DAZLA_XENLA
ID DAZLA_XENLA Reviewed; 286 AA.
AC O57437;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Deleted in azoospermia-like-A;
DE Short=DAZ-like protein A;
DE Short=xDazl-A;
GN Name=dazl-a;
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:0000305, ECO:0000312|EMBL:AAC41242.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Oocyte {ECO:0000269|PubMed:9486791};
RX PubMed=9486791; DOI=10.1242/dev.125.2.171;
RA Houston D.W., Zhang J., Maines J.Z., Wasserman S.A., King M.L.;
RT "A Xenopus DAZ-like gene encodes an RNA component of germ plasm and is a
RT functional homologue of Drosophila boule.";
RL Development 125:171-180(1998).
RN [2] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=10631166; DOI=10.1242/dev.127.3.447;
RA Houston D.W., King M.L.;
RT "A critical role for Xdazl, a germ plasm-localized RNA, in the
RT differentiation of primordial germ cells in Xenopus.";
RL Development 127:447-456(2000).
RN [3] {ECO:0000305}
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=10842082; DOI=10.1016/s0925-4773(00)00295-1;
RA Mita K., Yamashita M.;
RT "Expression of Xenopus Daz-like protein during gametogenesis and
RT embryogenesis.";
RL Mech. Dev. 94:251-255(2000).
RN [4] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11784096; DOI=10.1006/dbio.2001.0488;
RA Kloc M., Dougherty M.T., Bilinski S., Chan A.P., Brey E., King M.L.,
RA Patrick C.W. Jr., Etkin L.D.;
RT "Three-dimensional ultrastructural analysis of RNA distribution within
RT germinal granules of Xenopus.";
RL Dev. Biol. 241:79-93(2002).
RN [5] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=15292452; DOI=10.1091/mbc.e04-03-0265;
RA Chang P., Torres J., Lewis R.A., Mowry K.L., Houliston E., King M.L.;
RT "Localization of RNAs to the mitochondrial cloud in Xenopus oocytes through
RT entrapment and association with endoplasmic reticulum.";
RL Mol. Biol. Cell 15:4669-4681(2004).
RN [6] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=16287483; DOI=10.1111/j.1440-169x.2005.00826.x;
RA Kataoka K., Tazaki A., Kitayama A., Ueno N., Watanabe K., Mochii M.;
RT "Identification of asymmetrically localized transcripts along the animal-
RT vegetal axis of the Xenopus egg.";
RL Dev. Growth Differ. 47:511-521(2005).
RN [7] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH PABP1 AND EPABP.
RX PubMed=16001084; DOI=10.1038/sj.emboj.7600738;
RA Collier B., Gorgoni B., Loveridge C., Cooke H.J., Gray N.K.;
RT "The DAZL family proteins are PABP-binding proteins that regulate
RT translation in germ cells.";
RL EMBO J. 24:2656-2666(2005).
RN [8] {ECO:0000305}
RP IDENTIFICATION IN A COMPLEX WITH SPDY1 MRNA; PUM2 AND EPABP.
RX PubMed=16418484; DOI=10.1101/gad.1383106;
RA Padmanabhan K., Richter J.D.;
RT "Regulated Pumilio-2 binding controls RINGO/Spy mRNA translation and CPEB
RT activation.";
RL Genes Dev. 20:199-209(2006).
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). {ECO:0000269|PubMed:10631166,
CC ECO:0000269|PubMed:16001084, ECO:0000269|PubMed:9486791}.
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.
CC {ECO:0000269|PubMed:16001084, ECO:0000269|PubMed:16418484}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10842082,
CC ECO:0000269|PubMed:11784096, ECO:0000269|PubMed:9486791}.
CC -!- TISSUE SPECIFICITY: Germ-line specific. Oocyte mRNA expression is first
CC restricted to the granulo-fibrillar material (GFM) of the mitochondrial
CC cloud and then to the oocyte germ plasm at the vegetal cortex. Remains
CC an mRNA component of the germ plasm until the neurula stage. In 2-8
CC cell embryos, expressed in the germ plasm matrix between germinal
CC granules and mitochondria. Expressed in primordial germ cells (PGCs)
CC later in embryogenesis. In addition to the ovaries of adult females,
CC expressed in the testis of adult and juvenile males in spermatogonia
CC and spermatocytes. The protein is restricted to the embryonic germ
CC plasm and primordial germ cells. {ECO:0000269|PubMed:10631166,
CC ECO:0000269|PubMed:10842082, ECO:0000269|PubMed:11784096,
CC ECO:0000269|PubMed:15292452, ECO:0000269|PubMed:16287483,
CC ECO:0000269|PubMed:9486791}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Transcripts are first detected in the gonads of postmetamorphic
CC froglets, being present in the embryo at the time when germ plasm moves
CC to its perinuclear location (stage 10) and then decreasing in stages
CC immediately following. Protein is expressed in embryos from the
CC blastula to the early tailbud stage. {ECO:0000269|PubMed:10631166,
CC ECO:0000269|PubMed:10842082}.
CC -!- SIMILARITY: Belongs to the RRM DAZ family. {ECO:0000255|PROSITE-
CC ProRule:PRU01238}.
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DR EMBL; AF017778; AAC41242.1; -; mRNA.
DR RefSeq; NP_001081772.1; NM_001088303.1.
DR AlphaFoldDB; O57437; -.
DR SMR; O57437; -.
DR GeneID; 398041; -.
DR KEGG; xla:398041; -.
DR CTD; 398041; -.
DR Xenbase; XB-GENE-6078612; dazl.L.
DR OrthoDB; 1610446at2759; -.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 398041; Expressed in testis and 9 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0032019; C:mitochondrial cloud; IDA:UniProtKB.
DR GO; GO:0045495; C:pole plasm; IDA:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0008494; F:translation activator activity; IDA:UniProtKB.
DR GO; GO:0007281; P:germ cell development; IMP:UniProtKB.
DR GO; GO:0008354; P:germ cell migration; IMP:UniProtKB.
DR GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
DR GO; GO:0045948; P:positive regulation of translational initiation; IDA: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 1: Evidence at protein 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-A"
FT /id="PRO_0000248849"
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; 32298 MW; C5BA0FA29D0FD65E CRC64;
MSGKEESSNY AATAEEEAVN QGFVLPEGEI MPNTVFVGGI DITMDEIEIR DFFTRFGNVK
EVKIITDRTG VSKGYGFISF SDEVDVQKIV KSQISFHGKK LKLGPAIRKI CTYVQPRPVV
LSHPTPFHHA WNNQNADSYI QHSPIVSPIT QYVQACPYPS SPPMAIQQIP VGCQQPGYFQ
VSPQWPADQR SYMFPTPAFT FNYHCCDMDP NGGEPIPREY PIDQTVSASG ANPQKRYVEM
STQTIVSCLF DPANKFHSFV SQEDYLKDNR VHHLRRRESV IKRVSK
