Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 124 (18 Sep 2019)
Sequence version 1 (05 Jul 2004)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Anoctamin-6

Gene

Ano6

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

Small-conductance calcium-activated nonselective cation (SCAN) channel which acts as a regulator of phospholipid scrambling in platelets, osteoblasts and fetal thymocytes. Phospholipid scrambling results in surface exposure of phosphatidylserine which in platelets is essential to trigger the clotting system whereas in osteoblasts is essential for the deposition of hydroxyapatite during bone mineralization. Has calcium-dependent phospholipid scramblase activity; scrambles phosphatidylserine, phosphatidylcholine and galactosylceramide. Can generate outwardly rectifying chloride channel currents in airway epithelial cells and Jurkat T lymphocytes.7 Publications

Miscellaneous

The term 'anoctamin' was coined because these channels are anion selective and are predicted to have eight (OCT) transmembrane segments. There is some dissatisfaction in the field with the Ano nomenclature because it is not certain that all the members of this family are anion channels or have the 8-transmembrane topology.Curated

Caution

Contains ten transmembrane regions, not eight as predicted.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Exhibits synergistic gating by Ca2+ and voltage. Inhibited by some non-specific cation channel blockers such as: ruthenium red, 2-aminoethyl diphenylborinate (2APB), gadolinium and cadmium ions.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi624Calcium1 Publication1
Metal bindingi667Calcium1 Publication1
Metal bindingi670Calcium1 Publication1

<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 functionChloride channel, Ion channel, Voltage-gated channel
Biological processIon transport, Lipid transport, Transport
LigandCalcium, Chloride, Metal-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-2672351 Stimuli-sensing channels
R-MMU-6798695 Neutrophil degranulation

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000000373

<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:
Anoctamin-6
Alternative name(s):
Small-conductance calcium-activated nonselective cation channel
Short name:
SCAN channel
Transmembrane protein 16F
<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:Ano6
Synonyms:Tmem16f2 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 15

Organism-specific databases

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

More...
MGIi
MGI:2145890 Ano6

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 301Cytoplasmic1 PublicationAdd BLAST301
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei302 – 322Helical1 PublicationAdd BLAST21
Topological domaini323 – 376Extracellular1 PublicationAdd BLAST54
Transmembranei377 – 397Helical1 PublicationAdd BLAST21
Topological domaini398 – 456Cytoplasmic1 PublicationAdd BLAST59
Transmembranei457 – 477Helical1 PublicationAdd BLAST21
Topological domaini478 – 510Extracellular1 PublicationAdd BLAST33
Transmembranei511 – 531Helical1 PublicationAdd BLAST21
Topological domaini532 – 552Cytoplasmic1 PublicationAdd BLAST21
Transmembranei553 – 573Helical1 PublicationAdd BLAST21
Topological domaini574 – 602Extracellular1 PublicationAdd BLAST29
Transmembranei603 – 622Helical1 PublicationAdd BLAST20
Topological domaini623 – 664Cytoplasmic1 PublicationAdd BLAST42
Transmembranei665 – 685Helical1 PublicationAdd BLAST21
Transmembranei686 – 706Helical1 PublicationAdd BLAST21
Topological domaini707 – 723Cytoplasmic1 PublicationAdd BLAST17
Transmembranei724 – 744Helical1 PublicationAdd BLAST21
Topological domaini745 – 837Extracellular1 PublicationAdd BLAST93
Transmembranei838 – 858Helical1 PublicationAdd BLAST21
Topological domaini859 – 911Cytoplasmic1 PublicationAdd BLAST53

