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Entry version 177 (16 Jan 2019)
Sequence version 3 (06 Mar 2013)
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Protein

Agrin

Gene

AGRN

Organism
Gallus gallus (Chicken)
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. 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.
Isoform 9: transmembrane agrin (TM-agrin), the predominant 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 2, isoform 4 and isoform 7: muscle agrin isoforms, which lack the 8-amino acid insert at the 'B' site, but with the insert at the'A' site have no AChr clustering activity nor MUSK activation but bind heparin. Bind alpha-dystroglycan with lower affinity.
Isoform 5: muscle agrin A0B0 lacking inserts at both 'A' and 'B' sites has no heparin-binding nor AChR clustering activity but binds strongly alpha-dystroglycan.
Agrin N-terminal 110 kDa subunit: is involved in modulation of growth factor signaling (By similarity). Involved also in the 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 similarity7 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 'B' splice variants 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>Sitei1765Alternative splice site to produce 'A' isoformBy similarity1
Sitei1875Critical for cleavage by neurotrypsinBy similarity1
Sitei1901Alternative splice site to produce 'B' isoformsBy similarity1
Sitei1905Highly important for the agrin receptor complex activity of the 'B8' insertBy similarity1

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 bindingi1953 – 2022Add 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, Metal-binding

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

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
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>OrganismiGallus gallus (Chicken)
<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 identifieri9031 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
<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
  • UP000000539 <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

<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 junction, Cell membrane, Extracellular matrix, Membrane, Secreted, 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>Mutagenesisi1902 – 1908HLSNEIP → AAANEIA: No reduction in AGRN-induced MUSK phosphorylation. 1 Publication7
Mutagenesisi1905 – 1907NEI → AAA or AES: Large reduction in AGRN-induced MUSK phosphorylation. 1 Publication3
Mutagenesisi1905 – 1906NE → AA: Some reduction in AGRN-induced MUSK phosphorylation. 2
Mutagenesisi1905N → A: No effect on AGRN-induced MUSK phosphorylation. 1 Publication1
Mutagenesisi1906E → A: No effect on AGRN-induced MUSK phosphorylation. 1 Publication1
Mutagenesisi1907I → A: No effect on AGRN-induced MUSK phosphorylation. 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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 24Sequence analysisAdd BLAST24
<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_000005562425 – 2081AgrinAdd BLAST2057
ChainiPRO_000042162925 – 1116Agrin N-terminal 110 kDa subunitAdd BLAST1092
ChainiPRO_00004216301117 – 2081Agrin C-terminal 110 kDa subunitAdd BLAST965
ChainiPRO_00004216311117 – 1876Agrin C-terminal 90 kDa fragmentAdd BLAST760
ChainiPRO_00004216321877 – 2081Agrin 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 bondi26 ↔ 98
<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>Glycosylationi130N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi147 ↔ 179Or C-147 with C-185
Disulfide bondi199 ↔ 230PROSITE-ProRule annotation
Disulfide bondi204 ↔ 223PROSITE-ProRule annotation
Disulfide bondi212 ↔ 244PROSITE-ProRule annotation
Disulfide bondi274 ↔ 305PROSITE-ProRule annotation
Disulfide bondi278 ↔ 298PROSITE-ProRule annotation
Disulfide bondi287 ↔ 319PROSITE-ProRule annotation
Disulfide bondi351 ↔ 370PROSITE-ProRule annotation
Disulfide bondi359 ↔ 391PROSITE-ProRule annotation
Disulfide bondi415 ↔ 448PROSITE-ProRule annotation
Disulfide bondi422 ↔ 441PROSITE-ProRule annotation
Disulfide bondi430 ↔ 462PROSITE-ProRule annotation
Disulfide bondi492 ↔ 522PROSITE-ProRule annotation
Disulfide bondi496 ↔ 515PROSITE-ProRule annotation
Disulfide bondi504 ↔ 536PROSITE-ProRule annotation
Glycosylationi508N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi557 ↔ 587PROSITE-ProRule annotation
Disulfide bondi561 ↔ 580PROSITE-ProRule annotation
Disulfide bondi569 ↔ 601PROSITE-ProRule annotation
Disulfide bondi622 ↔ 652PROSITE-ProRule annotation
Disulfide bondi625 ↔ 645PROSITE-ProRule annotation
Disulfide bondi634 ↔ 666PROSITE-ProRule annotation
Disulfide bondi706 ↔ 737PROSITE-ProRule annotation
Disulfide bondi710 ↔ 730PROSITE-ProRule annotation
Disulfide bondi719 ↔ 751PROSITE-ProRule annotation
Glycosylationi777N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi793 ↔ 805By similarity
Disulfide bondi795 ↔ 812By similarity
Disulfide bondi814 ↔ 823By similarity
Disulfide bondi826 ↔ 844By similarity
Disulfide bondi847 ↔ 859By similarity
Disulfide bondi849 ↔ 866By similarity
Disulfide bondi868 ↔ 877By similarity
Disulfide bondi880 ↔ 891By similarity
Glycosylationi882N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi923 ↔ 955PROSITE-ProRule annotation
Disulfide bondi928 ↔ 948PROSITE-ProRule annotation
Glycosylationi932N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi937 ↔ 969PROSITE-ProRule annotation
Disulfide bondi1351 ↔ 1362By similarity
Disulfide bondi1356 ↔ 1371By similarity
Disulfide bondi1373 ↔ 1382By similarity
Disulfide bondi1568 ↔ 1579By similarity
Disulfide bondi1573 ↔ 1589By similarity
Disulfide bondi1591 ↔ 1600By similarity
Disulfide bondi1607 ↔ 1618By similarity
Disulfide bondi1612 ↔ 1628By similarity
Disulfide bondi1630 ↔ 1639By similarity
Disulfide bondi1836 ↔ 1849By similarity
Disulfide bondi1843 ↔ 1858By similarity
Disulfide bondi1860 ↔ 1869By similarity
Disulfide bondi2052 ↔ 2078

