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Entry version 170 (16 Jan 2019)
Sequence version 2 (01 Jul 1993)
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Protein

Agrin

Gene

Agrn

Organism
Rattus norvegicus (Rat)
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

Isoform 1: heparan sulfate basal lamina glycoprotein that plays a central role in the formation and the maintenance of the neuromuscular junction (NMJ) and directs key events in postsynaptic differentiation. This neuron-specific (z+) isoform is a component of the AGRN-LRP4 receptor complex that induces the phosphorylation and activation of MUSK. The activation of MUSK in myotubes induces the formation of NMJ by regulating different processes including the transcription of specific genes and the clustering of AChR in the postsynaptic membrane. Calcium ions are required for maximal AChR clustering. AGRN function in neurons is highly regulated by alternative splicing, glycan binding and proteolytic processing. Modulates calcium ion homeostasis in neurons, specifically by inducing an increase in cytoplasmic calcium ions. Functions differentially in the central nervous system (CNS) by inhibiting the alpha3-subtype of Na+/K+-ATPase and evoking depolarization at CNS synapses. This transmembrane agrin (TM-agrin) isoform, the predominate form in neurons of the brain, induces dendritic filopodia and synapse formation in mature hippocampal neurons in large part due to the attached glycosaminoglycan chains and the action of Rho-family GTPases.
Isoform 1, isoform 4, isoform 5 and isoform 6: neuron-specific (z+) isoforms that contain C-terminal insertions of 8-19 AA are potent activators of AChR clustering. Isoform 5, agrin (z+8), containing the 8-AA insert, forms a receptor complex in myotubules containing the neuronal AGRN, the muscle-specific kinase MUSK and LRP4, a member of the LDL receptor family. The splicing factors, NOVA1 and NOVA2, regulate AGRN splicing and production of the 'z' isoforms.
Agrin N-terminal 110 kDa subunit: is involved in regulation of neurite outgrowth probably due to the presence of the glycosaminoglcan (GAG) side chains of heparan and chondroitin sulfate attached to the Ser/Thr- and Gly/Ser-rich regions. Also involved in modulation of growth factor signaling (By similarity).By similarity8 Publications
Agrin C-terminal 22 kDa fragment: this released fragment is important for agrin signaling and to exert a maximal dendritic filopodia-inducing effect. All 'z' splice variants (z+) of this fragment also show an increase in the number of filopodia.

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>Sitei1143Alternative splice site to produce 'x' isoforms1
Sitei1642Alternative splice site to produce 'y' isoforms1
Sitei1753Critical for cleavage by neurotrypsin1
Sitei1779Alternative splice site to produce 'z' isoforms1
Sitei1783Highly important for the agrin receptor complex activity of the 'z(8)' insert1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi1831 – 1900Add BLAST70

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

GO - Biological processi

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

Molecular functionDevelopmental protein
Biological processDifferentiation
LigandCalcium

<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:
Agrin
Cleaved into the following 4 chains:
<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:Agrn
Synonyms:Agrin
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <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: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
2067 Agrn

<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 – 26CytoplasmicSequence analysisAdd BLAST26
<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>Transmembranei27 – 47Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini48 – 1959ExtracellularSequence analysisAdd BLAST1912

