PP4R1_CAEEL
ID PP4R1_CAEEL Reviewed; 1562 AA.
AC G5ECH5; G5ED93; G5EFI6;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Serine/threonine-protein phosphatase 4 regulatory subunit 1 {ECO:0000250|UniProtKB:Q8TF05};
GN Name=ppfr-1 {ECO:0000303|PubMed:19087961, ECO:0000312|WormBase:F16A11.3d};
GN ORFNames=F16A11.3 {ECO:0000312|WormBase:F16A11.3d};
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).
RN [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH MEL-26, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=23918937; DOI=10.1083/jcb.201304174;
RA Gomes J.E., Tavernier N., Richaudeau B., Formstecher E., Boulin T.,
RA Mains P.E., Dumont J., Pintard L.;
RT "Microtubule severing by the katanin complex is activated by PPFR-1-
RT dependent MEI-1 dephosphorylation.";
RL J. Cell Biol. 202:431-439(2013).
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 ECO:0000269|PubMed:23918937}.
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). Interacts (via C-terminus) with mel-26 (probably via
CC MATH domain); the interaction targets ppfr-1 for ubiquitin-mediated
CC proteolysis (PubMed:23918937). {ECO:0000250|UniProtKB:Q8TF05,
CC ECO:0000269|PubMed:23918937, ECO:0000305|PubMed:19087961}.
CC -!- INTERACTION:
CC G5ECH5; Q94420: mel-26; NbExp=4; IntAct=EBI-6691815, EBI-320790;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23918937}.
CC Note=Localizes to the cytoplasm during meiosis and mitosis.
CC {ECO:0000269|PubMed:23918937}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=d {ECO:0000312|WormBase:F16A11.3d};
CC IsoId=G5ECH5-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:F16A11.3a};
CC IsoId=G5ECH5-2; Sequence=VSP_059538;
CC Name=b {ECO:0000312|WormBase:F16A11.3b};
CC IsoId=G5ECH5-3; Sequence=VSP_059538, VSP_059539;
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos.
CC {ECO:0000269|PubMed:23918937}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal in 10 percent of animals and
CC slight increase in the number of males produced (PubMed:19087961). In
CC oocytes, slight increase in metaphase and anaphase meiotic spindle
CC length, persistence of microtubules around chromatids during anaphase
CC and delay in spindle assembly in meiosis II (PubMed:19087961,
CC PubMed:23918937). However, localization of spindle pole marker aspm-1
CC and the shape of the meiotic spindle are normal (PubMed:23918937). The
CC second polar body has a larger size and in 16 percent of animals its
CC extrusion fails resulting in aneuploidy (PubMed:19087961). The size of
CC the polar body is further increased in a mei-1 (or646) mutant
CC background (PubMed:23918937). Increases mei-1 phosphorylation in a gain
CC of function mei-1 (ct46) and tbb-2 (sb26) mutant background
CC (PubMed:23918937). In gain of function mei-1 (ct46) mutant background,
CC RNAi-mediated knockdown partially rescues embryonic lethality and
CC improves embryonic mitotic spindle morphology in terms of length and
CC orientation (PubMed:19087961). {ECO:0000269|PubMed:19087961,
CC ECO:0000269|PubMed:23918937}.
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DR EMBL; BX284601; CAH10794.1; -; Genomic_DNA.
DR EMBL; BX284601; CAH10795.1; -; Genomic_DNA.
DR EMBL; BX284601; CAP72367.2; -; Genomic_DNA.
DR RefSeq; NP_001021388.1; NM_001026217.3. [G5ECH5-2]
DR RefSeq; NP_001021389.1; NM_001026218.3. [G5ECH5-3]
DR RefSeq; NP_001122456.2; NM_001128984.2. [G5ECH5-1]
DR AlphaFoldDB; G5ECH5; -.
DR IntAct; G5ECH5; 1.
DR STRING; 6239.F16A11.3d; -.
DR EPD; G5ECH5; -.
DR PaxDb; G5ECH5; -.
DR PeptideAtlas; G5ECH5; -.
DR EnsemblMetazoa; F16A11.3a.1; F16A11.3a.1; WBGene00008878. [G5ECH5-2]
DR EnsemblMetazoa; F16A11.3b.1; F16A11.3b.1; WBGene00008878. [G5ECH5-3]
DR EnsemblMetazoa; F16A11.3d.1; F16A11.3d.1; WBGene00008878. [G5ECH5-1]
DR GeneID; 172761; -.
DR KEGG; cel:CELE_F16A11.3; -.
DR CTD; 172761; -.
DR WormBase; F16A11.3a; CE37103; WBGene00008878; ppfr-1. [G5ECH5-2]
DR WormBase; F16A11.3b; CE37104; WBGene00008878; ppfr-1. [G5ECH5-3]
DR WormBase; F16A11.3d; CE44414; WBGene00008878; ppfr-1. [G5ECH5-1]
DR eggNOG; KOG0211; Eukaryota.
DR HOGENOM; CLU_004062_0_0_1; -.
DR InParanoid; G5ECH5; -.
DR OMA; MNMSISS; -.
DR OrthoDB; 249499at2759; -.
DR PRO; PR:G5ECH5; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00008878; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; G5ECH5; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0019904; F:protein domain specific binding; IPI:WormBase.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IBA:GO_Central.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IGI:UniProtKB.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IGI:UniProtKB.
