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Protein

Deleted in azoospermia-like

Gene

Dazl

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • mRNA 3'-UTR binding Source: MGI
  • translation activator activity Source: UniProtKB

GO - Biological processi

  • 3'-UTR-mediated mRNA stabilization Source: GO_Central
  • female meiosis II Source: MGI
  • germ cell development Source: MGI
  • multicellular organism development Source: UniProtKB-KW
  • oocyte maturation Source: MGI
  • positive regulation of meiotic nuclear division Source: MGI
  • positive regulation of translational initiation Source: UniProtKB
  • spermatogenesis Source: UniProtKB-KW

Keywordsi

Molecular functionDevelopmental protein, RNA-binding
Biological processDifferentiation, Oogenesis, Spermatogenesis, Translation regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Deleted in azoospermia-like
Alternative name(s):
DAZ-like autosomal
Deleted in azoospermia-like 1
Gene namesi
Name:Dazl
Synonyms:Dazl1, Dazla
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1342328 Dazl

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi43F → D: Abolishes RNA-binding but not homodimerization; when associated with D-82; D-84 and D-87. 1 Publication1
Mutagenesisi82Y → D: Abolishes RNA-binding but not homodimerization; when associated with D-43; D-84 and D-87. 1 Publication1
Mutagenesisi84F → D: Abolishes RNA-binding but not homodimerization; when associated with D-43; D-82 and D-87. 1 Publication1
Mutagenesisi87F → D: Abolishes RNA-binding but not homodimerization; when associated with D-43; D-82 and D-84. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000815611 – 298Deleted in azoospermia-likeAdd BLAST298

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei276Phosphotyrosine1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ64368
PRIDEiQ64368

PTM databases

iPTMnetiQ64368
PhosphoSitePlusiQ64368

Expressioni

Tissue specificityi

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.1 Publication

Developmental stagei

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.

Gene expression databases

BgeeiENSMUSG00000010592
CleanExiMM_DAZL
GenevisibleiQ64368 MM

Interactioni

Subunit structurei

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.By similarity2 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

IntActiQ64368, 6 interactors
MINTiQ64368
STRINGi10090.ENSMUSP00000010736

Structurei

Secondary structure

1298
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi36 – 45Combined sources10
Helixi53 – 60Combined sources8
Helixi61 – 63Combined sources3
Beta strandi66 – 73Combined sources8
Beta strandi79 – 89Combined sources11
Helixi93 – 96Combined sources4
Beta strandi102 – 107Combined sources6
Beta strandi109 – 115Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2XS2X-ray1.35A32-132[»]
2XS5X-ray1.60A/B32-117[»]
2XS7X-ray1.45A32-117[»]
2XSFX-ray1.70A35-118[»]
ProteinModelPortaliQ64368
SMRiQ64368
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ64368

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini40 – 115RRMPROSITE-ProRule annotationAdd BLAST76
Domaini167 – 190DAZ-likeAdd BLAST24

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni80 – 132HomodimerizationAdd BLAST53

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi126 – 207Pro-richAdd BLAST82

Domaini

The DAZ-like domain mediates the interaction with DAZAP1 and DAZAP2.By similarity

Sequence similaritiesi

Belongs to the RRM DAZ family.Curated

Phylogenomic databases

eggNOGiKOG0118 Eukaryota
COG0724 LUCA
GeneTreeiENSGT00530000063480
HOGENOMiHOG000246400
HOVERGENiHBG000573
InParanoidiQ64368
OMAiRSYVIPP
OrthoDBiEOG091G02CS
PhylomeDBiQ64368
TreeFamiTF324396

Family and domain databases

CDDicd12672 RRM_DAZL, 1 hit
Gene3Di3.30.70.330, 1 hit
InterProiView protein in InterPro
IPR037366 BOULE/DAZ
IPR037551 DAZ_RRM_vert
IPR034779 DAZL
IPR012677 Nucleotide-bd_a/b_plait_sf
IPR035979 RBD_domain_sf
IPR000504 RRM_dom
PANTHERiPTHR11176 PTHR11176, 1 hit
PTHR11176:SF4 PTHR11176:SF4, 1 hit
PfamiView protein in Pfam
PF00076 RRM_1, 1 hit
SMARTiView protein in SMART
SM00360 RRM, 1 hit
SUPFAMiSSF54928 SSF54928, 1 hit
PROSITEiView protein in PROSITE
PS50102 RRM, 1 hit

Sequencei

Sequence statusi: Complete.

Q64368-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSATTSEAPN SAVSREASTQ SSSATTSQGY VLPEGKIMPN TVFVGGIDVR
60 70 80 90 100
MDETEIRSFF ARYGSVKEVK IITDRTGVSK GYGFVSFYND VDVQKIVESQ
110 120 130 140 150
INFHGKKLKL GPAIRKQNLC TYHVQPRPLI FNPPPPPQFQ SVWSSPNAET
160 170 180 190 200
YMQPPTMMNP ITQYVQAYPP YPSSPVQVIT GYQLPVYNYQ MPPQWPAGEQ
210 220 230 240 250
RSYVIPPAYT TVNYHCSEVD PGADILPNEC SVHDAAPASG NGPQKKSVDR
260 270 280 290
SIQTVVSCLF NPENRLRNSL VTQDDYFKDK RVHHFRRSRA VLKSDHLC
Length:298
Mass (Da):33,313
Last modified:November 1, 1996 - v1
Checksum:iFBF457BC388DB974
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95724 mRNA Translation: CAA65039.1
U38690 mRNA Translation: AAB46608.1
U46694 mRNA Translation: AAC52711.1
AK014854 mRNA Translation: BAB29585.1
AK033183 mRNA Translation: BAC28187.1
CCDSiCCDS37649.1
RefSeqiNP_001264792.1, NM_001277863.1
NP_034151.3, NM_010021.5
UniGeneiMm.280641

Genome annotation databases

EnsembliENSMUST00000010736; ENSMUSP00000010736; ENSMUSG00000010592
GeneIDi13164
KEGGimmu:13164
UCSCiuc008cyu.3 mouse

Similar proteinsi

Entry informationi

Entry nameiDAZL_MOUSE
AccessioniPrimary (citable) accession number: Q64368
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 17, 2003
Last sequence update: November 1, 1996
Last modified: May 23, 2018
This is version 151 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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