PP4RS_CAEEL
ID PP4RS_CAEEL Reviewed; 327 AA.
AC Q9N4E9;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Serine/threonine-protein phosphatase 4 regulatory subunit ppfr-4 {ECO:0000305};
GN Name=ppfr-4 {ECO:0000303|PubMed:19087961, ECO:0000312|WormBase:Y71H2B.3};
GN ORFNames=Y71H2B.3 {ECO:0000312|WormBase:Y71H2B.3};
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, SUBUNIT, AND DISRUPTION PHENOTYPE.
RX PubMed=19087961; DOI=10.1534/genetics.108.096016;
RA Han X., Gomes J.E., Birmingham C.L., Pintard L., Sugimoto A., Mains P.E.;
RT "The role of protein phosphatase 4 in regulating microtubule severing in
RT the Caenorhabditis elegans embryo.";
RL Genetics 181:933-943(2009).
CC -!- FUNCTION: Probable regulatory subunit of serine/threonine-protein
CC phosphatase PP4 which may play a role in meiosis and embryonic mitosis.
CC Probably in association with catalytic subunit pph-4.1, regulates
CC microtubule severing during oocyte meiosis II by dephosphorylating and
CC likely activating mei-1, a component of the katanin microtubule
CC severing complex. {ECO:0000269|PubMed:19087961}.
CC -!- SUBUNIT: Serine/threonine-protein phosphatase 4 (PP4) occurs in
CC different assemblies of the catalytic and one or more regulatory
CC subunits (By similarity). The catalytic subunit is likely to be pph-4.1
CC (PubMed:19087961). {ECO:0000250|UniProtKB:Q8TF05,
CC ECO:0000305|PubMed:19087961}.
CC -!- INTERACTION:
CC Q9N4E9; Q9XW79: pph-4.1; NbExp=3; IntAct=EBI-331766, EBI-331742;
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes 94 percent
CC embryonic lethality when injected compared to 20 percent when fed.
CC Partially rescues embryonic lethality in gain of function mei-1 (ct46)
CC mutant background. {ECO:0000269|PubMed:19087961}.
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DR EMBL; BX284603; CCD72402.1; -; Genomic_DNA.
DR RefSeq; NP_497591.1; NM_065190.4.
DR AlphaFoldDB; Q9N4E9; -.
DR SMR; Q9N4E9; -.
DR DIP; DIP-27072N; -.
DR IntAct; Q9N4E9; 5.
DR STRING; 6239.Y71H2B.3; -.
DR EPD; Q9N4E9; -.
DR PaxDb; Q9N4E9; -.
DR PeptideAtlas; Q9N4E9; -.
DR EnsemblMetazoa; Y71H2B.3.1; Y71H2B.3.1; WBGene00022193.
DR GeneID; 190617; -.
DR UCSC; Y71H2B.3; c. elegans.
DR CTD; 190617; -.
DR WormBase; Y71H2B.3; CE24630; WBGene00022193; ppfr-4.
DR eggNOG; KOG2830; Eukaryota.
DR GeneTree; ENSGT00390000002414; -.
DR HOGENOM; CLU_041824_1_0_1; -.
DR InParanoid; Q9N4E9; -.
DR OMA; RAWDEFT; -.
DR OrthoDB; 1348942at2759; -.
DR PhylomeDB; Q9N4E9; -.
DR SignaLink; Q9N4E9; -.
DR PRO; PR:Q9N4E9; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00022193; Expressed in adult organism and 3 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0051721; F:protein phosphatase 2A binding; IBA:GO_Central.
DR GO; GO:0019888; F:protein phosphatase regulator activity; ISS:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IGI:UniProtKB.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:1903361; P:protein localization to basolateral plasma membrane; IMP:WormBase.
DR GO; GO:0035303; P:regulation of dephosphorylation; IBA:GO_Central.
DR GO; GO:0009966; P:regulation of signal transduction; IEA:InterPro.
DR Gene3D; 1.25.40.540; -; 1.
DR InterPro; IPR038511; TAP42/TAP46-like_sf.
DR InterPro; IPR007304; TAP46-like.
DR PANTHER; PTHR10933; PTHR10933; 1.
DR Pfam; PF04177; TAP42; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Meiosis; Reference proteome.
FT CHAIN 1..327
FT /note="Serine/threonine-protein phosphatase 4 regulatory
FT subunit ppfr-4"
FT /id="PRO_0000443999"
FT REGION 271..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 141..185
FT /evidence="ECO:0000255"
FT COMPBIAS 274..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 327 AA; 37947 MW; 7E5003DB5EE0FFCD CRC64;
MSELSDEEIS LQALYDPSKK VIGDIEDGIF STPELQPRIK TGIDNLQLVT KLVNQMRLFS
SNEQIEDVPT NSLPYLLVPC FLGILHQNLM TEPGLKLDEL RKSKIYMRNF LDRLRDLCLI
TTRLPWEDED TEEQNLKEKP KLAVEEIRRL KLERHKKKQE LKMAELRIQK QLEAVSIDEQ
NLRELYITQL LFWSERCYEE LQAIDDELPL LKMMAERASH PHRHPAPPPA TKTVPTLKPF
IITRDAQQKQ VFGLGYPGIP AMSVDEWYHQ KFGHNPQNAP QSSAPAGAEA QESEEEVDDD
EARAKAMRWD EYKDDHRRGW GNMHNKG