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Synapse

<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

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>Mutagenesisi566 – 571SGGSGS → AGGAGA: Abolishes heparan sulfate (HS) binding, greatly reduced branched retraction fiber (BRF) formation, filopodia formation reduced by about 50% and lowered RAC1 and CDK1 activation. No chondroitin sulfate (CS) nor heparan sulfate attachment, almost no branched retraction fiber (BRF) formation, filopodia formation reduced by about 60% and lowered RAC1 and CDK1 activation; when associated with 953-AGA-955. 6
Mutagenesisi953 – 955SGS → AGA: Abolishes chondroitin sulfate (CS) binding, greatly reduced branched retraction fiber (BRF) formation, filopodia formation reduced by about 50% and lowered RAC1 and CDK1 activation. No chondroitin sulfate (CS) nor heparan sulfate (HS) binding almost no retraction fiber (BRF) formation, filopodia formation reduced by about 60% lowered RAC1 and CDK1 activation; when associated with 566-AGGAGA-571. 3
Mutagenesisi991P → A: About 13% reduction in cleavage by neurotrypsin. 1 Publication1
Mutagenesisi992P → A: About 64% reduction in cleavage by neurotrypsin. 1 Publication1
Mutagenesisi993I → A: About 60% reduction in cleavage by neurotrypsin. 1 Publication1
Mutagenesisi994E → A: Almost completely abolishes cleavage by neurotrypsin. 1 Publication1
Mutagenesisi995R → A: Completely abolishes cleavage by neurotrypsin. 1 Publication1
Mutagenesisi995R → K: About 30% reduction in cleavage by neurotrypsin. 1 Publication1
Mutagenesisi1726S → A: Abolishes fucosylation of muscle agrin. Stimulates MUSK phosphorylation and increases AChR clustering. 1 Publication1
Mutagenesisi1751L → A: About 23% reduction in cleavage by neurotrypsin. Reduces cleavage by neurotrypsin by about 90%; when associated with A-1752. Completely abolishes cleavage by neurotrypsin; when associated with A-1753. 1 Publication1
Mutagenesisi1752V → A: About 41% reduction in cleavage by neurotrypsin. Reduces cleavage by neurotrypsin by about 90%; when associated with A-1751. Completely abolishes cleavage by neurotrypsin; when associated with A-1753. 1 Publication1
Mutagenesisi1753E → A or K: Almost completely abolishes cleavage by neurotrypsin. Completely abolishes cleavage by neurotrypsin; when associated with A-1751 or A-1752. 1 Publication1
Mutagenesisi1753E → D, L or Q: About 20% reduction in cleavage by neurotrypsin. 1 Publication1
Mutagenesisi1754K → A: Completely abolishes cleavage by neurotrypsin. 1 Publication1
Mutagenesisi1754K → R: About 55% reduction in cleavage by neurotrypsin. 1 Publication1
Mutagenesisi1755S → A: About 62% reduction in cleavage by neurotrypsin. 1 Publication1
Mutagenesisi1756V → A: Slight reduction in cleavage by neurotrypsin. 1 Publication1
Mutagenesisi1757G → A: Slight reduction in cleavage by neurotrypsin. 1 Publication1
Mutagenesisi1780E → A: Slight reduction in AChR clustering ability. 1 Publication1
Mutagenesisi1781L → A: Slight reduction in AChR clustering ability. Slight reduction in AChR clustering ability. 1 Publication1
Mutagenesisi1782T → A: Slight reduction in AChR clustering ability. 1 Publication1
Mutagenesisi1783N → A: Abolishes formation of AGRN-LRP4 complex and MUSK activation. No AChR clustering activity. 2 Publications1
Mutagenesisi1784E → A: Significant reduction in AChR clustering ability. 1 Publication1
Mutagenesisi1785I → A: Significant reduction in AChR clustering ability. 2 Publications1
Mutagenesisi1785I → S: Abolishes formation of AGRN-LRP4 complex and MUSK activation. 2 Publications1
Mutagenesisi1786P → A: Significant reduction in AChR clustering ability. 1 Publication1
Mutagenesisi1806H → L: No effect on formation of AGRN-LRP4 complex nor on MUSK activation. 1 Publication1
Mutagenesisi1831D → A: Abolishes calcium binding, lowering of binding to myotubes and some loss of AChR clustering activity; when associated with A-1900. 1 Publication1
Mutagenesisi1876R → E: No effect formation of AGRN-LRP4 complex nor on MUSK activation. 1 Publication1
Mutagenesisi1900D → A: Abolishes calcium binding, lowering of binding to myotubes and some loss of AChR clustering activity; when associated with A-1831. 1 Publication1
Mutagenesisi1938H → L: No effect formation of AGRN-LRP4 complex nor on MUSK activation. 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_00000074721 – 1959AgrinAdd BLAST1959
ChainiPRO_000042162127 – 995Agrin N-terminal 110 kDa subunitAdd BLAST969
ChainiPRO_0000421622996 – 1959Agrin C-terminal 110 kDa subunitAdd BLAST964
ChainiPRO_0000421623996 – 1754Agrin C-terminal 90 kDa fragmentAdd BLAST759
ChainiPRO_00004216241755 – 1959Agrin C-terminal 22 kDa fragmentAdd BLAST205

