SYCP1_MOUSE
ID SYCP1_MOUSE Reviewed; 993 AA.
AC Q62209; B2RQK2; E9QP17; O09205; P70192; Q62329;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Synaptonemal complex protein 1 {ECO:0000303|PubMed:15944401};
DE Short=SCP-1;
GN Name=Sycp1 {ECO:0000303|PubMed:15937223, ECO:0000312|MGI:MGI:105931};
GN Synonyms=Scp1 {ECO:0000303|PubMed:7548215};
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 [MRNA].
RC STRAIN=CBA/J; TISSUE=Testis;
RX PubMed=7548215; DOI=10.1016/0167-4781(95)00126-2;
RA Sage J., Martin L., Cuzin F., Rassoulzadegan M.;
RT "cDNA sequence of the murine synaptonemal complex protein 1 (SCP1).";
RL Biochim. Biophys. Acta 1263:258-260(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=SWR/J; TISSUE=Testis;
RA Kerr S.M., Taggart M.H., Lee M., Cooke H.J.;
RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-149.
RC STRAIN=C57BL/6J;
RA Sage J., Li Y., Martin L., Mattei M.-G., Guenet J.-L., Liu J.G., Hoog C.,
RA Cuzin F., Rassoulzadegan M.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 95-787.
RC STRAIN=ICR; TISSUE=Testis;
RA Tsuchida J., Nishina Y., Nozaki M., Uchida K., Nishimune Y.;
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND TISSUE
RP SPECIFICITY.
RX PubMed=15937223; DOI=10.1101/gad.329705;
RA de Vries F.A., de Boer E., van den Bosch M., Baarends W.M., Ooms M.,
RA Yuan L., Liu J.G., van Zeeland A.A., Heyting C., Pastink A.;
RT "Mouse Sycp1 functions in synaptonemal complex assembly, meiotic
RT recombination, and XY body formation.";
RL Genes Dev. 19:1376-1389(2005).
RN [8]
RP IDENTIFICATION IN A COMPLEX WITH SYCE1 AND SYCE2, INTERACTION WITH SYCE1
RP AND SYCE2, AND SUBCELLULAR LOCATION.
RX PubMed=15944401; DOI=10.1242/jcs.02402;
RA Costa Y., Speed R., Oellinger R., Alsheimer M., Semple C.A., Gautier P.,
RA Maratou K., Novak I., Hoeoeg C., Benavente R., Cooke H.J.;
RT "Two novel proteins recruited by synaptonemal complex protein 1 (SYCP1) are
RT at the center of meiosis.";
RL J. Cell Sci. 118:2755-2762(2005).
RN [9]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
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 [10]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SYCE1.
RX PubMed=16968740; DOI=10.1242/jcs.03182;
RA Hamer G., Gell K., Kouznetsova A., Novak I., Benavente R., Hoeoeg C.;
RT "Characterization of a novel meiosis-specific protein within the central
RT element of the synaptonemal complex.";
RL J. Cell Sci. 119:4025-4032(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-820, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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 [12]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, 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 [13]
RP INTERACTION WITH PRDM9; EWSR1; SYCP3 AND REC8.
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 [14]
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 [15]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SPO16.
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 [16]
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: Major component of the transverse filaments of synaptonemal
CC complexes, formed between homologous chromosomes during meiotic
CC prophase (PubMed:16717126). Required for normal assembly of the central
CC element of the synaptonemal complexes (PubMed:15937223). Required for
CC normal centromere pairing during meiosis (PubMed:22761579). Required
CC for normal meiotic chromosome synapsis during oocyte and spermatocyte
CC development and for normal male and female fertility (PubMed:15937223).
CC {ECO:0000269|PubMed:15937223, ECO:0000269|PubMed:16717126,
CC ECO:0000269|PubMed:22761579}.