<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 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 (By similarity). C-terminal heparin and heparin sulfate binding 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. Inserts at the 'B' site have no effect on sialic acid binding.By similarity1 Publication
At synaptic junctions, cleaved at two conserved sites, alpha and beta, by neurotrypsin. Cleavage at the alpha-site produces the N- and C- terminal 110-kDa subunits. Further cleavage of the C-terminal at the beta site produces C-terminal fragments, C22 and C90, of 90 kDa and 22 kDa respectively (By similarity).By similarity
Proteolytically cleaved in vitro in both the N-terminal and C-terminal by several matrix metaloproteinases (MMPs).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei140 – 141Cleavage; by MMP12
Sitei153 – 154Cleavage; by MMP72
Sitei161 – 162Cleavage; by MMP122
Sitei1116 – 1117Cleavage, alpha site; by neurotrypsinBy similarity2
Sitei1821 – 1822Cleavage; by MMP12
Sitei1830 – 1831Cleavage; by MMP72
Sitei1876 – 1877Cleavage, beta site; by neurotrypsinBy similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein, Heparan sulfate, Proteoglycan

Proteomic databases

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

More...
PaxDbi
P31696

PRoteomics IDEntifications database

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PRIDEi
P31696

<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 embryonic brain, spinal cord, skeletal muscle, vitreous humor and liver (at protein level).1 Publication

<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 (By similarity). 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. 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 'B8' insert present in the B8 isoforms. Interacts with DAG1; the interaction is influenced by cell surface glycosaminoglycans and by alternative splicing of AGRN.By similarity7 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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
676782, 1 interactor

Protein interaction database and analysis system

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IntActi
P31696, 5 interactors

STRING: functional protein association networks

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STRINGi
9031.ENSGALP00000039379

<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

12081
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
1JB3X-ray1.60A26-156[»]
1JC7X-ray2.73A26-154[»]
1PXUX-ray2.20A25-155[»]
1PZ7X-ray1.42A/B1870-2081[»]
1PZ8X-ray2.35A/B/C/D1870-2081[»]
1PZ9X-ray2.80A/B1870-2081[»]
1Q56NMR-A1870-2081[»]
3I70X-ray2.30A26-153[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P31696

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

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SMRi
P31696

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...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P31696

