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SYCP3_MACFA
ID   SYCP3_MACFA             Reviewed;         236 AA.
AC   Q4R764;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Synaptonemal complex protein 3;
DE            Short=SCP-3;
GN   Name=SYCP3; ORFNames=QtsA-16181;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the synaptonemal complexes (SCS), formed between
CC       homologous chromosomes during meiotic prophase. Required for centromere
CC       pairing during meiosis in male germ cells. Required for normal meiosis
CC       during spermatogenesis and male fertility. Plays a lesser role in
CC       female fertility. Required for efficient phosphorylation of HORMAD1 and
CC       HORMAD2. {ECO:0000250|UniProtKB:P70281}.
CC   -!- SUBUNIT: Component of the lateral elements of synaptonemal complexes
CC       (By similarity). 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 (By similarity). 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 (By similarity).
CC       {ECO:0000250|UniProtKB:P70281, ECO:0000250|UniProtKB:Q8IZU3}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q60547}.
CC       Chromosome {ECO:0000250|UniProtKB:Q60547}. Chromosome, centromere
CC       {ECO:0000250|UniProtKB:Q60547}. 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. {ECO:0000250|UniProtKB:Q60547}.
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:0000250|UniProtKB:P70281}.
CC   -!- SIMILARITY: Belongs to the XLR/SYCP3 family. {ECO:0000305}.
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DR   EMBL; AB168961; BAE01059.1; -; mRNA.
DR   RefSeq; NP_001271503.1; NM_001284574.1.
DR   RefSeq; XP_005572078.1; XM_005572021.1.
DR   RefSeq; XP_005572079.1; XM_005572022.2.
DR   AlphaFoldDB; Q4R764; -.
DR   SMR; Q4R764; -.
DR   STRING; 9541.XP_005572077.1; -.
DR   Ensembl; ENSMFAT00000028666; ENSMFAP00000000497; ENSMFAG00000037508.
DR   GeneID; 102121878; -.
DR   KEGG; mcf:102121878; -.
DR   CTD; 50511; -.
DR   VEuPathDB; HostDB:ENSMFAG00000037508; -.
DR   eggNOG; ENOG502R883; Eukaryota.
DR   GeneTree; ENSGT00390000000062; -.
DR   OMA; TPVMDKH; -.
DR   OrthoDB; 1547468at2759; -.
DR   Proteomes; UP000233100; Chromosome 11.
DR   Bgee; ENSMFAG00000037508; Expressed in cerebellum and 13 other tissues.
DR   GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR   GO; GO:0000775; C:chromosome, centromeric region; ISS:UniProtKB.
DR   GO; GO:0000800; C:lateral element; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0035093; P:spermatogenesis, exchange of chromosomal proteins; IEA:Ensembl.
DR   InterPro; IPR006888; XLR/SYCP3/FAM9_dom.
DR   Pfam; PF04803; Cor1; 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..236
FT                   /note="Synaptonemal complex protein 3"
FT                   /id="PRO_0000229025"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          52..57
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IZU3"
FT   REGION          69..74
FT                   /note="Important for oligomerization and fiber formation"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IZU3"
FT   REGION          88..91
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IZU3"
FT   REGION          231..236
FT                   /note="Important for oligomerization and fiber formation"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IZU3"
FT   COILED          66..223
FT                   /evidence="ECO:0000255"
FT   MOTIF           88..91
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        11..42
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         36
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P70281"
FT   MOD_RES         38
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q63520"
FT   MOD_RES         59
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P70281"
SQ   SEQUENCE   236 AA;  27803 MW;  F804BE5F24AF0F10 CRC64;
     MVSSGKKYSR KSGKPSMEDQ FTRAYDFETE EKKDLSGSEE DVIEGKTAVI EKRRKKRSSA
     GVVEDMGGEV QNMLEGVGVD INKALLAKRK RLEMYTKASL KTSNQKIEHV WKTQQDQRQK
     LNQEYSQQFL TLFQQWDLDM QKAEEQEEKI LNMFRQQQKI LQQSRIVQSQ RLKTIRQLYE
     QFIKSMEELE KNHDNLLTGA QNEFKKEMAM LQKKIMMETQ QQEIASVRKS LQSMLF
 
 
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