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Deleted in azoospermia-like (DAZ-like autosomal) (Deleted in azoospermia-like 1)

 DAZL_MOUSE              Reviewed;         298 AA.
Q64368;
17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 146.
RecName: Full=Deleted in azoospermia-like;
AltName: Full=DAZ-like autosomal;
AltName: Full=Deleted in azoospermia-like 1;
Name=Dazl; Synonyms=Dazl1, Dazla;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=CD-1; TISSUE=Testis;
PubMed=8679003; DOI=10.1007/s003359900292;
Maiwald R., Luche R.M., Epstein C.J.;
"Isolation of a mouse homolog of the human DAZ (Deleted in
Azoospermia) gene.";
Mamm. Genome 7:628-628(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Testis;
PubMed=8845845; DOI=10.1093/hmg/5.4.513;
Cooke H.J., Lee M., Kerr S., Ruggiu M.;
"A murine homologue of the human DAZ gene is autosomal and expressed
only in male and female gonads.";
Hum. Mol. Genet. 5:513-516(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ; TISSUE=Testis;
PubMed=8661148; DOI=10.1006/geno.1996.0366;
Reijo R.A., Seligman J., Dinulos M.B., Jaffe T., Brown L.G.,
Disteche C.M., Page D.C.;
"Mouse autosomal homolog of DAZ, a candidate male sterility gene in
humans, is expressed in male germ cells before and after puberty.";
Genomics 35:346-352(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=9288969; DOI=10.1038/37987;
Ruggiu M., Speed R., Taggart M., McKay S.J., Kilanowski F.,
Saunders P.T.K., Dorin J., Cooke H.J.;
"The mouse Dazla gene encodes a cytoplasmic protein essential for
gametogenesis.";
Nature 389:73-77(1997).
[6]
HOMODIMERIZATION, AND INTERACTION WITH DAZ.
PubMed=10903443; DOI=10.1016/S0378-1119(00)00219-5;
Ruggiu M., Cooke H.J.;
"In vivo and in vitro analysis of homodimerisation activity of the
mouse Dazl1 protein.";
Gene 252:119-126(2000).
[7]
RNA-BINDING, AND MUTAGENESIS OF PHE-43; TYR-82; PHE-84 AND PHE-87.
PubMed=11410654; DOI=10.1093/nar/29.12.2479;
Venables J.P., Ruggiu M., Cooke H.J.;
"The RNA-binding specificity of the mouse Dazl protein.";
Nucleic Acids Res. 29:2479-2483(2001).
[8]
PHOSPHORYLATION AT TYR-276.
PubMed=15378723; DOI=10.1002/rcm.1604;
Jin W.-H., Dai J., Zhou H., Xia Q.-C., Zou H.-F., Zeng R.;
"Phosphoproteome analysis of mouse liver using immobilized metal
affinity purification and linear ion trap mass spectrometry.";
Rapid Commun. Mass Spectrom. 18:2169-2176(2004).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[10]
X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 32-132 ALONE AND IN COMPLEX
WITH RNA, FUNCTION, AND SUBUNIT.
PubMed=22021443; DOI=10.1073/pnas.1105211108;
Jenkins H.T., Malkova B., Edwards T.A.;
"Kinked beta-strands mediate high-affinity recognition of mRNA targets
by the germ-cell regulator DAZL.";
Proc. Natl. Acad. Sci. U.S.A. 108:18266-18271(2011).
-!- FUNCTION: RNA-binding protein, which is essential for
gametogenesis in both males and females. Plays a central role
during spermatogenesis. Acts by binding to the 3'-UTR of mRNA,
specifically recognizing GUU triplets, and thereby regulating the
translation of key transcripts. {ECO:0000269|PubMed:22021443,
ECO:0000269|PubMed:9288969}.
-!- SUBUNIT: Homodimer and heterodimer. Forms a heterodimer with DAZ.
Interacts with BOLL, DAZAP1 and DAZAP2. Interacts with PUM2 (By
similarity). Multiple DAZL RRMs can bind to a single RNA
containing multiple GUU triplets. {ECO:0000250,
ECO:0000269|PubMed:10903443, ECO:0000269|PubMed:22021443}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-2024439, EBI-2024439;
O88485:Dync1i1; NbExp=4; IntAct=EBI-2024439, EBI-492834;
P63168:Dynll1; NbExp=12; IntAct=EBI-2024439, EBI-349121;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9288969}.
-!- TISSUE SPECIFICITY: Expressed predominantly in testis with lower
levels in ovary. In testis, it is expressed in pachytene
spermatocytes and at lower level in type-B spermatogonia,
preleptotene and zygotene spermatocytes. In ovary, it is expressed
in maturing follicles. In embryonic and prepuberal ovary, it is
expressed in the oocyte and follicular cells.
{ECO:0000269|PubMed:9288969}.
-!- DEVELOPMENTAL STAGE: In the testis, expression increases steadily
after birth until the first spermatogonial cells appear, levels
off as the first spermatogenic cells enter meiosis (10 days after
birth) and remains at this level thereafter.
