DAZL_MOUSE
ID DAZL_MOUSE Reviewed; 298 AA.
AC Q64368;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Deleted in azoospermia-like;
DE AltName: Full=DAZ-like autosomal;
DE AltName: Full=Deleted in azoospermia-like 1;
GN Name=Dazl; Synonyms=Dazl1, Dazla;
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].
RC STRAIN=CD-1; TISSUE=Testis;
RX PubMed=8679003; DOI=10.1007/s003359900292;
RA Maiwald R., Luche R.M., Epstein C.J.;
RT "Isolation of a mouse homolog of the human DAZ (Deleted in Azoospermia)
RT gene.";
RL Mamm. Genome 7:628-628(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=8845845; DOI=10.1093/hmg/5.4.513;
RA Cooke H.J., Lee M., Kerr S., Ruggiu M.;
RT "A murine homologue of the human DAZ gene is autosomal and expressed only
RT in male and female gonads.";
RL Hum. Mol. Genet. 5:513-516(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=8661148; DOI=10.1006/geno.1996.0366;
RA Reijo R.A., Seligman J., Dinulos M.B., Jaffe T., Brown L.G., Disteche C.M.,
RA Page D.C.;
RT "Mouse autosomal homolog of DAZ, a candidate male sterility gene in humans,
RT is expressed in male germ cells before and after puberty.";
RL Genomics 35:346-352(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9288969; DOI=10.1038/37987;
RA Ruggiu M., Speed R., Taggart M., McKay S.J., Kilanowski F.,
RA Saunders P.T.K., Dorin J., Cooke H.J.;
RT "The mouse Dazla gene encodes a cytoplasmic protein essential for
RT gametogenesis.";
RL Nature 389:73-77(1997).
RN [6]
RP HOMODIMERIZATION, AND INTERACTION WITH DAZ.
RX PubMed=10903443; DOI=10.1016/s0378-1119(00)00219-5;
RA Ruggiu M., Cooke H.J.;
RT "In vivo and in vitro analysis of homodimerisation activity of the mouse
RT Dazl1 protein.";
RL Gene 252:119-126(2000).
RN [7]
RP RNA-BINDING, AND MUTAGENESIS OF PHE-43; TYR-82; PHE-84 AND PHE-87.
RX PubMed=11410654; DOI=10.1093/nar/29.12.2479;
RA Venables J.P., Ruggiu M., Cooke H.J.;
RT "The RNA-binding specificity of the mouse Dazl protein.";
RL Nucleic Acids Res. 29:2479-2483(2001).
RN [8]
RP PHOSPHORYLATION AT TYR-276.
RX PubMed=15378723; DOI=10.1002/rcm.1604;
RA Jin W.-H., Dai J., Zhou H., Xia Q.-C., Zou H.-F., Zeng R.;
RT "Phosphoproteome analysis of mouse liver using immobilized metal affinity
RT purification and linear ion trap mass spectrometry.";
RL Rapid Commun. Mass Spectrom. 18:2169-2176(2004).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [10]
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 32-132 ALONE AND IN COMPLEX WITH
RP RNA, FUNCTION, AND SUBUNIT.
RX PubMed=22021443; DOI=10.1073/pnas.1105211108;
RA Jenkins H.T., Malkova B., Edwards T.A.;
RT "Kinked beta-strands mediate high-affinity recognition of mRNA targets by
RT the germ-cell regulator DAZL.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:18266-18271(2011).
CC -!- FUNCTION: RNA-binding protein, which is essential for gametogenesis in
CC both males and females. Plays a central role during spermatogenesis.
CC Acts by binding to the 3'-UTR of mRNA, specifically recognizing GUU
CC triplets, and thereby regulating the translation of key transcripts.
CC {ECO:0000269|PubMed:22021443, ECO:0000269|PubMed:9288969}.
CC -!- SUBUNIT: Homodimer and heterodimer. Forms a heterodimer with DAZ.
CC Interacts with BOLL, DAZAP1 and DAZAP2. Interacts with PUM2 (By
CC similarity). Multiple DAZL RRMs can bind to a single RNA containing
CC multiple GUU triplets. {ECO:0000250, ECO:0000269|PubMed:10903443,
CC ECO:0000269|PubMed:22021443}.
CC -!- INTERACTION:
CC Q64368; Q64368: Dazl; NbExp=2; IntAct=EBI-2024439, EBI-2024439;
CC Q64368; O88485: Dync1i1; NbExp=4; IntAct=EBI-2024439, EBI-492834;
CC Q64368; P63168: Dynll1; NbExp=12; IntAct=EBI-2024439, EBI-349121;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9288969}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in testis with lower levels
CC in ovary. In testis, it is expressed in pachytene spermatocytes and at
CC lower level in type-B spermatogonia, preleptotene and zygotene
CC spermatocytes. In ovary, it is expressed in maturing follicles. In
CC embryonic and prepuberal ovary, it is expressed in the oocyte and
CC follicular cells. {ECO:0000269|PubMed:9288969}.
CC -!- DEVELOPMENTAL STAGE: In the testis, expression increases steadily after
CC birth until the first spermatogonial cells appear, levels off as the
CC first spermatogenic cells enter meiosis (10 days after birth) and
CC remains at this level thereafter.
CC -!- DOMAIN: The DAZ domain mediates the interaction with DAZAP1 and DAZAP2.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RRM DAZ family. {ECO:0000255|PROSITE-
CC ProRule:PRU01238}.
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DR EMBL; X95724; CAA65039.1; -; mRNA.
DR EMBL; U38690; AAB46608.1; -; mRNA.
