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Entry version 95 (17 Jun 2020)
Sequence version 1 (20 Feb 2007)
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Protein

Polycystic kidney disease 2-like 1 protein

Gene

Pkd2l1

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

Pore-forming subunit of a heteromeric, non-selective cation channel that is permeable to Ca2+ (PubMed:16891422, PubMed:15548533, PubMed:19464260, PubMed:20538909, PubMed:21185261, PubMed:22420714, PubMed:25820328, PubMed:28904867, PubMed:29567962). Pore-forming subunit of a calcium-permeant ion channel formed by PKD1L2 and PKD1L1 in primary cilia, where it controls cilium calcium concentration, but does not affect cytoplasmic calcium concentration (PubMed:24336288, PubMed:24336289). The channel formed by PKD1L2 and PKD1L1 in primary cilia regulates sonic hedgehog/SHH signaling and GLI2 transcription (PubMed:24336288). Pore-forming subunit of a channel formed by PKD1L2 and PKD1L3 that contributes to sour taste perception in gustatory cells (PubMed:16891422, PubMed:16929298, PubMed:20406802, PubMed:21098668, PubMed:21625513). The heteromeric channel formed by PKD1L2 and PKD1L3 is activated by low pH, but opens only when the extracellular pH rises again (PubMed:18535624, PubMed:19464260, PubMed:20538909, PubMed:20406802, PubMed:22420714, PubMed:28904867, PubMed:29567962). May play a role in the perception of carbonation taste (PubMed:19833970). May play a role in the sensory perception of water, via a mechanism that activates the channel in response to dilution of salivary bicarbonate and changes in salivary pH (PubMed:28553944).18 Publications

Caution

The active channel complex is an obligate tetramer (PubMed:29567962). In contrast, the isolated cytoplasmic C-terminal domain forms homotrimers in vitro (PubMed:25820328). Likewise, photobleaching experiments suggest formation of homotrimers in the membrane (By similarity).By similarity2 Publications
Pkd1l3 and Pkd2l1 have been defined as sour taste receptor in gustatory cells based on a number of indirect evidences: Pkd2l1 is expressed in a subset of taste receptor cells distinct from those responsible for sweet, bitter and unami taste and genetic elimination of cells expressing Pkd2l1 reduces gustatory nerve responses to sour taste stimuli (PubMed:16891422, PubMed:16929298). However, a number of experiments have recently shown that the sour taste receptor activity is probably indirect: mice lacking Pkd2l1 only show partial defects in sour taste perception (PubMed:21625513). Moreover, the PKD1L3-PKD2L1 heteromer, when expressed in cells does not respond to acid stimuli used to evoke proton currents in taste cells (PubMed:21098668).4 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

The ion channel is gated following an off-response property by acid: gated open after the removal of acid stimulus, but not during acid application (PubMed:18535624, PubMed:19464260, PubMed:20406802, PubMed:22420714, PubMed:28904867, PubMed:29567962). Responses to acid stimulus are inhibited by capsaicin (PubMed:22420714).6 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) of the calcium-binding region(s) within the protein. One common calcium-binding motif is the EF-hand, but other calcium-binding motifs also exist.<p><a href='/help/ca_bind' target='_top'>More...</a></p>Calcium bindingi643 – 654PROSITE-ProRule annotationAdd BLAST12

<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 functionCalcium channel, Ion channel
Biological processCalcium transport, Ion transport, Transport
LigandCalcium

Protein family/group databases

Transport Classification Database

More...
TCDBi
1.A.5.2.2 the polycystin cation channel (pcc) family

<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%5Fand%5Ftaxonomy%5Fsection">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:
Polycystic kidney disease 2-like 1 protein
Alternative name(s):
Polycystin-2 homolog
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:Pkd2l1
Synonyms:Trpp3
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 19

