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GCNA_MOUSE
ID   GCNA_MOUSE              Reviewed;         507 AA.
AC   A0A1D9BZF0;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   18-JAN-2017, sequence version 1.
DT   03-AUG-2022, entry version 10.
DE   RecName: Full=Germ cell nuclear acidic protein {ECO:0000305};
DE   AltName: Full=Acidic repeat-containing protein {ECO:0000250|UniProtKB:Q96QF7};
DE   AltName: Full=Germ cell nuclear antigen {ECO:0000303|PubMed:27718356};
GN   Name=Gcna {ECO:0000312|MGI:MGI:105113};
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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=C57BL/6J;
RX   PubMed=27718356; DOI=10.7554/elife.19993;
RA   Carmell M.A., Dokshin G.A., Skaletsky H., Hu Y.C., van Wolfswinkel J.C.,
RA   Igarashi K.J., Bellott D.W., Nefedov M., Reddien P.W., Enders G.C.,
RA   Uversky V.N., Mello C.C., Page D.C.;
RT   "A widely employed germ cell marker is an ancient disordered protein with
RT   reproductive functions in diverse eukaryotes.";
RL   Elife 5:0-0(2016).
RN   [2]
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   [3]
RP   SUBCELLULAR LOCATION, INTERACTION WITH TOP2A, DISRUPTION PHENOTYPE, AND
RP   FUNCTION.
RX   PubMed=31839538; DOI=10.1016/j.devcel.2019.11.006;
RA   Dokshin G.A., Davis G.M., Sawle A.D., Eldridge M.D., Nicholls P.K.,
RA   Gourley T.E., Romer K.A., Molesworth L.W., Tatnell H.R., Ozturk A.R.,
RA   de Rooij D.G., Hannon G.J., Page D.C., Mello C.C., Carmell M.A.;
RT   "GCNA Interacts with Spartan and Topoisomerase II to Regulate Genome
RT   Stability.";
RL   Dev. Cell 52:53-68(2020).
CC   -!- FUNCTION: May play a role in DNA-protein cross-links (DPCs) clearance
CC       through a SUMO-dependent recruitment to sites of DPCs, ensuring the
CC       genomic stability by protecting germ cells and early embryos from
CC       various sources of damage (PubMed:31839538). Can resolve the
CC       topoisomerase II (TOP2A) DPCs (PubMed:31839538).
CC       {ECO:0000269|PubMed:31839538}.
CC   -!- SUBUNIT: Interacts (via SIM domains) with SUMO2; this interaction
CC       allows the GCNA recruitment to DPCs sites (By similarity). Interacts
CC       with TOP2A; this interaction allows the resolution of topoisomerase II
CC       (TOP2A) DNA-protein cross-links (PubMed:31839538).
CC       {ECO:0000250|UniProtKB:Q96QF7, ECO:0000269|PubMed:31839538}.
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:31839538}.
CC       Nucleus, PML body {ECO:0000269|PubMed:31839538}. Nucleus
CC       {ECO:0000269|PubMed:27718356}. Note=Co-localizes with SUMO2 at PML
CC       bodies in all interphase cells (By similarity). Localizes on condensed
CC       chromosomes in spermatocytes in G2 and M during meiotic prophase
CC       (PubMed:31839538). {ECO:0000250|UniProtKB:Q96QF7,
CC       ECO:0000269|PubMed:31839538}.
CC   -!- TISSUE SPECIFICITY: Germ-cells specific. {ECO:0000269|PubMed:27718356}.
CC   -!- DOMAIN: SUMO interaction motif 1 (SIM) mediates the binding to
CC       polysumoylated substrates. {ECO:0000250|UniProtKB:Q96QF7}.
CC   -!- DISRUPTION PHENOTYPE: Mutant male mice are sterile and spermatocytes
CC       exhibit DNA damage, crossover defects, and chromatin condensation
CC       abnormalities. {ECO:0000269|PubMed:27718356,
CC       ECO:0000269|PubMed:31839538}.
CC   -!- SIMILARITY: Belongs to the serine-aspartate repeat-containing protein
CC       (SDr) family. {ECO:0000305}.
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DR   EMBL; KX981576; AOY07794.1; -; mRNA.
DR   EMBL; AL805980; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   MGI; MGI:105113; Gcna.
DR   Proteomes; UP000000589; Unplaced.
DR   GO; GO:0000793; C:condensed chromosome; IDA:UniProtKB.
DR   GO; GO:0016605; C:PML body; IDA:UniProtKB.
DR   GO; GO:0106300; P:protein-DNA covalent cross-linking repair; IMP:UniProtKB.
PE   1: Evidence at protein level;
KW   Chromosome; Nucleus; Reference proteome.
FT   CHAIN           1..507
FT                   /note="Germ cell nuclear acidic protein"
FT                   /id="PRO_0000454372"
FT   REGION          1..507
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           12..15
FT                   /note="SUMO interaction motif 1 (SIM)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96QF7"
FT   MOTIF           66..69
FT                   /note="SUMO interaction motif 1 (SIM)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96QF7"
FT   MOTIF           86..89
FT                   /note="SUMO interaction motif 1 (SIM)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96QF7"
FT   MOTIF           108..111
FT                   /note="SUMO interaction motif 1 (SIM)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96QF7"
FT   COMPBIAS        1..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        109..136
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        175..358
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        388..413
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        414..446
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        478..507
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   507 AA;  53394 MW;  02F8C91C30C38E6C CRC64;
     MDSGSSSSSS SSGSSSGSCS TSGSGSTSGS STTSSSSSSS SSSSSSSSSS SKEYMPELPK
     QRKASCVVID SESDSDNTSD EKNTTVCEIS SGDETSDIDR PGGQKLPLIV IDDDDDGSPD
     LKNTKQKSDE PQMSVLEKEG VECIGSDSTS PHDVCEIWDV CGSSNQTSSE LEPEGEPESE
     AKGEPESEAK GEPESEAKGE PESEAKGESE SEAKGEMETE AKGESESEAK GEMETEAKGE
     SESEAKGEME TEAKGEPESE AKGEMETEAK GEPESEAKGE METEAKGESE SEAKGEMETE
     AKGESESEAK GEMETEAKGE PESEAKGEME TEAKGEPESE AKGEPEPEAA KGEMETEAAM
     GEVETEAAMG EPEQEITAEE AKKKRAAYLL AQQRKRKRKN RFICMSSSKP RRKRRRADPQ
     DGADPQDGAD PQDRADPQDL ADPQDRGDSQ DMPSLPGTSD EPIPSGQPVC PRKGMASSRG
     RGRGRGRGRG RGRGRGRGRG RGAKAGK
 
 
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