SYCP3_MOUSE
ID SYCP3_MOUSE Reviewed; 254 AA.
AC P70281; Q3V2A4; Q549A7;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Synaptonemal complex protein 3;
DE Short=SCP-3;
GN Name=Sycp3; Synonyms=Scp3 {ECO:0000303|PubMed:10678170};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Liver, and Testis;
RX PubMed=9133341; DOI=10.1007/s003359900638;
RA Klink A., Lee M., Cooke H.J.;
RT "The mouse synaptosomal complex protein gene Sycp3 maps to band C of
RT chromosome 10.";
RL Mamm. Genome 8:376-377(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RX PubMed=11311943; DOI=10.1016/s0167-4781(01)00171-3;
RA Botelho R.J., DiNicolo L., Tsao N., Karaiskakis A., Tarsounas M.,
RA Moens P.B., Pearlman R.E.;
RT "The genomic structure of SYCP3, a meiosis-specific gene encoding a protein
RT of the chromosome core.";
RL Biochim. Biophys. Acta 1518:294-299(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic stem cell;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=10678170; DOI=10.1016/s1097-2765(00)80404-9;
RA Yuan L., Liu J.G., Zhao J., Brundell E., Daneholt B., Hoog C.;
RT "The murine SCP3 gene is required for synaptonemal complex assembly,
RT chromosome synapsis, and male fertility.";
RL Mol. Cell 5:73-83(2000).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=12004129; DOI=10.1126/science.1070594;
RA Yuan L., Liu J.G., Hoja M.R., Wilbertz J., Nordqvist K., Hoeoeg C.;
RT "Female germ cell aneuploidy and embryo death in mice lacking the meiosis-
RT specific protein SCP3.";
RL Science 296:1115-1118(2002).
RN [6]
RP INTERACTION WITH SYCP2, SUBCELLULAR LOCATION, SUBUNIT, FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=16717126; DOI=10.1083/jcb.200603063;
RA Yang F., De La Fuente R., Leu N.A., Baumann C., McLaughlin K.J., Wang P.J.;
RT "Mouse SYCP2 is required for synaptonemal complex assembly and chromosomal
RT synapsis during male meiosis.";
RL J. Cell Biol. 173:497-507(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-10; SER-11; SER-55;
RP SER-77 AND THR-218, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=22761579; DOI=10.1371/journal.pgen.1002701;
RA Bisig C.G., Guiraldelli M.F., Kouznetsova A., Scherthan H., Hoeoeg C.,
RA Dawson D.S., Pezza R.J.;
RT "Synaptonemal complex components persist at centromeres and are required
RT for homologous centromere pairing in mouse spermatocytes.";
RL PLoS Genet. 8:E1002701-E1002701(2012).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=22346761; DOI=10.1371/journal.pgen.1002485;
RA Fukuda T., Pratto F., Schimenti J.C., Turner J.M., Camerini-Otero R.D.,
RA Hoeoeg C.;
RT "Phosphorylation of chromosome core components may serve as axis marks for
RT the status of chromosomal events during mammalian meiosis.";
RL PLoS Genet. 8:E1002485-E1002485(2012).
RN [10]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=24287868; DOI=10.1007/s00412-013-0444-7;
RA Visnes T., Giordano F., Kuznetsova A., Suja J.A., Lander A.D., Calof A.L.,
RA Stroem L.;
RT "Localisation of the SMC loading complex Nipbl/Mau2 during mammalian
RT meiotic prophase I.";
RL Chromosoma 123:239-252(2014).
RN [11]
RP INTERACTION WITH PRDM9; EWSR1; REC8 AND SYCP1.
RX PubMed=27932493; DOI=10.1091/mbc.e16-09-0686;
RA Parvanov E.D., Tian H., Billings T., Saxl R.L., Spruce C., Aithal R.,
RA Krejci L., Paigen K., Petkov P.M.;
RT "PRDM9 interactions with other proteins provide a link between
RT recombination hotspots and the chromosomal axis in meiosis.";
RL Mol. Biol. Cell 28:488-499(2017).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=30272023; DOI=10.1038/s42003-018-0154-z;
RA Zhang Q., Shao J., Fan H.Y., Yu C.;
RT "Evolutionarily-conserved MZIP2 is essential for crossover formation in
RT mammalian meiosis.";
RL Commun. Biol. 1:147-147(2018).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=30949703; DOI=10.1093/nar/gkz226;
RA Liu H., Huang T., Li M., Li M., Zhang C., Jiang J., Yu X., Yin Y.,
RA Zhang F., Lu G., Luo M.C., Zhang L.R., Li J., Liu K., Chen Z.J.;
RT "SCRE serves as a unique synaptonemal complex fastener and is essential for
RT progression of meiosis prophase I in mice.";
RL Nucleic Acids Res. 47:5670-5683(2019).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=30746471; DOI=10.1126/sciadv.aau9780;
RA Zhang Q., Ji S.Y., Busayavalasa K., Yu C.;
RT "SPO16 binds SHOC1 to promote homologous recombination and crossing-over in
RT meiotic prophase I.";
RL Sci. Adv. 5:eaau9780-eaau9780(2019).
