ID   DAZP1_XENLA             Reviewed;         360 AA.
AC   Q98SJ2;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=DAZ-associated protein 1;
DE   AltName: Full=Deleted in azoospermia-associated protein 1;
DE   AltName: Full=Proline-rich Vg1 mRNA-binding protein;
GN   Name=dazap1; Synonyms=prrp;
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]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION,
RP   TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INTERACTION WITH PROFILIN.
RC   TISSUE=Ovary;
RX   PubMed=11331596; DOI=10.1093/emboj/20.9.2315;
RA   Zhao W.-M., Jiang C., Kroll T.T., Huber P.W.;
RT   "A proline-rich protein binds to the localization element of Xenopus Vg1
RT   mRNA and to ligands involved in actin polymerization.";
RL   EMBO J. 20:2315-2325(2001).
RN   [2]
RP   INTERACTION WITH VGRBP71.
RX   PubMed=12421702; DOI=10.1242/dev.00160;
RA   Kroll T.T., Zhao W.-M., Jiang C., Huber P.W.;
RT   "A homolog of FBP2/KSRP binds to localized mRNAs in Xenopus oocytes.";
RL   Development 129:5609-5619(2002).
RN   [3]
RP   IDENTIFICATION IN A MRNP COMPLEX WITH IGF2BP3-A; STAU AND VGRBP60.
RX   PubMed=15096527; DOI=10.1083/jcb.200309145;
RA   Kress T.L., Yoon Y.J., Mowry K.L.;
RT   "Nuclear RNP complex assembly initiates cytoplasmic RNA localization.";
RL   J. Cell Biol. 165:203-211(2004).
CC   -!- FUNCTION: RNA-binding protein, which is required during gametogenesis.
CC       May be involved in the actin-dependent anchoring of Vg1 mRNA in the
CC       vegetal cortex of the oocyte. {ECO:0000269|PubMed:11331596}.
CC   -!- SUBUNIT: Component of a mRNP complex, at least composed of DAZAP1,
CC       IGF2BP3-A, STAU and VgRBP60. Binds to the 3'-UTR of Vg1 mRNA. Interacts
CC       with profilin, a protein involved in actin assembly. Interacts with
CC       VgRBP71. {ECO:0000269|PubMed:11331596, ECO:0000269|PubMed:12421702,
CC       ECO:0000269|PubMed:15096527}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11331596}.
CC       Note=Concentrated in the vegetal cortex of stage III/IV oocytes.
CC   -!- TISSUE SPECIFICITY: Expressed in oocytes.
CC       {ECO:0000269|PubMed:11331596}.
CC   -!- DEVELOPMENTAL STAGE: Expressed gradually during oogenesis. First
CC       expressed in stage I-II oocytes at a low level. Strongly expressed
CC       during stage III-IV, and thereafter for the remainder of oogenesis.
CC       {ECO:0000269|PubMed:11331596}.
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DR   EMBL; AY028920; AAK26172.1; -; mRNA.
DR   RefSeq; NP_001082088.1; NM_001088619.1.
DR   AlphaFoldDB; Q98SJ2; -.
DR   SMR; Q98SJ2; -.
DR   DNASU; 398218; -.
DR   GeneID; 398218; -.
DR   KEGG; xla:398218; -.
DR   CTD; 398218; -.
DR   Xenbase; XB-GENE-864805; dazap1.S.
DR   OrthoDB; 1565323at2759; -.
DR   Proteomes; UP000186698; Chromosome 1S.
DR   Bgee; 398218; Expressed in neurula embryo and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IDA:MGI.
DR   GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
DR   CDD; cd12574; RRM1_DAZAP1; 1.
DR   CDD; cd12327; RRM2_DAZAP1; 1.
DR   Gene3D; 3.30.70.330; -; 2.
DR   InterPro; IPR034134; DAZAP1_RRM1.
DR   InterPro; IPR034131; DAZAP1_RRM2.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   Pfam; PF00076; RRM_1; 2.
DR   SMART; SM00360; RRM; 2.
DR   SUPFAM; SSF54928; SSF54928; 2.
DR   PROSITE; PS50102; RRM; 2.
PE   1: Evidence at protein level;
KW   Cytoplasm; Developmental protein; Differentiation; Oogenesis;
KW   Reference proteome; Repeat; RNA-binding.
FT   CHAIN           1..360
FT                   /note="DAZ-associated protein 1"
FT                   /id="PRO_0000081567"
FT   DOMAIN          10..97
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          114..191
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          73..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          184..345
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..111
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        197..238
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..331
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   360 AA;  39229 MW;  E12F31961CBADAF6 CRC64;
     MNNQGGDEIG KLFVGGLDWS TTQETLRSYF SQYGEVVDCV IMKDKTTNQS RGFGFVKFKD
     PNCVGTVLAS RPHTLDGRNI DPKPCTPRGM QPERSRPREG WQQKEPRTEN SRSNKIFVGG
     IPHNCGETEL KEYFNRFGVV TEVVMIYDAE KQRPRGFGFI TFEDEQSVDQ AVNMHFHDIM
     GKKVEVKRAE PRDSKSQTPG PPGSNQWGSR AMQSTANGWT GQPPQTWQGY SPQGMWMPTG
     QTIGGYGQPA GRGGPPPPPS FAPFLVSTTP GPFPPPQGFP PGYATPPPFG YGYGPPPPPP
     DQFVSSGVPP PPGTPGAAPL AFPPPPGQSA QDLSKPPSGQ QDFPFSQFGN ACFVKLSEWI