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Entry version 127 (17 Jun 2020)
Sequence version 2 (25 Jan 2012)
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Protein

Serine/threonine-protein phosphatase 2B catalytic subunit

Gene

tax-6

Organism
Caenorhabditis elegans
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

Calcium-dependent, calmodulin-stimulated protein phosphatase (PubMed:12221132, PubMed:16481400, PubMed:22300764, PubMed:23805378). Dephosphorylates arrd-17 (PubMed:22300764). Dephosphorylates daf-16 at 'Ser-319' which regulates daf-16 nuclear translocation (PubMed:23805378). Dephosphorylates calcium permeable cation channel pkd-2 at 'Ser-534' (PubMed:16481400). Regulates male mating behavior including response to hermaphrodite contact and vulva location and localization of pkd-2 to neuronal cilium (PubMed:16481400). Negatively regulates several sensory behaviors including thermotaxis in ADF neurons, osmosensation in ASH neurons, olfaction adaptation in AWC neurons and sensitivity to CO2 levels (PubMed:18524955, PubMed:11879652). Plays a role in modulating temperature-dependent calcium responses in AFD neurons and together with tax-6 inhibitor rcan-1 regulates thermotaxis in AFD neurons (PubMed:26232604). Regulates expression of rcan-1 (PubMed:12684004). In response to changes in intracellular calcium levels may also regulate nuclear translocation of transcriptional regulators such as crtc-1 (PubMed:26232604). Plays a role in egg-laying, body-size, fertility, growth, movement and cuticle development (PubMed:12684004, PubMed:15522306, PubMed:17113567, PubMed:22300764, PubMed:27871170). Negatively regulates lifespan (PubMed:19279398). Promotes transcription activator crtc-1 nuclear localization, probably by dephosphorylating crtc-1 and thereby negatively regulates lifespan (PubMed:21331044). Regulates expression of chemoreceptor srt-2 in AWC neurons probably downstream of Ser/Thr kinase kin-29 (PubMed:17113567). Negatively regulates nicotinic acetylcholine receptor (nAChR) sensitivity to nicotine (PubMed:15990870). Plays a role in several endocytic processes including in coelomocyte endocytosis, intestine apical endocytosis and synaptic vesicle recycling (PubMed:20803083, PubMed:21345307). May negatively regulate excitatory GABA receptor exp-1 during enteric muscle contraction (PubMed:16084527). May negatively regulate autophagy (PubMed:19279398).17 Publications

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

Protein has several cofactor binding sites:

<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

Activated by Ca2+-bound calmodulin following an increase in intracellular Ca2+ (By similarity). At low Ca2+ concentrations, the catalytic subunit (also known as calcineurin A) is inactive and is bound to the regulatory subunit (also known as calcineurin B) in which only two high-affinity binding sites are occupied by Ca2+ (PubMed:12221132). In response to elevated calcium levels, the occupancy of the low-affinity sites on calcineurin B by Ca2+ causes a conformational change of the C-terminal regulatory domain of calcineurin A, resulting in the exposure of the calmodulin-binding domain and in the partial activation of calcineurin A (PubMed:12221132). The subsequent binding of Ca2+-bound calmodulin leads to the displacement of the autoinhibitory domain from the active site and possibly of the autoinhibitory segment from the substrate binding site which fully activates calcineurin A (By similarity). Inhibited by immunosuppressant cyclosporin A (CsA) (PubMed:12221132).By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi115IronBy similarity1
Metal bindingi117Iron; via tele nitrogenBy similarity1
Metal bindingi143IronBy similarity1
Metal bindingi143ZincBy similarity1
Metal bindingi175ZincBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei176Proton donorBy similarity1
Metal bindingi224Zinc; via tele nitrogenBy similarity1
Metal bindingi306Zinc; via pros nitrogenBy 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 functionCalmodulin-binding, Hydrolase, Protein phosphatase
Biological processBehavior, Chemotaxis, Endocytosis
LigandIron, Metal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-CEL-2871809 FCERI mediated Ca+2 mobilization
R-CEL-4086398 Ca2+ pathway
R-CEL-5607763 CLEC7A (Dectin-1) induces NFAT activation

<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:
Serine/threonine-protein phosphatase 2B catalytic subunitCurated (EC:3.1.3.16UniRule annotation4 Publications)
Alternative name(s):
Abnormal chemotaxis protein 6Imported
Calmodulin-dependent calcineurin subunit A1 Publication
<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:tax-6Imported
Synonyms:cna-1Imported
ORF Names:C02F4.2Imported
<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>OrganismiCaenorhabditis elegansImported
<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 identifieri6239 [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 lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditinaRhabditomorphaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
<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
  • UP000001940 <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 IV