Organism-specific databases

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

More...
MGIi
MGI:1352448 Pkd2l1

<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%5Flocation%5Fsection">'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 – 103Cytoplasmic1 PublicationAdd BLAST103
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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>Transmembranei104 – 124Helical1 PublicationAdd BLAST21
Topological domaini125 – 356Extracellular1 PublicationAdd BLAST232
Transmembranei357 – 376Helical1 PublicationAdd BLAST20
Topological domaini377 – 384Cytoplasmic1 Publication8
Transmembranei385 – 405Helical1 PublicationAdd BLAST21
Topological domaini406 – 433Extracellular1 PublicationAdd BLAST28
Transmembranei434 – 454Helical1 PublicationAdd BLAST21
Topological domaini455 – 479Cytoplasmic1 PublicationAdd BLAST25
Transmembranei480 – 499Helical1 PublicationAdd BLAST20
Topological domaini500 – 511Extracellular1 PublicationAdd BLAST12
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a region that is buried within a membrane, but does not cross it.<p><a href='/help/intramem' target='_top'>More...</a></p>Intramembranei512 – 526Pore-forming1 PublicationAdd BLAST15
Topological domaini527 – 536Extracellular1 Publication10
Transmembranei537 – 557Helical1 PublicationAdd BLAST21
Topological domaini558 – 760Cytoplasmic1 PublicationAdd BLAST203

Keywords - Cellular componenti

Cell membrane, Cell projection, Cilium, Cytoplasmic vesicle, 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

Intestinal malrotation in 50% of animals, while other organs do not show major organ laterality defects. Intestinal malformations are associated with SHH pathway defects during early development (PubMed:24336288). Partial reduction of chorda tympani nerve response to sour stimuli, without affecting sweet, salty, bitter, and umami perception (PubMed:21625513).2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi522G → L: Loss of channel activity. 1 Publication1
Mutagenesisi523D → E: Little or no effect on calcium channel activity. 1 Publication1
Mutagenesisi523D → N: Impaired calcium channel activity. 1 Publication1
Mutagenesisi525D → N: Little or no effect on calcium channel activity. 1 Publication1
Mutagenesisi530D → N: Little or no effect on calcium channel activity. 1 Publication1
Mutagenesisi531N → Q: No effect on activation by low pH. 1 Publication1
Mutagenesisi533N → Q: Loss of activation by low pH. 1 Publication1
Mutagenesisi560I → F: Loss of channel activity. 1 Publication1
Mutagenesisi568K → A: Increases localization at the cell surface when expressed in absence of PKD1. 1 Publication1
Mutagenesisi576D → A: Induces localization to the endoplasmic reticulum when expressed in absence of PKD1. 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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004255511 – 760Polycystic kidney disease 2-like 1 proteinAdd BLAST760

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi38S-palmitoyl cysteineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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>Glycosylationi177N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Glycosylationi207N-linked (GlcNAc...) asparagineCombined sources1 Publication1
<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 bondi210 ↔ 223Combined sources1 Publication
Glycosylationi241N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Glycosylationi505N-linked (GlcNAc...) asparagineSequence analysis1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Palmitoylation is important for expression at the cell membrane and for channel activity.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Proteomic databases

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

More...
PaxDbi
A2A259

PeptideAtlas

More...
PeptideAtlasi
A2A259

PRoteomics IDEntifications database

More...
PRIDEi
A2A259

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
A2A259

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

More...
PhosphoSitePlusi
A2A259

<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

Detected in kidney, testis and brain, (PubMed:25820328). Expressed in all 4 taste areas in taste buds. Detected in the taste pore region of circumvallate papillae, foliate papillae, fungiform papillae and palate (PubMed:16891422, PubMed:16929298, PubMed:20538909, PubMed:21625513). Expressed in cells distinct from those mediating sweet, umami and bitter taste (at protein level) (PubMed:16891422). Expressed in type III taste cells (at protein level) (PubMed:18156604). Ubiquitous (PubMed:15548533). Detected in circumvallate, foliate, fungiform and palate taste buds, in cells distinct from those mediating sweet, umami and bitter taste (PubMed:16929298, PubMed:21625513). Detected in taste tissues and testis (PubMed:16891422).7 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000037578 Expressed in lumbar subsegment of spinal cord and 30 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
A2A259 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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotetramer (PubMed:25820328, PubMed:29567962). Heterotetramer with either PKD1L1, PKD1L3 or PKD1; the heterotetrameric complex probably contains 3 PKD1L2 chains plus one chain from another family member (PubMed:16891422, PubMed:15548533, PubMed:25820328, PubMed:29567962).

Interacts with PKD1L1, forming a ciliary calcium channel (PubMed:24336289).

