DAZL_DANRE
ID DAZL_DANRE Reviewed; 229 AA.
AC Q9YGW7;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Deleted in azoospermia-like;
DE Short=DAZ-like protein;
DE Short=zDazl;
GN Name=dazl; Synonyms=zdazl;
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 [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10330505; DOI=10.1016/s0925-4773(98)00242-1;
RA Maegawa S., Yasuda K., Inoue K.;
RT "Maternal mRNA localization of zebrafish DAZ-like gene.";
RL Mech. Dev. 81:223-226(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, DOMAIN, AND MUTAGENESIS OF PHE-91.
RX PubMed=12296827; DOI=10.1046/j.1365-2443.2002.00576.x;
RA Maegawa S., Yamashita M., Yasuda K., Inoue K.;
RT "Zebrafish DAZ-like protein controls translation via the sequence 'GUUC'.";
RL Genes Cells 7:971-984(2002).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18582455; DOI=10.1016/j.ydbio.2008.05.557;
RA Marlow F.L., Mullins M.C.;
RT "Bucky ball functions in Balbiani body assembly and animal-vegetal polarity
RT in the oocyte and follicle cell layer in zebrafish.";
RL Dev. Biol. 321:40-50(2008).
RN [5]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=24496621; DOI=10.1242/dev.090449;
RA Heim A.E., Hartung O., Rothhaemel S., Ferreira E., Jenny A., Marlow F.L.;
RT "Oocyte polarity requires a Bucky ball-dependent feedback amplification
RT loop.";
RL Development 141:842-854(2014).
CC -!- FUNCTION: RNA-binding protein involved in gametogenesis in both males
CC and females (PubMed:12296827). Acts by binding to the 3'-UTR of mRNA,
CC specifically recognizing GUU triplets, and promoting the translation of
CC key transcripts (PubMed:12296827). Establishes oocyte polarity through
CC interaction with Bucky ball (BUC) (Probable). Interacts with Bucky ball
CC (BUC) mRNA to mediate Balbiani body formation and oocyte polarity
CC during early oogenesis (By similarity). {ECO:0000250|UniProtKB:Q92904,
CC ECO:0000269|PubMed:12296827, ECO:0000305|PubMed:24496621}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10330505}.
CC -!- TISSUE SPECIFICITY: Testis and ovary specific. In ovary, it is
CC localized in the cortex of oocytes (PubMed:10330505). At the onset of
CC embryogenesis, maternal product is located at the vegetal pole, before
CC migrating toward blastomeres through cytoplasmic streams as early
CC embryogenesis proceededs (PubMed:10330505).
CC {ECO:0000269|PubMed:10330505}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Transcripts localizes to the Balbiani body during oogenesis
CC (PubMed:18582455). {ECO:0000269|PubMed:18582455}.
CC -!- DOMAIN: The DAZ domain is essential for the translation activation
CC activity. {ECO:0000269|PubMed:12296827}.
CC -!- SIMILARITY: Belongs to the RRM DAZ family. {ECO:0000255|PROSITE-
CC ProRule:PRU01238}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB018191; BAA75800.1; -; mRNA.
DR EMBL; BC076423; AAH76423.1; -; mRNA.
DR RefSeq; NP_571599.1; NM_131524.1.
DR AlphaFoldDB; Q9YGW7; -.
DR SMR; Q9YGW7; -.
DR STRING; 7955.ENSDARP00000113712; -.
DR PaxDb; Q9YGW7; -.
DR GeneID; 58039; -.
DR KEGG; dre:58039; -.
DR CTD; 1618; -.
DR ZFIN; ZDB-GENE-000405-6; dazl.
DR eggNOG; KOG0118; Eukaryota.
DR InParanoid; Q9YGW7; -.
DR OrthoDB; 1610446at2759; -.
DR PhylomeDB; Q9YGW7; -.
DR PRO; PR:Q9YGW7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:ZFIN.
DR GO; GO:0003729; F:mRNA binding; IDA:ZFIN.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IMP:ZFIN.
DR GO; GO:0008494; F:translation activator activity; IDA:UniProtKB.
DR GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; IDA:ZFIN.
DR GO; GO:0060965; P:negative regulation of miRNA-mediated gene silencing; IDA:ZFIN.
DR GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:ZFIN.
DR GO; GO:0045948; P:positive regulation of translational initiation; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR CDD; cd12672; RRM_DAZL; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR037366; BOULE/DAZ.
DR InterPro; IPR043628; DAZ_dom.
DR InterPro; IPR037551; DAZ_RRM_vert.
DR InterPro; IPR034779; DAZL.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR11176; PTHR11176; 1.
DR PANTHER; PTHR11176:SF4; PTHR11176:SF4; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS51890; DAZ; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Activator; Cytoplasm; Developmental protein; Differentiation; Oogenesis;
KW Reference proteome; RNA-binding; Spermatogenesis; Translation regulation.
FT CHAIN 1..229
FT /note="Deleted in azoospermia-like"
FT /id="PRO_0000081562"
FT DOMAIN 47..128
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 172..198
FT /note="DAZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01238"
FT MUTAGEN 91
FT /note="F->A: Abolishes the RNA-binding activity."
FT /evidence="ECO:0000269|PubMed:12296827"
SQ SEQUENCE 229 AA; 25548 MW; B38C72218F009654 CRC64;
MVQGVQLPVC LICGLYSQDI QKHRQGFPSS LKLSNGYILP EGKMTPNTLF VGGIDMKVDE
NEIREFFAKY GSVKEVKIIT YRGGICKGYG FVYFSEDVDI QTIVDQPISF KGKKLKLGPA
IMKERSSRSV SSPMIGPSQW VNPTPYMYCS CCPPGLAPPS PVFSGGNQYM QPYSYSSPPG
IMVPQVPMNY AQTTYAYQYP LPQWCGEQRT RLVNQNFVDC GVQTLLTLM