<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>Domaini25 – 159NtAPROSITE-ProRule annotationAdd BLAST135
Domaini193 – 246Kazal-like 1PROSITE-ProRule annotationAdd BLAST54
Domaini268 – 321Kazal-like 2PROSITE-ProRule annotationAdd BLAST54
Domaini339 – 393Kazal-like 3PROSITE-ProRule annotationAdd BLAST55
Domaini409 – 464Kazal-like 4PROSITE-ProRule annotationAdd BLAST56
Domaini486 – 538Kazal-like 5PROSITE-ProRule annotationAdd BLAST53
Domaini551 – 603Kazal-like 6PROSITE-ProRule annotationAdd BLAST53
Domaini616 – 668Kazal-like 7PROSITE-ProRule annotationAdd BLAST53
Domaini700 – 753Kazal-like 8PROSITE-ProRule annotationAdd BLAST54
Domaini793 – 846Laminin EGF-like 1PROSITE-ProRule annotationAdd BLAST54
Domaini847 – 893Laminin EGF-like 2PROSITE-ProRule annotationAdd BLAST47
Domaini917 – 971Kazal-like 9PROSITE-ProRule annotationAdd BLAST55
Domaini1144 – 1266SEAPROSITE-ProRule annotationAdd BLAST123
Domaini1347 – 1383EGF-like 1PROSITE-ProRule annotationAdd BLAST37
Domaini1388 – 1563Laminin G-like 1PROSITE-ProRule annotationAdd BLAST176
Domaini1564 – 1601EGF-like 2PROSITE-ProRule annotationAdd BLAST38
Domaini1603 – 1640EGF-like 3PROSITE-ProRule annotationAdd BLAST38
Domaini1650 – 1831Laminin G-like 2PROSITE-ProRule annotationAdd BLAST182
Domaini1832 – 1870EGF-like 4PROSITE-ProRule annotationAdd BLAST39
Domaini1894 – 2078Laminin G-like 3PROSITE-ProRule annotationAdd BLAST185

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 biasi671 – 678Gly/Ser-rich8
Compositional biasi974 – 1113Ser/Thr-richAdd BLAST140
Compositional biasi1072 – 1099Gly/Ser-richAdd BLAST28
Compositional biasi1268 – 1337Ser/Thr-richAdd BLAST70

<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 4 amino acid insert at the 'A' site is required for effecient binding of heparin.
The NtA domain, absent in TM-Agrin, is required for binding laminin and connecting to basal lamina.
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, Transmembrane

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG410ITSI Eukaryota
ENOG410YKSA LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000033860

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG080471

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P31696

Database of Orthologous Groups

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OrthoDBi
414294at2759

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.30.70.960, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR013320 ConA-like_dom_sf
IPR001881 EGF-like_Ca-bd_dom
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR000152 EGF-type_Asp/Asn_hydroxyl_site
IPR003884 FacI_MAC
IPR003645 Fol_N
IPR002350 Kazal_dom
IPR036058 Kazal_dom_sf
IPR002049 Laminin_EGF
IPR001791 Laminin_G
IPR004850 NtA_dom
IPR000082 SEA_dom
IPR036364 SEA_dom_sf
IPR008993 TIMP-like_OB-fold

Pfam protein domain database

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Pfami
View protein in Pfam
PF00008 EGF, 4 hits
PF00050 Kazal_1, 2 hits
PF07648 Kazal_2, 7 hits
PF00053 Laminin_EGF, 2 hits
PF00054 Laminin_G_1, 3 hits
PF03146 NtA, 1 hit
PF01390 SEA, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00181 EGF, 8 hits
SM00179 EGF_CA, 3 hits
SM00180 EGF_Lam, 2 hits
SM00057 FIMAC, 2 hits
SM00274 FOLN, 6 hits
SM00280 KAZAL, 9 hits
SM00282 LamG, 3 hits
SM00200 SEA, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF100895 SSF100895, 9 hits
SSF49899 SSF49899, 3 hits
SSF50242 SSF50242, 1 hit
SSF82671 SSF82671, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00010 ASX_HYDROXYL, 1 hit
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
PS51121 NTA, 1 hit
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 (10)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 10 <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 including secreted and transmembrane forms, isoforms with different length inserts produced at the 'B' splice site, B0, B8, B11 and B19, with or without the 'A' splice site insert.
Isoform 1 (identifier: P31696-1) [UniParc]FASTAAdd to basket
Also known as: LN-agrin, agrin A4B19

