GCNA_DANRE
ID GCNA_DANRE Reviewed; 586 AA.
AC A0A0R4IWG9;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Germ cell nuclear acidic protein {ECO:0000250|UniProtKB:Q96QF7};
DE AltName: Full=Acidic repeat-containing protein {ECO:0000250|UniProtKB:Q96QF7};
DE AltName: Full=Germ cell nuclear acidic peptidase {ECO:0000303|PubMed:31839537};
GN Name=gcna {ECO:0000312|ZFIN:ZDB-GENE-050320-153};
GN Synonyms=acrc {ECO:0000312|ZFIN:ZDB-GENE-050320-153};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=31839537; DOI=10.1016/j.devcel.2019.11.007;
RA Bhargava V., Goldstein C.D., Russell L., Xu L., Ahmed M., Li W., Casey A.,
RA Servage K., Kollipara R., Picciarelli Z., Kittler R., Yatsenko A.,
RA Carmell M., Orth K., Amatruda J.F., Yanowitz J.L., Buszczak M.;
RT "GCNA Preserves Genome Integrity and Fertility Across Species.";
RL Dev. Cell 52:38-52(2020).
CC -!- FUNCTION: May play a role in DNA-protein cross-links (DPCs) clearance,
CC ensuring the genomic stability by protecting germ cells and early
CC embryos from various sources of damage. {ECO:0000269|PubMed:31839537}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96QF7}. Nucleus,
CC PML body {ECO:0000250|UniProtKB:Q96QF7}. Chromosome
CC {ECO:0000250|UniProtKB:A0A1D9BZF0}. 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 (By
CC similarity). {ECO:0000250|UniProtKB:A0A1D9BZF0,
CC ECO:0000250|UniProtKB:Q96QF7}.
CC -!- DISRUPTION PHENOTYPE: Progeny of mutant females display widespread
CC morphological defects and cell death and early embryos have
CC asynchronous mitotic divisions and tangled chromosomes.
CC {ECO:0000269|PubMed:31839537}.
CC -!- SIMILARITY: Belongs to the serine-aspartate repeat-containing protein
CC (SDr) family. {ECO:0000305}.
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DR EMBL; CR753843; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A0R4IWG9; -.
DR STRING; 7955.ENSDARP00000104895; -.
DR PaxDb; A0A0R4IWG9; -.
DR Ensembl; ENSDART00000169970; ENSDARP00000141634; ENSDARG00000101060.
DR ZFIN; ZDB-GENE-050320-153; gcna.
DR eggNOG; KOG3854; Eukaryota.
DR GeneTree; ENSGT00440000040163; -.
DR OrthoDB; 1562651at2759; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 14.
DR Bgee; ENSDARG00000101060; Expressed in mature ovarian follicle and 26 other tissues.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0106300; P:protein-DNA covalent cross-linking repair; IMP:UniProtKB.
DR InterPro; IPR006640; SprT-like_domain.
DR InterPro; IPR035240; SprT_Zn_ribbon.
DR Pfam; PF10263; SprT-like; 1.
DR Pfam; PF17283; Zn_ribbon_SprT; 1.
DR SMART; SM00731; SprT; 1.
PE 3: Inferred from homology;
KW Chromosome; Nucleus; Reference proteome.
FT CHAIN 1..586
FT /note="Germ cell nuclear acidic protein"
FT /id="PRO_0000454373"
FT DOMAIN 383..482
FT /note="SprT-like"
FT /evidence="ECO:0000255"
FT REGION 17..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 586 AA; 65421 MW; BC2F3F158ABB60AC CRC64;
MDPGTLSLFQ RVSTKLGWDR DGGLDDAEEK LRKSLKKTRR PALASSDSST GPAQRLELSD
SDNSSGKENR SQEEHILLTS DDEDFEKFLA SKATPKSTFK QSASSAQKPR EPVPVLSSES
DNEFELFLNR VKTPKAKVQP QSMSSSDESL KHFIVDSMSS DDDFVTEKKP SIYKGKAKTV
KTPKSVQKTK KPAPSLCNSP VFLSDSDDDC NIVIKSTWRT RHSRPPSDEH QATSKDREET
EKPRVPQPTI TVKSHTSRDD TCSSEEEFQS LLDRVRQNLG GRTSASPMPS AEPKPQRPCL
STPSATGRKT GSQVPVKDSP VIHTPVQQMP SSRPVLSHTE PRALPNSRVV VCKTPGCFLQ
SLSAPGSVYC RSFKQNKDEL TSKLYQLYNT SVFDSQLPVD MSVTWNNKMR KTAGYCISGQ
ERGTGKRYAR IELSVKVCDS ADRLRDTLIH EMCHAATWLI NNVRDGHGPF WRLYARKAML
AHPELPMVSR CHSYDINYKF QYQCNRCKNT IGRHSKSLDT TKFVCALCTG QLVLLTPSKP
RAPTPFATFV KENYGSTKQE LTGQSHAEIM RKLSADFASK TRLSQS
