SZY20_CAEEL
ID SZY20_CAEEL Reviewed; 558 AA.
AC G5EGU9; A9P338; A9P339; G5EEB4;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Suppressor of zyg-1 protein 20 {ECO:0000312|WormBase:C18E9.3f};
GN Name=szy-20 {ECO:0000312|WormBase:C18E9.3f};
GN Synonyms=pqn-14 {ECO:0000312|WormBase:C18E9.3f};
GN ORFNames=C18E9.3 {ECO:0000312|WormBase:C18E9.3f};
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:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS F AND E), FUNCTION, SUBCELLULAR
RP LOCATION (ISOFORM F), DEVELOPMENTAL STAGE, DOMAIN, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF 138-ARG--ARG-140.
RX PubMed=19081077; DOI=10.1016/j.devcel.2008.09.018;
RA Song M.H., Aravind L., Mueller-Reichert T., O'Connell K.F.;
RT "The conserved protein SZY-20 opposes the Plk4-related kinase ZYG-1 to
RT limit centrosome size.";
RL Dev. Cell 15:901-912(2008).
RN [2] {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 [3] {ECO:0000305}
RP INTERACTION WITH LET-92, PHOSPHORYLATION, AND DEPHOSPHORYLATION BY LET-92.
RX PubMed=21497766; DOI=10.1016/j.devcel.2011.03.007;
RA Song M.H., Liu Y., Anderson D.E., Jahng W.J., O'Connell K.F.;
RT "Protein phosphatase 2A-SUR-6/B55 regulates centriole duplication in C.
RT elegans by controlling the levels of centriole assembly factors.";
RL Dev. Cell 20:563-571(2011).
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH ATX-2, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=27689799; DOI=10.1371/journal.pgen.1006370;
RA Stubenvoll M.D., Medley J.C., Irwin M., Song M.H.;
RT "ATX-2, the C. elegans ortholog of human Ataxin-2, regulates centrosome
RT size and microtubule dynamics.";
RL PLoS Genet. 12:E1006370-E1006370(2016).
CC -!- FUNCTION: RNA binding protein that is required for normal cell division
CC and cytokinesis during embryonic development (PubMed:19081077,
CC PubMed:27689799). Functions with RNA-binding protein atx-2 to ensure
CC embryonic cell division, and to this end, plays a role in the
CC regulation of centrosome assembly, position and size, and in astral
CC microtubule outgrowth and nucleation (PubMed:19081077,
CC PubMed:27689799). Furthermore, negatively regulates the levels of the
CC protein kinase zyg-1 at the centrosome (PubMed:19081077,
CC PubMed:27689799). Also involved in ensuring centrosome attachment to
CC the nuclear envelope (PubMed:19081077). {ECO:0000269|PubMed:19081077,
CC ECO:0000269|PubMed:27689799}.
CC -!- SUBUNIT: Interacts (via C-terminus) with atx-2 (via C-terminus); the
CC interaction is RNA independent (PubMed:27689799). Interacts with let-92
CC (PubMed:21497766). {ECO:0000269|PubMed:21497766,
CC ECO:0000269|PubMed:27689799}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27689799}. Note=Co-
CC localizes with atx-2 in the cytoplasm. {ECO:0000269|PubMed:27689799}.
CC -!- SUBCELLULAR LOCATION: [Isoform f]: Cytoplasm
CC {ECO:0000269|PubMed:19081077}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:19081077}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriole
CC {ECO:0000269|PubMed:19081077}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:19081077}. Chromosome
CC {ECO:0000269|PubMed:19081077}. Note=Co-localizes with sas-4 at
CC centrioles. Localizes to nucleoli during interphase and to the surface
CC of chromosomes during meiosis and mitosis. Localizes in puncta adjacent
CC to the male pronucleus at the centrosome during meiosis. Localization
CC at the centrosome peaks at prometaphase and metaphase, but then
CC decreases and expression is at its most minimal during interphase.
CC {ECO:0000269|PubMed:19081077}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=f {ECO:0000312|WormBase:C18E9.3f}; Synonyms=a
CC {ECO:0000303|PubMed:19081077};
CC IsoId=G5EGU9-1; Sequence=Displayed;
CC Name=e {ECO:0000312|WormBase:C18E9.3e}; Synonyms=b
CC {ECO:0000303|PubMed:19081077};
CC IsoId=G5EGU9-2; Sequence=VSP_059230;
CC -!- DEVELOPMENTAL STAGE: Expressed during embryonic development.
CC {ECO:0000269|PubMed:19081077}.
CC -!- DOMAIN: The C-terminal part is necessary for interaction with atx-2.
CC {ECO:0000269|PubMed:27689799}.
CC -!- DOMAIN: The SUZ domain is necessary for RNA binding.
CC {ECO:0000269|PubMed:19081077}.
CC -!- PTM: Phosphorylated. May be dephosphorylated by let-92.
CC {ECO:0000269|PubMed:21497766}.
CC -!- DISRUPTION PHENOTYPE: Temperature-sensitive with embryonic lethality at
CC 25 degrees Celsius. RNAi-mediated knockdown results in 10% embryonic
CC lethality at 20 degrees Celsius and 90% embryonic lethality at 25
CC degrees Celsius due to cell division and cytokinesis defects including
CC centrosome duplication and attachment defects, and failed bipolar
CC spindle formation in embryos. RNAi-mediated knockdown in a zyg-20
CC (it25) mutant background results in suppression of the embryonic
CC lethality phenotype in the zyg-1 single mutant at 24 degrees Celsius.
