GCNA1_CAEEL
ID GCNA1_CAEEL Reviewed; 532 AA.
AC Q23462;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Germ cell nuclear acidic-1 protein {ECO:0000305};
DE AltName: Full=Germ cell nuclear acidic-1 peptidase {ECO:0000303|PubMed:31839537};
GN Name=gcna-1 {ECO:0000303|PubMed:27718356, ECO:0000312|WormBase:ZK328.4};
GN ORFNames=ZK328.4 {ECO:0000312|WormBase:ZK328.4};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
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 [3]
RP TISSUE SPECIFICITY, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30914427; DOI=10.15252/embj.2019101496;
RA Borgermann N., Ackermann L., Schwertman P., Hendriks I.A., Thijssen K.,
RA Liu J.C., Lans H., Nielsen M.L., Mailand N.;
RT "SUMOylation promotes protective responses to DNA-protein cross-links.";
RL EMBO J. 38:0-0(2019).
RN [4]
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).
RN [5]
RP DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP TOP-2.
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:30914427, PubMed:31839537,
CC PubMed:31839538). May resolve the topoisomerase II (top-2) DPCs
CC (PubMed:31839537, PubMed:31839538). Limits replication stress and DNA
CC double-strand breaks (PubMed:31839537). {ECO:0000269|PubMed:30914427,
CC ECO:0000269|PubMed:31839537, ECO:0000269|PubMed:31839538}.
CC -!- SUBUNIT: Interacts with top-2; this interaction allows the resolution
CC of topoisomerase II (top-2) DNA-protein cross-links.
CC {ECO:0000269|PubMed:31839538}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:31839538}.
CC Note=Localizes on condensed chromosomes in spermatocytes in G2 and M
CC during meiotic prophase (PubMed:31839538). Colocalizes with top-2 on
CC condensed chromosomes during embryonic cell divisions
CC (PubMed:31839538). {ECO:0000269|PubMed:31839538}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in germ cells and early embryonic,
CC proliferating cells. {ECO:0000269|PubMed:27718356,
CC ECO:0000269|PubMed:30914427}.
CC -!- DISRUPTION PHENOTYPE: Mutant worms become hypersensitive to
CC formaldehyde-induced DNA damage (PubMed:30914427). Mutant worms exhibit
CC significant reduction in brood size at 25 degrees Celsius and also
CC exhibit a high incidence of male progeny at both 20 and 25 degrees
CC Celsius (PubMed:27718356, PubMed:31839537). Moreover, exhibit a mortal
CC germline (MRT) phenotype characterized by transgenerational loss of
CC fecundity and vitality, marked by reduced lifespan, decreased mobility,
CC and loss of fertility in later generations (PubMed:31839537). Mutants
CC have a mortal germline, where brood sizes become progressively smaller
CC and the population fails to survive beyond 12 generations
CC (PubMed:31839538). {ECO:0000269|PubMed:27718356,
CC ECO:0000269|PubMed:30914427, ECO:0000269|PubMed:31839537,
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; BX284603; CCD70950.1; -; Genomic_DNA.
DR PIR; T29006; T29006.
DR RefSeq; NP_498307.1; NM_065906.4.
DR AlphaFoldDB; Q23462; -.
DR SMR; Q23462; -.
DR STRING; 6239.ZK328.4; -.
DR EPD; Q23462; -.
DR PaxDb; Q23462; -.
DR EnsemblMetazoa; ZK328.4.1; ZK328.4.1; WBGene00022694.
DR GeneID; 175850; -.
DR KEGG; cel:CELE_ZK328.4; -.
DR UCSC; ZK328.4; c. elegans.
DR CTD; 175850; -.
DR WormBase; ZK328.4; CE28182; WBGene00022694; gcna-1.
DR eggNOG; KOG3854; Eukaryota.
DR GeneTree; ENSGT00440000040163; -.
DR HOGENOM; CLU_512136_0_0_1; -.
DR InParanoid; Q23462; -.
DR OMA; PFIERCH; -.
DR OrthoDB; 1002399at2759; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00022694; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0000793; C:condensed chromosome; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016605; C:PML body; IDA:UniProtKB.
DR GO; GO:0032184; F:SUMO polymer binding; IDA:UniProtKB.
DR GO; GO:0045132; P:meiotic chromosome segregation; IMP:WormBase.
DR GO; GO:0106300; P:protein-DNA covalent cross-linking repair; IMP:UniProtKB.
DR InterPro; IPR006640; SprT-like_domain.
DR Pfam; PF10263; SprT-like; 1.
DR SMART; SM00731; SprT; 1.
PE 1: Evidence at protein level;
KW Chromosome; Reference proteome.
FT CHAIN 1..532
FT /note="Germ cell nuclear acidic-1 protein"
FT /id="PRO_0000454374"
FT DOMAIN 308..398
FT /note="SprT-like"
FT /evidence="ECO:0000255"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..237
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 532 AA; 61677 MW; 2CEB92007E096D40 CRC64;
MPTPFRDLHN KSNASASSYE TAWSSSFSSR RSTNNDSKSN LKEIKDEPIS NLDESISILE
NNISMMSVSS PTPAYRTPAR VIAREAPMTP GDRLLQKIEK EDERDMLRQL YPEMFDSNQK
PRQKPKEVKK ALKVESLSDY ENDDKENVPP CGKPSKEKEE KKQRTKKIVI SSDSEDDGNF
ENYLKTLREK PTEPAKPERK IPVKKDFVVD DDYISEESSE EESEEEEEDV DDEEYRESSP
EVEAKISYSD RKQKKRPTDE EEWFLLSLSE KFSGPIHEDA KVYIKETSLR YKKHRESLLT
RLQDILVRRI FSAIPSEKLK VIWNARLRKS AGQCRNHSNG NSTVEMSPVV CTTAERVRDT
LIHELCHAAT WVVDRLHKEG HGPGWKRWGA RCSSVFKSLP FIERCHSYEI EAKFFYVCEK
DGCDVEIKRQ SKSLDTSRKA CGRCFGRFIL YRYCRRTNTR IRIEDPKAKP VGPILSNSSK
PSPPAPRRIV SEHPEGFKEY SEEHYWKYTA QGLKHSDVMG KLLKEFKELK QL
