SYCP3_RAT
ID SYCP3_RAT Reviewed; 257 AA.
AC Q63520;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Synaptonemal complex protein 3;
DE Short=SCP-3;
GN Name=Sycp3; Synonyms=Scp3 {ECO:0000303|PubMed:9933407};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC STRAIN=Wistar;
RX PubMed=8289794; DOI=10.1128/mcb.14.2.1137-1146.1994;
RA Lammers J.H.M., Offenberg H.H., van Aalderen M., Vink A.C.G.,
RA Dietrich A.J.J., Heyting C.;
RT "The gene encoding a major component of the lateral elements of
RT synaptonemal complexes of the rat is related to X-linked lymphocyte-
RT regulated genes.";
RL Mol. Cell. Biol. 14:1137-1146(1994).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=9933407; DOI=10.1007/s004120050340;
RA Schalk J.A.C., Dietrich A.J.J., Vink A.C.G., Offenberg H.H.,
RA van Aalderen M., Heyting C.;
RT "Localization of SCP2 and SCP3 protein molecules within synaptonemal
RT complexes of the rat.";
RL Chromosoma 107:540-548(1998).
RN [3]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=9679134; DOI=10.1083/jcb.142.2.331;
RA Yuan L., Pelttari J., Brundell E., Bjoerkroth B., Zhao J., Liu J.G.,
RA Brismar H., Daneholt B., Hoeoeg C.;
RT "The synaptonemal complex protein SCP3 can form multistranded, cross-
RT striated fibers in vivo.";
RL J. Cell Biol. 142:331-339(1998).
RN [4]
RP INTERACTION WITH SYCP2.
RX PubMed=10652260; DOI=10.1242/jcs.113.4.673;
RA Eijpe M., Heyting C., Gross B., Jessberger R.;
RT "Association of mammalian SMC1 and SMC3 proteins with meiotic chromosomes
RT and synaptonemal complexes.";
RL J. Cell Sci. 113:673-682(2000).
RN [5]
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=18391527; DOI=10.1159/000102105;
RA Baier A., Alsheimer M., Volff J.N., Benavente R.;
RT "Synaptonemal complex protein SYCP3 of the rat: evolutionarily conserved
RT domains and the assembly of higher order structures.";
RL Sex. Dev. 1:161-168(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-58; SER-60 AND
RP SER-80, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Component of the synaptonemal complexes (SCS), formed between
CC homologous chromosomes during meiotic prophase (PubMed:8289794,
CC PubMed:9933407). Required for centromere pairing during meiosis in male
CC germ cells. Required for normal meiosis during spermatogenesis and male
CC fertility. Plays a lesser role in female fertility. Required for
CC efficient phosphorylation of HORMAD1 and HORMAD2.
CC {ECO:0000250|UniProtKB:P70281, ECO:0000269|PubMed:8289794,
CC ECO:0000269|PubMed:9933407}.
CC -!- SUBUNIT: Component of the lateral elements of synaptonemal complexes
CC (PubMed:8289794, PubMed:9933407). Homotetramer; the tetrameric helix
CC bundles assemble end to end into long homopolimeric fibers (in vitro)
CC (By similarity). Homooligomer that assembles into fibers; the fibers
CC exhibit a transversal striation with a periodicity of about 20 nm (in
CC vitro) (PubMed:9679134, PubMed:18391527). Interacts with SYCP2
CC (PubMed:10652260). Forms a complex with EWSR1, PRDM9, REC8 and SYCP1;
CC complex formation is dependent of phosphorylated form of REC8 and
CC requires PRDM9 bound to hotspot DNA; EWSR1 joins PRDM9 with the
CC chromosomal axis through REC8 (By similarity).
CC {ECO:0000250|UniProtKB:P70281, ECO:0000250|UniProtKB:Q8IZU3,
CC ECO:0000269|PubMed:10652260, ECO:0000269|PubMed:8289794,
CC ECO:0000269|PubMed:9679134, ECO:0000269|PubMed:9933407}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18391527,
CC ECO:0000269|PubMed:9679134}. Chromosome {ECO:0000269|PubMed:8289794,
CC ECO:0000269|PubMed:9933407}. 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 -!- TISSUE SPECIFICITY: Detected in spermatocytes and testis (at protein
CC level) (PubMed:8289794, PubMed:9933407). Testis-specific
CC (PubMed:8289794). {ECO:0000269|PubMed:8289794}.
