ID   SYCP3_BOVIN             Reviewed;         225 AA.
AC   Q3T0E2;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Synaptonemal complex protein 3;
DE            Short=SCP-3;
GN   Name=SYCP3;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the synaptonemal complexes (SCS), formed between
CC       homologous chromosomes during meiotic prophase. Required for centromere
CC       pairing during meiosis in male germ cells. Required for normal meiosis
CC       during spermatogenesis and male fertility. Plays a lesser role in
CC       female fertility. Required for efficient phosphorylation of HORMAD1 and
CC       HORMAD2. {ECO:0000250|UniProtKB:P70281}.
CC   -!- SUBUNIT: Component of the lateral elements of synaptonemal complexes
CC       (By similarity). 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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q60547}.
CC       Chromosome {ECO:0000250|UniProtKB:Q60547}. Chromosome, centromere
CC       {ECO:0000250|UniProtKB:Q60547}. 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:0000250|UniProtKB:Q60547}.
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; BC102433; AAI02434.1; -; mRNA.
DR   RefSeq; NP_001035678.1; NM_001040588.2.
DR   AlphaFoldDB; Q3T0E2; -.
DR   SMR; Q3T0E2; -.
DR   STRING; 9913.ENSBTAP00000027778; -.
DR   PaxDb; Q3T0E2; -.
DR   GeneID; 615896; -.
DR   KEGG; bta:615896; -.
DR   CTD; 50511; -.
DR   eggNOG; ENOG502R883; Eukaryota.
DR   InParanoid; Q3T0E2; -.
DR   OrthoDB; 1547468at2759; -.
DR   Proteomes; UP000009136; 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:0000795; C:synaptonemal complex; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0007286; P:spermatid development; IBA:GO_Central.
DR   InterPro; IPR006888; XLR/SYCP3/FAM9_dom.
DR   Pfam; PF04803; Cor1; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Centromere; Chromosome; Coiled coil;
KW   DNA-binding; Meiosis; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..225
FT                   /note="Synaptonemal complex protein 3"
FT                   /id="PRO_0000229023"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          52..57
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IZU3"
FT   REGION          68..73
FT                   /note="Important for oligomerization and fiber formation"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IZU3"
FT   REGION          87..90
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IZU3"
FT   COILED          65..218
FT                   /evidence="ECO:0000250|UniProtKB:Q8IZU3, ECO:0000255"
FT   MOTIF           87..90
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        24..59
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         36
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P70281"
FT   MOD_RES         38
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q63520"
SQ   SEQUENCE   225 AA;  26341 MW;  BDCAE30EAD49D339 CRC64;
     MVPSGRKHSG KLAKPSVGDQ AIRAYEFEQE DKKDLSGSEE DAIEEKTPTL EKQGKKRTSA
     AVEDMGGEVQ NMLERFGADI NKSLLAKRKR LEMYTKASLK TSNQKLENVW KIQQEQRQKL
     NQEYSQQFLT LFQQWDIDMQ KAEEQEEKLA NLFRQQQKVF QQSRIVQSQR LKTIRQLYEQ
     FIKSMEDLEK NHENLLTGAQ NELKKEMALL QKKIMMETVS CYSEL