SYP4_CAEEL
ID SYP4_CAEEL Reviewed; 605 AA.
AC Q9N5K3;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Synaptonemal complex protein 4 {ECO:0000305};
GN Name=syp-4 {ECO:0000312|WormBase:H27M09.3};
GN ORFNames=H27M09.3 {ECO:0000312|WormBase:H27M09.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=19798442; DOI=10.1371/journal.pgen.1000669;
RA Smolikov S., Schild-Pruefert K., Colaiacovo M.P.;
RT "A yeast two-hybrid screen for SYP-3 interactors identifies SYP-4, a
RT component required for synaptonemal complex assembly and chiasma formation
RT in Caenorhabditis elegans meiosis.";
RL PLoS Genet. 5:E1000669-E1000669(2009).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21840865; DOI=10.1534/genetics.111.132431;
RA Schild-Pruefert K., Saito T.T., Smolikov S., Gu Y., Hincapie M., Hill D.E.,
RA Vidal M., McDonald K., Colaiacovo M.P.;
RT "Organization of the synaptonemal complex during meiosis in Caenorhabditis
RT elegans.";
RL Genetics 189:411-421(2011).
RN [4]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-269, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF SER-269.
RX PubMed=28346135; DOI=10.7554/elife.23437;
RA Nadarajan S., Lambert T.J., Altendorfer E., Gao J., Blower M.D.,
RA Waters J.C., Colaiacovo M.P.;
RT "Polo-like kinase-dependent phosphorylation of the synaptonemal complex
RT protein SYP-4 regulates double-strand break formation through a negative
RT feedback loop.";
RL Elife 6:E23437-E23437(2017).
CC -!- FUNCTION: Constitutes an element of the transverse filaments of the
CC synaptonemal complex (SC), formed between homologous chromosomes during
CC meiotic prophase I, and is required for the assembly of the central
CC region of the SC (PubMed:19798442, PubMed:21840865). Required for
CC chromosome synapsis and chiasma formation between homologous
CC chromosomes during meiosis, mechanisms that are crucial for crossover
CC formation and meiotic recombination (PubMed:19798442).
CC {ECO:0000269|PubMed:19798442, ECO:0000269|PubMed:21840865}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:19798442,
CC ECO:0000269|PubMed:21840865, ECO:0000269|PubMed:28346135}.
CC Note=Localizes to chromosomes during meiotic prophase I
CC (PubMed:19798442). During leptotene and zygotene, localizes in foci on
CC chromosomes (PubMed:19798442). Localizes to the central region of the
CC synaptonemal complex at the interface between synapsed chromosomes
CC throughout pachytene (PubMed:19798442, PubMed:28346135,
CC PubMed:21840865). During diplotene, becomes concentrated towards one
CC end of each chromosome (PubMed:19798442). Localizes to the short axes
CC of the bivalents during diakinesis and disappears from chromosomes by
CC the end of diakinesis (PubMed:19798442). {ECO:0000269|PubMed:19798442,
CC ECO:0000269|PubMed:21840865, ECO:0000269|PubMed:28346135}.
CC -!- PTM: Phosphorylated at Ser-269 by plk-1 and plk-2. Phosphorylation
CC starts at the pachytene stage during oogenesis and depends on crossover
CC precursor formation. Phosphorylation negatively regulates meiotic DNA
CC double-strand break (DSB) formation. {ECO:0000269|PubMed:28346135}.
CC -!- DISRUPTION PHENOTYPE: High levels of embryonic lethality and a high
CC percentage of males among the surviving progeny (PubMed:19798442).
CC Failure to localize syp-1 and syp-3, components of the synaptonemal
CC complex central region, to chromosomes (PubMed:19798442). Failure to
CC form chromosome synapses and lack of synaptonemal complex formation
CC leading to a delay in meiotic progression (PubMed:19798442). Impaired
CC stabilization of homologous pairing interactions (PubMed:19798442).
CC Lack of chiasmata formation during diakinesis (PubMed:19798442).
CC Reduced crossover frequency (PubMed:19798442). Increased rad-51 foci
CC during pachytene indicating impaired DNA double-strand break (DSB)
CC repair progression (PubMed:19798442). Elevated germ cell apoptosis
CC (PubMed:19798442). Disruption of plk-2 localization to synapsed
CC chromosomes during pachytene (PubMed:28346135).
CC {ECO:0000269|PubMed:19798442, ECO:0000269|PubMed:28346135}.