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
MGGSGAAATL ALGLALGLAL GGWANCPERE LQRREEEANV VLTGTVEEIM
60 70 80 90 100
NVDPVHHTYS CKVRVWRYLK GKDIVTHEIL LDGGNKVVIG GFGDPLICDN
110 120 130 140 150
QVSTGDTRIF FVNPAPQYMW PAHRNELMLN SSLMRITLRN LEEVEHCVEE
160 170 180 190 200
HRKLLADKPN SYFTQTPPTP RDACRGMLCG FGAVCERSPT DPSQASCVCK
210 220 230 240 250
KTACPVVVAP VCGSDYSTYS NECELEKAQC NQQRRIKVIS KGPCGSKDPC
260 270 280 290 300
AEVTCSFGST CVRSADGQTA GCVCPASCSG VAESIVCGSD GKDYRSECDL
310 320 330 340 350
NKHACDKQEN VFKKFDGACD PCKGILNDMN RVCRVNPRTR RVELLSRPEN
360 370 380 390 400
CPSKREPVCG DDGVTYASEC VMGRTGAIRG LEIQKVRSGQ CQHQDKCKDE
410 420 430 440 450
CKFNAVCLKR WHARCSCDRI TCDGTYRPVC ARDSRTYSND CERQKAECHQ
460 470 480 490 500
KAAIPVKHSG PCDLGTPSPC LSVECTFGAT CVVKNREPVC ECQQVCQGRY
510 520 530 540 550
DPVCGSDNRT YGNPCELNAM ACVLKREIRV KHKGPCDRCG KCQFGAICEA
560 570 580 590 600
ETGRCVCPTE CVPSSQPVCG TDGNTYGSEC ELHVRACTQQ KNILVAAQGD
610 620 630 640 650
CKSCGTTVCS FGSTCVGGQC VCPRCEQQPL AQVCGTDGLT YDNRCELRAA
660 670 680 690 700
SCQQQKSIEV AKMGPCEDEC GSGGSGSGDG SECEQDRCRH YGGWWDEDAE
710 720 730 740 750
DDRCVCDFTC LAVPRSPVCG SDDVTYANEC ELKKTRCEKR QNLYVTSQGA
760 770 780 790 800
CRALTTTPPP LPVVHCSQTI YGCCPDNMTL ALGVGAAGCP STCQCNPYGS
810 820 830 840 850
YGGTCDPATG QCSCKPGVGG LKCDRCEPGF WNFRGIVTDS KSGCTPCNCD
860 870 880 890 900
PVGSVRDDCE QMTGLCSCKT GITGMKCNQC PNGSKMGMAG CEKDPSAPKS
910 920 930 940 950
CEEMSCEFGA TCVEVNGFAH CECPSPLCSE ANMTKVCGSD GVTYGDQCQL
960 970 980 990 1000
KTIACRQGQL ITVKHVGQCH ESITHTSHTM PPTPLPTLPL DKLIVPPPLQ
1010 1020 1030 1040 1050
LTTQAPEPTE LATTSLLMEA SPTTRSHPTT RRVTTTRPVT TPWMTHGVLK
1060 1070 1080 1090 1100
TTVRPLSTSP VVLATTQPPY AESGSAEGSG DQEMSISGDQ ESSGAGSAGE
1110 1120 1130 1140 1150
EEVEESQVTP TPAIERATCY NTPLGCCSDG KTAAADAEGS NCPATKVFQG
1160 1170 1180 1190 1200
VLILEEVEGQ ELFYTPEMAD PKSELFGETA RSIESALDEL FRNSDVKNDF
1210 1220 1230 1240 1250
KSIRVRDLGQ SSAVRVIVES HFDPATSYTA ADVQAASLKQ IRASKKRTIL
1260 1270 1280 1290 1300
VKKPQQEHVK FMDFDWIPRI FTTTITTTTA TTMAPATTRR HTTASAATTA
1310 1320 1330 1340 1350
HILRQDTVGH PSAKLAAPAS TRRPTSTLPT TARRKPTRQP PSTTKKPSRP
1360 1370 1380 1390 1400
CDSHPCLHGG TCEDDGREFT CRCPAGKGGA VCEKPIRYFI PSFGGKSYLA
1410 1420 1430 1440 1450
FKMMKAYHTV RIAMEFRATE LSGLLLYNGQ NRGKDFISLA LVGGFVELRF
1460 1470 1480 1490 1500
NTGSGTGVIT SKVRVEPGKW HQLVVNRNRR SGMLAVDGEH VSGESPTGTD
1510 1520 1530 1540 1550
GLNLDTDLFV GGAPEDQMAV VAERTAATVG LKGSIRLLDV NNQMYDLREK
1560 1570 1580 1590 1600
GSDVLYGSGV GECGNDPCHP NPCHHGASCH VKEAEMFHCE CLHSYTGPTC
1610 1620 1630 1640 1650
ADERNPCDPT PCHISATCLV LPEGGAMCAC PMGREGEFCE RVTEQDHTMP
1660 1670 1680 1690 1700
FLPEFNGFSY LELNGLQTLF LTCRQMSMEV VFLAKSPSGM IFYNGQKTDG
1710 1720 1730 1740 1750
KGDFVSLALH DGYLEYRYDL GKGAAVLRSK EPVPLNTWIS VLLERSGRKG
1760 1770 1780 1790 1800
VMRINNGERV MGESPKSRKV PHAFLNLKEP FYVGGAPDFS KLARAAAIST
1810 1820 1830 1840 1850
SFYGAVQRIS IKGVPLLKEQ HIRSAVEIST FRAHPCTQKP NPCQNGGTCS
1860 1870 1880 1890 1900
PRLESYECAC QRGFSGAHCE KVIIEKAAGD AEAIAFDGRT YMEYHNAVTK
1910 1920 1930 1940 1950
SHLSNEIPAP DALDYPAEPS EKALQSNHFE LSIKTEATQG LILWSGKGLE
1960 1970 1980 1990 2000
RSDYIALAIV DGFVQMMYDL GSKPVVLRST VPINTNHWTH IKAYRVQREG
2010 2020 2030 2040 2050
SLQVGNEAPI TGSSPLGATQ LDTDGALWLG GMERLSVAHK LPKAYSTGFI
2060 2070 2080
GCIRDVIVDR QELHLVEDAL NNPTILHCSA K
Length:2,081
Mass (Da):224,980
Last modified:March 6, 2013 - v3
<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:i87FEFE1A11664F0E
GO
Isoform 2 (identifier: P31696-2) [UniParc]FASTAAdd to basket
Also known as: Agrin-related protein 1, agrin A4B0

