O00468 (AGRIN_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 124.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Agrin Cleaved into the following 4 chains: | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) [Reference proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo![]() |
Protein attributes
| Sequence length | 2067 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | 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 homestasis in neurons, specifically by inducing an increase in cytoplasmic calcium ions. Functions differentially in the central nervous system (CNS) by inhibiting the alpha(3)-subtype of Na+/K+-ATPase and evoking depolarization at CNS synapses. This secreted isoform forms a bridge, after release from motor neurons, to basal lamina through binding laminin via the NtA domain. Ref.11 Ref.13 Isoform 2: transmembrane form that is 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. Ref.11 Ref.13 Isoform 1, isoform 4 and isoform 5: 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. Ref.11 Ref.13 Isoform 3 and isoform 6: lack any 'z' insert, are muscle-specific and may be involved in endothelial cell differentiation. Ref.11 Ref.13 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. Ref.11 Ref.13 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. Ref.11 Ref.13 |
| Subunit structure | 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 By similarity. 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 with DAG1; the interaction is influenced by cell surface glycosaminoglycans and by alternative splicing of AGRN. Ref.4 Ref.11 Ref.15 |
| Subcellular location | Isoform 1: Secreted › extracellular space › extracellular matrix. Note: Synaptic basal lamina at the neuromuscular junction By similarity. Ref.10 Isoform 2: Cell junction › synapse. Cell membrane; Single-pass type II membrane protein Ref.10. |
| Tissue specificity | Expressed in basement membranes of lung and kidney. Muscle- and neuron-specific isoforms are found. Isoforms (y+) with the 4 AA insert and (z+8) isoforms with the 8 AA insert are all neuron-specific. Isoforms (z+11) are found in both neuronal and non-neuronal tissues. Ref.1 Ref.7 Ref.10 |
| Domain | 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/DAG1 binding. G3 domain is required for C-terminal heparin, heparan sulfate and sialic acid binding By similarity. |
| Post-translational modification | 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. Heparin and heparin sulfate binding in the G3 domain 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 By similarity. 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). |
| Involvement in disease | Myasthenia, limb-girdle, familial (LGM) [MIM:254300]: A congenital myasthenic syndrome characterized by a typical 'limb girdle' pattern of muscle weakness with small, simplified neuromuscular junctions but normal acetylcholine receptor and acetylcholinesterase function. |
| Miscellaneous | Cleaved C-terminal fragments may be used as a biomarker for sarcopenia, age-related progressive loss of skeletal muscle (Ref.12). |
| Sequence similarities | Contains 4 EGF-like domains. Contains 9 Kazal-like domains. Contains 2 laminin EGF-like domains. Contains 3 laminin G-like domains. Contains 1 NtA (N-terminal agrin) domain. Contains 1 SEA domain. |