-!- DOMAIN: The DAZ-like domain mediates the interaction with DAZAP1
and DAZAP2. {ECO:0000250}.
-!- SIMILARITY: Belongs to the RRM DAZ family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X95724; CAA65039.1; -; mRNA.
EMBL; U38690; AAB46608.1; -; mRNA.
EMBL; U46694; AAC52711.1; -; mRNA.
EMBL; AK014854; BAB29585.1; -; mRNA.
EMBL; AK033183; BAC28187.1; -; mRNA.
CCDS; CCDS37649.1; -.
RefSeq; NP_001264792.1; NM_001277863.1.
RefSeq; NP_034151.3; NM_010021.5.
UniGene; Mm.280641; -.
PDB; 2XS2; X-ray; 1.35 A; A=32-132.
PDB; 2XS5; X-ray; 1.60 A; A/B=32-117.
PDB; 2XS7; X-ray; 1.45 A; A=32-117.
PDB; 2XSF; X-ray; 1.70 A; A=35-118.
PDBsum; 2XS2; -.
PDBsum; 2XS5; -.
PDBsum; 2XS7; -.
PDBsum; 2XSF; -.
ProteinModelPortal; Q64368; -.
SMR; Q64368; -.
IntAct; Q64368; 6.
MINT; MINT-133503; -.
STRING; 10090.ENSMUSP00000010736; -.
iPTMnet; Q64368; -.
PhosphoSitePlus; Q64368; -.
PaxDb; Q64368; -.
PRIDE; Q64368; -.
Ensembl; ENSMUST00000010736; ENSMUSP00000010736; ENSMUSG00000010592.
GeneID; 13164; -.
KEGG; mmu:13164; -.
UCSC; uc008cyu.3; mouse.
CTD; 1618; -.
MGI; MGI:1342328; Dazl.
eggNOG; KOG0118; Eukaryota.
eggNOG; COG0724; LUCA.
GeneTree; ENSGT00530000063480; -.
HOGENOM; HOG000246400; -.
HOVERGEN; HBG000573; -.
InParanoid; Q64368; -.
OMA; RSYVIPP; -.
OrthoDB; EOG091G02CS; -.
PhylomeDB; Q64368; -.
TreeFam; TF324396; -.
EvolutionaryTrace; Q64368; -.
PRO; PR:Q64368; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000010592; -.
CleanEx; MM_DAZL; -.
Genevisible; Q64368; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005844; C:polysome; IDA:MGI.
GO; GO:0043234; C:protein complex; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:MGI.
GO; GO:0008494; F:translation activator activity; IDA:UniProtKB.
GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; IBA:GO_Central.
GO; GO:0007147; P:female meiosis II; IMP:MGI.
GO; GO:0007281; P:germ cell development; IMP:MGI.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0001556; P:oocyte maturation; IMP:MGI.
GO; GO:0045836; P:positive regulation of meiotic nuclear division; IMP:MGI.
GO; GO:0045948; P:positive regulation of translational initiation; IDA:UniProtKB.
GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
InterPro; IPR034779; DAZL.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
PANTHER; PTHR11176:SF4; PTHR11176:SF4; 1.
Pfam; PF00076; RRM_1; 1.
SMART; SM00360; RRM; 1.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS50102; RRM; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Developmental protein;
Differentiation; Oogenesis; Phosphoprotein; Reference proteome;
RNA-binding; Spermatogenesis; Translation regulation.
CHAIN 1 298 Deleted in azoospermia-like.
/FTId=PRO_0000081561.
DOMAIN 40 115 RRM. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 167 190 DAZ-like.
REGION 80 132 Homodimerization.
COMPBIAS 126 207 Pro-rich.
MOD_RES 276 276 Phosphotyrosine.
{ECO:0000269|PubMed:15378723}.
MUTAGEN 43 43 F->D: Abolishes RNA-binding but not
homodimerization; when associated with D-
82; D-84 and D-87.
{ECO:0000269|PubMed:11410654}.
MUTAGEN 82 82 Y->D: Abolishes RNA-binding but not
homodimerization; when associated with D-
43; D-84 and D-87.
{ECO:0000269|PubMed:11410654}.
MUTAGEN 84 84 F->D: Abolishes RNA-binding but not
homodimerization; when associated with D-
43; D-82 and D-87.
{ECO:0000269|PubMed:11410654}.
MUTAGEN 87 87 F->D: Abolishes RNA-binding but not
homodimerization; when associated with D-
43; D-82 and D-84.
{ECO:0000269|PubMed:11410654}.
STRAND 36 45 {ECO:0000244|PDB:2XS2}.
HELIX 53 60 {ECO:0000244|PDB:2XS2}.
HELIX 61 63 {ECO:0000244|PDB:2XS2}.
STRAND 66 73 {ECO:0000244|PDB:2XS2}.
STRAND 79 89 {ECO:0000244|PDB:2XS2}.
HELIX 93 96 {ECO:0000244|PDB:2XS2}.
STRAND 102 107 {ECO:0000244|PDB:2XS7}.
STRAND 109 115 {ECO:0000244|PDB:2XS2}.
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


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