The sequence of this isoform differs from the canonical sequence as follows:
     1902-1920: Missing.

Show »
Length:2,062
Mass (Da):222,962
Checksum:i76AE3422BAD30EB3
GO
Isoform 3 (identifier: P31696-3) [UniParc]FASTAAdd to basket
Also known as: Agrin-related protein 2, agrin A4B8

The sequence of this isoform differs from the canonical sequence as follows:
     1910-1920: Missing.

Show »
Length:2,070
Mass (Da):223,824
Checksum:iF3B5C882943686E2
GO
Isoform 4 (identifier: P31696-4) [UniParc]FASTAAdd to basket
Also known as: Agrin A4B11

The sequence of this isoform differs from the canonical sequence as follows:
     1902-1909: Missing.

Show »
Length:2,073
Mass (Da):224,118
Checksum:i6E67129075A4E130
GO
Isoform 5 (identifier: P31696-5) [UniParc]FASTAAdd to basket
Also known as: Muscle agrin, agrin A0B0

The sequence of this isoform differs from the canonical sequence as follows:
     1766-1769: Missing.
     1902-1920: Missing.

Show »
Length:2,058
Mass (Da):222,462
Checksum:i7716B82777335B3A
GO
Isoform 6 (identifier: P31696-6) [UniParc]FASTAAdd to basket
Also known as: Agrin A0B8

The sequence of this isoform differs from the canonical sequence as follows:
     1766-1769: Missing.
     1910-1920: Missing.

Show »
Length:2,066
Mass (Da):223,324
Checksum:iDFFD9BC55A44F646
GO
Isoform 7 (identifier: P31696-7) [UniParc]FASTAAdd to basket
Also known as: Muscle agrin, agrin A0B11

The sequence of this isoform differs from the canonical sequence as follows:
     1766-1769: Missing.
     1902-1909: Missing.

Show »
Length:2,069
Mass (Da):223,619
Checksum:i2C46FA7C3DF7A6FE
GO
Isoform 8 (identifier: P31696-8) [UniParc]FASTAAdd to basket
Also known as: Agrin A0B19

The sequence of this isoform differs from the canonical sequence as follows:
     1766-1769: Missing.

Show »
Length:2,077
Mass (Da):224,480
Checksum:iDEA9C1133093F7A2
GO
Isoform 9 (identifier: P31696-9) [UniParc]FASTAAdd to basket
Also known as: TM-agrin, SN-agrin

The sequence of this isoform differs from the canonical sequence as follows:
     1-60: MGGSGAAATL...NVDPVHHTYS → MTACQYPMAP...FAVLLFLNNY
     61-157: Missing.

Note: Transmembrane isoform produced by usage of an alternative first exon.
Show »
Length:1,981
Mass (Da):214,057
Checksum:i1976A4A4FF374688
GO
Isoform 10 (identifier: P31696-10) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     150-156: Missing.