Keywords - Cellular componenti

Cell membrane, Membrane

<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 are viable and fertile, and display no major morphological defects. They exhibit deficiencies in Ca2+-dependent phospholipid scramblase activity in platelets and defects in blood coagulation (PubMed:23021219). They also show reduced skeleton size and skeletal deformities.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>Mutagenesisi370K → A: No effect on lipid scramblase activity. 1 Publication1
Mutagenesisi409D → G: Increased speed of phospholipid scrambling. 1 Publication1
Mutagenesisi409D → G: Reduced channel activity and sensitivity to Ca(2+). 1 Publication1
Mutagenesisi478R → A: Decreased lipid scramblase and ion channel activity. Requires lower calcium levels for activation of ion channel activity. 1 Publication1
Mutagenesisi518F → A: Increased speed of phospholipid scrambling. Constitutive scramblase activity at basal cytosolic calcium levels; when associated with A-563 and A-612. 1 Publication1
Mutagenesisi518F → E, K or Q: Constitutive lipid scramblase activity at basal cytosolic calcium levels. 1 Publication1
Mutagenesisi518F → L: Decreased lipid scramblase activity. 1 Publication1
Mutagenesisi518F → W: Slightly increased lipid scramblase activity. 1 Publication1
Mutagenesisi559Q → K: Moderately decreased sensitivity to activation by calcium. 1 Publication1
Mutagenesisi559Q → K: Slower channel activation. Increased permeability to chloride ions. 1 Publication1
Mutagenesisi563Y → A: Increased speed of phospholipid scrambling. Requires lower calcium levels for activation of scramblase and ion channel activity. Constitutive scramblase activity at basal cytosolic calcium levels; when associated with A-518 and A-612. 1 Publication1
Mutagenesisi563Y → K or Q: Constitutive lipid scramblase activity at basal cytosolic calcium levels. 1 Publication1
Mutagenesisi563Y → S: No effect on lipid scramblase activity. 1 Publication1
Mutagenesisi563Y → W: Loss of lipid scramblase activity. 1 Publication1
Mutagenesisi612I → A: Increased speed of phospholipid scrambling. Constitutive scramblase activity at basal cytosolic calcium levels; when associated with A-518 and A-563. 1 Publication1
Mutagenesisi612I → E or K: Constitutive lipid scramblase activity at basal cytosolic calcium levels. 1 Publication1
Mutagenesisi612I → W: Decreased lipid scramblase activity. 1 Publication1
Mutagenesisi615G → A: Requires lower calcium levels for activation of scramblase and ion channel activity. 1 Publication1
Mutagenesisi623Q → F: No effect on lipid scramblase activity. 1 Publication1
Mutagenesisi624E → Q: Expected to disrupt calcium binding. Loss of scramblase and ion channel activity. 1 Publication1
Mutagenesisi667E → Q: Requires much higher calcium levels for the activation of scramblase and ion channel activity. 2 Publications1
Mutagenesisi703D → R: Expected to disrupt calcium binding. Loss of scramblase activity. 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_00001917581 – 911Anoctamin-6Add BLAST911

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi330N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi331 ↔ 372Combined sources1 Publication
Disulfide bondi338 ↔ 365Combined sources1 Publication
Disulfide bondi349 ↔ 807Combined sources1 Publication
Disulfide bondi352 ↔ 356Combined sources1 Publication
Glycosylationi362N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi494N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi596 ↔ 601Combined sources1 Publication
Glycosylationi778N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi785N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi803N-linked (GlcNAc...) asparagine1 Publication1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q6P9J9

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q6P9J9

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

More...
PaxDbi
Q6P9J9

PeptideAtlas

More...
PeptideAtlasi
Q6P9J9

PRoteomics IDEntifications database

More...
PRIDEi
Q6P9J9

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q6P9J9

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

More...
PhosphoSitePlusi
Q6P9J9

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q6P9J9

<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

Predominant expression seen in epithelial tissues. Also found in skeletal system where it is primarily expressed in osteoblasts.2 Publications

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

At 14.5 dpc, expressed in lung epithelium and mesenchyme. At 16.5 dpc, expressed in esophageal epithelium and mesenchyme. In the caudal digestive tract, detected in small intestine epithelium at 14.5 dpc. Also detected at 14.5 dpc in epithelium and mesenchyme of trachea, ovary, kidney and stomach. In the developing skeleton, expressed in developing rib perichondria at 14.5 dpc. Also expressed in the neural tube and dorsal root ganglia at 14.5 dpc. In developing skin, expression is restricted to basal layers of the epidermis at 16.5 dpc.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000064210 Expressed in 275 organ(s), highest expression level in intestine

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q6P9J9 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q6P9J9 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

Homodimer.

