SYCP1_RAT
ID SYCP1_RAT Reviewed; 997 AA.
AC Q03410;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Synaptonemal complex protein 1 {ECO:0000250|UniProtKB:Q62209};
DE Short=SCP-1;
GN Name=Sycp1 {ECO:0000312|RGD:3794};
GN Synonyms=Scp1 {ECO:0000303|PubMed:1464329};
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, SUBCELLULAR LOCATION, SUBUNIT, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND DOMAIN.
RC TISSUE=Testis;
RX PubMed=1464329; DOI=10.1002/j.1460-2075.1992.tb05616.x;
RA Meuwissen R.L.J., Offenberg H.H., Dietrich A.J., Riesewijk A., Iersel M.,
RA Heyting C.;
RT "A coiled-coil related protein specific for synapsed regions of meiotic
RT prophase chromosomes.";
RL EMBO J. 11:5091-5100(1992).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-824 AND THR-940, AND
RP 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: Major component of the transverse filaments of synaptonemal
CC complexes, formed between homologous chromosomes during meiotic
CC prophase (PubMed:1464329). Required for normal assembly of the central
CC element of the synaptonemal complexes. Required for normal centromere
CC pairing during meiosis. Required for normal meiotic chromosome synapsis
CC during oocyte and spermatocyte development and for normal male and
CC female fertility. {ECO:0000250|UniProtKB:Q62209,
CC ECO:0000269|PubMed:1464329}.
CC -!- SUBUNIT: Structural component of synaptonemal complexes (By
CC similarity). Homotetramer that consists of an N-terminal four-helical
CC bundle that bifurcates into two elongated C-terminal dimeric coiled
CC coils. This tetrameric building block potentially self-assembles into a
CC supramolecular zipper-like lattice to mediate meiotic chromosome
CC synapsis. Self-assembly is likely initiated by local proton density at
CC chromosome axis, which is predicted to trigger antiparallel back to
CC back assembly of adjacent C-terminal ends into tetrameric structures
CC that anchor to chromosomal DNA. Then the N-terminal ends are predicted
CC to undergo cooperative antiparallel head to head assembly at the
CC midline of synaptonemal complexes central element to form a zipper-like
CC lattice between properly aligned homologous chromosomes (By
CC similarity). The nascent synapsis generated by SYCP1 is stabilized
CC through interaction with central element proteins SYCE1 and SYCE2 (By
CC similarity). Forms a complex with EWSR1, PRDM9, SYCP3 and REC8; complex
CC formation is dependent of phosphorylated form of REC8 and requires
CC PRDM9 bound to hotspot DNA; EWSR1 joins PRDM9 with the chromosomal axis
CC through REC8 (By similarity). Interacts with SPO16 (By similarity).
CC {ECO:0000250|UniProtKB:Q15431, ECO:0000250|UniProtKB:Q62209}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q62209}.
CC Chromosome {ECO:0000269|PubMed:1464329}. Chromosome, centromere
CC {ECO:0000250|UniProtKB:Q62209}. 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 (PubMed:1464329). 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 (By similarity).
CC {ECO:0000250|UniProtKB:Q62209, ECO:0000269|PubMed:1464329}.
CC -!- TISSUE SPECIFICITY: Testis. {ECO:0000269|PubMed:1464329}.
CC -!- DEVELOPMENTAL STAGE: Expressed exclusively in meiotic prophase cells.
CC {ECO:0000269|PubMed:1464329}.
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 ECO:0000305|PubMed:1464329}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA48006.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X67805; CAA48006.1; ALT_FRAME; mRNA.
DR PIR; S28061; S28061.
DR RefSeq; NP_036942.1; NM_012810.1.
DR AlphaFoldDB; Q03410; -.
DR SMR; Q03410; -.
DR IntAct; Q03410; 1.
DR MINT; Q03410; -.
DR STRING; 10116.ENSRNOP00000023333; -.
DR iPTMnet; Q03410; -.
DR PhosphoSitePlus; Q03410; -.
DR PaxDb; Q03410; -.
DR PRIDE; Q03410; -.
DR GeneID; 25276; -.
DR KEGG; rno:25276; -.
DR UCSC; RGD:3794; rat.
DR CTD; 6847; -.
DR RGD; 3794; Sycp1.
DR eggNOG; ENOG502QTHX; Eukaryota.
DR InParanoid; Q03410; -.
DR OrthoDB; 286986at2759; -.
