CHAIN 1..305
FT /note="Serine/threonine-protein phosphatase PP1-gamma"
FT /evidence="ECO:0000305"
FT /id="PRO_0000436388"
FT ACT_SITE 123
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 62
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 64
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 90
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 90
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 122
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 172
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 247
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P36873"
SQ SEQUENCE 305 AA; 34596 MW; 1D503E11DE0A5B6F CRC64;
MTAPMDVDNL MSRLLNVGMS GGRLTTSVNE QELQTCCAVA KSVFASQASL LEVEPPIIVC
GDIHGQYSDL LRIFDKNGFP PDVNFLFLGD YVDRGRQNIE TICLMLCFKI KYPENFFMLR
GNHECPAINR VYGFYEECNR RYKSTRLWSI FQDTFNWMPL CGLIGSRILC MHGGLSPHLQ
TLDQLRQLPR PQDPPNPSIG IDLLWADPDQ WVKGWQANTR GVSYVFGQDV VADVCSRLDI
DLVARAHQVV QDGYEFFASK KMVTIFSAPH YCGQFDNSAA TMKVDENMVC TFVMYKPTPK
SMRRG
//