| Caution | The unknown residue 'x' in the transmembrane isoform is probably a proline residue by similarity to mouse and rat sequences. |
Ontologies
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| ATXN7 | O15265 | 2 | EBI-947482,EBI-708350 |
Alternative products
| This entry describes 7 isoforms produced by alternative splicing. [Align] [Select] Note: Many isoforms may exist depending on the occurrence and length of inserts at the x, y or z splice site. Four 'z' isoforms can be produced with inserts of 0, 8, 11 or 19 AA. Isoforms differ in their acetylcholine receptor clustering activity and tissue specificity. | ||||||
| Isoform 1 (identifier: O00468-1) Also known as: Secreted agrin; LN-agrin; 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. | ||||||
| Isoform 2 (identifier: O00468-2) Also known as: Transmembrane agrin; TM-agrin; The sequence of this isoform differs from the canonical sequence as follows: 1-104: Missing. 105-154: NQVSTGDTRI...NLEEVEFCVE → MPXLAVARDT...FAVLLFLNNY | ||||||
| Note: Produced by usage of an alternative first exon. | ||||||
| Isoform 3 (identifier: O00468-3) Also known as: Agrin z(0); The sequence of this isoform differs from the canonical sequence as follows: 1889-1906: Missing. | ||||||
| Isoform 4 (identifier: O00468-4) Also known as: Agrin z(+11); The sequence of this isoform differs from the canonical sequence as follows: 1889-1896: Missing. | ||||||
| Isoform 5 (identifier: O00468-5) Also known as: Agrin z(+8); The sequence of this isoform differs from the canonical sequence as follows: 1897-1906: Missing. | ||||||
| Isoform 6 (identifier: O00468-6) Also known as: Agrin y(0)z(0); The sequence of this isoform differs from the canonical sequence as follows: 1752-1755: Missing. 1889-1906: Missing. | ||||||
| Isoform 7 (identifier: O00468-7) Also known as: y(0); The sequence of this isoform differs from the canonical sequence as follows: 1752-1755: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 29 | 29 | Potential | ||||||||
| Chain | 30 – 2067 | 2038 | Agrin | PRO_0000007471 | |||||||
| Chain | 30 – 1102 | 1073 | Agrin N-terminal 110 kDa subunit By similarity | PRO_0000421613 | |||||||
| Chain | 1103 – 2067 | 965 | Agrin C-terminal 110 kDa subunit By similarity | PRO_0000421614 | |||||||
| Chain | 1103 – 1863 | 761 | Agrin C-terminal 90 kDa fragment By similarity | PRO_0000421615 | |||||||
| Chain | 1864 – 2067 | 204 | Agrin C-terminal 22 kDa fragment By similarity | PRO_0000421616 | |||||||
Regions | |||||||||||
| Domain | 30 – 157 | 128 | NtA | ||||||||
| Domain | 191 – 244 | 54 | Kazal-like 1 | ||||||||
| Domain | 264 – 319 | 56 | Kazal-like 2 | ||||||||
| Domain | 337 – 391 | 55 | Kazal-like 3 | ||||||||
| Domain | 408 – 463 | 56 | Kazal-like 4 | ||||||||
| Domain | 484 – 536 | 53 | Kazal-like 5 | ||||||||
| Domain | 540 – 601 | 62 | Kazal-like 6 | ||||||||
| Domain | 607 – 666 | 60 | Kazal-like 7 | ||||||||
| Domain | 699 – 752 | 54 | Kazal-like 8 | ||||||||
| Domain | 793 – 846 | 54 | Laminin EGF-like 1 | ||||||||
| Domain | 847 – 893 | 47 | Laminin EGF-like 2 | ||||||||
| Domain | 917 – 971 | 55 | Kazal-like 9 | ||||||||
| Domain | 1130 – 1252 | 123 | SEA | ||||||||
| Domain | 1329 – 1367 | 39 | EGF-like 1 | ||||||||
| Domain | 1372 – 1548 | 177 | Laminin G-like 1 | ||||||||
| Domain | 1549 – 1586 | 38 | EGF-like 2 | ||||||||
