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Entry version 131 (16 Oct 2019)
Sequence version 1 (01 Oct 2000)
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Protein

Piwi-like protein 1

Gene

Piwil1

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

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Endoribonuclease that plays a central role in postnatal germ cells by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity (PubMed:11578866, PubMed:22121019, PubMed:21237665). Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons (PubMed:11578866, PubMed:22121019, PubMed:21237665). Directly binds methylated piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a Dicer-independent mechanism and are primarily derived from transposons and other repeated sequence elements (PubMed:11578866, PubMed:22121019, PubMed:21237665). Strongly prefers a uridine in the first position of their guide (g1U preference, also named 1U-bias) (PubMed:24757166). Not involved in the piRNA amplification loop, also named ping-pong amplification cycle (PubMed:22121019). Acts as an endoribonuclease that cleaves transposon messenger RNAs (PubMed:22121019). Besides their function in transposable elements repression, piRNAs are probably involved in other processes during meiosis such as translation regulation (PubMed:16938833). Probable component of some RISC complex, which mediates RNA cleavage and translational silencing (PubMed:16938833). Also plays a role in the formation of chromatoid bodies and is required for some miRNAs stability (PubMed:16787948). Required to sequester RNF8 in the cytoplasm until late spermatogenesis; RNF8 being released upon ubiquitination and degradation of PIWIL1 (PubMed:28552346).7 Publications

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei382Required for binding 2'-O-methylated 3'-end of piRNAs1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei6331 Publication1
Active sitei671By similarity1
Active sitei703By similarity1
Active sitei837By similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDevelopmental protein, Endonuclease, Hydrolase, Nuclease, RNA-binding
Biological processDifferentiation, Meiosis, RNA-mediated gene silencing, Spermatogenesis, Translation regulation
LigandMagnesium, Metal-binding

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Piwi-like protein 1Curated (EC:3.1.26.-1 Publication)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Piwil1Imported
Synonyms:Miwi2 Publications
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 5

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1928897 Piwil1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Mice display spermatogenic arrest at the beginning of the round spermatid stage, resembling the phenotype of CREM, a master regulator of spermiogenesis; mRNAs of FHL5/activator of CREM and CREM target genes are down-regulated in testes. Female are fertile but male are completely sterile, no sperm is found in the epididimus. Chromatoid bodies from round spermatids are not fully compacted and remain as a diffuse chromatoid material.2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi218 – 221RRLL → ARLA: Does not affect piRNA-binding but abolishes ubiquitination by the APC/C. Causes male sterility. 2 Publications4
Mutagenesisi330 – 335KSTFKK → ASTFAA: Abolishes ubiquitination by the APC/C. 1 Publication6
Mutagenesisi343F → A: Impairs binding to 2'-O-methylated 3'-end of piRNAs. 1 Publication1
Mutagenesisi346 – 347YY → AA: Abolishes piRNA-binding and ubiquitination by the APC/C. 1 Publication2
Mutagenesisi382M → A: Impairs binding to 2'-O-methylated 3'-end of piRNAs. 1 Publication1
Mutagenesisi633D → A in DAH mutant; causes male infertility due to derepression of LINE1 retrotransposons transcripts. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002345681 – 862Piwi-like protein 1Add BLAST862

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei14Omega-N-methylarginine; by PRMT5; alternate1 Publication1
Modified residuei14Symmetric dimethylarginine; by PRMT5; alternate1 Publication1
Modified residuei49Omega-N-methylarginine; by PRMT51 Publication1
Modified residuei53Omega-N-methylarginine; alternate1 Publication1
Modified residuei53Symmetric dimethylarginine; alternate1 Publication1
Modified residuei371Omega-N-methylarginine; by PRMT51 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Ubiquitinated by the anaphase promoting complex/cyclosome (APC/C) in late spermatids, leading to its degradation (PubMed:23328397). Ubiquitination only takes place following piRNA-binding in adult testis (PubMed:23328397). Ubiquitination and degradation in late spermatogenesis by APC/C is probably required to release RNF8 from the cytoplasm and promote histone to protamine exchange by RNF8 (PubMed:28552346).2 Publications
Arginine methylation by PRMT5 is required for the interaction with Tudor domain-containing protein (TDRD1, TDRKH/TDRD2, RNF17/TDRD4, TDRD6, TDRD7 and TDRD9) and subsequent localization to the meiotic nuage, also named P granule.5 Publications

