ID   DAZP1_MOUSE             Reviewed;         406 AA.
AC   Q9JII5;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 2.
DT   27-MAR-2024, entry version 158.
DE   RecName: Full=DAZ-associated protein 1;
DE   AltName: Full=Deleted in azoospermia-associated protein 1;
GN   Name=Dazap1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Testis;
RX   PubMed=11604102; DOI=10.1186/1471-2164-2-6;
RA   Dai T., Vera Y., Salido E.C., Yen P.H.;
RT   "Characterization of the mouse Dazap1 gene encoding an RNA-binding protein
RT   that interacts with infertility factors DAZ and DAZL.";
RL   BMC Genomics 2:6-6(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   SUBCELLULAR LOCATION.
RX   PubMed=12185095;
RA   Vera Y., Dai T., Hikim A.P., Lue Y., Salido E.C., Swerdloff R.S., Yen P.H.;
RT   "Deleted in azoospermia associated protein 1 shuttles between nucleus and
RT   cytoplasm during normal germ cell maturation.";
RL   J. Androl. 23:622-628(2002).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-253, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryo;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
CC   -!- FUNCTION: RNA-binding protein, which may be required during
CC       spermatogenesis. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with DAZ and DAZL. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly
CC       cytoplasmic. Nuclear at some stages of spermatozoides development. In
CC       midpachytene spermatocytes, it is localized in both the cytoplasm and
CC       the nuclei and is clearly excluded from the sex vesicles. In round
CC       spermatids, it localizes mainly in the nuclei, whereas in elongated
CC       spermatids, it localizes to the cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9JII5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9JII5-2; Sequence=VSP_009443;
CC   -!- TISSUE SPECIFICITY: Mainly expressed in testis. Expressed at much lower
CC       level in liver, heart and brain. Also expressed in ovary. Expressed
CC       throughout testes development, in both the prenatal and postnatal
CC       periods. {ECO:0000269|PubMed:11604102}.
CC   -!- DEVELOPMENTAL STAGE: First expressed in midpachytene spermatocytes in
CC       stage VII tubules.
CC   -!- PTM: Acetylation at Lys-150 is predominantly observed in the nuclear
CC       fraction, and may regulate nucleocytoplasmic transport. {ECO:0000250}.
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DR   EMBL; AF225910; AAF81071.1; -; mRNA.
DR   EMBL; BC049355; AAH49355.1; -; mRNA.
DR   CCDS; CCDS35977.1; -. [Q9JII5-2]
DR   CCDS; CCDS48626.1; -. [Q9JII5-1]
DR   RefSeq; NP_001116076.1; NM_001122604.1. [Q9JII5-1]
DR   RefSeq; NP_001116077.1; NM_001122605.1.
DR   RefSeq; NP_573451.2; NM_133188.2. [Q9JII5-2]
DR   AlphaFoldDB; Q9JII5; -.
DR   SMR; Q9JII5; -.
DR   BioGRID; 213939; 17.
DR   STRING; 10090.ENSMUSP00000089958; -.
DR   iPTMnet; Q9JII5; -.
DR   PhosphoSitePlus; Q9JII5; -.
DR   SwissPalm; Q9JII5; -.
DR   REPRODUCTION-2DPAGE; Q9JII5; -.
DR   EPD; Q9JII5; -.
DR   jPOST; Q9JII5; -.
DR   MaxQB; Q9JII5; -.
DR   PaxDb; 10090-ENSMUSP00000089958; -.
DR   ProteomicsDB; 277951; -. [Q9JII5-1]
DR   ProteomicsDB; 277952; -. [Q9JII5-2]
DR   Pumba; Q9JII5; -.
DR   Antibodypedia; 1414; 225 antibodies from 26 providers.
DR   DNASU; 70248; -.
DR   Ensembl; ENSMUST00000092305.6; ENSMUSP00000089958.6; ENSMUSG00000069565.13. [Q9JII5-1]
DR   Ensembl; ENSMUST00000105362.8; ENSMUSP00000101001.2; ENSMUSG00000069565.13. [Q9JII5-2]
DR   GeneID; 70248; -.
DR   KEGG; mmu:70248; -.