| Domain | 1588 – 1625 | 38 | EGF-like 3 | ||||||||
| Domain | 1635 – 1822 | 188 | Laminin G-like 2 | ||||||||
| Domain | 1818 – 1857 | 40 | EGF-like 4 | ||||||||
| Domain | 1868 – 2064 | 197 | Laminin G-like 3 | ||||||||
| Calcium binding | 1940 – 2008 | 69 | By similarity | ||||||||
| Compositional bias | 671 – 677 | 7 | Gly/Ser-rich | ||||||||
| Compositional bias | 974 – 1099 | 126 | Ser/Thr-rich | ||||||||
| Compositional bias | 1058 – 1097 | 40 | Gly/Ser-rich | ||||||||
| Compositional bias | 1254 – 1324 | 71 | Ser/Thr-rich | ||||||||
Sites | |||||||||||
| Site | 1102 – 1103 | 2 | Cleavage, alpha site; by neurotrypsin By similarity | ||||||||
| Site | 1250 | 1 | Alternative splice site to produce 'x' isoforms By similarity | ||||||||
| Site | 1751 | 1 | Alternative splice site to produce 'y' isoforms By similarity | ||||||||
| Site | 1862 | 1 | Critical for cleavage by neurotrypsin By similarity | ||||||||
| Site | 1863 – 1864 | 2 | Cleavage, beta site; by neurotrypsin By similarity | ||||||||
| Site | 1888 | 1 | Alternative splice site to produce 'z' isoforms By similarity | ||||||||
| Site | 1892 | 1 | Highly important for the agrin receptor complex activity of the 'z(8)' insert By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 135 | 1 | N-linked (GlcNAc...) Ref.9 | ||||||||
| Glycosylation | 250 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 777 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 932 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1835 | 1 | O-linked (Fuc...) By similarity | ||||||||
| Disulfide bond | 31 ↔ 103 | By similarity | |||||||||
| Disulfide bond | 152 ↔ 177 | Or C-152 with C-183 By similarity | |||||||||
| Disulfide bond | 793 ↔ 805 | By similarity | |||||||||
| Disulfide bond | 795 ↔ 812 | By similarity | |||||||||
| Disulfide bond | 814 ↔ 823 | By similarity | |||||||||
| Disulfide bond | 826 ↔ 844 | By similarity | |||||||||
| Disulfide bond | 847 ↔ 859 | By similarity | |||||||||
| Disulfide bond | 849 ↔ 866 | By similarity | |||||||||
| Disulfide bond | 868 ↔ 877 | By similarity | |||||||||
| Disulfide bond | 880 ↔ 891 | By similarity | |||||||||
| Disulfide bond | 1333 ↔ 1344 | By similarity | |||||||||
| Disulfide bond | 1338 ↔ 1355 | By similarity | |||||||||
| Disulfide bond | 1357 ↔ 1366 | By similarity | |||||||||
| Disulfide bond | 1519 ↔ 1548 | By similarity | |||||||||
| Disulfide bond | 1553 ↔ 1564 | By similarity | |||||||||
| Disulfide bond | 1558 ↔ 1574 | By similarity | |||||||||
| Disulfide bond | 1576 ↔ 1585 | By similarity | |||||||||
| Disulfide bond | 1592 ↔ 1603 | By similarity | |||||||||
| Disulfide bond | 1597 ↔ 1613 | By similarity | |||||||||
| Disulfide bond | 1615 ↔ 1624 | By similarity | |||||||||
| Disulfide bond | 1822 ↔ 1836 | By similarity | |||||||||
| Disulfide bond | 1830 ↔ 1845 | By similarity | |||||||||
| Disulfide bond | 1847 ↔ 1856 | By similarity | |||||||||
| Disulfide bond | 2038 ↔ 2064 | By similarity | |||||||||
Natural variations | |||||||||||
| Alternative sequence | 1 – 104 | 104 | Missing in isoform 2. | VSP_045753 | |||||||
| Alternative sequence | 105 – 154 | 50 | NQVST…EFCVE → MPXLAVARDTRQPAGASLLV RGFMVPCNACLILLATATLG FAVLLFLNNY in isoform 2. | VSP_045754 | |||||||
| Alternative sequence | 1752 – 1755 | 4 | Missing in isoform 6 and isoform 7. | VSP_045755 | |||||||