Organism-specific databases

WormBase

More...
WormBasei
C02F4.2a ; CE07853 ; WBGene00006527 ; tax-6
C02F4.2b ; CE52450 ; WBGene00006527 ; tax-6
C02F4.2c ; CE46586 ; WBGene00006527 ; tax-6

<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

Cell projection, 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

Shorter body length and reduced serotinin-induced egg laying as compared to wild-type (PubMed:27871170). Reduced calcium responses in AFD neurons upon a temperature increase from 16 to 20 degrees Celsius as compared to wild-type. At 17 degrees Celsius displays thermophilic behavior, preferentially migrating towards hotter regions (PubMed:26232604). RNAi-mediated knockdown results in an increase in lifespan (PubMed:21331044, PubMed:23805378). Also causes nuclear exclusion of crtc-1 (PubMed:21331044).4 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>Mutagenesisi259D → N in p675; impaired thermotaxis and chemotaxis towards NaCl, hypersensitivity to low osmotic conditions, enhanced olfactory adaptation to isoamyl alcohol. Slow growth rate and body is smaller and slender with a transparent appearance resulting from a thinner cuticle. Reduced brood size associated with egg retention. Partially resistant to serotonin-induced egg laying. Increased susceptibility to nicotine-mediated paralysis. Impaired mating behavior and reduced localization of pkd-2 to neuronal cilium. Impaired CO2 avoidance. Impaired coelomocyte endocytosis, apical endocytosis in intestine and recycling of synaptic vesicles at synapses. 7 Publications1

<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_00004369041 – 542Serine/threonine-protein phosphatase 2B catalytic subunitCuratedAdd BLAST542

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q0G819

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

More...
PaxDbi
Q0G819

PeptideAtlas

More...
PeptideAtlasi
Q0G819

<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 head and tail neurons, ventral nerve cord, body wall and vulva muscles, sperm and spermatheca (PubMed:12221132). Expressed in hypodermal seam cells (PubMed:15522306). Expressed in intestinal and anal depressor muscles (PubMed:16084527). In male, expressed in CEM, HOB and ray RnB neurons (PubMed:16481400). Isoform a: Expressed in thermosensory ADF neurons, chemosensory ASE, AWA and AWC neurons, osmosensory ASH neurons and AIY and AIZ interneurons (PubMed:11879652). Expressed in body wall, vulva and pharyngeal muscles (PubMed:11879652).5 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

Expressed in embryos and at all larval stages.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
WBGene00006527 Expressed in multi-cellular organism and 3 other tissues

<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

Forms a complex composed of a calmodulin-dependent catalytic subunit tax-6 (also known as calcineurin A) and a regulatory Ca2+-binding subunit cnb-1 (also known as calcineurin B) (PubMed:12221132). In response to an increase in Ca2+ intracellular levels, forms a complex composed of tax-6, cnb-1 and cmd-1/calmodulin (By similarity).

Interacts with cmd-1/calmodulin in a Ca2+-dependent manner (PubMed:17854888).

Interacts (via catalytic domain) with rcan-1; the interaction is calcium-dependent and inhibits tax-6 catalytic activity (PubMed:12684004, PubMed:26232604).

Interacts with exp-1; the interaction is calcium and cnb-1-independent (PubMed:16084527).

Interacts with arrd-17 (PubMed:22300764).

Interacts with kin-29 (PubMed:17113567).

Interacts with cnp-2 (PubMed:18593529).

Interacts with daf-16 (PubMed:23805378).

Interacts with dyn-1 (PubMed:20803083).