DR GO; GO:1902120; P:negative regulation of meiotic spindle elongation; IMP:WormBase.
DR GO; GO:0040038; P:polar body extrusion after meiotic divisions; IMP:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IMP:WormBase.
DR GO; GO:0032888; P:regulation of mitotic spindle elongation; IGI:UniProtKB.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR021133; HEAT_type_2.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Meiosis; Reference proteome;
KW Repeat.
FT CHAIN 1..1562
FT /note="Serine/threonine-protein phosphatase 4 regulatory
FT subunit 1"
FT /id="PRO_0000443998"
FT REPEAT 330..366
FT /note="HEAT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00103"
FT REPEAT 369..406
FT /note="HEAT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00103"
FT REPEAT 408..446
FT /note="HEAT 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00103"
FT REPEAT 1062..1100
FT /note="HEAT 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00103"
FT REPEAT 1101..1139
FT /note="HEAT 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00103"
FT REPEAT 1295..1333
FT /note="HEAT 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00103"
FT REGION 98..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 905..943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1480..1562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1479..1528
FT /evidence="ECO:0000255"
FT COMPBIAS 98..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..635
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..773
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..818
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..847
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1485..1502
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1503..1527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1540..1562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..72
FT /note="Missing (in isoform a and isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_059538"
FT VAR_SEQ 650..775
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_059539"
SQ SEQUENCE 1562 AA; 174187 MW; 3346A9020A9D8B82 CRC64;
MIKSQFATLI RVLIDFQKFW VFLSIFCTFL VVFKFDNLMF QKVRRVFQQN RKNSESIQPK
LSTVSGSNSG EGMDKRNTGF SNLQQLGGAI FIDDAEDEPP RVKSSEDSRP APHWLDSPRD
STTLPDIIAS TYSDFIDEAE YATKQMLAIL ETLNPIEEYI ELFESSFKAI EVRLPFDVIL
NDEKKPDWDA IRRKLIMGSL TVNTTSEKPG ITTNQMTAIF DAIPFLFDAV ACNPELYEYQ
NTLSMIVMIA MTGNSMIRRQ SINAVQALME RNMLDQDFMR DGVVPGLFNI YQSGVGAFQS
NDLRMECVQA LCQVISYDAI HDRRWLFDNF LPRFSQMLKD PTMHVRKSAL HIFGNLGNMF
GQKFTEVFLV PHLITLSCDM TWAVRKVACE IFVKVAECAS NQVRIDILSP NFVRLLNDPN
KWVSFIAYQQ LGPFISLFAN PDITGLELRN GQVVVRDPVV LEPSVTEQED PSNSTFSEDT
SDDFRTLPKD TWLPEVDFND DFEYQLGSID NTQNQKELTT VTTALVKTPK RGERVMDSVL
SGINKMFGSL ERSSPKSKEV EKIAATFSSP SKRSPLSLHS AVSLIDKFSK RSNPNNPQRF
PVFDSANSDS TLSSNSSNNN SSEQQNSTGI AAKCSSTDDL TKLGLEDDDS PDAAEDSDDF
TSETRTTSPR GRRIATNAWS KLDIRQKIFL RRLGALPPSF PKKKATHSSS SSPRKSPTRS
PLLSSRKKGL LFDFAAPIEI KSSSSDHSET IPVRTANQQQ EKADDDKLNT DERQQYMENS
GPKFNTDEDS TNDSDSDDED NDFEKSFVAD EDDGEQDDSP LSIEIKSSSS SDFESVSAAT
PTSQEPVSNE FSLTYWSSNY AISSIEDELK PFGSSSSFTN SPTSNSYLES RFDVMKVNLS
PRARSVSFGT NGSPISTSPR RKANSTSEPS PPNTGNLKSD DSIVMLNTEE KEKLGILDFD
EMNMSISSNS SIHGEAAMTE DSDISLTSIE QAALQHVPVD LVESYMRVMG PIGGSGSGGG
GNGSSTTIAT GDPSLCAETY RHCAHNFPAV CYTLGRAAWP RLKLVFRKLA MDEQARVRQS
ISHSIHEIAN MLGQEITDED LLPVFYDLRN DQNPDVRNGI LIHLYDFVKF LSPEKRDEMI
LSLPQFFPIG AQPGNQAQNG DWRSRFELIS QLSKLCSLYS IQDVNFHMSG IALTLADDRV
AEVRREAVML VSTIVGALVT AEWDNIKGVR DIENGHVDVK KKSNKTDFLS EQFVDDIVSS
FAKTQKWTRR QTFCFICAQI LRDKQCDGIQ FRYFFATPLQ QLAQDKVPNV RLASCEALSV
WRKTLIAARA QERRGQSPIS SPASEPSAIR RDINLVSDMM VKLSNDSDID AAFIAKKCQG
LTDDHQPVDV ASRTTRMRER EEQFFGDIIL SYSPGCNARV SGKEIKQLIR HDQGAVQKAA
PLQSMEDFGD EILAHAADSV NIQTPPEVVA TVQRVSITNE QFEDNTEAVD MEIEEDEDEN
STEKKENTEK TAEEESENVK NTEDELDIPM DPAPTLPPPV TSKNQSSSPI TASSSDNNET
SA