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DR EMBL; BX284601; CCD72468.1; -; Genomic_DNA.
DR RefSeq; NP_491960.1; NM_059559.4.
DR AlphaFoldDB; Q9N5K3; -.
DR ComplexPortal; CPX-3388; Synaptonemal complex.
DR STRING; 6239.H27M09.3; -.
DR iPTMnet; Q9N5K3; -.
DR EPD; Q9N5K3; -.
DR PaxDb; Q9N5K3; -.
DR PeptideAtlas; Q9N5K3; -.
DR EnsemblMetazoa; H27M09.3.1; H27M09.3.1; WBGene00019247.
DR GeneID; 172411; -.
DR KEGG; cel:CELE_H27M09.3; -.
DR UCSC; H27M09.3; c. elegans.
DR CTD; 172411; -.
DR WormBase; H27M09.3; CE23830; WBGene00019247; syp-4.
DR eggNOG; ENOG502TG9M; Eukaryota.
DR HOGENOM; CLU_451471_0_0_1; -.
DR InParanoid; Q9N5K3; -.
DR OMA; IECAKHY; -.
DR PhylomeDB; Q9N5K3; -.
DR PRO; PR:Q9N5K3; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00019247; Expressed in adult organism and 3 other tissues.
DR GO; GO:0000801; C:central element; IDA:WormBase.
DR GO; GO:0005694; C:chromosome; IC:ComplexPortal.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:WormBase.
DR GO; GO:0000795; C:synaptonemal complex; IC:ComplexPortal.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IC:ComplexPortal.
DR GO; GO:0045132; P:meiotic chromosome segregation; IC:ComplexPortal.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IC:ComplexPortal.
PE 1: Evidence at protein level;
KW Chromosome; Coiled coil; Meiosis; Phosphoprotein; Reference proteome.
FT CHAIN 1..605
FT /note="Synaptonemal complex protein 4"
FT /id="PRO_0000441705"
FT REGION 288..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 115..201
FT /evidence="ECO:0000255"
FT COMPBIAS 288..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..425
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 269
FT /note="Phosphoserine; by plk-1 and plk-2"
FT /evidence="ECO:0000269|PubMed:28346135"
FT MUTAGEN 269
FT /note="S->A: Abolishes phosphorylation. Prolonged dynamic
FT state of syp-3 at the synaptonemal complex during
FT pachytene, increased DNA double-strand break formation,
FT increased germ cell apoptosis and reduced brood size."
FT /evidence="ECO:0000269|PubMed:28346135"
FT MUTAGEN 269
FT /note="S->D: Phosphomimetic mutant. Less dynamic state of
FT syp-3 at the synaptonemal complex during pachytene,
FT decreased DNA double-strand break formation, increased germ
FT cell apoptosis and reduced brood size."
FT /evidence="ECO:0000269|PubMed:28346135"
SQ SEQUENCE 605 AA; 67287 MW; 280118638E98F661 CRC64;
MSFPTLQVRP NEKNPKVLRC HEFLRQSNQL VERNMINTEG RKMLAKLLTK MVSEAKGIYA
LDERRAELAK SGKLQEKLKS AYQTSLTVME DRLHIAELSR QVQEKKLTVQ QKYYECDDLR
KSVQETNTEA RRVQEINEQR LVDTTRATEE LIVKSASILK NLENSSDVHK LRAMEEEKRI
LEEVVEGLRD QKKCLADDIR TKKATLKAES KKSFEKTVIE CAKHYKLHQS LMPKLDKSKR
SLETLKDEEE NRRICGSLSL DETMQFDRSF ILASMDKTNK PEKAVQQLTS KSSEVSITPQ
ISETAKSSFS KEPIPTQHPM EVGEEPVIEH SAEESVHIEP PNVTEIREVV PQITIQPTRQ
DSVVQRDAEE LDTSAVPSPQ PESILDEPEE EEEELSNHEN HADQSMDVME VDQEVPEESP
MEVGEQEEIE QPSVFKDILA TEQAALSQEQ EPEIVEKQAD NDVQFVDDQQ VGAQLDVEDE
EEVMSENGSN KSNNFSFNFF GNSKGTSAGE GGGEGNFDFN FDGIGAGDDG SNNGGSTGDL
DFLNYDGEDE GKGSGNTQSD PFGFASNGNA AGGGGDGSFN FNFDGDGEGG ATSGAGGNST
SFFNF
