ID   DAZLB_XENLA             Reviewed;         286 AA.
AC   Q4V7Y4; Q6IR77;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 2.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Deleted in azoospermia-like-B;
DE            Short=DAZ-like protein B;
DE            Short=xDazl-B;
GN   Name=dazl-b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1] {ECO:0000312|EMBL:AAH97658.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney {ECO:0000312|EMBL:AAH71023.1}, and
RC   Ovary {ECO:0000312|EMBL:AAH97658.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: RNA-binding protein that is required for primordial germ cell
CC       (PGC) differentiation and indirectly necessary for the migration of
CC       PGCs through the endoderm. May promote meiotic cell division during
CC       spermatogenesis. Shows a preference for G- and U-rich RNAs and probably
CC       binds the 3'-UTR of target mRNAs. Stimulates the initiation of
CC       translation of mRNAs through the recruitment of poly(A)-binding
CC       proteins (PABPs) (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with the C-terminus of pabp1 and with epabp. Prior
CC       to oocyte maturation, found in a complex with epabp and pum2 proteins
CC       and spdy1 mRNA; pum2 dissociates from the complex during maturation (By
CC       similarity). {ECO:0000250|UniProtKB:O57437}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O57437}.
CC   -!- SIMILARITY: Belongs to the RRM DAZ family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01238}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH71023.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAH97658.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC071023; AAH71023.1; ALT_INIT; mRNA.
DR   EMBL; BC097658; AAH97658.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; Q4V7Y4; -.
DR   SMR; Q4V7Y4; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0032019; C:mitochondrial cloud; ISS:UniProtKB.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR   GO; GO:0008494; F:translation activator activity; ISS:UniProtKB.
DR   GO; GO:0007281; P:germ cell development; ISS:UniProtKB.
DR   GO; GO:0008354; P:germ cell migration; ISS:UniProtKB.
DR   GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0045948; P:positive regulation of translational initiation; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Cytoplasm; Developmental protein; Differentiation; Oogenesis;
KW   Reference proteome; RNA-binding; Spermatogenesis; Translation regulation.
FT   CHAIN           1..286
FT                   /note="Deleted in azoospermia-like-B"
FT                   /id="PRO_0000248850"
FT   DOMAIN          33..114
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          155..180
FT                   /note="DAZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01238"
SQ   SEQUENCE   286 AA;  32311 MW;  27BF52DB2F0D3346 CRC64;
     MSGKEESSNY AATAEEEAVN QGFVLPEGKI MPNTVFVGGI DITMDEIEIR DFFTRFGNVK
     EVKIITDRTG VSKGYGFISF SDEVDIQKIV KSQISFHGKK LKLGPAIRKI CTYVQPRPVV
     LSHPTPFHHA WNNQNADSYI QHSPIVSPIT QYVQACPYPS SPPMAIQQIP VGCQQPGYFQ
     VSPQWPADQR SYMFPTPAFT FNYHCCDMDP NGGEPIPREY PIDQTVSASG ANPQKRYVEM
     STQTIVSCLF DPANKFHSFV SQEDYLKDNR VHHLRRRESV IKRVSK