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 bondi92 ↔ 123PROSITE-ProRule annotation
Disulfide bondi97 ↔ 116PROSITE-ProRule annotation
Disulfide bondi105 ↔ 137PROSITE-ProRule annotation
<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>Glycosylationi145N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi165 ↔ 198PROSITE-ProRule annotation
Disulfide bondi171 ↔ 191PROSITE-ProRule annotation
Disulfide bondi180 ↔ 212PROSITE-ProRule annotation
Disulfide bondi244 ↔ 263PROSITE-ProRule annotation
Disulfide bondi252 ↔ 284PROSITE-ProRule annotation
Disulfide bondi309 ↔ 342PROSITE-ProRule annotation
Disulfide bondi316 ↔ 335PROSITE-ProRule annotation
Disulfide bondi324 ↔ 356PROSITE-ProRule annotation
Disulfide bondi385 ↔ 415PROSITE-ProRule annotation
Disulfide bondi389 ↔ 408PROSITE-ProRule annotation
Disulfide bondi397 ↔ 429PROSITE-ProRule annotation
Disulfide bondi448 ↔ 480PROSITE-ProRule annotation
Disulfide bondi454 ↔ 473PROSITE-ProRule annotation
Disulfide bondi462 ↔ 494PROSITE-ProRule annotation
Disulfide bondi508 ↔ 545PROSITE-ProRule annotation
Disulfide bondi518 ↔ 538PROSITE-ProRule annotation
Disulfide bondi527 ↔ 559PROSITE-ProRule annotation
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei569PhosphoserineBy similarity1
Modified residuei571PhosphoserineBy similarity1
Disulfide bondi600 ↔ 631PROSITE-ProRule annotation
Disulfide bondi604 ↔ 624PROSITE-ProRule annotation
Disulfide bondi613 ↔ 645PROSITE-ProRule annotation
Glycosylationi672N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi688 ↔ 700By similarity
Disulfide bondi690 ↔ 707By similarity
Disulfide bondi709 ↔ 718By similarity
Disulfide bondi721 ↔ 739By similarity
Disulfide bondi742 ↔ 754By similarity
Disulfide bondi744 ↔ 761By similarity
Disulfide bondi763 ↔ 772By similarity
Disulfide bondi775 ↔ 786By similarity
Disulfide bondi816 ↔ 850PROSITE-ProRule annotation
Disulfide bondi823 ↔ 843PROSITE-ProRule annotation
Glycosylationi827N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi832 ↔ 864PROSITE-ProRule annotation
Glycosylationi957N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1224 ↔ 1235By similarity
Disulfide bondi1229 ↔ 1246By similarity
Disulfide bondi1248 ↔ 1257By similarity
Disulfide bondi1410 ↔ 1439By similarity
Disulfide bondi1483 ↔ 1494By similarity
Disulfide bondi1488 ↔ 1504By similarity
Disulfide bondi1506 ↔ 1515By similarity
Disulfide bondi1713 ↔ 1727By similarity
Disulfide bondi1721 ↔ 1736By similarity
Glycosylationi1726O-linked (Fuc...) serine1 Publication1
Disulfide bondi1738 ↔ 1747By similarity
Disulfide bondi1930 ↔ 1956By similarity