1 Publication

GO - Molecular functioni

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
Q6P9J9, 2 interactors

Molecular INTeraction database

More...
MINTi
Q6P9J9

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000071770

<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

1911
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

More...
SMRi
Q6P9J9

Database of comparative protein structure models

More...
ModBasei
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

<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 anoctamin family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2514 Eukaryota
ENOG410XS4S LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000158969

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000006509

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q6P9J9

KEGG Orthology (KO)

More...
KOi
K19500

Identification of Orthologs from Complete Genome Data

More...
OMAi
YVTPQMA

Database of Orthologous Groups

More...
OrthoDBi
1263362at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q6P9J9

TreeFam database of animal gene trees

More...
TreeFami
TF314265

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR032394 Anoct_dimer
IPR007632 Anoctamin
IPR031295 Anoctamin-6

The PANTHER Classification System

More...
PANTHERi
PTHR12308 PTHR12308, 1 hit
PTHR12308:SF21 PTHR12308:SF21, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF16178 Anoct_dimer, 1 hit
PF04547 Anoctamin, 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 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q6P9J9-1) [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
MQMMTRKVLL NMELEEDDDE DGDIVLENFD QTIVCPTFGS LENQQDFRTP
60 70 80 90 100
EFEEFNGKPD SLFFTDGQRR IDFILVYEDE SKKENNKKGT NEKQKRKRQA
110 120 130 140 150
YESNLICHGL QLEATRSVSD DKLVFVKVHA PWEVLCTYAE IMHIKLPLKP
160 170 180 190 200
NDLKTRSPFG NLNWFTKVLR VNESVIKPEQ EFFTAPFEKS RMNDFYILDR
210 220 230 240 250
DSFFNPATRS RIVYFILSRV KYQVMNNVNK FGINRLVSSG IYKAAFPLHD
260 270 280 290 300
CRFNYESEDI SCPSERYLLY REWAHPRSIY KKQPLDLIRK YYGEKIGIYF
310 320 330 340 350
AWLGYYTQML LLAAVVGVAC FLYGYLDQDN CTWSKEVCDP DIGGQILMCP
360 370 380 390 400
QCDRLCPFWR LNITCESSKK LCIFDSFGTL IFAVFMGVWV TLFLEFWKRR
410 420 430 440 450
QAELEYEWDT VELQQEEQAR PEYEAQCNHV VINEITQEEE RIPFTTCGKC
460 470 480 490 500
IRVTLCASAV FFWILLIIAS VIGIIVYRLS VFIVFSTTLP KNPNGTDPIQ
510 520 530 540 550
KYLTPQMATS ITASIISFII IMILNTIYEK VAIMITNFEL PRTQTDYENS
560 570 580 590 600
LTMKMFLFQF VNYYSSCFYI AFFKGKFVGY PGDPVYLLGK YRSEECDPGG
610 620 630 640 650
CLLELTTQLT IIMGGKAIWN NIQEVLLPWV MNLIGRYKRV SGSEKITPRW
660 670 680 690 700
EQDYHLQPMG KLGLFYEYLE MIIQFGFVTL FVASFPLAPL LALVNNILEI
710 720 730 740 750
RVDAWKLTTQ FRRMVPEKAQ DIGAWQPIMQ GIAILAVVTN AMIIAFTSDM
760 770 780 790 800
IPRLVYYWSF SIPPYGDHTY YTMDGYINNT LSVFNITDFK NTDKENPYIG
810 820 830 840 850
LGNYTLCRYR DFRNPPGHPQ EYKHNIYYWH VIAAKLAFII VMEHIIYSVK
860 870 880 890 900
FFISYAIPDV SKITKSKIKR EKYLTQKLLH ESHLKDLTKN MGIIAERIGG
910
TVDNSVRPKL E
Length:911
Mass (Da):106,255
Last modified:July 5, 2004 - 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:i33D7A6EF02635B39
GO
Isoform 2 (identifier: Q6P9J9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-427: Missing.
     428-436: NHVVINEIT → MALMAESLC