Interacts with PKD1L3, forming a cation channel that is activated by low extracellular pH (PubMed:16891422, PubMed:18535624, PubMed:19464260, PubMed:20538909, PubMed:20406802, PubMed:22420714, PubMed:25820328, PubMed:29567962).

Interacts with PKD1 (PubMed:15548533).

Interacts with RACK1; inhibits the channel activity possibly by impairing localization to the cell membrane (By similarity).

By similarity10 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
236700, 1 interactor

Database of interacting proteins

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DIPi
DIP-61250N

Protein interaction database and analysis system

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IntActi
A2A259, 1 interactor

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000045675

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

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RNActi
A2A259 protein

<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

1760
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
A2A259

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%5Fand%5Fdomains%5Fsection">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>Domaini630 – 665EF-handPROSITE-ProRule annotationAdd BLAST36

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>Regioni701 – 760Required for homooligomerizationBy similarityAdd BLAST60

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili559 – 580Sequence analysisAdd BLAST22
Coiled coili650 – 682Sequence analysisAdd BLAST33

<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 EF-hand domain probably mediates calcium-binding. It is not required for channel activation.By similarity
Interaction of the cytoplasmic N- and C-terminal domains is important for channel activity.By similarity

<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 polycystin family.Curated

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3599 Eukaryota
ENOG410XTGE LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000157274

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_012097_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
A2A259

KEGG Orthology (KO)

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KOi
K04990

Identification of Orthologs from Complete Genome Data

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OMAi
PDPWGVQ

Database of Orthologous Groups

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OrthoDBi
426073at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
A2A259

TreeFam database of animal gene trees

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TreeFami
TF316484

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.20.120.350, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR011992 EF-hand-dom_pair
IPR002048 EF_hand_dom
IPR013122 PKD1_2_channel
IPR003915 PKD_2
IPR027359 Volt_channel_dom_sf

Pfam protein domain database

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Pfami
View protein in Pfam
PF08016 PKD_channel, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR01433 POLYCYSTIN2

Superfamily database of structural and functional annotation

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SUPFAMi
SSF47473 SSF47473, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50222 EF_HAND_2, 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%5Flength">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>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

A2A259-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNSMESPKNQ ELQTLGNRAW DNPAYSDPPS PNRTLRICTV SSVALPETQP
60 70 80 90 100
KKPEVRCQEK TQRTLVSSCC LHICRSIRGL WGTTLTENTA ENRELYVKTT
110 120 130 140 150
LRELVVYIVF LVDICLLTYG MTSSSAYYYT KVMSELFLHT PSDSGVSFQT
160 170 180 190 200
ISSMSDFWDF AQGPLLDSLY WTKWYNNQSL GRGSHSFIYY ENLLLGAPRL
210 220 230 240 250
RQLRVRNDSC VVHEDFREDI LNCYDVYSPD KEDQLPFGPQ NGTAWTYHSQ
260 270 280 290 300
NELGGSSHWG RLTSYSGGGY YLDLPGSRQA SAEALQGLQE GLWLDRGTRV
310 320 330 340 350
VFIDFSVYNA NINLFCILRL VVEFPATGGT IPSWQIRTVK LIRYVNNWDF
360 370 380 390 400
FIVGCEVVFC VFIFYYVVEE ILEIHLHRLR YLSSVWNILD LVVILLSIVA
410 420 430 440 450
VGFHIFRTLE VNRLMGKLLQ QPDTYADFEF LAFWQTQYNN MNAVNLFFAW
460 470 480 490 500
IKIFKYISFN KTMTQLSSTL ARCAKDILGF AIMFFIVFFA YAQLGYLLFG
510 520 530 540 550
TQVENFSTFV KCIFTQFRII LGDFDYNAID NANRILGPVY FVTYVFFVFF
560 570 580 590 600
VLLNMFLAII NDTYSEVKEE LAGQKDQLQL SDFLKQSYNK TLLRLRLRKE
610 620 630 640 650
RVSDVQKVLK GGEPEIQFED FTSTLRELGH EEHEITAAFT RFDQDGDHIL
660 670 680 690 700
DEEEQEQMRQ GLEEERVTLN AEIENLGRSV GHSPPGELGA EAARGQSWVS
710 720 730 740 750
GEEFDMLTRR VLQLQCVLEG VVSQIDAVGS KLKMLERKGE LAPSPGMGEP
760
AVWENLYNPS
Length:760
Mass (Da):87,234
Last modified:February 20, 2007 - 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:i4C76777051CFC2EF
GO