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; X75785; CAA53430.1; -; mRNA.
DR PIR; A55925; A55925.
DR RefSeq; NP_037173.1; NM_013041.1.
DR AlphaFoldDB; Q63520; -.
DR SMR; Q63520; -.
DR STRING; 10116.ENSRNOP00000007088; -.
DR iPTMnet; Q63520; -.
DR PhosphoSitePlus; Q63520; -.
DR PaxDb; Q63520; -.
DR Ensembl; ENSRNOT00000007088; ENSRNOP00000007088; ENSRNOG00000005270.
DR GeneID; 25561; -.
DR KEGG; rno:25561; -.
DR CTD; 50511; -.
DR RGD; 3795; Sycp3.
DR eggNOG; ENOG502R883; Eukaryota.
DR GeneTree; ENSGT00390000000062; -.
DR HOGENOM; CLU_101820_2_0_1; -.
DR InParanoid; Q63520; -.
DR OMA; TPVMDKH; -.
DR OrthoDB; 847100at2759; -.
DR PhylomeDB; Q63520; -.
DR PRO; PR:Q63520; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000005270; Expressed in testis and 17 other tissues.
DR Genevisible; Q63520; RN.
DR GO; GO:0005694; C:chromosome; ISO:RGD.
DR GO; GO:0000775; C:chromosome, centromeric region; ISS:UniProtKB.
DR GO; GO:0000793; C:condensed chromosome; ISO:RGD.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; ISO:RGD.
DR GO; GO:0000794; C:condensed nuclear chromosome; ISO:RGD.
DR GO; GO:0000800; C:lateral element; IDA:UniProtKB.
DR GO; GO:0001673; C:male germ cell nucleus; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0000795; C:synaptonemal complex; ISO:RGD.
DR GO; GO:0000802; C:transverse filament; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; ISO:RGD.
DR GO; GO:0051026; P:chiasma assembly; ISO:RGD.
DR GO; GO:0016321; P:female meiosis chromosome segregation; ISO:RGD.
DR GO; GO:0007066; P:female meiosis sister chromatid cohesion; ISO:RGD.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; ISO:RGD.
DR GO; GO:0051878; P:lateral element assembly; ISO:RGD.
DR GO; GO:0051321; P:meiotic cell cycle; ISO:RGD.
DR GO; GO:0000711; P:meiotic DNA repair synthesis; ISO:RGD.
DR GO; GO:0000278; P:mitotic cell cycle; ISO:RGD.
DR GO; GO:0035092; P:sperm DNA condensation; ISO:RGD.
DR GO; GO:0007286; P:spermatid development; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; ISO:RGD.
DR GO; GO:0035093; P:spermatogenesis, exchange of chromosomal proteins; ISO:RGD.
DR GO; GO:0007130; P:synaptonemal complex assembly; ISO:RGD.
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..257
FT /note="Synaptonemal complex protein 3"
FT /id="PRO_0000223045"
FT REGION 23..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..79
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:Q8IZU3"
FT REGION 90..95
FT /note="Important for oligomerization and fiber formation"
FT /evidence="ECO:0000250|UniProtKB:Q8IZU3"
FT REGION 109..112
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:Q8IZU3"
FT REGION 252..257
FT /note="Important for oligomerization and fiber formation"
FT /evidence="ECO:0000250|UniProtKB:Q8IZU3"
FT COILED 87..244
FT /evidence="ECO:0000250|UniProtKB:Q8IZU3, ECO:0000255"
FT MOTIF 109..112
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 44..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 221
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P70281"
SQ SEQUENCE 257 AA; 29733 MW; 97C709F56918AF32 CRC64;
MLRGCGEVGA VDCSPEQLNK HLKMVPGGRK HSGKSGKPPL IDQPKKAFDF EKEDKDLSGS
EEDAVDEKTQ VFDKHGKKRS AGIIEDVGGE VQNMLEKFGA DINKALLAKK KRIEMYTKAS
FKASNQKIEQ IWKTQQEEIQ KLNNEYSQQF LSVLQQWELD MQKFEEQGEK LTNLFRQQQK
IFQQTRIVQS QRMKAIKQLH EQFIKSLEDV EKNNDNLFTG TQSELKKEMA MLQKKVMMET
QQQEMANVRK SLQSMLF
