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Agrin [Cleaved into: Agrin N-terminal 110 kDa subunit; Agrin C-terminal 110 kDa subunit; Agrin C-terminal 90 kDa fragment (C90); Agrin C-terminal 22 kDa fragment (C22)]

 AGRIN_MOUSE             Reviewed;        1950 AA.
A2ASQ1; A2ASP9; A2ASQ0; B2RWU1;
16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
20-FEB-2007, sequence version 1.
28-MAR-2018, entry version 104.
RecName: Full=Agrin;
Contains:
RecName: Full=Agrin N-terminal 110 kDa subunit;
Contains:
RecName: Full=Agrin C-terminal 110 kDa subunit;
Contains:
RecName: Full=Agrin C-terminal 90 kDa fragment;
Short=C90;
Contains:
RecName: Full=Agrin C-terminal 22 kDa fragment;
Short=C22;
Name=Agrn; Synonyms=Agrin;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
FUNCTION IN NEUROMUSCULAR JUNCTION DEVELOPMENT, SUBCELLULAR LOCATION,
FUNCTION IN PHOSPHORYLATION OF MUSK, AND INTERACTION WITH LRP4.
PubMed=8653787; DOI=10.1016/S0092-8674(00)81252-0;
Glass D.J., Bowen D.C., Stitt T.N., Radziejewski C., Bruno J.,
Ryan T.E., Gies D.R., Shah S., Mattsson K., Burden S.J.,
DiStefano P.S., Valenzuela D.M., DeChiara T.M., Yancopoulos G.D.;
"Agrin acts via a MuSK receptor complex.";
Cell 85:513-523(1996).
[4]
REGULATION OF ALTERNATIVE SPLICING.
PubMed=9188458; DOI=10.1074/jbc.272.25.15675;
Smith M.A., Fanger G.R., O'Connor L.T., Bridle P., Maue R.A.;
"Selective regulation of agrin mRNA induction and alternative splicing
in PC12 cells by Ras-dependent actions of nerve growth factor.";
J. Biol. Chem. 272:15675-15681(1997).
[5]
LAMININ BINDING.
PubMed=10581249; DOI=10.1093/emboj/18.23.6762;
Kammerer R.A., Schulthess T., Landwehr R., Schumacher B., Lustig A.,
Yurchenco P.D., Ruegg M.A., Engel J., Denzer A.J.;
"Interaction of agrin with laminin requires a coiled-coil conformation
of the agrin-binding site within the laminin gamma1 chain.";
EMBO J. 18:6762-6770(1999).
[6]
ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE,
TISSUE SPECIFICITY, AND FUNCTION.
PubMed=10402191; DOI=10.1016/S0896-6273(00)80751-5;
Burgess R.W., Nguyen Q.T., Son Y.J., Lichtman J.W., Sanes J.R.;
"Alternatively spliced isoforms of nerve- and muscle-derived agrin:
their roles at the neuromuscular junction.";
Neuron 23:33-44(1999).
[7]
ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
FUNCTION.
PubMed=11018052; DOI=10.1083/jcb.151.1.41;
Burgess R.W., Skarnes W.C., Sanes J.R.;
"Agrin isoforms with distinct amino termini: differential expression,
localization, and function.";
J. Cell Biol. 151:41-52(2000).
[8]
ALTERNATIVE SPLICING, AND SUBCELLULAR LOCATION.
PubMed=11161480; DOI=10.1006/mcne.2000.0932;
Neumann F.R., Bittcher G., Annies M., Schumacher B., Kroger S.,
Ruegg M.A.;
"An alternative amino-terminus expressed in the central nervous system
converts agrin to a type II transmembrane protein.";
Mol. Cell. Neurosci. 17:208-225(2001).
[9]
FUNCTION OF AGRIN C-TERMINAL 22 KDA FRAGMENT, AND SUBCELLULAR
LOCATION.