By similarity10 Publications

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>Sitei377Interaction with PxVP motif in substrateBy similarity1

<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

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-1128 Calcineurin-Calmodulin complex

Database of interacting proteins

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DIPi
DIP-25135N

Protein interaction database and analysis system

More...
IntActi
Q0G819, 5 interactors

Molecular INTeraction database

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MINTi
Q0G819

STRING: functional protein association networks

More...
STRINGi
6239.C02F4.2c

<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

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>Regioni81 – 365CatalyticCuratedAdd BLAST285
Regioni352 – 361Interaction with PxIxIF motif in substrateBy similarity10
Regioni366 – 394Calcineurin B bindingBy similarityAdd BLAST29
Regioni418 – 432Calmodulin-bindingBy similarityAdd BLAST15
Regioni433 – 440Autoinhibitory segmentBy similarity8
Regioni490 – 512Autoinhibitory domainBy similarityAdd BLAST23

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>Motifi332 – 336SAPNY motifBy similarity5

<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 autoinhibitory domain prevents access to the catalytic site.By similarity
The autoinhibitory segment prevents access to the substrate binding site.By similarity
Possible isomerization of Pro-334 within the SAPNY motif triggers a conformation switch which affects the organization and thus accessibility of the active site and the substrate binding region (PxIxIF motif). The trans- to cis-transition may favor calcineurin A activation and substrate binding. The reverse cis- to trans-transition may be enhanced by peptidyl-prolyl isomerases such as PPIA.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 PPP phosphatase family. PP-2B subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0375 Eukaryota
COG0639 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000154115

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q0G819

KEGG Orthology (KO)

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KOi
K04348

Identification of Orthologs from Complete Genome Data

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OMAi
WSLKIWY

Family and domain databases

Conserved Domains Database

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CDDi
cd07416 MPP_PP2B, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.60.21.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR004843 Calcineurin-like_PHP_ApaH
IPR029052 Metallo-depent_PP-like
IPR041751 MPP_PP2B
IPR043360 PP2B
IPR006186 Ser/Thr-sp_prot-phosphatase

The PANTHER Classification System

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PANTHERi
PTHR45673 PTHR45673, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00149 Metallophos, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00114 STPHPHTASE

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00156 PP2Ac, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00125 SER_THR_PHOSPHATASE, 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>Sequences (3)i

<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.

This entry describes 3 <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. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform cImported (identifier: Q0G819-1) [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
MASTSAGQNS AAKPDTTNTT TTASNNNRER ERDLKQFTER FVKTVQFPVS
60 70 80 90 100
ERLTVDQVYD RRTGKPRHEV LRDHFIKEGR IEEEAAIRVI QECSSLFRNE
110 120 130 140 150
KTMLEIEAPV TVCGDIHGQF YDLMKLFEVG GSPATTKYLF LGDYVDRGYF
160 170 180 190 200
SIECVLYLWA LKICYPTTLF LLRGNHECRH LTEYFTFKQE CKIKYSERVY
210 220 230 240 250
DVCMESFDAL PLAALMNQQF LCVHGGLSPE IHTLEDIRRI DRFKEPPAFG
260 270 280 290 300
PMCDLLWSDP LEDFGNERNS EQFSHNSVRG CSYFYSYAAC CDFLQHNNLL
310 320 330 340 350
SIIRAHEAQD AGYRMYRKSQ ATGFPSLITI FSAPNYLDVY NNKAAILKYE
360 370 380 390 400
NNVMNIRQFN CSPHPYWLPN FMDVFTWSLP FVGEKVTEML VHILNICSDD
410 420 430 440 450
ELMAECDDTF EGGVGSARKE VIRHKIRAIG KMARAFSVLR HESESVLQLK
460 470 480 490 500
GLNAGGKLPQ GALSEGRTGL NAAYRIEQSV AAESGCDSGH LIQSFEEARR
510 520 530 540
LDKINERMPP TMATPPAQSP SQSPIPSRQT TPQPPQNGPS NS
Length:542
Mass (Da):61,505
Last modified:January 25, 2012 - v2
<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:i60983B8A0C504883
GO
Isoform aImported (identifier: Q0G819-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     441-441: H → E
     448-479: QLKGLNAGGKLPQGALSEGRTGLNAAYRIEQS → ALKGLTPTGALPMGTLQGGSRGVRE

Show »
Length:535
Mass (Da):60,666
Checksum:iFC0363809D04103E
GO
Isoform bImported (identifier: Q0G819-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     413-450: GVGSARKEVI...HESESVLQLK → ADGKWIFPYP...IFYQTFFGTP
     451-542: Missing.

