PPH6R_CAEEL
ID PPH6R_CAEEL Reviewed; 778 AA.
AC B2D6K9; A5Z2S4; Q18696;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Serine/threonine-protein phosphatase 6 regulatory subunit {ECO:0000305};
GN Name=saps-1 {ECO:0000303|PubMed:20040490, ECO:0000312|WormBase:C47G2.5c};
GN ORFNames=C47G2.5 {ECO:0000312|WormBase:C47G2.5c};
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, IDENTIFICATION IN A COMPLEX WITH PPH-6, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=20040490; DOI=10.1242/dev.042754;
RA Afshar K., Werner M.E., Tse Y.C., Glotzer M., Goenczy P.;
RT "Regulation of cortical contractility and spindle positioning by the
RT protein phosphatase 6 PPH-6 in one-cell stage C. elegans embryos.";
RL Development 137:237-247(2010).
RN [3]
RP ERRATUM OF PUBMED:20040490.
RX PubMed=27436042; DOI=10.1242/dev.141515;
RA Afshar K., Werner M.E., Tse Y.C., Glotzer M., Goenczy P.;
RL Development 143:2689-2689(2016).
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH AIR-1, AND DISRUPTION PHENOTYPE.
RX PubMed=27335426; DOI=10.1242/jcs.184416;
RA Kotak S., Afshar K., Busso C., Goenczy P.;
RT "Aurora A kinase regulates proper spindle positioning in C. elegans and in
RT human cells.";
RL J. Cell Sci. 129:3015-3025(2016).
CC -!- FUNCTION: Regulatory subunit of protein phosphatase 6 (PP6) (Probable).
CC In complex with pph-6, promotes actomyosin contractility during
CC cytokinesis by regulating the organization of cortical non-muscle
CC myosin II nmy-2 and thus contributing to correct spindle positioning
CC (PubMed:20040490). Also required for the proper generation of pulling
CC forces on spindle poles during anaphase by regulating the cortical
CC localization of gpr-1, gpr-2 and lin-5 (PubMed:20040490). Negatively
CC regulates kinase air-1 localization at the cell cortex
CC (PubMed:27335426). {ECO:0000269|PubMed:20040490,
CC ECO:0000269|PubMed:27335426, ECO:0000305|PubMed:20040490}.
CC -!- SUBUNIT: Forms a complex composed of catalytic subunit pph-6 and
CC regulatory subunit saps-1; the interaction increases pph-6 and saps-1
CC protein stability (PubMed:20040490). Interacts with kinase air-1
CC (PubMed:27335426). {ECO:0000269|PubMed:20040490,
CC ECO:0000269|PubMed:27335426}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20040490}.
CC Cytoplasm, cell cortex {ECO:0000269|PubMed:20040490}. Cytoplasm,
CC cytoskeleton {ECO:0000269|PubMed:20040490}. Cytoplasm, cytoskeleton,
CC spindle pole {ECO:0000269|PubMed:20040490}. Note=In embryos, localizes
CC mainly to the cytoplasm and to a lesser extent with microtubule asters.
CC {ECO:0000269|PubMed:20040490}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=c {ECO:0000312|WormBase:C47G2.5c};
CC IsoId=B2D6K9-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:C47G2.5a};
CC IsoId=B2D6K9-2; Sequence=VSP_060067;
CC Name=b {ECO:0000312|WormBase:C47G2.5b};
CC IsoId=B2D6K9-3; Sequence=VSP_060067, VSP_060068;
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos.
CC {ECO:0000269|PubMed:20040490}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes severe reduction
CC in cortical contractions and lack of pseudocleavage furrow formation in
CC the 1-cell embryo (PubMed:20040490, PubMed:27335426). Positioning of
CC the spindle is abnormal due to reduced pulling forces that prevent
CC oscillatory movements of the posterior spindle pole during anaphase
CC (PubMed:20040490, PubMed:27335426). {ECO:0000269|PubMed:20040490,
CC ECO:0000269|PubMed:27335426}.
CC -!- SIMILARITY: Belongs to the SAPS family. {ECO:0000305}.
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DR EMBL; BX284602; CAA88937.2; -; Genomic_DNA.
DR EMBL; BX284602; CAN99660.1; -; Genomic_DNA.
DR EMBL; BX284602; CAQ35025.1; -; Genomic_DNA.
DR PIR; T20035; T20035.
DR RefSeq; NP_001122596.1; NM_001129124.2. [B2D6K9-3]
DR RefSeq; NP_001122597.1; NM_001129125.1. [B2D6K9-1]
DR RefSeq; NP_496414.2; NM_064013.4. [B2D6K9-2]
DR AlphaFoldDB; B2D6K9; -.
DR ComplexPortal; CPX-4025; pph-6-saps-1 phosphatase complex.
DR DIP; DIP-25761N; -.
DR IntAct; B2D6K9; 1.