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

Contains heparan and chondroitin sulfate chains and alpha-dystroglycan as well as N-linked and O-linked oligosaccharides. Glycosaminoglycans (GAGs), present in the agrin N-terminal 110 kDa fragment, are required for induction of filopodia in hippocampal neurons. The first cluster (Gly/Ser-rich) for GAG attachment contains heparan sulfate (HS) chains and the second cluster (Ser/Thr-rich), contains chondroitin sulfate (CS) chains. Heparin and heparin sulfate binding in the G3 doamin is independent of calcium ions. Binds heparin with a stoichiometry of 2:1. Binds sialic acid with a stoichiometry of 1:1 and binding requires calcium ions.2 Publications
At synaptic junctions, cleaved at two conserved sites, alpha and beta, by neurotrypsin. Cleavage at the alpha-site produces the agrin N-terminal 110-kDa subunit and the agrin C-terminal 110-kDa subunit. Further cleavage of agrin C-terminal 110-kDa subunit at the beta site produces the C-terminal fragments, agrin C-terminal 90 kDa fragment and agrin C-terminal 22 kDa fragment. Excessive cleavage at the beta-site releases large amounts of the agrin C-terminal 22 kDa fragment leading to destabilization at the neuromuscular junction (NMJ).2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei995 – 996Cleavage, alpha site; by neurotrypsin2
Sitei1754 – 1755Cleavage, beta site; by neurotrypsin2

Keywords - PTMi

Disulfide bond, Glycoprotein, Heparan sulfate, Phosphoprotein, Proteoglycan

Proteomic databases

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

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PaxDbi
P25304

PRoteomics IDEntifications database

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PRIDEi
P25304

PTM databases

CarbonylDB database of protein carbonylation sites

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CarbonylDBi
P25304

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P25304

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

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PhosphoSitePlusi
P25304

SwissPalm database of S-palmitoylation events

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SwissPalmi
P25304

<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

Embryonic nervous system and muscle.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

More abundant early in development. At E13, highly expressed in the developing nervous system. Isoform y(+4)z(0), containing the 'y' insert but no 'z' insert, is the most prevelant at this stage with pronounced expression in developing spinal and sympathetic ganglia. Isoforms with no 'y' insert (y0) localized to peripheral tissue. At E15, y(+4) isoform continues to be highly expressed in neural tissue predominantly in the spinal column and developing brain. The y0 isoform is weakly expressed in capillaries and meninges and the y0(z0) in non-neural tissues, predominantly in epithelial cells lining the developing lung bronchioles and kidney tubules. Isoforms Z(+8) and z(+19) are highly expressed in ventral motor columns and facial nerve with weaker expression throughout spinal cord tissue. At later stages of development, isoform y(4)z(0) is the most prominent form in developing cortex, corpus striatum, hippocampus and cerebellum. Isoform y(0)z(0) expression is still detected in brain capillaries at stage P1. The z(+19) isoform is most highly expressed from E15 to E18 and declines slightly to P1. Isoforms y14z0 and y(+4)z(+8) are still expressed in adulthood, the former scattered throughout the spinal cord gray matter and, the latter, in motor neurons of the ventral spinal cord.2 Publications

<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

Monomer. Component of the AGRN-LRP4 complex that consists of a tetramer of two AGRN-LRP4 heterodimers. Interacts (via the laminin G-like 3 domain) directly with LRP4; the interaction is required for activation of MUSK and clustering of AChR and requires the 'z8' insert present in the z(+8) isoforms. Interacts (N-terminal subunit) with TGF-beta family members, BMP2 AND BMP4; the interactions inhibit the activity of these growth factors. Interacts with TGFB1; the interaction enhances the activity of TGFB1. Interacts with DAG1; the interaction is influenced by cell surface glycosaminoglycans and by alternative splicing of AGRN.4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
Lrp4Q8VI563EBI-2106099,EBI-2106160From Mus musculus.

GO - Molecular functioni

Protein-protein interaction databases

Protein interaction database and analysis system

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IntActi
P25304, 3 interactors

STRING: functional protein association networks

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STRINGi
10116.ENSRNOP00000050623

<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

11959
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
3V64X-ray2.85A/B1759-1959[»]
3V65X-ray3.30A/C1759-1959[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P25304