Keywords - PTMi

Methylation, Ubl conjugation

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q9JMB7

PeptideAtlas

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PeptideAtlasi
Q9JMB7

PRoteomics IDEntifications database

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PRIDEi
Q9JMB7

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q9JMB7

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q9JMB7

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in brain. Expressed in testis, specifically in spermatocytes (at protein level). Only detected in germ lineage cells of adult testis. Expressed in male gonads 2 weeks after birth at the initiation of spermatogenesis, but not expressed in female gonads.4 Publications

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Expression is activated by MYBL1/A-MYB.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSMUSG00000029423 Expressed in 25 organ(s), highest expression level in testis

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q9JMB7 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q9JMB7 MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts (via Piwi domain) with DICER1, suggesting that it forms ribonucleoprotein RISC complexes; this interaction is regulated by HSP90AB1 activity (PubMed:16938833).

Interacts with MAEL, KIF17, PABPC1, PRMT5 and WDR77 (PubMed:16787948, PubMed:16787967, PubMed:19020299, PubMed:19584108).

Interacts (when methylated on arginine residues) with TDRD1, TDRKH/TDRD2, RNF17/TDRD4, TDRD6, TDRD7 and TDRD9 (PubMed:19584108, PubMed:19918066, PubMed:19926723, PubMed:23714778).

Interacts with CLOCK (PubMed:22900038).

Interacts with MOV10L1 (PubMed:20534472).

Interacts with ANAPC10; interaction oly takes place following piRNA-binding (PubMed:23328397).

Interacts with RNF8; leading to sequester RNF8 in the cytoplasm (PubMed:28552346).

Interacts with Tex19.1 and, probably, Tex19.2 (PubMed:28254886).

13 Publications

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
208311, 1 interactor

Database of interacting proteins

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DIPi
DIP-59456N

Protein interaction database and analysis system

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IntActi
Q9JMB7, 5 interactors

Molecular INTeraction database

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MINTi
Q9JMB7

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000083222

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1862
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q9JMB7

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini278 – 392PAZPROSITE-ProRule annotationAdd BLAST115
Domaini556 – 848PiwiPROSITE-ProRule annotationAdd BLAST293

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni317 – 319Required for binding 2'-O-methylated 3'-end of piRNAs1 Publication3
Regioni480 – 616MID region1 PublicationAdd BLAST137

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi218 – 225D-box1 Publication8

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The D-box (destruction box) acts as a recognition signal for association with the APC/C complex, ubiquitination and degradation (PubMed:23328397).1 Publication
The PAZ domain specifically recognizes binds the 2'-O-methylated 3'-end of piRNAs (PubMed:21237665). The MID region is required for recognition of uridine in the first position of piRNAs (g1U preference, also named 1U-bias) (PubMed:24757166).2 Publications

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the argonaute family. Piwi subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG1042 Eukaryota
ENOG410XNRH LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00950000183200

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000254789

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9JMB7

KEGG Orthology (KO)

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KOi
K02156

Identification of Orthologs from Complete Genome Data

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OMAi
CVAPTHY

Database of Orthologous Groups

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OrthoDBi
220258at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q9JMB7

TreeFam database of animal gene trees

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TreeFami
TF354206

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.30.420.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR014811 ArgoL1
IPR031320 GAGE
IPR003100 PAZ_dom
IPR036085 PAZ_dom_sf
IPR003165 Piwi
IPR031326 PIWIL1
IPR012337 RNaseH-like_sf
IPR036397 RNaseH_sf