PubMed=12796478; DOI=10.1083/jcb.200301013;
Hoover C.L., Hilgenberg L.G., Smith M.A.;
"The COOH-terminal domain of agrin signals via a synaptic receptor in
central nervous system neurons.";
J. Cell Biol. 161:923-932(2003).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[11]
DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
FUNCTION.
PubMed=17611272; DOI=10.1523/JNEUROSCI.1609-07.2007;
Ksiazek I., Burkhardt C., Lin S., Seddik R., Maj M., Bezakova G.,
Jucker M., Arber S., Caroni P., Sanes J.R., Bettler B., Ruegg M.A.;
"Synapse loss in cortex of agrin-deficient mice after genetic rescue
of perinatal death.";
J. Neurosci. 27:7183-7195(2007).
[12]
PROTEOLYTIC PROCESSING, IDENTIFICATION OF PROTEOLYTICALLY CLEAVED
FRAGMENTS BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=18230682; DOI=10.1096/fj.07-100008;
Stephan A., Mateos J.M., Kozlov S.V., Cinelli P., Kistler A.D.,
Hettwer S., Rulicke T., Streit P., Kunz B., Sonderegger P.;
"Neurotrypsin cleaves agrin locally at the synapse.";
FASEB J. 22:1861-1873(2008).
[13]
PROTEOLYTIC PROCESSING, AND FUNCTION.
PubMed=19303856; DOI=10.1016/j.cell.2009.02.034;
Matsumoto-Miyai K., Sokolowska E., Zurlinden A., Gee C.E., Luscher D.,
Hettwer S., Wolfel J., Ladner A.P., Ster J., Gerber U., Rulicke T.,
Kunz B., Sonderegger P.;
"Coincident pre- and postsynaptic activation induces dendritic
filopodia via neurotrypsin-dependent agrin cleavage.";
Cell 136:1161-1171(2009).
[14]
REGULATION OF ALTERNATIVE SPLICING AT THE Z SITE.
PubMed=19221030; DOI=10.1073/pnas.0813112106;
Ruggiu M., Herbst R., Kim N., Jevsek M., Fak J.J., Mann M.A.,
Fischbach G., Burden S.J., Darnell R.B.;
"Rescuing Z+ agrin splicing in Nova null mice restores synapse
formation and unmasks a physiologic defect in motor neuron firing.";
Proc. Natl. Acad. Sci. U.S.A. 106:3513-3518(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569 AND SER-571, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and
Pancreas;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[16]
PROTEOLYTIC PROCESSING, FUNCTION, AND MOUSE MODEL OF PRECOCIOUS
SARCOPENIA.
PubMed=21885656; DOI=10.1096/fj.11-191262;
Butikofer L., Zurlinden A., Bolliger M.F., Kunz B., Sonderegger P.;
"Destabilization of the neuromuscular junction by proteolytic cleavage
of agrin results in precocious sarcopenia.";
FASEB J. 25:4378-4393(2011).
[17]
VARIANT A MUTANT STRAIN SER-1061, AND CHARACTERIZATION OF A MOUSE
MODEL OF AGRIN-ASSOCIATED CONGENITAL MYASTHENIC SYNDROME.
PubMed=21890498; DOI=10.1093/hmg/ddr396;
Bogdanik L.P., Burgess R.W.;
"A valid mouse model of AGRIN-associated congenital myasthenic
syndrome.";
Hum. Mol. Genet. 20:4617-4633(2011).
[18]
STRUCTURAL CHARACTERISTICS OF LAMININ G3 DOMAIN.
PubMed=21037280; DOI=10.1093/protein/gzq082;
Tidow H., Mattle D., Nissen P.;
"Structural and biophysical characterisation of agrin laminin G3
domain constructs.";
Protein Eng. Des. Sel. 24:219-224(2011).
[19]
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1510-1701.
New York structural genomix research consortium (NYSGXRC);
"Crystal structure of the g2 domain of agrin from Mus musculus.";
Submitted (JAN-2011) to the PDB data bank.
-!- 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. 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 alpha(3)-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.