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

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SMRi
P25304

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini86 – 139Kazal-like 1PROSITE-ProRule annotationAdd BLAST54
Domaini159 – 214Kazal-like 2PROSITE-ProRule annotationAdd BLAST56
Domaini232 – 286Kazal-like 3PROSITE-ProRule annotationAdd BLAST55
Domaini303 – 358Kazal-like 4PROSITE-ProRule annotationAdd BLAST56
Domaini379 – 431Kazal-like 5PROSITE-ProRule annotationAdd BLAST53
Domaini442 – 496Kazal-like 6PROSITE-ProRule annotationAdd BLAST55
Domaini502 – 561Kazal-like 7PROSITE-ProRule annotationAdd BLAST60
Domaini594 – 647Kazal-like 8PROSITE-ProRule annotationAdd BLAST54
Domaini688 – 741Laminin EGF-like 1PROSITE-ProRule annotationAdd BLAST54
Domaini742 – 788Laminin EGF-like 2PROSITE-ProRule annotationAdd BLAST47
Domaini810 – 866Kazal-like 9PROSITE-ProRule annotationAdd BLAST57
Domaini1023 – 1145SEAPROSITE-ProRule annotationAdd BLAST123
Domaini1220 – 1258EGF-like 1PROSITE-ProRule annotationAdd BLAST39
Domaini1263 – 1439Laminin G-like 1PROSITE-ProRule annotationAdd BLAST177
Domaini1440 – 1477EGF-like 2PROSITE-ProRule annotationAdd BLAST38
Domaini1479 – 1516EGF-like 3PROSITE-ProRule annotationAdd BLAST38
Domaini1526 – 1708Laminin G-like 2PROSITE-ProRule annotationAdd BLAST183
Domaini1709 – 1748EGF-like 4PROSITE-ProRule annotationAdd BLAST40
Domaini1784 – 1956Laminin G-like 3PROSITE-ProRule annotationAdd BLAST173

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi565 – 572Gly/Ser-rich8
Compositional biasi857 – 948Ser/Thr-richAdd BLAST92
Compositional biasi953 – 960Gly/Ser-rich8
Compositional biasi971 – 977Gly/Ser-rich7
Compositional biasi1147 – 1214Ser/Thr-richAdd BLAST68
Compositional biasi1676 – 1690Gly/Ser-richAdd BLAST15

<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

Both laminin G-like 2 (G2) and laminin G-like 3 (G3) domains are required for alpha-dystroglycan binding. G3 domain is required for C-terminal heparin, heparan sulfate and sialic acid binding.

Keywords - Domaini

EGF-like domain, Laminin EGF-like domain, Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410ITSI Eukaryota
ENOG410YKSA LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000033860

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG080471

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P25304

KEGG Orthology (KO)

More...
KOi
K06254

Database of Orthologous Groups

More...
OrthoDBi
414294at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P25304

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.70.960, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR013320 ConA-like_dom_sf
IPR001881 EGF-like_Ca-bd_dom
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR003884 FacI_MAC
IPR003645 Fol_N
IPR002350 Kazal_dom
IPR036058 Kazal_dom_sf
IPR002049 Laminin_EGF
IPR001791 Laminin_G
IPR000082 SEA_dom
IPR036364 SEA_dom_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00008 EGF, 3 hits
PF00050 Kazal_1, 1 hit
PF07648 Kazal_2, 8 hits
PF00053 Laminin_EGF, 2 hits
PF00054 Laminin_G_1, 3 hits
PF01390 SEA, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00181 EGF, 6 hits
SM00179 EGF_CA, 3 hits
SM00180 EGF_Lam, 2 hits
SM00057 FIMAC, 3 hits
SM00274 FOLN, 5 hits
SM00280 KAZAL, 9 hits
SM00282 LamG, 3 hits
SM00200 SEA, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF100895 SSF100895, 9 hits
SSF49899 SSF49899, 3 hits
SSF82671 SSF82671, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00022 EGF_1, 6 hits
PS01186 EGF_2, 1 hit
PS50026 EGF_3, 4 hits
PS01248 EGF_LAM_1, 1 hit
PS50027 EGF_LAM_2, 2 hits
PS51465 KAZAL_2, 9 hits
PS50025 LAM_G_DOMAIN, 3 hits
PS50024 SEA, 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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (6+)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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 6 <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
Note: Many isoforms exist depending on the occurrence and length of inserts at the x, y or z splice site. There are 4 'z' isoforms produced with inserts of 0, 8, 11 or 19 AA. Isoforms differ in their acetylcholine receptor clustering activity and tissue specificity. In addition, a secreted isoform may be produced by alternative usage of the first exon.