DR EMBL; U46694; AAC52711.1; -; mRNA.
DR EMBL; AK014854; BAB29585.1; -; mRNA.
DR EMBL; AK033183; BAC28187.1; -; mRNA.
DR CCDS; CCDS37649.1; -.
DR RefSeq; NP_001264792.1; NM_001277863.1.
DR RefSeq; NP_034151.3; NM_010021.5.
DR PDB; 2XS2; X-ray; 1.35 A; A=32-132.
DR PDB; 2XS5; X-ray; 1.60 A; A/B=32-117.
DR PDB; 2XS7; X-ray; 1.45 A; A=32-117.
DR PDB; 2XSF; X-ray; 1.70 A; A=35-118.
DR PDBsum; 2XS2; -.
DR PDBsum; 2XS5; -.
DR PDBsum; 2XS7; -.
DR PDBsum; 2XSF; -.
DR AlphaFoldDB; Q64368; -.
DR SMR; Q64368; -.
DR IntAct; Q64368; 6.
DR MINT; Q64368; -.
DR STRING; 10090.ENSMUSP00000010736; -.
DR iPTMnet; Q64368; -.
DR PhosphoSitePlus; Q64368; -.
DR PaxDb; Q64368; -.
DR PRIDE; Q64368; -.
DR ProteomicsDB; 277946; -.
DR DNASU; 13164; -.
DR Ensembl; ENSMUST00000010736; ENSMUSP00000010736; ENSMUSG00000010592.
DR GeneID; 13164; -.
DR KEGG; mmu:13164; -.
DR UCSC; uc008cyu.3; mouse.
DR CTD; 1618; -.
DR MGI; MGI:1342328; Dazl.
DR VEuPathDB; HostDB:ENSMUSG00000010592; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00530000063480; -.
DR HOGENOM; CLU_084802_0_0_1; -.
DR InParanoid; Q64368; -.
DR OMA; QSECSVH; -.
DR OrthoDB; 1610446at2759; -.
DR PhylomeDB; Q64368; -.
DR TreeFam; TF324396; -.
DR BioGRID-ORCS; 13164; 3 hits in 74 CRISPR screens.
DR EvolutionaryTrace; Q64368; -.
DR PRO; PR:Q64368; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q64368; protein.
DR Bgee; ENSMUSG00000010592; Expressed in spermatocyte and 54 other tissues.
DR ExpressionAtlas; Q64368; baseline and differential.
DR Genevisible; Q64368; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005844; C:polysome; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:MGI.
DR GO; GO:0008494; F:translation activator activity; IDA:UniProtKB.
DR GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; IBA:GO_Central.
DR GO; GO:0007147; P:female meiosis II; IMP:MGI.
DR GO; GO:0007281; P:germ cell development; IMP:MGI.
DR GO; GO:0001556; P:oocyte maturation; IMP:MGI.
DR GO; GO:0045836; P:positive regulation of meiotic nuclear division; IMP:MGI.
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; PF18872; Daz; 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 3D-structure; Cytoplasm; Developmental protein; Differentiation; Oogenesis;
KW Phosphoprotein; Reference proteome; RNA-binding; Spermatogenesis;
KW Translation regulation.
FT CHAIN 1..298
FT /note="Deleted in azoospermia-like"
FT /id="PRO_0000081561"
FT DOMAIN 40..115
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 167..190
FT /note="DAZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01238"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..132
FT /note="Homodimerization"
FT MOD_RES 276
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:15378723"
FT MUTAGEN 43
FT /note="F->D: Abolishes RNA-binding but not
FT homodimerization; when associated with D-82; D-84 and D-
FT 87."
FT /evidence="ECO:0000269|PubMed:11410654"
FT MUTAGEN 82
FT /note="Y->D: Abolishes RNA-binding but not
FT homodimerization; when associated with D-43; D-84 and D-
FT 87."
FT /evidence="ECO:0000269|PubMed:11410654"
FT MUTAGEN 84
FT /note="F->D: Abolishes RNA-binding but not
FT homodimerization; when associated with D-43; D-82 and D-
FT 87."
FT /evidence="ECO:0000269|PubMed:11410654"
FT MUTAGEN 87
FT /note="F->D: Abolishes RNA-binding but not
FT homodimerization; when associated with D-43; D-82 and D-
FT 84."
FT /evidence="ECO:0000269|PubMed:11410654"
FT STRAND 36..45
FT /evidence="ECO:0007829|PDB:2XS2"
FT HELIX 53..60
FT /evidence="ECO:0007829|PDB:2XS2"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:2XS2"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:2XS2"
FT STRAND 79..89
FT /evidence="ECO:0007829|PDB:2XS2"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:2XS2"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:2XS7"
FT STRAND 109..115
FT /evidence="ECO:0007829|PDB:2XS2"
SQ SEQUENCE 298 AA; 33313 MW; FBF457BC388DB974 CRC64;
MSATTSEAPN SAVSREASTQ SSSATTSQGY VLPEGKIMPN TVFVGGIDVR MDETEIRSFF
ARYGSVKEVK IITDRTGVSK GYGFVSFYND VDVQKIVESQ INFHGKKLKL GPAIRKQNLC
TYHVQPRPLI FNPPPPPQFQ SVWSSPNAET YMQPPTMMNP ITQYVQAYPP YPSSPVQVIT
GYQLPVYNYQ MPPQWPAGEQ RSYVIPPAYT TVNYHCSEVD PGADILPNEC SVHDAAPASG
NGPQKKSVDR SIQTVVSCLF NPENRLRNSL VTQDDYFKDK RVHHFRRSRA VLKSDHLC