| Alternative sequence | 1889 – 1906 | 18 | Missing in isoform 3 and isoform 6. | VSP_045756 | |||||||
| Alternative sequence | 1889 – 1896 | 8 | Missing in isoform 4. | VSP_045757 | |||||||
| Alternative sequence | 1897 – 1906 | 10 | Missing in isoform 5. | VSP_045758 | |||||||
| Natural variant | 23 | 1 | V → L. Ref.13 | VAR_068724 | |||||||
| Natural variant | 58 | 1 | D → N. Ref.13 | VAR_068725 | |||||||
| Natural variant | 105 | 1 | N → I. Ref.13 | VAR_068726 | |||||||
| Natural variant | 267 | 1 | T → M. Ref.13 | VAR_068727 | |||||||
| Natural variant | 375 | 1 | A → S. Ref.13 | VAR_068728 | |||||||
| Natural variant | 728 | 1 | E → V. Ref.13 | VAR_068729 | |||||||
| Natural variant | 852 | 1 | Q → R. Ref.13 | VAR_068730 | |||||||
| Natural variant | 984 | 1 | V → M. Ref.13 | VAR_068731 | |||||||
| Natural variant | 1088 | 1 | L → F. Ref.13 | VAR_068732 | |||||||
| Natural variant | 1118 | 1 | T → K. Ref.13 | VAR_068733 | |||||||
| Natural variant | 1135 | 1 | Q → R. Ref.13 | VAR_068734 | |||||||
| Natural variant | 1240 | 1 | P → L. Ref.13 | VAR_068735 | |||||||
| Natural variant | 1341 | 1 | G → R. Ref.13 | VAR_068736 | |||||||
| Natural variant | 1451 | 1 | P → L. Ref.13 | VAR_068737 | |||||||
| Natural variant | 1514 | 1 | A → T. Ref.13 | VAR_068738 | |||||||
| Natural variant | 1565 | 1 | Q → H. Ref.13 | VAR_068739 | |||||||
| Natural variant | 1666 | 1 | V → I. Ref.13 Corresponds to variant rs17160775 [ dbSNP | Ensembl ]. | VAR_048966 | |||||||
| Natural variant | 1671 | 1 | R → Q. Ref.13 | VAR_068740 | |||||||
| Natural variant | 1698 | 1 | R → P. Ref.13 | VAR_068741 | |||||||
| Natural variant | 1709 | 1 | G → R in LGM; results in disruption of the neuromuscular junction architecture; does not affect phosphorylation of MUSK; does not affect AChR clustering. Ref.13 | VAR_068742 | |||||||
| Natural variant | 1727 | 1 | V → F in LGM; decreased AGRN-induced clustering of AChR by >100-fold and decreased phosphorylation of the MUSK receptor and AChR beta subunit by about 10-fold. Increased binding to alpha-dystroglycan. Ref.15 | VAR_069066 | |||||||
| Natural variant | 1734 | 1 | R → H. Ref.13 | VAR_068743 | |||||||
| Natural variant | 1789 | 1 | D → N. Ref.13 | VAR_068744 | |||||||
| Natural variant | 2045 | 1 | G → V. Ref.13 | VAR_068745 | |||||||
Experimental info | |||||||||||
| Sequence conflict | 343 | 1 | L → R in AAB52917. Ref.1 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Primary structure and high expression of human agrin in basement membranes of adult lung and kidney." Groffen A.J.A., Buskens C.A.F., Van Kuppevelt T.H., Veerkamp J.H., Monnens L.A.H., Van den Heuvel L.P.W.J. Eur. J. Biochem. 254:123-128(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY. |
| [2] | Kato S. Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). Tissue: Retinal pigment epithelium. |
| [3] | "The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. Bentley D.R.Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 3), NUCLEOTIDE SEQEUNCE [LARGE SCALE GENOMIC DNA] OF 1703-1949 (ISOFORM 6). |
| [4] | "Agrin binds to the nerve-muscle basal lamina via laminin." Denzer A.J., Brandenberger R., Gesemann M., Chiquet M., Ruegg M.A. J. Cell Biol. 137:671-683(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-172, INTERACTION WITH LAMININ. |