DR PhylomeDB; Q03410; -.
DR PRO; PR:Q03410; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0000801; C:central element; ISO:RGD.
DR GO; GO:0005694; C:chromosome; ISO:RGD.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0000794; C:condensed nuclear chromosome; ISO:RGD.
DR GO; GO:0001673; C:male germ cell nucleus; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0000795; C:synaptonemal complex; IDA:RGD.
DR GO; GO:0000802; C:transverse filament; IDA:RGD.
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; ISO:RGD.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; ISS:UniProtKB.
DR GO; GO:0051878; P:lateral element assembly; ISO:RGD.
DR GO; GO:0000711; P:meiotic DNA repair synthesis; ISO:RGD.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR GO; GO:0007131; P:reciprocal meiotic recombination; ISS:UniProtKB.
DR GO; GO:0032880; P:regulation of protein localization; ISO:RGD.
DR GO; GO:0035092; P:sperm DNA condensation; ISO:RGD.
DR GO; GO:0007283; P:spermatogenesis; ISO:RGD.
DR GO; GO:0007130; P:synaptonemal complex assembly; ISS:UniProtKB.
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..997
FT /note="Synaptonemal complex protein 1"
FT /id="PRO_0000072365"
FT REGION 698..792
FT /note="Required for pH-induced assembly of C-terminal ends
FT into antiparallel tetramers"
FT /evidence="ECO:0000250|UniProtKB:Q15431"
FT REGION 805..997
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q15431"
FT REGION 828..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 121..176
FT /evidence="ECO:0000255"
FT COILED 212..696
FT /evidence="ECO:0000255"
FT COILED 768..806
FT /evidence="ECO:0000255"
FT MOTIF 102..112
FT /note="Mediates head to head self-assembly of N-terminal
FT ends"
FT /evidence="ECO:0000250|UniProtKB:Q15431"
FT MOTIF 118..121
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 701..704
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 902..905
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 828..850
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 824
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 940
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 997 AA; 116511 MW; 229D59823FD684BE CRC64;
MEKQKPFTLF VPPRLSSSQV SAVKPQTAGG DSNYFKTVNK CTEGDFGVPL TMSSLSKNRE
NIDTDPAFQK LSILPMLEQV ANSGSCHYQE GVNDSDFENS EPMSRLYSKL YKEAEKIKKW
KVSIESELKQ KENKLQENRK IIEAQRKAIQ ELQFENEKVS LKLEEEIQEN KDLIKENNAT
RHWCNLLKET CARSAEKTSK YEYEREETRQ VYVDLNNNIE KMILAFEELR VQAENARLEM
HFKLKEDHEK IQHLEEEYQK EVNNKENQVS LLLIQSTEKE NKMKDLTFLL EESRDKANQL
EEKTKLQDEN LKELNEKKDH LTSELEDIKM SMQRSMSTQK TLEEDLQIAT KTIYQLTEEK
EAQMEELNKA KTTHSLVVTE LKATTCTLEE LLRTEQQRLE NNEDQLKLIT MELQKKSSEL
EEMTKFKNNK EVELEELKTI LAEDQKLLDE KKQVEKLAEE LQGKEQELTF LLQTREKEIH
DLEVQVTVTK TSEEHYLKQV EEMKTELEKE KLKNIELTAN SDMLLLENKK LVQEASDMVL
ELKKHQEDII NCKKQEERML KQIETLEEKE MNLRDELESV RKEFIQQGDE VKCKLDKSEE
NARSIEYEVL KKEKQMKILE NKCNNLKKQI ENKSKNIEEL HQENKALKKK SSAENKQLNA
YEIKVNKLEL ELASTKQKFE EMINNYQKEI EIKKISEEKL LGEVEKAKAT VDEAVKLQKE
IDLRCQHKIA EMVALMEKHK HQYDKIVEER DSELGLYKNR EQEQSSAKVA LETELSNIRN
ELVSLKKQLE VEKEEKEKLK MEQENTAILT DKKDKKIQAS LLESPEATSW KFDSKTTPSQ
NISRLSSSMD SGKSKDNRDS LRASAKSILS TTVTKEYTVK TPTKKSIYQR ENKYLPTGGS
NKKRKTVFEF DVNSDSSETT DLLSLVSEED ISNRIYNNNT PDSHLLVKTP KQTPLSLSTP
ASFTKFGSLK KMREDRWATI AKIDRKRRLK EAEKLFT