The PANTHER Classification System

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PANTHERi
PTHR22891:SF46 PTHR22891:SF46, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF08699 ArgoL1, 1 hit
PF05831 GAGE, 1 hit
PF02170 PAZ, 1 hit
PF02171 Piwi, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM01379 GAGE, 1 hit
SM00949 PAZ, 1 hit
SM00950 Piwi, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF101690 SSF101690, 1 hit
SSF53098 SSF53098, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50821 PAZ, 1 hit
PS50822 PIWI, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: Q9JMB7-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MTGRARARAR GRARGQETVQ HVGAAASQQP GYIPPRPQQS PTEGDLVGRG
60 70 80 90 100
RQRGMVVGAT SKSQELQISA GFQELSLAER GGRRRDFHDL GVNTRQNLDH
110 120 130 140 150
VKESKTGSSG IIVKLSTNHF RLTSRPQWAL YQYHIDYNPL MEARRLRSAL
160 170 180 190 200
LFQHEDLIGR CHAFDGTILF LPKRLQHKVT EVFSQTRNGE HVRITITLTN
210 220 230 240 250
ELPPTSPTCL QFYNIIFRRL LKIMNLQQIG RNYYNPSDPI DIPNHRLVIW
260 270 280 290 300
PGFTTSILQY ENNIMLCTDV SHKVLRSETV LDFMFNLYQQ TEEHKFQEQV
310 320 330 340 350
SKELIGLIVL TKYNNKTYRV DDIDWDQNPK STFKKADGSE VSFLEYYRKQ
360 370 380 390 400
YNQEITDLKQ PVLVSQPKRR RGPGGTLPGP AMLIPELCYL TGLTDKMRND
410 420 430 440 450
FNVMKDLAVH TRLTPEQRQR EVGRLIDYIH KDDNVQRELR DWGLSFDSNL
460 470 480 490 500
LSFSGRILQS EKIHQGGKTF DYNPQFADWS KETRGAPLIS VKPLDNWLLI
510 520 530 540 550
YTRRNYEAAN SLIQNLFKVT PAMGIQMKKA IMIEVDDRTE AYLRALQQKV
560 570 580 590 600
TSDTQIVVCL LSSNRKDKYD AIKKYLCTDC PTPSQCVVAR TLGKQQTVMA
610 620 630 640 650
IATKIALQMN CKMGGELWRV DMPLKLAMIV GIDCYHDTTA GRRSIAGFVA
660 670 680 690 700
SINEGMTRWF SRCVFQDRGQ ELVDGLKVCL QAALRAWSGC NEYMPSRVIV
710 720 730 740 750
YRDGVGDGQL KTLVNYEVPQ FLDCLKSVGR GYNPRLTVIV VKKRVNARFF
760 770 780 790 800
AQSGGRLQNP LPGTVIDVEV TRPEWYDFFI VSQAVRSGSV SPTHYNVIYD
810 820 830 840 850
SSGLKPDHIQ RLTYKLCHVY YNWPGVIRVP APCQYAHKLA FLVGQSIHRE
860
PNLSLSNRLY YL
Length:862
Mass (Da):98,574
Last modified:October 1, 2000 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i45588D13284CCC4C
GO
Isoform 2 (identifier: Q9JMB7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     825-862: GVIRVPAPCQYAHKLAFLVGQSIHREPNLSLSNRLYYL → VSVLLWTTYPG

Note: No experimental confirmation available.
Show »
Length:835
Mass (Da):95,484
Checksum:i3F96A55A0DEE610F
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0G2JEK6A0A0G2JEK6_MOUSE
Piwi-like protein 1
Piwil1
493Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAH66846 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti374G → S in AAH66846 (PubMed:15489334).Curated1
Sequence conflicti468K → R in AAH66846 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_036663825 – 862GVIRV…RLYYL → VSVLLWTTYPG in isoform 2. 1 PublicationAdd BLAST38

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AB032604 mRNA Translation: BAA93705.1
AF438405 mRNA Translation: AAL31014.1
EF196092 mRNA Translation: ABM69181.1
BC066846 mRNA Translation: AAH66846.1 Sequence problems.
BC129857 mRNA Translation: AAI29858.1
BC129858 mRNA Translation: AAI29859.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS19690.1 [Q9JMB7-1]