-!- FUNCTION: Isoform 2 and isoform 3: these isoforms lacking the 'z'
insert (z0) are muscle-specific, have no AChR clustering ability
and may be involved in nervous system endothelial cell
differentiation.
-!- FUNCTION: Agrin N-terminal 110 kDa subunit: 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).
{ECO:0000250, ECO:0000269|PubMed:10402191,
ECO:0000269|PubMed:11018052, ECO:0000269|PubMed:12796478,
ECO:0000269|PubMed:17611272, ECO:0000269|PubMed:19303856,
ECO:0000269|PubMed:21885656, ECO:0000269|PubMed:8653787}.
-!- FUNCTION: 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.
-!- SUBUNIT: 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. Interacts
with DAG1; the interaction is influenced by cell surface
glycosaminoglycans and by alternative splicing of AGRN (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. {ECO:0000250,
ECO:0000269|PubMed:8653787}.
-!- SUBCELLULAR LOCATION: Cell junction, synapse
{ECO:0000269|PubMed:10402191, ECO:0000269|PubMed:12796478,
ECO:0000269|PubMed:17611272, ECO:0000269|PubMed:18230682,
ECO:0000269|PubMed:8653787}. Cell membrane
{ECO:0000269|PubMed:11018052, ECO:0000269|PubMed:11161480};
Single-pass type II membrane protein {ECO:0000269|PubMed:11018052,
ECO:0000269|PubMed:11161480}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Comment=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 is produced
by alternative usage of the first exon.;
Name=1; Synonyms=Transmembrane agrin, TM-agrin;
IsoId=A2ASQ1-1; Sequence=Displayed;
Name=2;
IsoId=A2ASQ1-2; Sequence=VSP_035996, VSP_035997;
Name=3;
IsoId=A2ASQ1-3; Sequence=VSP_035995, VSP_035996, VSP_035997;
-!- TISSUE SPECIFICITY: Expressed in central nervous system (CNS)
synapses such as in the cerebral cortex and hippocampus. Localizes
to basal lamina of hippocampal blood vessels. Both (z+) and (z-)
isoforms found in kidney, heart and cerebral vasculature.
{ECO:0000269|PubMed:10402191, ECO:0000269|PubMed:11018052,
ECO:0000269|PubMed:17611272, ECO:0000269|PubMed:18230682}.
-!- DEVELOPMENTAL STAGE: All (z+), (z-), (y+) and (y-) isoforms
present throughout muscle fiber basal laminae in neonatal animals.
-!- DOMAIN: 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 (By similarity). {ECO:0000250}.
-!- PTM: Contains heparan and chondroitin sulfate chains and alpha-
dystroglycan as well as N-linked and O-linked oligosaccharides.
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). 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. {ECO:0000250}.
-!- PTM: 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). Cleavage is developmentally
regulated. In developing brain, neurotrypsin-mediated cleavage
occurs mainly during late fetal days and in the first postnatal
week. {ECO:0000269|PubMed:18230682, ECO:0000269|PubMed:19303856,
ECO:0000269|PubMed:21885656}.
-!- DISRUPTION PHENOTYPE: Z(-)/z(-) mice lacking the 'z' insert are
stillborn or die immediately after birth. They did not inflate
their lungs and were never seen to move spontaneously. An
intramuscular nerve is formed and axons leave the nerve and branch
but do not stop and arborize. AChR clusters were fewer in number,
about 30% smaller in size and lower in density. Transgenic null
(Tg/Agrn -/-) mice, exhibit atrophied muscle due to denervation
and are smaller than normal littermates. There is impairment of
locomotory behavior and half the mice die after 50 days. There is
a greatly reduced number of synapses and about 30% loss of
postsynaptic spines and a decrease in the length of dendrites in
cortical neurons. {ECO:0000269|PubMed:10402191,
ECO:0000269|PubMed:17611272}.
-!- MISCELLANEOUS: Mice that have excessive neurotrypsin-mediated
agrin cleavage, exhibit pathological symptoms characteristic of
precocious sarcopenia, with fragmentation and disassembly of the
neuromuscular junction (NMJ). {ECO:0000305|PubMed:21885656}.