This entry has 6 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P25304-1) [UniParc]FASTAAdd to basket
Also known as: Transmembrane agrin, TM-agrin, Agrin z(+19)

This isoform has been chosen as the 'canonical' 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
MPPLPLEHRP RQEPGASMLV RYFMIPCNIC LILLATSTLG FAVLLFLSNY
60 70 80 90 100
KPGIHFTPAP PTPPDVCRGM LCGFGAVCEP SVEDPGRASC VCKKNACPAT
110 120 130 140 150
VAPVCGSDAS TYSNECELQR AQCNQQRRIR LLRQGPCGSR DPCANVTCSF
160 170 180 190 200
GSTCVPSADG QTASCLCPTT CFGAPDGTVC GSDGVDYPSE CQLLSHACAS
210 220 230 240 250
QEHIFKKFNG PCDPCQGSMS DLNHICRVNP RTRHPEMLLR PENCPAQHTP
260 270 280 290 300
ICGDDGVTYE NDCVMSRIGA TRGLLLQKVR SGQCQTRDQC PETCQFNSVC
310 320 330 340 350
LSRRGRPHCS CDRVTCDGSY RPVCAQDGHT YNNDCWRQQA ECRQQRAIPP
360 370 380 390 400
KHQGPCDQTP SPCHGVQCAF GAVCTVKNGK AECECQRVCS GIYDPVCGSD
410 420 430 440 450
GVTYGSVCEL ESMACTLGRE IQVARRGPCD PCGQCRFGSL CEVETGRCVC
460 470 480 490 500
PSECVESAQP VCGSDGHTYA SECELHVHAC THQISLYVAS AGHCQTCGEK
510 520 530 540 550
VCTFGAVCSA GQCVCPRCEH PPPGPVCGSD GVTYLSACEL REAACQQQVQ
560 570 580 590 600
IEEAHAGPCE PAECGSGGSG SGEDDECEQE LCRQRGGIWD EDSEDGPCVC
610 620 630 640 650
DFSCQSVPRS PVCGSDGVTY GTECDLKKAR CESQQELYVA AQGACRGPTL
660 670 680 690 700
APLLPVAFPH CAQTPYGCCQ DNFTAAQGVG LAGCPSTCHC NPHGSYSGTC
710 720 730 740 750
DPATGQCSCR PGVGGLRCDR CEPGFWNFRG IVTDGHSGCT PCSCDPRGAV
760 770 780 790 800
RDDCEQMTGL CSCRPGVAGP KCGQCPDGQV LGHLGCEADP MTPVTCVEIH
810 820 830 840 850
CEFGASCVEK AGFAQCICPT LTCPEANSTK VCGSDGVTYG NECQLKAIAC
860 870 880 890 900
RQRLDISTQS LGPCQESVTP GASPTSASMT TPRHILSKTL PFPHNSLPLS
910 920 930 940 950
PGSTTHDWPT PLPISPHTTV SIPRSTAWPV LTVPPTAAAS DVTSLATSIF
960 970 980 990 1000
SESGSANGSG DEELSGDEEA SGGGSGGLEP PVGSIVVTHG PPIERASCYN
1010 1020 1030 1040 1050
SPLGCCSDGK TPSLDSEGSN CPATKAFQGV LELEGVEGQE LFYTPEMADP
1060 1070 1080 1090 1100
KSELFGETAR SIESTLDDLF RNSDVKKDFW SVRLRELGPG KLVRAIVDVH
1110 1120 1130 1140 1150
FDPTTAFQAS DVGQALLRQI QVSRPWALAV RRPLQEHVRF LDFDWFPTFF
1160 1170 1180 1190 1200
TGAATGTTAA MATARATTVS RLPASSVTPR VYPSHTSRPV GRTTAPPTTR
1210 1220 1230 1240 1250
RPPTTATNMD RPRTPGHQQP SKSCDSQPCL HGGTCQDQDS GKGFTCSCTA
1260 1270 1280 1290 1300
GRGGSVCEKV QPPSMPAFKG HSFLAFPTLR AYHTLRLALE FRALETEGLL
1310 1320 1330 1340 1350
LYNGNARGKD FLALALLDGR VQFRFDTGSG PAVLTSLVPV EPGRWHRLEL
1360 1370 1380 1390 1400
SRHWRQGTLS VDGETPVVGE SPSGTDGLNL DTNLYVGGIP EEQVAMVLDR
1410 1420 1430 1440 1450
TSVGVGLKGC IRMLDINNQQ LELSDWQRAA VQSSGVGECG DHPCLPNPCH
1460 1470 1480 1490 1500
GGALCQALEA GMFLCQCPPG RFGPTCADEK SPCQPNPCHG AAPCRVLSSG
1510 1520 1530 1540 1550
GAKCECPLGR SGTFCQTVLE TAGSRPFLAD FNGFSYLELK GLHTFERDLG
1560 1570 1580 1590 1600
EKMALEMVFL ARGPSGLLLY NGQKTDGKGD FVSLALHNRH LEFCYDLGKG
1610 1620 1630 1640 1650
AAVIRSKEPI ALGTWVRVFL ERNGRKGALQ VGDGPRVLGE SPKSRKVPHT
1660 1670 1680 1690 1700
MLNLKEPLYI GGAPDFSKLA RGAAVSSGFS GVIQLVSLRG HQLLTQEHVL
1710 1720 1730 1740 1750
RAVDVSPFAD HPCTQALGNP CLNGGSCVPR EATYECLCPG GFSGLHCEKG
1760 1770 1780 1790 1800
LVEKSVGDLE TLAFDGRTYI EYLNAVIESE LTNEIPAPET LDSRALFSEK
1810 1820 1830 1840 1850
ALQSNHFELS LRTEATQGLV LWIGKAAERA DYMALAIVDG HLQLSYDLGS
1860 1870 1880 1890 1900
QPVVLRSTVK VNTNRWLRIR AHREHREGSL QVGNEAPVTG SSPLGATQLD
1910 1920 1930 1940 1950
TDGALWLGGL QKLPVGQALP KAYGTGFVGC LRDVVVGHRQ LHLLEDAVTK