NCBI Reference Sequences

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RefSeqi
NP_067286.1, NM_021311.3 [Q9JMB7-1]
XP_006504381.1, XM_006504318.1 [Q9JMB7-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000086056; ENSMUSP00000083222; ENSMUSG00000029423 [Q9JMB7-1]
ENSMUST00000195959; ENSMUSP00000142386; ENSMUSG00000029423 [Q9JMB7-2]

Database of genes from NCBI RefSeq genomes

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GeneIDi
57749

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:57749

UCSC genome browser

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UCSCi
uc008zsi.1 mouse [Q9JMB7-1]
uc008zsj.1 mouse [Q9JMB7-2]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB032604 mRNA Translation: BAA93705.1
AF438405 mRNA Translation: AAL31014.1
EF196092 mRNA Translation: ABM69181.1
BC066846 mRNA Translation: AAH66846.1 Sequence problems.
BC129857 mRNA Translation: AAI29858.1
BC129858 mRNA Translation: AAI29859.1
CCDSiCCDS19690.1 [Q9JMB7-1]
RefSeqiNP_067286.1, NM_021311.3 [Q9JMB7-1]
XP_006504381.1, XM_006504318.1 [Q9JMB7-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2XFMNMR-A276-425[»]
4P1ZX-ray2.30A/B/C/D485-612[»]
SMRiQ9JMB7
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi208311, 1 interactor
DIPiDIP-59456N
IntActiQ9JMB7, 5 interactors
MINTiQ9JMB7
STRINGi10090.ENSMUSP00000083222

PTM databases

iPTMnetiQ9JMB7
PhosphoSitePlusiQ9JMB7

Proteomic databases

PaxDbiQ9JMB7
PeptideAtlasiQ9JMB7
PRIDEiQ9JMB7

Genome annotation databases

EnsembliENSMUST00000086056; ENSMUSP00000083222; ENSMUSG00000029423 [Q9JMB7-1]
ENSMUST00000195959; ENSMUSP00000142386; ENSMUSG00000029423 [Q9JMB7-2]
GeneIDi57749
KEGGimmu:57749
UCSCiuc008zsi.1 mouse [Q9JMB7-1]
uc008zsj.1 mouse [Q9JMB7-2]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
9271
MGIiMGI:1928897 Piwil1

Phylogenomic databases

eggNOGiKOG1042 Eukaryota
ENOG410XNRH LUCA
GeneTreeiENSGT00950000183200
HOGENOMiHOG000254789
InParanoidiQ9JMB7
KOiK02156
OMAiCVAPTHY
OrthoDBi220258at2759
PhylomeDBiQ9JMB7
TreeFamiTF354206

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
Piwil1 mouse

Protein Ontology

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PROi
PR:Q9JMB7

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000029423 Expressed in 25 organ(s), highest expression level in testis
ExpressionAtlasiQ9JMB7 baseline and differential
GenevisibleiQ9JMB7 MM

Family and domain databases

Gene3Di3.30.420.10, 1 hit
InterProiView protein in InterPro
IPR014811 ArgoL1
IPR031320 GAGE
IPR003100 PAZ_dom
IPR036085 PAZ_dom_sf
IPR003165 Piwi
IPR031326 PIWIL1
IPR012337 RNaseH-like_sf
IPR036397 RNaseH_sf
PANTHERiPTHR22891:SF46 PTHR22891:SF46, 1 hit
PfamiView protein in Pfam
PF08699 ArgoL1, 1 hit
PF05831 GAGE, 1 hit
PF02170 PAZ, 1 hit
PF02171 Piwi, 1 hit
SMARTiView protein in SMART
SM01379 GAGE, 1 hit
SM00949 PAZ, 1 hit
SM00950 Piwi, 1 hit
SUPFAMiSSF101690 SSF101690, 1 hit
SSF53098 SSF53098, 1 hit
PROSITEiView protein in PROSITE
PS50821 PAZ, 1 hit
PS50822 PIWI, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPIWL1_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9JMB7
Secondary accession number(s): A1L324, A1L325, Q6NXX0
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: October 1, 2000
Last modified: October 16, 2019
This is version 131 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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