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Protein

Deleted in azoospermia-like

Gene

Dazl

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

  • mRNA 3'-UTR binding Source: MGI
  • nucleotide binding Source: InterPro
  • 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
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Oogenesis, Spermatogenesis, Translation regulation

Keywords - Ligandi

RNA-binding

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1342328. Dazl.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • polysome Source: MGI
Complete GO annotation...

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

WithEntry#Exp.IntActNotes
itself2EBI-2024439,EBI-2024439
Dync1i1O884854EBI-2024439,EBI-492834
Dynll1P6316812EBI-2024439,EBI-349121

Protein-protein interaction databases

IntActiQ64368. 6 interactors.
MINTiMINT-133503.
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
Contains 1 DAZ-like domain.Curated
Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Phylogenomic databases

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

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

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.

Cross-referencesi

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.

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...

Protein-protein interaction databases

IntActiQ64368. 6 interactors.
MINTiMINT-133503.
STRINGi10090.ENSMUSP00000010736.

PTM databases

iPTMnetiQ64368.
PhosphoSitePlusiQ64368.

Proteomic databases

PaxDbiQ64368.
PRIDEiQ64368.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1618.
MGIiMGI:1342328. Dazl.

Phylogenomic databases

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

Miscellaneous databases

EvolutionaryTraceiQ64368.
PROiQ64368.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000010592.
CleanExiMM_DAZL.
GenevisibleiQ64368. MM.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDAZL_MOUSE
AccessioniPrimary (citable) accession number: Q64368
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 17, 2003
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.