PELRPCPTP
Length:1,959
Mass (Da):208,646
Last modified:July 1, 1993 - 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:i7FEFDFDAFF89CC31
GO
Isoform 2 (identifier: P25304-2) [UniParc]FASTAAdd to basket
Also known as: Agrin x(0)

The sequence of this isoform differs from the canonical sequence as follows:
     1144-1152: Missing.

Show »
Length:1,950
Mass (Da):207,547
Checksum:iDA0C31258A7BE9E7
GO
Isoform 3 (identifier: P25304-3) [UniParc]FASTAAdd to basket
Also known as: Agrin z(0)

The sequence of this isoform differs from the canonical sequence as follows:
     1780-1798: Missing.

Show »
Length:1,940
Mass (Da):206,561
Checksum:i47D7E361C3169B25
GO
Isoform 4 (identifier: P25304-4) [UniParc]FASTAAdd to basket
Also known as: Agrin z(+11)

The sequence of this isoform differs from the canonical sequence as follows:
     1788-1798: Missing.

Show »
Length:1,948
Mass (Da):207,429
Checksum:i69C99FF177D5B036
GO
Isoform 5 (identifier: P25304-5) [UniParc]FASTAAdd to basket
Also known as: Agrin z(+8)

The sequence of this isoform differs from the canonical sequence as follows:
     1780-1787: Missing.

Show »
Length:1,951
Mass (Da):207,778
Checksum:i3BC18F7BCCE34FC2
GO
Isoform 6 (identifier: P25304-6) [UniParc]FASTAAdd to basket
Also known as: Agrin y(0)

The sequence of this isoform differs from the canonical sequence as follows:
     1643-1646: Missing.