Show »
Length:450
Mass (Da):52,057
Checksum:iEC01B58E6C8F3E43
GO

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_058441413 – 450GVGSA…VLQLK → ADGKWIFPYPPHTGDVCLTI RFSFIFSLIFYQTFFGTP in isoform b. Add BLAST38
Alternative sequenceiVSP_058442441H → E in isoform a. Curated1
Alternative sequenceiVSP_058443448 – 479QLKGL…RIEQS → ALKGLTPTGALPMGTLQGGS RGVRE in isoform a. Add BLAST32
Alternative sequenceiVSP_058444451 – 542Missing in isoform b. CuratedAdd BLAST92

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
BX284604 Genomic DNA Translation: CAB02719.1
BX284604 Genomic DNA Translation: CAD88213.2
BX284604 Genomic DNA Translation: CAL36491.2

Protein sequence database of the Protein Information Resource

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PIRi
T18864

NCBI Reference Sequences

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RefSeqi
NP_001021292.1, NM_001026121.1 [Q0G819-2]
NP_001021293.2, NM_001026122.3
NP_001076658.2, NM_001083189.4 [Q0G819-1]

Genome annotation databases

Ensembl metazoan genome annotation project

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EnsemblMetazoai
C02F4.2a.1; C02F4.2a.1; WBGene00006527 [Q0G819-2]
C02F4.2b.1; C02F4.2b.1; WBGene00006527
C02F4.2c.1; C02F4.2c.1; WBGene00006527 [Q0G819-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
177943

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
cel:CELE_C02F4.2

UCSC genome browser

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UCSCi
C02F4.2c c. elegans [Q0G819-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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
BX284604 Genomic DNA Translation: CAB02719.1
BX284604 Genomic DNA Translation: CAD88213.2
BX284604 Genomic DNA Translation: CAL36491.2
PIRiT18864
RefSeqiNP_001021292.1, NM_001026121.1 [Q0G819-2]
NP_001021293.2, NM_001026122.3
NP_001076658.2, NM_001083189.4 [Q0G819-1]

3D structure databases

Database of comparative protein structure models

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ModBasei
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SWISS-MODEL Interactive Workspace

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SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein-protein interaction databases

ComplexPortaliCPX-1128 Calcineurin-Calmodulin complex
DIPiDIP-25135N
IntActiQ0G819, 5 interactors
MINTiQ0G819
STRINGi6239.C02F4.2c

Proteomic databases

EPDiQ0G819
PaxDbiQ0G819
PeptideAtlasiQ0G819

Genome annotation databases

EnsemblMetazoaiC02F4.2a.1; C02F4.2a.1; WBGene00006527 [Q0G819-2]
C02F4.2b.1; C02F4.2b.1; WBGene00006527
C02F4.2c.1; C02F4.2c.1; WBGene00006527 [Q0G819-1]
GeneIDi177943
KEGGicel:CELE_C02F4.2
UCSCiC02F4.2c c. elegans [Q0G819-1]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
177943
WormBaseiC02F4.2a ; CE07853 ; WBGene00006527 ; tax-6
C02F4.2b ; CE52450 ; WBGene00006527 ; tax-6
C02F4.2c ; CE46586 ; WBGene00006527 ; tax-6

Phylogenomic databases

eggNOGiKOG0375 Eukaryota
COG0639 LUCA
GeneTreeiENSGT00940000154115
InParanoidiQ0G819
KOiK04348
OMAiWSLKIWY

Enzyme and pathway databases

ReactomeiR-CEL-2871809 FCERI mediated Ca+2 mobilization
R-CEL-4086398 Ca2+ pathway
R-CEL-5607763 CLEC7A (Dectin-1) induces NFAT activation

Miscellaneous databases

Protein Ontology

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PROi
PR:Q0G819

Gene expression databases

BgeeiWBGene00006527 Expressed in multi-cellular organism and 3 other tissues

Family and domain databases

CDDicd07416 MPP_PP2B, 1 hit
Gene3Di3.60.21.10, 1 hit
InterProiView protein in InterPro
IPR004843 Calcineurin-like_PHP_ApaH
IPR029052 Metallo-depent_PP-like
IPR041751 MPP_PP2B
IPR043360 PP2B
IPR006186 Ser/Thr-sp_prot-phosphatase
PANTHERiPTHR45673 PTHR45673, 1 hit
PfamiView protein in Pfam
PF00149 Metallophos, 1 hit
PRINTSiPR00114 STPHPHTASE
SMARTiView protein in SMART
SM00156 PP2Ac, 1 hit
PROSITEiView protein in PROSITE
PS00125 SER_THR_PHOSPHATASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiPP2B_CAEEL
<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: Q0G819
Secondary accession number(s): Q86MD4, Q95002
<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: July 6, 2016
Last sequence update: January 25, 2012
Last modified: June 17, 2020
This is version 127 of the entry and version 2 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 programCaenorhabditis annotation project

<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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
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