| [5] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1558-2045. Tissue: Brain, Colon and Kidney. |
| [6] | "An alternative amino-terminus expressed in the central nervous system converts agrin to a type II transmembrane protein." Neumann F.R., Bittcher G., Annies M., Schumacher B., Kroger S., Ruegg M.A. Mol. Cell. Neurosci. 17:208-225(2001) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION OF TRANSMEMBRANE ISOFORM (ISOFORM 2). |
| [7] | "Identification of agrinSN isoform and muscle-specific receptor tyrosine kinase (MuSK) in sperm." Kumar P., Ferns M.J., Meizel S. Biochem. Biophys. Res. Commun. 342:522-528(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION OF TRANSMEMBRANE ISOFORM (ISOFORM 2), ALTERNATIVE SPLICING, TISSUE SPECIFICITY. |
| [8] | Erratum Kumar P., Ferns M.J., Meizel S. Biochem. Biophys. Res. Commun. 344:453-453(2006) |
| [9] | "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-135, MASS SPECTROMETRY. Tissue: Liver. |
| [10] | "Proteomics characterization of extracellular space components in the human aorta." Didangelos A., Yin X., Mandal K., Baumert M., Jahangiri M., Mayr M. Mol. Cell. Proteomics 9:2048-2062(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. |
| [11] | "Agrin binds to the N-terminal region of Lrp4 protein and stimulates association between Lrp4 and the first immunoglobulin-like domain in muscle-specific kinase (MuSK)." Zhang W., Coldefy A.S., Hubbard S.R., Burden S.J. J. Biol. Chem. 286:40624-40630(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH LRP4, FUNCTION. |
| [12] | "C-terminal Agrin Fragment as a potential marker for sarcopenia caused by degeneration of the neuromuscular junction." Drey M., Sieber C.C., Bauer J.M., Uter W., Dahinden P., Fariello R.G., Vrijbloed J.W. Exp. Gerontol. 48:76-80(2013) [PubMed] [Europe PMC] [Abstract] Cited for: POTENTIAL USAGE AS A BIOMARKER FOR SARCOPENIA. |
| [13] | "Identification of an agrin mutation that causes congenital myasthenia and affects synapse function." Huze C., Bauche S., Richard P., Chevessier F., Goillot E., Gaudon K., Ben Ammar A., Chaboud A., Grosjean I., Lecuyer H.A., Bernard V., Rouche A., Alexandri N., Kuntzer T., Fardeau M., Fournier E., Brancaccio A., Ruegg M.A. Hantai D.Am. J. Hum. Genet. 85:155-167(2009) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT LGM ARG-1709, VARIANTS LEU-23; ASN-58; ILE-105; MET-267; SER-375; VAL-728; ARG-852; MET-984; PHE-1088; LYS-1118; ARG-1135; LEU-1240; ARG-1341; LEU-1451; THR-1514; HIS-1565; ILE-1666; GLN-1671; PRO-1698; HIS-1734; ASN-1789 AND VAL-2045, FUNCTION, CHARACTERIZATION OF VARIANT LGM ARG-1709. |
| [14] | Erratum Huze C., Bauche S., Richard P., Chevessier F., Goillot E., Gaudon K., Ben Ammar A., Chaboud A., Grosjean I., Lecuyer H.A., Bernard V., Rouche A., Alexandri N., Kuntzer T., Fardeau M., Fournier E., Brancaccio A., Ruegg M.A. Hantai D.Am. J. Hum. Genet. 85:536-536(2009) |
| [15] | "LG2 agrin mutation causing severe congenital myasthenic syndrome mimics functional characteristics of non-neural (z-) agrin." Maselli R.A., Fernandez J.M., Arredondo J., Navarro C., Ngo M., Beeson D., Cagney O., Williams D.C., Wollmann R.L., Yarov-Yarovoy V., Ferns M.J. Hum. Genet. 131:1123-1135(2012) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT LGM PHE-1727, INTERACTION WITH DAG1, CHARACTERIZATION OF PHE-1727. |