DR   UCSC; uc007gcl.2; mouse. [Q9JII5-2]
DR   UCSC; uc007gcm.2; mouse. [Q9JII5-1]
DR   AGR; MGI:1917498; -.
DR   CTD; 26528; -.
DR   MGI; MGI:1917498; Dazap1.
DR   VEuPathDB; HostDB:ENSMUSG00000069565; -.
DR   eggNOG; KOG4205; Eukaryota.
DR   GeneTree; ENSGT00940000156757; -.
DR   HOGENOM; CLU_028569_1_0_1; -.
DR   InParanoid; Q9JII5; -.
DR   OMA; LRWAMGP; -.
DR   OrthoDB; 3127428at2759; -.
DR   BioGRID-ORCS; 70248; 10 hits in 80 CRISPR screens.
DR   ChiTaRS; Dazap1; mouse.
DR   PRO; PR:Q9JII5; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; Q9JII5; Protein.
DR   Bgee; ENSMUSG00000069565; Expressed in embryonic brain and 268 other cell types or tissues.
DR   ExpressionAtlas; Q9JII5; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:1990904; C:ribonucleoprotein complex; ISO:MGI.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR   GO; GO:0034046; F:poly(G) binding; ISO:MGI.
DR   GO; GO:0008266; F:poly(U) RNA binding; ISO:MGI.
DR   GO; GO:0003723; F:RNA binding; ISA:MGI.
DR   GO; GO:0035613; F:RNA stem-loop binding; IDA:MGI.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0048144; P:fibroblast proliferation; IMP:MGI.
DR   GO; GO:0001893; P:maternal placenta development; IMP:MGI.
DR   GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IMP:MGI.
DR   GO; GO:0007283; P:spermatogenesis; IMP:MGI.
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   PANTHER; PTHR48032:SF16; DAZ-ASSOCIATED PROTEIN 1; 1.
DR   PANTHER; PTHR48032; RNA-BINDING PROTEIN MUSASHI HOMOLOG RBP6; 1.
DR   Pfam; PF00076; RRM_1; 2.
DR   SMART; SM00360; RRM; 2.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 2.
DR   PROSITE; PS50102; RRM; 2.
DR   Genevisible; Q9JII5; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm; Developmental protein;
KW   Differentiation; Methylation; Nucleus; Reference proteome; Repeat;
KW   RNA-binding; Spermatogenesis.
FT   CHAIN           1..406
FT                   /note="DAZ-associated protein 1"
FT                   /id="PRO_0000081566"
FT   DOMAIN          10..97
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          113..190
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          74..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          186..406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        197..211
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        250..283
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        291..333
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        359..374
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96EP5"
FT   MOD_RES         150
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96EP5"
FT   MOD_RES         253
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   VAR_SEQ         102
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11604102"
FT                   /id="VSP_009443"
FT   CONFLICT        241
FT                   /note="Q -> R (in Ref. 1; AAF81071)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        358
FT                   /note="F -> L (in Ref. 1; AAF81071)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   406 AA;  43214 MW;  B0C71A7AED2F50D7 CRC64;
     MNSAGADEIG KLFVGGLDWS TTQETLRSYF SQYGEVVDCV IMKDKTTNQS RGFGFVKFKD
     PNCVGTVLAS RPHTLDGRNI DPKPCTPRGM QPERTRPKEG WQKGPRSDSS KSNKIFVGGI
     PHNCGETELR EYFKKFGVVT EVVMIYDAEK QRPRGFGFIT FEDEQSVDQA VNMHFHDIMG
     KKVEVKRAEP RDSKNQAPGQ PGASQWGSRV APSAANGWAG QPPPTWQQGY GPQGMWVPAG
     QAIGGYGPPP AGRGAPPPPP PFTSYIVSTP PGGFPPPQGF PQGYGAPPQF SFGYGPPPPP
     PDQFAPPGVP PPPATPGAAP LAFPPPPSQA APDMSKPPTA QPDFPYGQYG YGQDLSGFGQ
     GFSDPSQQPP SYGGPSVPGS GGPPAGGSGF GRGQNHNVQG FHPYRR
//