SYCP3_MESAU
ID SYCP3_MESAU Reviewed; 234 AA.
AC Q60547;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Synaptonemal complex protein 3;
DE Short=SCP-3;
DE AltName: Full=Meiotic chromosome core protein;
DE AltName: Full=Synaptonemal complex protein COR1 {ECO:0000303|PubMed:7876343};
GN Name=SYCP3; Synonyms=COR1 {ECO:0000303|PubMed:7876343};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=7876343; DOI=10.1242/jcs.107.10.2749;
RA Dobson M.J., Pearlman R.E., Karaiskakis A., Spyropoulos B., Moens P.B.;
RT "Synaptonemal complex proteins: occurrence, epitope mapping and chromosome
RT disjunction.";
RL J. Cell Sci. 107:2749-2760(1994).
CC -!- FUNCTION: Component of the synaptonemal complexes (SCS), formed between
CC homologous chromosomes during meiotic prophase (PubMed:7876343).
CC Required for centromere pairing during meiosis in male germ cells.
CC Required for normal meiosis during spermatogenesis and male fertility.
CC Plays a lesser role in female fertility. Required for efficient
CC phosphorylation of HORMAD1 and HORMAD2. {ECO:0000250|UniProtKB:P70281,
CC ECO:0000269|PubMed:7876343}.
CC -!- SUBUNIT: Component of the lateral elements of synaptonemal complexes
CC (PubMed:7876343). Homotetramer; the tetrameric helix bundles assemble
CC end to end into long homopolimeric fibers that exhibit a transversal
CC striation with a periodicity of about 20 nm (in vitro) (By similarity).
CC Interacts with SYCP2 (By similarity). Forms a complex with EWSR1,
CC PRDM9, REC8 and SYCP1; complex formation is dependent of phosphorylated
CC form of REC8 and requires PRDM9 bound to hotspot DNA; EWSR1 joins PRDM9
CC with the chromosomal axis through REC8 (By similarity).
CC {ECO:0000250|UniProtKB:P70281, ECO:0000250|UniProtKB:Q8IZU3,
CC ECO:0000269|PubMed:7876343}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7876343}. Chromosome
CC {ECO:0000269|PubMed:7876343}. Chromosome, centromere
CC {ECO:0000269|PubMed:7876343}. Note=It is present in early unpaired
CC cores, in the lateral domains of the synaptonemal complex and in the
CC chromosome cores when they separate at diplotene. It is found axial to
CC the metaphase I chromosomes and in association with pairs of sister
CC centromeres. The centromere-associated protein becomes dissociated from
CC the centromeres at anaphase II and is not found in mitotic metaphase
CC centromeres. {ECO:0000269|PubMed:7876343}.
CC -!- TISSUE SPECIFICITY: Detected in spermatocytes (at protein level).
CC {ECO:0000269|PubMed:7876343}.
CC -!- DOMAIN: Composed of a long central coiled coil domain. The N-terminal
CC and C-terminal regions interact with DNA.
CC {ECO:0000250|UniProtKB:Q8IZU3}.
CC -!- PTM: Phosphorylated. {ECO:0000250|UniProtKB:P70281}.
CC -!- SIMILARITY: Belongs to the XLR/SYCP3 family. {ECO:0000305}.
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DR EMBL; X77371; CAA54560.1; -; mRNA.
DR PIR; S41906; S41906.
DR RefSeq; NP_001268526.1; NM_001281597.1.
DR AlphaFoldDB; Q60547; -.
DR SMR; Q60547; -.
DR STRING; 10036.XP_005068034.1; -.
DR GeneID; 101825388; -.
DR CTD; 50511; -.
DR eggNOG; ENOG502R883; Eukaryota.
DR OrthoDB; 1547468at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR GO; GO:0000775; C:chromosome, centromeric region; ISS:UniProtKB.
DR GO; GO:0000800; C:lateral element; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR InterPro; IPR006888; XLR/SYCP3/FAM9_dom.
DR Pfam; PF04803; Cor1; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Centromere; Chromosome; Coiled coil;
KW DNA-binding; Meiosis; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..234
FT /note="Synaptonemal complex protein 3"
FT /id="PRO_0000223043"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..56
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:Q8IZU3"
FT REGION 67..72
FT /note="Important for oligomerization and fiber formation"
FT /evidence="ECO:0000250|UniProtKB:Q8IZU3"
FT REGION 86..89
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:Q8IZU3"
FT REGION 229..234
FT /note="Important for oligomerization and fiber formation"
FT /evidence="ECO:0000250|UniProtKB:Q8IZU3"
FT COILED 64..221
FT /evidence="ECO:0000250|UniProtKB:Q8IZU3, ECO:0000255"
FT MOTIF 86..89
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 23..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70281"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63520"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70281"
FT MOD_RES 198
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P70281"
SQ SEQUENCE 234 AA; 27134 MW; 7965AEDD9B989BF6 CRC64;
MVPGGRKHSG KSGKPPLVDQ AKTAFDFEKE DKELSGSEED VADEKTPVID KHGKKRSGGL
VEDVGGEVQN MLEKFGADIN KALLAKRKRI EMYTKASFKA SNQKIEQIWK TQQEEIQKLN
SEYSQQFMSV LQQWELDMQK FEEQGEKLTN LFRQQQKIFQ QSRIVQSQRL KAIKQLHEQF
IKNLEDVEKN NDNLFTGTQS ELKKEMAMLQ KKVMMETQQQ EMANVRKSLQ SMLF