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 conflicti114I → V in AAK58371 (Ref. 2) Curated1
Sequence conflicti114I → V in AAI16324 (PubMed:15489334).Curated1
Sequence conflicti114I → V in AAI16298 (PubMed:15489334).Curated1
Sequence conflicti202 – 203QL → HV in AAK58371 (Ref. 2) Curated2
Sequence conflicti438Y → D in AAK58371 (Ref. 2) Curated1
Sequence conflicti482I → V in AAK58371 (Ref. 2) Curated1
Sequence conflicti756L → P in AAI16324 (PubMed:15489334).Curated1
Sequence conflicti756L → P in AAI16298 (PubMed:15489334).Curated1

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
AB290927 mRNA Translation: BAF45380.1
AF271381 mRNA Translation: AAK58371.1
AC125101 Genomic DNA No translation available.
BC116297 mRNA Translation: AAI16298.1
BC116323 mRNA Translation: AAI16324.2

The Consensus CDS (CCDS) project

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CCDSi
CCDS29846.1

NCBI Reference Sequences

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RefSeqi
NP_852087.2, NM_181422.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000042026; ENSMUSP00000045675; ENSMUSG00000037578

Database of genes from NCBI RefSeq genomes

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GeneIDi
329064

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:329064

UCSC genome browser

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UCSCi
uc008hpm.2 mouse

<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
AB290927 mRNA Translation: BAF45380.1
AF271381 mRNA Translation: AAK58371.1
AC125101 Genomic DNA No translation available.
BC116297 mRNA Translation: AAI16298.1
BC116323 mRNA Translation: AAI16324.2
CCDSiCCDS29846.1
RefSeqiNP_852087.2, NM_181422.3

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
5Z1Welectron microscopy3.38A/B/C/D64-629[»]
SMRiA2A259
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi236700, 1 interactor
DIPiDIP-61250N
IntActiA2A259, 1 interactor
STRINGi10090.ENSMUSP00000045675

Protein family/group databases

TCDBi1.A.5.2.2 the polycystin cation channel (pcc) family

PTM databases

iPTMnetiA2A259
PhosphoSitePlusiA2A259

Proteomic databases

PaxDbiA2A259
PeptideAtlasiA2A259
PRIDEiA2A259

Protocols and materials databases

Antibodypedia a portal for validated antibodies

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Antibodypediai
31169 127 antibodies

Genome annotation databases

EnsembliENSMUST00000042026; ENSMUSP00000045675; ENSMUSG00000037578
GeneIDi329064
KEGGimmu:329064
UCSCiuc008hpm.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
9033
MGIiMGI:1352448 Pkd2l1

Phylogenomic databases

eggNOGiKOG3599 Eukaryota
ENOG410XTGE LUCA
GeneTreeiENSGT00940000157274
HOGENOMiCLU_012097_0_0_1
InParanoidiA2A259
KOiK04990
OMAiPDPWGVQ
OrthoDBi426073at2759
PhylomeDBiA2A259
TreeFamiTF316484

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

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BioGRID-ORCSi
329064 3 hits in 12 CRISPR screens

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

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ChiTaRSi
Pkd2l1 mouse

Protein Ontology

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PROi
PR:A2A259
RNActiA2A259 protein

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000037578 Expressed in lumbar subsegment of spinal cord and 30 other tissues
GenevisibleiA2A259 MM

Family and domain databases

Gene3Di1.20.120.350, 1 hit
InterProiView protein in InterPro
IPR011992 EF-hand-dom_pair
IPR002048 EF_hand_dom
IPR013122 PKD1_2_channel
IPR003915 PKD_2
IPR027359 Volt_channel_dom_sf
PfamiView protein in Pfam
PF08016 PKD_channel, 1 hit
PRINTSiPR01433 POLYCYSTIN2
SUPFAMiSSF47473 SSF47473, 1 hit
PROSITEiView protein in PROSITE
PS50222 EF_HAND_2, 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 nameiPK2L1_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: A2A259
Secondary accession number(s): Q14B55, Q14B73, Q80ZH4
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 19, 2014
Last sequence update: February 20, 2007
Last modified: June 17, 2020
This is version 95 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, 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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