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 27-MAR-2024, entry version 150. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 10090-ENSMUSP00000020252; -. DR ProteomicsDB; 254733; -. DR DNASU; 20962; -. DR GeneID; 20962; -. DR KEGG; mmu:20962; -. DR AGR; MGI:109542; -. DR CTD; 50511; -. DR MGI; MGI:109542; Sycp3. DR eggNOG; ENOG502R883; Eukaryota. DR InParanoid; P70281; -. DR OrthoDB; 5398012at2759; -. DR PhylomeDB; P70281; -. DR BioGRID-ORCS; 20962; 2 hits in 112 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:0007130; P:synaptonemal complex assembly; IDA:UniProtKB. DR InterPro; IPR006888; XLR/SYCP3/FAM9_dom. DR PANTHER; PTHR19368:SF19; SYNAPTONEMAL COMPLEX PROTEIN 3; 1. DR PANTHER; PTHR19368; XLR/SCP3/FAM9; 1. 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 //