Show »
Length:1,955
Mass (Da):208,146
Checksum:i8A100E409BFEEB51
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 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F1LPF2F1LPF2_RAT
Agrin
Agrn
1,941Annotation 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>
D4A2F1D4A2F1_RAT
Agrin
Agrn
1,940Annotation 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>

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 conflicti315 – 317Missing in AAA40702 (PubMed:1851019).Curated3

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_0013651144 – 1152Missing in isoform 2. 1 Publication9
Alternative sequenceiVSP_0457591643 – 1646Missing in isoform 6. Curated4
Alternative sequenceiVSP_0013661780 – 1798Missing in isoform 3. 2 PublicationsAdd BLAST19
Alternative sequenceiVSP_0013681780 – 1787Missing in isoform 5. 1 Publication8
Alternative sequenceiVSP_0013671788 – 1798Missing in isoform 4. 1 PublicationAdd BLAST11

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
M64780 mRNA Translation: AAA40702.1
M64780 mRNA Translation: AAA40703.1
S44194 mRNA Translation: AAB23326.1

Protein sequence database of the Protein Information Resource

More...
PIRi
JH0399 AGRT

NCBI Reference Sequences

More...
RefSeqi
NP_786930.1, NM_175754.1 [P25304-3]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Rn.2163

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
25592

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:25592

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
M64780 mRNA Translation: AAA40702.1
M64780 mRNA Translation: AAA40703.1
S44194 mRNA Translation: AAB23326.1
PIRiJH0399 AGRT
RefSeqiNP_786930.1, NM_175754.1 [P25304-3]
UniGeneiRn.2163

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3V64X-ray2.85A/B1759-1959[»]
3V65X-ray3.30A/C1759-1959[»]
ProteinModelPortaliP25304
SMRiP25304
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP25304, 3 interactors
STRINGi10116.ENSRNOP00000050623

PTM databases

CarbonylDBiP25304
iPTMnetiP25304
PhosphoSitePlusiP25304
SwissPalmiP25304

Proteomic databases

PaxDbiP25304
PRIDEiP25304

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25592
KEGGirno:25592

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
375790
RGDi2067 Agrn

Phylogenomic databases

eggNOGiENOG410ITSI Eukaryota
ENOG410YKSA LUCA
HOGENOMiHOG000033860
HOVERGENiHBG080471
InParanoidiP25304
KOiK06254
OrthoDBi414294at2759
PhylomeDBiP25304

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P25304

Family and domain databases

Gene3Di3.30.70.960, 1 hit
InterProiView protein in InterPro
IPR013320 ConA-like_dom_sf
IPR001881 EGF-like_Ca-bd_dom
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR003884 FacI_MAC
IPR003645 Fol_N
IPR002350 Kazal_dom
IPR036058 Kazal_dom_sf
IPR002049 Laminin_EGF
IPR001791 Laminin_G
IPR000082 SEA_dom
IPR036364 SEA_dom_sf
PfamiView protein in Pfam
PF00008 EGF, 3 hits
PF00050 Kazal_1, 1 hit
PF07648 Kazal_2, 8 hits
PF00053 Laminin_EGF, 2 hits
PF00054 Laminin_G_1, 3 hits
PF01390 SEA, 1 hit
SMARTiView protein in SMART
SM00181 EGF, 6 hits
SM00179 EGF_CA, 3 hits
SM00180 EGF_Lam, 2 hits
SM00057 FIMAC, 3 hits
SM00274 FOLN, 5 hits
SM00280 KAZAL, 9 hits
SM00282 LamG, 3 hits
SM00200 SEA, 1 hit
SUPFAMiSSF100895 SSF100895, 9 hits
SSF49899 SSF49899, 3 hits
SSF82671 SSF82671, 1 hit
PROSITEiView protein in PROSITE
PS00022 EGF_1, 6 hits
PS01186 EGF_2, 1 hit
PS50026 EGF_3, 4 hits
PS01248 EGF_LAM_1, 1 hit
PS50027 EGF_LAM_2, 2 hits
PS51465 KAZAL_2, 9 hits
PS50025 LAM_G_DOMAIN, 3 hits
PS50024 SEA, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiAGRIN_RAT
<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: P25304
Secondary accession number(s): Q63034
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: July 1, 1993
Last modified: January 16, 2019
This is version 170 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 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
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