DAZP1_MOUSE
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 03-AUG-2022, entry version 149.
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, Spleen,
RC 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; 16.
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; Q9JII5; -.
DR PRIDE; Q9JII5; -.
DR ProteomicsDB; 277951; -. [Q9JII5-1]
DR ProteomicsDB; 277952; -. [Q9JII5-2]
DR Antibodypedia; 1414; 198 antibodies from 26 providers.
DR DNASU; 70248; -.
DR Ensembl; ENSMUST00000092305; ENSMUSP00000089958; ENSMUSG00000069565. [Q9JII5-1]
DR Ensembl; ENSMUST00000105362; ENSMUSP00000101001; ENSMUSG00000069565. [Q9JII5-2]
DR GeneID; 70248; -.
DR KEGG; mmu:70248; -.
DR UCSC; uc007gcl.2; mouse. [Q9JII5-2]
DR UCSC; uc007gcm.2; mouse. [Q9JII5-1]
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; NWNSWNM; -.
DR OrthoDB; 1565323at2759; -.
DR BioGRID-ORCS; 70248; 10 hits in 75 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 265 other tissues.
DR ExpressionAtlas; Q9JII5; baseline and differential.
DR Genevisible; Q9JII5; MM.
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:0003729; F:mRNA 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 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 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