CC {ECO:0000269|PubMed:19081077}.
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DR EMBL; EF100714; ABQ41319.1; -; mRNA.
DR EMBL; EF100715; ABQ41320.1; -; mRNA.
DR EMBL; EF100716; ABQ41321.1; -; mRNA.
DR EMBL; EF656060; ABV23716.1; -; mRNA.
DR EMBL; EF656061; ABV23717.1; -; mRNA.
DR EMBL; BX284602; CAQ58414.1; -; Genomic_DNA.
DR EMBL; BX284602; CBI68022.1; -; Genomic_DNA.
DR RefSeq; NP_001129808.1; NM_001136336.2. [G5EGU9-2]
DR RefSeq; NP_001254187.1; NM_001267258.1. [G5EGU9-1]
DR AlphaFoldDB; G5EGU9; -.
DR SMR; G5EGU9; -.
DR IntAct; G5EGU9; 1.
DR STRING; 6239.C18E9.3a; -.
DR EnsemblMetazoa; C18E9.3e.1; C18E9.3e.1; WBGene00004105. [G5EGU9-2]
DR EnsemblMetazoa; C18E9.3f.1; C18E9.3f.1; WBGene00004105. [G5EGU9-1]
DR GeneID; 174430; -.
DR KEGG; cel:CELE_C18E9.3; -.
DR CTD; 174430; -.
DR WormBase; C18E9.3e; CE42669; WBGene00004105; szy-20. [G5EGU9-2]
DR WormBase; C18E9.3f; CE38277; WBGene00004105; szy-20. [G5EGU9-1]
DR eggNOG; ENOG502TH1G; Eukaryota.
DR PRO; PR:G5EGU9; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00004105; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; G5EGU9; baseline and differential.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; IDA:WormBase.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IMP:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0045132; P:meiotic chromosome segregation; IMP:WormBase.
DR GO; GO:1904780; P:negative regulation of protein localization to centrosome; IMP:UniProtKB.
DR GO; GO:1905516; P:positive regulation of fertilization; IGI:UniProtKB.
DR GO; GO:0045977; P:positive regulation of mitotic cell cycle, embryonic; IMP:UniProtKB.
DR GO; GO:1903438; P:positive regulation of mitotic cytokinetic process; IMP:UniProtKB.
DR GO; GO:0010824; P:regulation of centrosome duplication; IGI:WormBase.
DR GO; GO:0009794; P:regulation of mitotic cell cycle, embryonic; IGI:UniProtKB.
DR GO; GO:1903436; P:regulation of mitotic cytokinetic process; IGI:UniProtKB.
DR GO; GO:0090169; P:regulation of spindle assembly; IGI:UniProtKB.
DR InterPro; IPR024771; SUZ.
DR Pfam; PF12752; SUZ; 1.
DR PROSITE; PS51673; SUZ; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Chromosome; Cytoplasm;
KW Cytoskeleton; Nucleus; Phosphoprotein; Reference proteome; RNA-binding.
FT CHAIN 1..558
FT /note="Suppressor of zyg-1 protein 20"
FT /evidence="ECO:0000305"
FT /id="PRO_0000442344"
FT DOMAIN 45..146
FT /note="SUZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01009"
FT REGION 50..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 207..307
FT /note="Missing (in isoform e)"
FT /evidence="ECO:0000305"
FT /id="VSP_059230"
FT MUTAGEN 138..140
FT /note="RNR->GNG: Reduced RNA binding."
FT /evidence="ECO:0000269|PubMed:19081077"
FT CONFLICT 234
FT /note="P -> L (in Ref. 1; ABQ41320)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 558 AA; 63776 MW; FEDB89D216835BB7 CRC64;
MSKENVVADS WDDADADPVK ELMDKVEKVK LLQRKEEKKE AFFEKVKAEE SSGVVSKLQT
EEGLGPSAEE PKRVFLRRPK DGFAASENVI EASPPTSADT EEQPVTNVRS RSHHKLNQKE
KQPAPTYEER QAAYQAARNR ILGTEYKPDN QEIKEIKFID RSKSPETLKM TQQNMVEHYG
EELSRELMEQ PAEIVPPERQ YTPDFTQPPP SVSESGGVYN GPPGFQQKQP NFQPTLQQQS
LHQQQYLDNQ YMMQMNVQIP IQYHNQTQHQ FVPHEASAIS TTSQNSNGDG QNDQAIYYYQ
APTQQPMNYI PYNLPNMAYP PPNFQPQGQL HHQMNAGQLH QIQQQQQQCQ QIQHQPPQQH
QQVINGQVMN QQNQRNQVNS YPQQNGAGRG QNRQPMMYQM PCNSGPTAKP PPLMNQMQNR
CMTNNGQNYQ NRNMQQQGQQ RSYSSQPQNG QFYQNGNSNQ NNPNNGRKQQ HQPQQQQNKS
GKFGQNRNDM QKNNYQPNLQ QPPMSQNPIP FGCPPRNVNA IREQHANNGS PNTGAGILGP
HPMMSASQWP ALQQNRPQ
