ID   DAZL_CALJA              Reviewed;         296 AA.
AC   Q9BGN8;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Deleted in azoospermia-like;
DE   AltName: Full=DAZ-like autosomal;
DE   AltName: Full=Deleted in azoospermia-like 1;
GN   Name=DAZL; Synonyms=DAZL1, DAZLA;
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RA   Grossmann B., Saunders P.T.K., Edelmann A., Roos C.H., Weinbauer G.,
RA   Vogt P.H.;
RT   "Evolution of the germ line locus DAZL1 (Deleted in AZoospermia-Like 1 is
RT   different in Platyrrhini and Catarrhini.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   SUBCELLULAR LOCATION.
RX   PubMed=10819456;
RA   Ruggiu M., Saunders P.T.K., Cooke H.J.;
RT   "Dynamic subcellular distribution of the DAZL protein is confined to
RT   primate male germ cells.";
RL   J. Androl. 21:470-477(2000).
CC   -!- FUNCTION: RNA-binding protein, which is essential for gametogenesis in
CC       both males and females. Plays a central role during spermatogenesis.
CC       Acts by binding to the 3'-UTR of mRNA, specifically recognizing GUU
CC       triplets, and thereby regulating the translation of key transcripts (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer and heterodimer. Forms a heterodimer with DAZ.
CC       Interacts with BOLL, DAZAP1 and DAZAP2. Interacts with PUM2 Multiple
CC       DAZL RRMs can bind to a single RNA containing multiple GUU triplets (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10819456}. Nucleus
CC       {ECO:0000269|PubMed:10819456}. Note=Predominantly cytoplasmic. Nuclear
CC       in spermatogonia until near the end of the meiotic prophase and
CC       cytoplasmic localization from then onward.
CC   -!- TISSUE SPECIFICITY: Testis specific.
CC   -!- DOMAIN: The DAZ domain mediates the interaction with DAZAP1 and DAZAP2.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RRM DAZ family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01238}.
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DR   EMBL; AF144131; AAG50425.1; -; mRNA.
DR   RefSeq; NP_001171972.1; NM_001185043.1.
DR   AlphaFoldDB; Q9BGN8; -.
DR   SMR; Q9BGN8; -.
DR   STRING; 9483.ENSCJAP00000006526; -.
DR   Ensembl; ENSCJAT00000072147; ENSCJAP00000056614; ENSCJAG00000039120.
DR   GeneID; 100410648; -.
DR   KEGG; cjc:100410648; -.
DR   CTD; 1618; -.
DR   GeneTree; ENSGT00530000063480; -.
DR   InParanoid; Q9BGN8; -.
DR   OrthoDB; 1610446at2759; -.
DR   Proteomes; UP000008225; Chromosome 17.
DR   Bgee; ENSCJAG00000039120; Expressed in testis and 1 other tissue.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; IEA:InterPro.
DR   GO; GO:0008494; F:translation activator activity; IEA:InterPro.
DR   GO; GO:0007281; P:germ cell development; IEA:InterPro.
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; PF18872; Daz; 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   2: Evidence at transcript level;
KW   Cytoplasm; Developmental protein; Differentiation; Nucleus; Phosphoprotein;
KW   Reference proteome; RNA-binding; Spermatogenesis; Translation regulation.
FT   CHAIN           1..296
FT                   /note="Deleted in azoospermia-like"
FT                   /id="PRO_0000081558"
FT   DOMAIN          40..115
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          167..190
FT                   /note="DAZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01238"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          80..132
FT                   /note="Homodimerization"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         277
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q64368"
SQ   SEQUENCE   296 AA;  33209 MW;  F2C29A8795F145D2 CRC64;
     MSAANPETPN STISREANTQ SSSAATSQGY VLPEGKIMPN TVFVGGIDVR MDETEIRGFF
     ARYGSVKEVK IITDRTGVSK GYGFVSFFND VDVQKIVESQ INFHGKKLKL GPAIRKQNLC
     AYHVQPRPLV FNHPPPPQFQ NVWSNPNTET YMHPPTTMNP VTQYVQAYPP YPNSPVQVIT
     GYQLPVYNYQ MPPQWPVGEQ RSYVVPPAYS SVNYYCNEID PGAEVVPNEC SVCEATPPSG
     NGPQKKSVDR SIQTVVSCLF NPENSRLRNS VVTQDDYFRD KRVHHFRRSR AVLKSV