CC -!- SUBUNIT: Structural component of synaptonemal complexes
CC (PubMed:15937223, PubMed:16717126, PubMed:22761579). Homotetramer that
CC consists of an N-terminal four-helical bundle that bifurcates into two
CC elongated C-terminal dimeric coiled coils. This tetrameric building
CC block potentially self-assembles into a supramolecular zipper-like
CC lattice to mediate meiotic chromosome synapsis. Self-assembly is likely
CC initiated by local proton density at chromosome axis, which is
CC predicted to trigger antiparallel back to back assembly of adjacent C-
CC terminal ends into tetrameric structures that anchor to chromosomal
CC DNA. Then the N-terminal ends are predicted to undergo cooperative
CC antiparallel head to head assembly at the midline of synaptonemal
CC complexes central element to form a zipper-like lattice between
CC properly aligned homologous chromosomes (By similarity). The nascent
CC synapsis generated by SYCP1 is stabilized through interaction with
CC central element proteins SYCE1 and SYCE2 (PubMed:15944401,
CC PubMed:16968740). Forms a complex with EWSR1, PRDM9, SYCP3 and REC8;
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 (PubMed:27932493). Interacts with SPO16
CC (PubMed:30949703). {ECO:0000250|UniProtKB:Q15431,
CC ECO:0000269|PubMed:15937223, ECO:0000269|PubMed:15944401,
CC ECO:0000269|PubMed:16717126, ECO:0000269|PubMed:16968740,
CC ECO:0000269|PubMed:22761579, ECO:0000269|PubMed:27932493,
CC ECO:0000269|PubMed:30949703}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16717126}. Chromosome
CC {ECO:0000269|PubMed:15937223, ECO:0000269|PubMed:16717126,
CC ECO:0000269|PubMed:16968740, ECO:0000269|PubMed:22761579,
CC ECO:0000269|PubMed:30272023, ECO:0000269|PubMed:30746471,
CC ECO:0000269|PubMed:30949703}. Chromosome, centromere
CC {ECO:0000269|PubMed:22761579}. Note=In tripartite segments of
CC synaptonemal complexes, between lateral elements in the nucleus. Its N-
CC terminus is found towards the center of the synaptonemal complex while
CC the C-terminus extends well into the lateral domain of the synaptonemal
CC complex (By similarity). Only rarely detected at centromeres during
CC leptotene and zygotene. Detected at centromeres during mid-diplotene,
CC when it is no longer present along chromosome arms. No longer detected
CC at centromeres at later stages of meiosis (PubMed:22761579).
CC {ECO:0000250|UniProtKB:Q03410, ECO:0000269|PubMed:22761579}.
CC -!- TISSUE SPECIFICITY: Detected in testis (PubMed:15937223). Detected in
CC spermatocytes (at protein level) (PubMed:22761579).
CC {ECO:0000269|PubMed:15937223, ECO:0000269|PubMed:22761579}.
CC -!- DOMAIN: The molecule is in a coiled coil structure that is formed by 4
CC polypeptide chains. The N-terminal region exhibits a prominent seven-
CC residues periodicity. {ECO:0000250|UniProtKB:Q15431}.
CC -!- DISRUPTION PHENOTYPE: Mice appear generally healthy, but display
CC complete sterility, due to defective meiosis during germ cell
CC development. Ovaries and testes from mutant mice have strongly reduced
CC weight relative to wild-type. Ovaries display an absence of growing
CC follicles and oocytes. Testes show a complete lack of spermatids and
CC spermatozoa. Synaptonemal complexes from mutant spermatocytes form
CC normal axial elements, but lack the central element; chromosomes do not
CC synapse properly, cross-overs are rare, and DNA repair after meiotic
CC double-strand breaks is impaired. {ECO:0000269|PubMed:15937223}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA64514.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z38118; CAA86262.1; -; mRNA.
DR EMBL; L41069; AAA64514.1; ALT_INIT; mRNA.
DR EMBL; AH006782; AAC53335.1; -; Genomic_DNA.
DR EMBL; AC122219; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC134871; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC137967; AAI37968.1; -; mRNA.
DR EMBL; D88539; BAA13639.1; -; mRNA.
DR CCDS; CCDS38567.1; -.
DR PIR; S49461; S49461.
DR RefSeq; NP_035646.2; NM_011516.2.
DR AlphaFoldDB; Q62209; -.
DR SMR; Q62209; -.
DR BioGRID; 203596; 3.
DR CORUM; Q62209; -.
DR MINT; Q62209; -.
DR STRING; 10090.ENSMUSP00000029448; -.
DR iPTMnet; Q62209; -.
DR PhosphoSitePlus; Q62209; -.
DR PaxDb; Q62209; -.
DR PRIDE; Q62209; -.
DR ProteomicsDB; 254503; -.
DR Antibodypedia; 20167; 231 antibodies from 25 providers.
DR DNASU; 20957; -.
DR Ensembl; ENSMUST00000029448; ENSMUSP00000029448; ENSMUSG00000027855.
DR Ensembl; ENSMUST00000196988; ENSMUSP00000143651; ENSMUSG00000027855.
DR GeneID; 20957; -.
DR KEGG; mmu:20957; -.
DR UCSC; uc008qrz.2; mouse.
DR CTD; 6847; -.
DR MGI; MGI:105931; Sycp1.
DR VEuPathDB; HostDB:ENSMUSG00000027855; -.
DR eggNOG; ENOG502QTHX; Eukaryota.
DR GeneTree; ENSGT00390000003368; -.
DR HOGENOM; CLU_311150_0_0_1; -.
DR InParanoid; Q62209; -.
DR OMA; RLEMCFK; -.
DR OrthoDB; 286986at2759; -.
DR PhylomeDB; Q62209; -.
DR TreeFam; TF331737; -.
DR BioGRID-ORCS; 20957; 4 hits in 107 CRISPR screens.