CC -!- FUNCTION: Component of the synaptonemal complexes (SCS), formed between
CC homologous chromosomes during meiotic prophase (PubMed:11311943,
CC PubMed:22761579). Required for centromere pairing during meiosis in
CC male germ cells (PubMed:22761579). Required for normal meiosis during
CC spermatogenesis and male fertility (PubMed:10678170). Plays a lesser
CC role in female fertility (PubMed:10678170, PubMed:12004129). Required
CC for efficient phosphorylation of HORMAD1 and HORMAD2 (PubMed:22346761).
CC {ECO:0000269|PubMed:10678170, ECO:0000269|PubMed:11311943,
CC ECO:0000269|PubMed:12004129, ECO:0000269|PubMed:22346761,
CC ECO:0000269|PubMed:22761579}.
CC -!- SUBUNIT: Component of the lateral elements of synaptonemal complexes
CC (PubMed:16717126). 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 (PubMed:16717126). 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 (PubMed:27932493).
CC {ECO:0000250|UniProtKB:Q8IZU3, ECO:0000269|PubMed:16717126,
CC ECO:0000269|PubMed:27932493}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16717126}. Chromosome
CC {ECO:0000269|PubMed:16717126, ECO:0000269|PubMed:22346761,
CC ECO:0000269|PubMed:22761579, ECO:0000269|PubMed:24287868,
CC ECO:0000269|PubMed:30272023, ECO:0000269|PubMed:30746471,
CC ECO:0000269|PubMed:30949703}. Chromosome, centromere
CC {ECO:0000269|PubMed:22761579}. 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 (By similarity). The phosphorylated form localizes
CC preferentially to unsynapsed chromosomal regions (PubMed:22346761).
CC {ECO:0000250|UniProtKB:Q60547, ECO:0000269|PubMed:22346761}.
CC -!- TISSUE SPECIFICITY: Detected in oocytes (PubMed:16717126). Detected in
CC spermatocytes and testis (at protein level) (PubMed:10678170,
CC PubMed:16717126, PubMed:22761579). {ECO:0000269|PubMed:10678170,
CC ECO:0000269|PubMed:16717126, ECO:0000269|PubMed:22761579,
CC ECO:0000269|PubMed:24287868}.
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:0000269|PubMed:22346761}.
CC -!- DISRUPTION PHENOTYPE: Homozygous males with null mutations have smaller
CC testes and are sterile, due to massive apoptotic cell death of male
CC germ cells during meiotic prophase. Spermatocytes fail to form
CC axial/lateral elements and synaptonemal complexes, and the chromosomes
CC in the mutant spermatocytes do not synapse (PubMed:10678170). In
CC contrast, females are fertile and generate healthy offspring. However,
CC they exhibit a sharp reduction in litter size that increases with
CC advancing maternal age (PubMed:10678170, PubMed:12004129). In contrast
CC to wild-type, a high percentage of the mutant embryos display
CC aneuploidy (PubMed:12004129). {ECO:0000269|PubMed:10678170,
CC ECO:0000269|PubMed:12004129}.
CC -!- SIMILARITY: Belongs to the XLR/SYCP3 family. {ECO:0000305}.
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DR EMBL; Y08485; CAA69719.1; -; mRNA.
DR EMBL; Y08486; CAA69720.1; -; Genomic_DNA.
DR EMBL; AF181478; AAG17538.1; -; Genomic_DNA.
DR EMBL; AF181473; AAG17538.1; JOINED; Genomic_DNA.
DR EMBL; AF181474; AAG17538.1; JOINED; Genomic_DNA.
DR EMBL; AF181475; AAG17538.1; JOINED; Genomic_DNA.
DR EMBL; AF181476; AAG17538.1; JOINED; Genomic_DNA.
DR EMBL; AF181477; AAG17538.1; JOINED; Genomic_DNA.
DR EMBL; AK131949; BAE20894.1; -; mRNA.
DR CCDS; CCDS24111.1; -.
DR RefSeq; NP_035647.2; NM_011517.2.
DR PDB; 6DD8; X-ray; 2.60 A; A/B/C/D=105-248.
DR PDB; 6DD9; X-ray; 2.30 A; A/B/C/D=105-248.