Note: No experimental confirmation available.
Show »
Length:484
Mass (Da):55,725
Checksum:iC3DCED460A9892A7
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 are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A2I3BPY8A0A2I3BPY8_MOUSE
Anoctamin
Ano6
466Annotation score:

Annotation score:2 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>
A0A2I3BPX3A0A2I3BPX3_MOUSE
Anoctamin
Ano6
932Annotation score:

Annotation score:2 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>
A0A2I3BRD2A0A2I3BRD2_MOUSE
Anoctamin-6
Ano6
193Annotation 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>

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_0156541 – 427Missing in isoform 2. 1 PublicationAdd BLAST427
Alternative sequenceiVSP_015655428 – 436NHVVINEIT → MALMAESLC in isoform 2. 1 Publication9

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AK089300 mRNA Translation: BAC40833.1
BC060732 mRNA Translation: AAH60732.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS37184.1 [Q6P9J9-1]

NCBI Reference Sequences

More...
RefSeqi
NP_001240742.1, NM_001253813.1
NP_780553.2, NM_175344.4 [Q6P9J9-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000071874; ENSMUSP00000071770; ENSMUSG00000064210 [Q6P9J9-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
105722

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:105722

UCSC genome browser

More...
UCSCi
uc007xju.2 mouse [Q6P9J9-1]

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
AK089300 mRNA Translation: BAC40833.1
BC060732 mRNA Translation: AAH60732.1
CCDSiCCDS37184.1 [Q6P9J9-1]
RefSeqiNP_001240742.1, NM_001253813.1
NP_780553.2, NM_175344.4 [Q6P9J9-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6QP6electron microscopy3.20A/B1-911[»]
6QPBelectron microscopy3.60A/B1-911[»]
6QPCelectron microscopy3.50A/B1-911[»]
6QPIelectron microscopy3.30A/B1-911[»]
SMRiQ6P9J9
ModBaseiSearch...

Protein-protein interaction databases

IntActiQ6P9J9, 2 interactors
MINTiQ6P9J9
STRINGi10090.ENSMUSP00000071770

Chemistry databases

SwissLipidsiSLP:000000373

PTM databases

iPTMnetiQ6P9J9
PhosphoSitePlusiQ6P9J9
SwissPalmiQ6P9J9

Proteomic databases

EPDiQ6P9J9
jPOSTiQ6P9J9
PaxDbiQ6P9J9
PeptideAtlasiQ6P9J9
PRIDEiQ6P9J9

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000071874; ENSMUSP00000071770; ENSMUSG00000064210 [Q6P9J9-1]
GeneIDi105722
KEGGimmu:105722
UCSCiuc007xju.2 mouse [Q6P9J9-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
196527
MGIiMGI:2145890 Ano6

Phylogenomic databases

eggNOGiKOG2514 Eukaryota
ENOG410XS4S LUCA
GeneTreeiENSGT00940000158969
HOGENOMiHOG000006509
InParanoidiQ6P9J9
KOiK19500
OMAiYVTPQMA
OrthoDBi1263362at2759
PhylomeDBiQ6P9J9
TreeFamiTF314265

Enzyme and pathway databases

ReactomeiR-MMU-2672351 Stimuli-sensing channels
R-MMU-6798695 Neutrophil degranulation

Miscellaneous databases

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

More...
ChiTaRSi
Ano6 mouse

Protein Ontology

More...
PROi
PR:Q6P9J9

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000064210 Expressed in 275 organ(s), highest expression level in intestine
ExpressionAtlasiQ6P9J9 baseline and differential
GenevisibleiQ6P9J9 MM

Family and domain databases

InterProiView protein in InterPro
IPR032394 Anoct_dimer
IPR007632 Anoctamin
IPR031295 Anoctamin-6
PANTHERiPTHR12308 PTHR12308, 1 hit
PTHR12308:SF21 PTHR12308:SF21, 1 hit
PfamiView protein in Pfam
PF16178 Anoct_dimer, 1 hit
PF04547 Anoctamin, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
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 nameiANO6_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: Q6P9J9
Secondary accession number(s): Q8C242
<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: September 13, 2005
Last sequence update: July 5, 2004
Last modified: September 18, 2019
This is version 124 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again