SYCP1_MESAU
ID SYCP1_MESAU Reviewed; 845 AA.
AC Q60563;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Synaptonemal complex protein 1 {ECO:0000250|UniProtKB:Q62209};
DE Short=SCP-1;
DE AltName: Full=Meiotic chromosome synaptic protein;
DE Flags: Fragment;
GN Name=SCP1 {ECO:0000250|UniProtKB:Q62209}; Synonyms=SYN1;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=7876343; DOI=10.1242/jcs.107.10.2749;
RA Dobson M.J., Pearlman R.E., Karaiskakis A., Spyropoulos B., Moens P.B.;
RT "Synaptonemal complex proteins: occurrence, epitope mapping and chromosome
RT disjunction.";
RL J. Cell Sci. 107:2749-2760(1994).
CC -!- FUNCTION: Major component of the transverse filaments of synaptonemal
CC complexes, formed between homologous chromosomes during meiotic
CC prophase (By similarity). Has non-specific DNA binding capability.
CC {ECO:0000250}.
CC -!- SUBUNIT: Structural component of synaptonemal complexes (By
CC similarity). Homotetramer that potentially self-assembles into a
CC supramolecular zipper-like lattice to mediate meiotic chromosome
CC synapsis (By similarity). The nascent synapsis generated by SYCP1 is
CC stabilized through interaction with central element proteins SYCE1 and
CC SYCE2 (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:0000250|UniProtKB:Q62209}. Chromosome, centromere
CC {ECO:0000250|UniProtKB:Q62209}. Note=In tripartite segments of
CC synaptonemal complexes, between lateral elements in the nucleus. Found
CC only where the chromosome cores are synapsed. Its N-terminus is found
CC towards the center of the synaptonemal complex while the C-terminus
CC extends well into the lateral domain of the synaptonemal complex.
CC {ECO:0000250|UniProtKB:Q03410, ECO:0000250|UniProtKB:Q62209}.
CC -!- DOMAIN: The molecule is in a coiled coil structure.
CC {ECO:0000250|UniProtKB:Q15431}.
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DR EMBL; L32978; AAC42039.1; -; mRNA.
DR PIR; I48176; I48176.
DR AlphaFoldDB; Q60563; -.
DR SMR; Q60563; -.
DR PRIDE; Q60563; -.
DR eggNOG; ENOG502QTHX; Eukaryota.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0000795; C:synaptonemal complex; IEA:InterPro.
DR GO; GO:0003690; F:double-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR GO; GO:0007130; P:synaptonemal complex assembly; IEA:InterPro.
DR InterPro; IPR008827; SYCP1.
DR PANTHER; PTHR46918; PTHR46918; 1.
DR Pfam; PF05483; SCP-1; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Centromere; Chromosome; Coiled coil;
KW DNA-binding; Meiosis; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN <1..845
FT /note="Synaptonemal complex protein 1"
FT /id="PRO_0000072363"
FT REGION 550..644
FT /note="Required for pH-induced assembly of C-terminal ends
FT into antiparallel tetramers"
FT /evidence="ECO:0000250|UniProtKB:Q15431"
FT REGION 657..845
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q15431"
FT REGION 684..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 64..211
FT /evidence="ECO:0000255"
FT COILED 244..544
FT /evidence="ECO:0000255"
FT COILED 620..663
FT /evidence="ECO:0000255"
FT MOTIF 553..556
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 753..756
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 684..702
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 676
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62209"
FT NON_TER 1
SQ SEQUENCE 845 AA; 99401 MW; D7F28873C824C6A8 CRC64;
IVELQFEKEK VSLKLEEEIQ ENKDLIKENN ATRHLCNLLK ETSARSAEKT NKYEYEREET
RQVYVDLNNN IEKMILAFEE LRVQAENARL DMHFKLKEDH EKIQHLQEEY KKEVNDKENQ
VSLLLIQRTE KENKMKDLTF LLEESRDKVN QLEDKTKLQD ENVKELNKKK DHLTSELEDT
KMSLQRSMNT QKALEEDLQI ATKTIYQLTE EKEAQMEEFN KAKTDHSFMV TELKATTCTL
EELLRTEQQR LVKNEDQLKI LTMELQKKSN ELDEMTKFKN NNEVKLEELK KILAEDQKLL
DEKKQVEKLA EELQGKEQEL TLLLQTREKE VHDLEEQLLV TKISDQNYSK QVEELKTKLE
EEKLKNAELT ASCGKLSLEN NKLTQETNDM ALELKKYQED ITNSKKQEER MLKQIENLEE
KETHLRDELE SVRKEFIQQG NEVKCKLDKS EENARSIECE VLKKEKQMKI LENKCNNLRK
QAENKSKYIE ELHQENKALK KKSSAESKQL NAYEIKVNKL QLELESAKQK FQEMTDNYQK
EIEVKKISEE KLLGEVEKAK AMVDEAVKLQ KEIDLRCQHK IAEMVALMEK HKHQYDKIVE
ERDSELGLCK NREQEQLSVK TALETELSNI RNELVSLKKQ LEIEREEKEK LKLEKENTAI
LKDKKDKKIQ TSLLESAETT CQKFDSKTTP SQNISRISSS MESGKTKDNR DCLRTSAKIL
STAFVKEYTV KTPTKMQMYQ RENKYIPTGR SNKKRKTVFE FDVNSDSSET TDLLSMVSEE
EISNRLYNNN SPNSHLTPKQ TPLSLSTPES FVSLGGVRKM REDRWATIAK TDRKRRLKEA
EKLFA