DR STRING; 6239.C47G2.5c; -.
DR EPD; B2D6K9; -.
DR PaxDb; B2D6K9; -.
DR PeptideAtlas; B2D6K9; -.
DR EnsemblMetazoa; C47G2.5a.1; C47G2.5a.1; WBGene00008166. [B2D6K9-2]
DR EnsemblMetazoa; C47G2.5b.1; C47G2.5b.1; WBGene00008166. [B2D6K9-3]
DR EnsemblMetazoa; C47G2.5c.1; C47G2.5c.1; WBGene00008166. [B2D6K9-1]
DR GeneID; 174725; -.
DR KEGG; cel:CELE_C47G2.5; -.
DR UCSC; C47G2.5a; c. elegans.
DR CTD; 174725; -.
DR WormBase; C47G2.5a; CE38162; WBGene00008166; saps-1. [B2D6K9-2]
DR WormBase; C47G2.5b; CE41110; WBGene00008166; saps-1. [B2D6K9-3]
DR WormBase; C47G2.5c; CE42481; WBGene00008166; saps-1. [B2D6K9-1]
DR eggNOG; KOG2073; Eukaryota.
DR GeneTree; ENSGT00390000009899; -.
DR HOGENOM; CLU_360662_0_0_1; -.
DR InParanoid; B2D6K9; -.
DR OMA; VWQPDAG; -.
DR OrthoDB; 355471at2759; -.
DR PRO; PR:B2D6K9; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00008166; Expressed in embryo and 4 other tissues.
DR GO; GO:0000235; C:astral microtubule; IDA:WormBase.
DR GO; GO:0005938; C:cell cortex; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:1903293; C:phosphatase complex; IPI:ComplexPortal.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:WormBase.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IBA:GO_Central.
DR GO; GO:0000916; P:actomyosin contractile ring contraction; IC:ComplexPortal.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:WormBase.
DR GO; GO:0040001; P:establishment of mitotic spindle localization; IMP:WormBase.
DR GO; GO:0030590; P:first cell cycle pseudocleavage; IMP:WormBase.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; IC:ComplexPortal.
DR GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; IBA:GO_Central.
DR GO; GO:0051653; P:spindle localization; IC:ComplexPortal.
DR InterPro; IPR007587; SAPS.
DR PANTHER; PTHR12634; PTHR12634; 1.
DR Pfam; PF04499; SAPS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cytoplasm; Cytoskeleton;
KW Reference proteome.
FT CHAIN 1..778
FT /note="Serine/threonine-protein phosphatase 6 regulatory
FT subunit"
FT /id="PRO_0000446363"
FT REGION 609..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..735
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 140..141
FT /note="Missing (in isoform a and isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_060067"
FT VAR_SEQ 638..697
FT /note="STYPQQTNGNQAFLEQEEGDGEWVWPTVPPLGETEVVTQTGHRPENNWVDET
FT APDFSHLD -> N (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_060068"
SQ SEQUENCE 778 AA; 87402 MW; 6EC8469012BAC11A CRC64;
MFWAKEEEEN SLMRLLKTDN FTLEDVLLNE FVVQESRYGK AELVQYITSR ENMKALLELS
LNPKINTDLP MKQQYRLSFI ASEILTIRGT DVFQKQIVTT EETRKCLVDF LNDKTPLNHL
VAGFFAKIME CLLSRHFDLF QTFSLLQETK FFDKCLRNIN LGAIECLLEN LVRIPTTSEG
TRIVKEWMIS ENLFEKIVDR MRESETDDEK ECLAEVYCEI LRELRDKLYI MESKVDELHA
KSMDETLIAK IADNLIVEEG CPAEELVKKS ALISASAKIL EAFIKTNFVS NAPAQQLEEI
ERNLIEERHY SYGLMRPCMD NDPYEHSYQP DPERIVEGIL ANRLPNILQT VLRDIEANGS
VWQPLLRLII ELCNTNCMST HEKIAVAFRS LPFINLIKAA KMLPRASVLH CLLVKVVILL
LHSSFPCDEL SPAAEYLLTE GGLIQNIYDT ATSPNPGSSV ACSGLRSFNQ NLGDAINRAK
KAGIPNQKLL AILSADNTWT ELEDIIHLYN LKHRPQMQHD FNDSSVVSSI RNDSHGFNDS
EEWTDASTKF AEMDATSSAK QAFSGFSSPF EPNMQRFSDF EGQFDDTPDE DEFRKLCSER
ANSSSCAGIS FETSPIKWPG EAEKTSEKAS EPPSVVASTY PQQTNGNQAF LEQEEGDGEW
VWPTVPPLGE TEVVTQTGHR PENNWVDETA PDFSHLDMAP PKEDDMWADF SSFPTISPTA
AANSASSSSS DAWPGSDIHL QGEASDWPLN NSHESKASDP VMVGLAASIS HPGDSSEA