DR ChiTaRS; Sycp1; mouse.
DR PRO; PR:Q62209; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q62209; protein.
DR Bgee; ENSMUSG00000027855; Expressed in spermatocyte and 45 other tissues.
DR ExpressionAtlas; Q62209; baseline and differential.
DR Genevisible; Q62209; MM.
DR GO; GO:0000801; C:central element; IDA:MGI.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:MGI.
DR GO; GO:0000800; C:lateral element; TAS:HGNC-UCL.
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:0003690; F:double-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051026; P:chiasma assembly; IGI:MGI.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IMP:UniProtKB.
DR GO; GO:0051878; P:lateral element assembly; IGI:MGI.
DR GO; GO:0000711; P:meiotic DNA repair synthesis; IMP:MGI.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP:UniProtKB.
DR GO; GO:0032880; P:regulation of protein localization; IMP:MGI.
DR GO; GO:0035092; P:sperm DNA condensation; IGI:MGI.
DR GO; GO:0007283; P:spermatogenesis; IGI:MGI.
DR GO; GO:0007130; P:synaptonemal complex assembly; IDA:HGNC-UCL.
DR InterPro; IPR008827; SYCP1.
DR PANTHER; PTHR46918; PTHR46918; 1.
DR Pfam; PF05483; SCP-1; 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..993
FT /note="Synaptonemal complex protein 1"
FT /id="PRO_0000072364"
FT REGION 694..788
FT /note="Required for pH-induced assembly of C-terminal ends
FT into antiparallel tetramers"
FT /evidence="ECO:0000250|UniProtKB:Q15431"
FT REGION 801..993
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q15431"
FT REGION 824..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 117..172
FT /evidence="ECO:0000255"
FT COILED 215..688
FT /evidence="ECO:0000255"
FT COILED 764..808
FT /evidence="ECO:0000255"
FT MOTIF 98..108
FT /note="Mediates head to head self-assembly of N-terminal
FT ends"
FT /evidence="ECO:0000250|UniProtKB:Q15431"
FT MOTIF 114..117
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 697..700
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 898..901
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 824..846
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 820
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 38
FT /note="A -> V (in Ref. 1; AAC53335/CAA86262, 2; AAA64514
FT and 4; AAI37968)"
FT /evidence="ECO:0000305"
FT CONFLICT 527
FT /note="F -> L (in Ref. 2; AAA64514)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 993 AA; 115935 MW; FF4930F279FBC251 CRC64;
MEKQKPFTLF VPPRLSSSQV SAVKPQTAGG DSNYFKTANK CTEGDFGVPF TMSSRENIDK
DPAFQKLSIL PMLEQVANSG SCHYQEGVND SDFENSEPMS RLYSKLYKEA EKIKKWKVSI
ESELKQKENK LQENRKIIEA QRKAIQELQF ENEKVSLKLE EEIQENKDLI KENNATIHWC
NLLKETCARS AEKTNKYEYE REETRQVYVD LNSNIEKMIL AFEELRVQAE NARLEMHFKL
KEDHEKIQHL EEEYQKEVNN KENQVSELLI QSAEKENKMK DLTFLLEESR DKANQLEEKT
KLQDENLKEL SEKKDHLTSE LEDIKMSMQR SMSTQKALEE DLQIATKTIS QLTEVKEAQM
EELNKAKTTH SFVVTELKAT TCTLEELLRT EQQRLEKNED QLKLITVELQ KKSNELEEMT
KFKNNKEVEL EELKNILAED QKLLDEKKQV EKLAEELQEK EQELTFLLET REKEVHDLQE
QVTVTKTSEQ HYLKQVEEMK TELEKEKLKN TELTASCDML LLENKKFVQE ASDMALELKK
HQEDIINCKK QEERLLKQIE NLEEKEMHLR DELESVRKEF IQQGDEVKCK LDKSEENARS
IECEVLKKEK QMKILESKCN NLKKQVENKS KNIEELHQEN KTLKKKSSAE IKQLNAYEIK
VSKLELELES TKQRFEEMTN NYQKEIENKK ISEGKLLGEV EKAKATVDEA VKLQKEIDLR
CQHKIAEMVA LMEKHKHQYD KIVEERDSEL GLYKNREQEQ SSAKIALETE LSNIRNELVS
LKKQLEIEKE EKEKLKMAKE NTAILKDKKD KKIQASLLES PEATSWKFDS KTTPSQNISR
LSSSMDSGKS KDNRDNLRAS AKSILPTTVT KEYTVKTPTK KSIYQRENKY IPTGGSNKKR
KTAFEFDVNS DSSETADLLS LVSEEDVSNR LYDNNPPDSH LLVKTPKQTP LSLSTPASFM
KFGSLKKMRE DRWTTIAKID RKRRLKEAEK LFS