-!- SEQUENCE CAUTION:
Sequence=CAM14888.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AL928667; CAM14888.1; ALT_SEQ; Genomic_DNA.
EMBL; AL928667; CAM14889.1; -; Genomic_DNA.
EMBL; AL928667; CAM14890.1; -; Genomic_DNA.
EMBL; BC150703; AAI50704.1; -; mRNA.
RefSeq; XP_011248479.1; XM_011250177.2. [A2ASQ1-1]
UniGene; Mm.273098; -.
PDB; 3PVE; X-ray; 1.40 A; A/B=1510-1701.
PDBsum; 3PVE; -.
ProteinModelPortal; A2ASQ1; -.
SMR; A2ASQ1; -.
IntAct; A2ASQ1; 2.
STRING; 10090.ENSMUSP00000137931; -.
iPTMnet; A2ASQ1; -.
PhosphoSitePlus; A2ASQ1; -.
MaxQB; A2ASQ1; -.
PaxDb; A2ASQ1; -.
PeptideAtlas; A2ASQ1; -.
PRIDE; A2ASQ1; -.
Ensembl; ENSMUST00000105575; ENSMUSP00000101200; ENSMUSG00000041936. [A2ASQ1-1]
GeneID; 11603; -.
UCSC; uc008wgg.1; mouse. [A2ASQ1-1]
CTD; 375790; -.
MGI; MGI:87961; Agrn.
eggNOG; ENOG410ITSI; Eukaryota.
eggNOG; ENOG410YKSA; LUCA.
GeneTree; ENSGT00530000063501; -.
HOGENOM; HOG000033860; -.
HOVERGEN; HBG080471; -.
InParanoid; A2ASQ1; -.
PhylomeDB; A2ASQ1; -.
TreeFam; TF326548; -.
Reactome; R-MMU-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
Reactome; R-MMU-2022928; HS-GAG biosynthesis.
Reactome; R-MMU-2024096; HS-GAG degradation.
Reactome; R-MMU-3000178; ECM proteoglycans.
Reactome; R-MMU-975634; Retinoid metabolism and transport.
ChiTaRS; Agrn; mouse.
EvolutionaryTrace; A2ASQ1; -.
PRO; PR:A2ASQ1; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000041936; -.
ExpressionAtlas; A2ASQ1; baseline and differential.
Genevisible; A2ASQ1; MM.
GO; GO:0005605; C:basal lamina; IDA:MGI.
GO; GO:0005604; C:basement membrane; IDA:MGI.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0031012; C:extracellular matrix; ISO:MGI.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0045202; C:synapse; IDA:MGI.
GO; GO:0043083; C:synaptic cleft; IDA:SynGO.
GO; GO:0030548; F:acetylcholine receptor regulator activity; IDA:MGI.
GO; GO:0042030; F:ATPase inhibitor activity; IDA:BHF-UCL.
GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
GO; GO:0035374; F:chondroitin sulfate binding; IDA:UniProtKB.
GO; GO:0002162; F:dystroglycan binding; ISS:UniProtKB.
GO; GO:0043395; F:heparan sulfate proteoglycan binding; IDA:UniProtKB.
GO; GO:0044325; F:ion channel binding; IPI:BHF-UCL.
GO; GO:0033691; F:sialic acid binding; ISS:UniProtKB.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0007268; P:chemical synaptic transmission; IDA:MGI.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:1903277; P:negative regulation of sodium ion export across plasma membrane; IDA:BHF-UCL.
GO; GO:1903407; P:negative regulation of sodium:potassium-exchanging ATPase activity; IDA:BHF-UCL.
GO; GO:0007528; P:neuromuscular junction development; IGI:MGI.
GO; GO:0045213; P:neurotransmitter receptor metabolic process; IDA:MGI.
GO; GO:0007009; P:plasma membrane organization; IMP:MGI.