| + | Additional computationally mapped references. |
Web resources
| The Leiden Muscular Dystrophy pages, Agrin (AGRN) Leiden Open Variation Database (LOVD) |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U84406 mRNA. Translation: AAB52917.1. AB191264 mRNA. Translation: BAD52440.1. AL645608 Genomic DNA. Translation: CAI15575.2. AL645608 Genomic DNA. Translation: CAI15576.1. AF016903 mRNA. Translation: AAC39776.1. BC004220 mRNA. Translation: AAH04220.2. BC007649 mRNA. Translation: AAH07649.1. BC034009 mRNA. Translation: AAH34009.1. BC063620 mRNA. Translation: AAH63620.1. |
| IPI | IPI00374563. |
| RefSeq | NP_940978.2. NM_198576.3. |
| UniGene | Hs.273330. |
3D structure databases | |
| ProteinModelPortal | O00468. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | O00468. 5 interactions. |
| MINT | MINT-4053526. |
| STRING | 9606.ENSP00000368678. |
PTM databases | |
| PhosphoSite | O00468. |
Proteomic databases | |
| PaxDb | O00468. |
| PRIDE | O00468. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENST00000379370; ENSP00000368678; ENSG00000188157. |
| GeneID | 375790. |
| KEGG | hsa:375790. |
| UCSC | uc001ack.2. human. |
Organism-specific databases | |
| CTD | 375790. |
| GeneCards | GC01P000946. |
| HGNC | HGNC:329. AGRN. |
| HPA | HPA040090. |
| MIM | 103320. gene. 254300. phenotype. |
| neXtProt | NX_O00468. |
| Orphanet | 98913. Postsynaptic congenital myasthenic syndromes. |
| PharmGKB | PA24626. |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | NOG312635. |
| HOGENOM | HOG000033860. |
| HOVERGEN | HBG080471. |
| InParanoid | O00468. |
| KO | K06254. |
| OMA | TNRWLRV. |
| OrthoDB | EOG4HQDHD. |
Enzyme and pathway databases | |
| Reactome | REACT_111045. Developmental Biology. REACT_111217. Metabolism. REACT_116125. Disease. |
Gene expression databases | |
| ArrayExpress | O00468. |
| Bgee | O00468. |
| CleanEx | HS_AGRN. |
| Genevestigator | O00468. |
| GermOnline | ENSG00000188157. Homo sapiens. |
Family and domain databases | |
| Gene3D | 2.60.120.200. 3 hits. |
| InterPro | IPR004850. Agrin_NtA. IPR008985. ConA-like_lec_gl_sf. IPR013320. ConA-like_subgrp. IPR000742. EG-like_dom. IPR013032. EGF-like_CS. IPR002049. EGF_laminin. IPR003645. Fol_N. IPR002350. Kazal_dom. IPR001791. Laminin_G. IPR000082. SEA. IPR008993. TIMP-like_OB-fold. [Graphical view] |
| Pfam | PF00008. EGF. 3 hits. PF00050. Kazal_1. 3 hits. PF07648. Kazal_2. 6 hits. PF00053. Laminin_EGF. 2 hits. PF00054. Laminin_G_1. 3 hits. PF03146. NtA. 1 hit. PF01390. SEA. 1 hit. [Graphical view] |
| SMART | SM00181. EGF. 4 hits. SM00180. EGF_Lam. 2 hits. SM00274. FOLN. 5 hits. SM00280. KAZAL. 9 hits. SM00282. LamG. 3 hits. SM00200. SEA. 1 hit. [Graphical view] |
| SUPFAM | SSF49899. ConA_like_lec_gl. 3 hits. SSF50242. TIMP_like. 1 hit. |
| 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. PS51121. NTA. 1 hit. PS50024. SEA. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| GenomeRNAi | 375790. |
| NextBio | 100617. |
| SOURCE | Search... |
Entry information
| Entry name | AGRIN_HUMAN | ||||||||
| Accession | Primary (citable) accession number: O00468 Secondary accession number(s): Q5SVA1 Q9BTD4 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | ||||||||
Relevant documents
| Human chromosome 1 Human chromosome 1: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with