Show »
Length:2,074
Mass (Da):224,132
Checksum:i976F97F9A1E6EDF7
GO

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

The sequence AAA48585 differs from that shown. Reason: Frameshift at position 110.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti1247 – 1249RTI → SIL in AAA48586 (PubMed:1314620).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_0457701 – 60MGGSG…HHTYS → MTACQYPMAPGALERDRLYQ HKVSLVVRYFMIPCNICLIL LATSTLGFAVLLFLNNY in isoform 9. 1 PublicationAdd BLAST60
Alternative sequenceiVSP_04577161 – 157Missing in isoform 9. 1 PublicationAdd BLAST97
Alternative sequenceiVSP_045772150 – 156Missing in isoform 10. Curated7
Alternative sequenceiVSP_0457731766 – 1769Missing in isoform 5, isoform 6, isoform 7 and isoform 8. 1 Publication4
Alternative sequenceiVSP_0457741902 – 1920Missing in isoform 2 and isoform 5. 1 PublicationAdd BLAST19
Alternative sequenceiVSP_0457751902 – 1909Missing in isoform 4 and isoform 7. 1 Publication8
Alternative sequenceiVSP_0457761910 – 1920Missing in isoform 3 and isoform 6. 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
U35613 mRNA Translation: AAC59740.1
M94271 mRNA Translation: AAA48585.1 Frameshift.
M97371 mRNA Translation: AAA48586.1
M97372 mRNA No translation available.
U07271 mRNA Translation: AAA16788.1

Protein sequence database of the Protein Information Resource

More...
PIRi
JH0591 AGCH

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Gga.4448
Gga.48948

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
U35613 mRNA Translation: AAC59740.1
M94271 mRNA Translation: AAA48585.1 Frameshift.
M97371 mRNA Translation: AAA48586.1
M97372 mRNA No translation available.
U07271 mRNA Translation: AAA16788.1
PIRiJH0591 AGCH
UniGeneiGga.4448
Gga.48948

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JB3X-ray1.60A26-156[»]
1JC7X-ray2.73A26-154[»]
1PXUX-ray2.20A25-155[»]
1PZ7X-ray1.42A/B1870-2081[»]
1PZ8X-ray2.35A/B/C/D1870-2081[»]
1PZ9X-ray2.80A/B1870-2081[»]
1Q56NMR-A1870-2081[»]
3I70X-ray2.30A26-153[»]
ProteinModelPortaliP31696
SMRiP31696
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi676782, 1 interactor
IntActiP31696, 5 interactors
STRINGi9031.ENSGALP00000039379

Proteomic databases

PaxDbiP31696
PRIDEiP31696

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410ITSI Eukaryota
ENOG410YKSA LUCA
HOGENOMiHOG000033860
HOVERGENiHBG080471
InParanoidiP31696
OrthoDBi414294at2759

Miscellaneous databases

EvolutionaryTraceiP31696

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
IPR000152 EGF-type_Asp/Asn_hydroxyl_site
IPR003884 FacI_MAC
IPR003645 Fol_N
IPR002350 Kazal_dom
IPR036058 Kazal_dom_sf
IPR002049 Laminin_EGF
IPR001791 Laminin_G
IPR004850 NtA_dom
IPR000082 SEA_dom
IPR036364 SEA_dom_sf
IPR008993 TIMP-like_OB-fold
PfamiView protein in Pfam
PF00008 EGF, 4 hits
PF00050 Kazal_1, 2 hits
PF07648 Kazal_2, 7 hits
PF00053 Laminin_EGF, 2 hits
PF00054 Laminin_G_1, 3 hits
PF03146 NtA, 1 hit
PF01390 SEA, 1 hit
SMARTiView protein in SMART
SM00181 EGF, 8 hits
SM00179 EGF_CA, 3 hits
SM00180 EGF_Lam, 2 hits
SM00057 FIMAC, 2 hits
SM00274 FOLN, 6 hits
SM00280 KAZAL, 9 hits
SM00282 LamG, 3 hits
SM00200 SEA, 1 hit
SUPFAMiSSF100895 SSF100895, 9 hits
SSF49899 SSF49899, 3 hits
SSF50242 SSF50242, 1 hit
SSF82671 SSF82671, 1 hit
PROSITEiView protein in PROSITE
PS00010 ASX_HYDROXYL, 1 hit
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
PS51121 NTA, 1 hit
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_CHICK
<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: P31696
Secondary accession number(s): Q90609, Q90685
<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: July 1, 1993
Last sequence update: March 6, 2013
Last modified: January 16, 2019
This is version 177 of the entry and version 3 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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