DR PDBsum; 6DD8; -.
DR PDBsum; 6DD9; -.
DR AlphaFoldDB; P70281; -.
DR SMR; P70281; -.
DR BioGRID; 203598; 3.
DR CORUM; P70281; -.
DR IntAct; P70281; 3.
DR MINT; P70281; -.
DR STRING; 10090.ENSMUSP00000020252; -.
DR iPTMnet; P70281; -.
DR PhosphoSitePlus; P70281; -.
DR PaxDb; P70281; -.
DR PRIDE; P70281; -.
DR ProteomicsDB; 254733; -.
DR DNASU; 20962; -.
DR GeneID; 20962; -.
DR KEGG; mmu:20962; -.
DR CTD; 50511; -.
DR MGI; MGI:109542; Sycp3.
DR eggNOG; ENOG502R883; Eukaryota.
DR InParanoid; P70281; -.
DR OrthoDB; 1547468at2759; -.
DR PhylomeDB; P70281; -.
DR BioGRID-ORCS; 20962; 2 hits in 107 CRISPR screens.
DR ChiTaRS; Sycp3; mouse.
DR PRO; PR:P70281; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P70281; protein.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
DR GO; GO:0000793; C:condensed chromosome; IDA:MGI.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:MGI.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:MGI.
DR GO; GO:0001674; C:female germ cell nucleus; IDA:MGI.
DR GO; GO:0000800; C:lateral element; IDA:UniProtKB.
DR GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0000795; C:synaptonemal complex; IDA:MGI.
DR GO; GO:0000802; C:transverse filament; IDA:MGI.
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; IEP:MGI.
DR GO; GO:0051026; P:chiasma assembly; IDA:UniProtKB.
DR GO; GO:0016321; P:female meiosis chromosome segregation; IDA:UniProtKB.
DR GO; GO:0051309; P:female meiosis chromosome separation; NAS:UniProtKB.
DR GO; GO:0007066; P:female meiosis sister chromatid cohesion; IDA:UniProtKB.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IMP:MGI.
DR GO; GO:0051878; P:lateral element assembly; IGI:MGI.
DR GO; GO:0051321; P:meiotic cell cycle; IDA:MGI.
DR GO; GO:0000711; P:meiotic DNA repair synthesis; IGI:MGI.
DR GO; GO:0000278; P:mitotic cell cycle; IDA:MGI.
DR GO; GO:0035092; P:sperm DNA condensation; IGI:MGI.
DR GO; GO:0007286; P:spermatid development; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR GO; GO:0035093; P:spermatogenesis, exchange of chromosomal proteins; ISO:MGI.
DR GO; GO:0007130; P:synaptonemal complex assembly; IDA:UniProtKB.
DR InterPro; IPR006888; XLR/SYCP3/FAM9_dom.
DR Pfam; PF04803; Cor1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Centromere; Chromosome;
KW Coiled coil; DNA-binding; Meiosis; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..254
FT /note="Synaptonemal complex protein 3"
FT /id="PRO_0000223044"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..76
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:Q8IZU3"
FT REGION 87..92
FT /note="Important for oligomerization and fiber formation"
FT /evidence="ECO:0000250|UniProtKB:Q8IZU3"
FT REGION 106..109
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:Q8IZU3"
FT REGION 249..254
FT /note="Important for oligomerization and fiber formation"
FT /evidence="ECO:0000250|UniProtKB:Q8IZU3"
FT COILED 84..241
FT /evidence="ECO:0000250|UniProtKB:Q8IZU3, ECO:0000255"
FT MOTIF 106..109
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 41..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63520"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 218
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 191
FT /note="F -> K (in Ref. 3; BAE20894)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="M -> I (in Ref. 3; BAE20894)"
FT /evidence="ECO:0000305"
FT HELIX 112..211
FT /evidence="ECO:0007829|PDB:6DD9"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:6DD9"
FT HELIX 218..237
FT /evidence="ECO:0007829|PDB:6DD9"
SQ SEQUENCE 254 AA; 29347 MW; E0121D58A8DCD2EA CRC64;
MLRGCGDSDS SPEPLSKHLK MVPGGRKHSG KSGKPPLVDQ PKKAFDFEKD DKDLSGSEED
VADEKAPVID KHGKKRSAGI IEDVGGEVQN MLEKFGADIN KALLAKRKRI EMYTKASFKA
SNQKIEQIWK TQQEEIQKLN NEYSQQFMNV LQQWELDIQK FEEQGEKLSN LFRQQQKIFQ
QSRIVQSQRM FAMKQIHEQF IKSLEDVEKN NDNLFTGTQS ELKKEMAMLQ KKVMMETQQQ
EMANVRKSLQ SMLF