GO; GO:0051491; P:positive regulation of filopodium assembly; ISS:UniProtKB.
GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:MGI.
GO; GO:0032092; P:positive regulation of protein binding; IDA:UniProtKB.
GO; GO:2000541; P:positive regulation of protein geranylgeranylation; IMP:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:UniProtKB.
GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IDA:BHF-UCL.
GO; GO:0045887; P:positive regulation of synaptic growth at neuromuscular junction; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:0043113; P:receptor clustering; IDA:MGI.
GO; GO:0086036; P:regulation of cardiac muscle cell membrane potential; IDA:BHF-UCL.
GO; GO:0055117; P:regulation of cardiac muscle contraction; IDA:BHF-UCL.
GO; GO:0043087; P:regulation of GTPase activity; IDA:UniProtKB.
GO; GO:0008582; P:regulation of synaptic growth at neuromuscular junction; IMP:MGI.
Gene3D; 3.30.70.960; -; 1.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR003884; FacI_MAC.
InterPro; IPR003645; Fol_N.
InterPro; IPR002350; Kazal_dom.
InterPro; IPR036058; Kazal_dom_sf.
InterPro; IPR002049; Laminin_EGF.
InterPro; IPR001791; Laminin_G.
InterPro; IPR000082; SEA_dom.
InterPro; IPR036364; SEA_dom_sf.
Pfam; PF00008; EGF; 3.
Pfam; PF00050; Kazal_1; 1.
Pfam; PF07648; Kazal_2; 8.
Pfam; PF00053; Laminin_EGF; 2.
Pfam; PF00054; Laminin_G_1; 3.
Pfam; PF01390; SEA; 1.
SMART; SM00181; EGF; 6.
SMART; SM00179; EGF_CA; 3.
SMART; SM00180; EGF_Lam; 2.
SMART; SM00057; FIMAC; 3.
SMART; SM00274; FOLN; 5.
SMART; SM00280; KAZAL; 9.
SMART; SM00282; LamG; 3.
SMART; SM00200; SEA; 1.
SUPFAM; SSF100895; SSF100895; 9.
SUPFAM; SSF49899; SSF49899; 3.
SUPFAM; SSF82671; SSF82671; 1.
PROSITE; PS00022; EGF_1; 6.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS50026; EGF_3; 4.
PROSITE; PS01248; EGF_LAM_1; 1.
PROSITE; PS50027; EGF_LAM_2; 2.
PROSITE; PS51465; KAZAL_2; 9.
PROSITE; PS50025; LAM_G_DOMAIN; 3.
PROSITE; PS50024; SEA; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Cell junction;
Cell membrane; Complete proteome; Developmental protein;
Differentiation; Disulfide bond; EGF-like domain; Glycoprotein;
Heparan sulfate; Laminin EGF-like domain; Membrane; Phosphoprotein;
Polymorphism; Proteoglycan; Reference proteome; Repeat; Signal-anchor;
Synapse; Transmembrane; Transmembrane helix.
CHAIN 1 1950 Agrin.
/FTId=PRO_0000356178.
CHAIN 48 986 Agrin N-terminal 110 kDa subunit.
/FTId=PRO_0000421617.
CHAIN 987 1950 Agrin C-terminal 110 kDa subunit.
/FTId=PRO_0000421618.
CHAIN 987 1745 Agrin C-terminal 90 kDa fragment.
/FTId=PRO_0000421619.
CHAIN 1746 1950 Agrin C-terminal 22 kDa fragment.
/FTId=PRO_0000421620.
TOPO_DOM 1 26 Cytoplasmic. {ECO:0000255}.
TRANSMEM 27 47 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 48 1950 Extracellular. {ECO:0000255}.
DOMAIN 86 139 Kazal-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
DOMAIN 159 214 Kazal-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
DOMAIN 232 286 Kazal-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
DOMAIN 303 358 Kazal-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
DOMAIN 379 431 Kazal-like 5. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
DOMAIN 442 496 Kazal-like 6. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
DOMAIN 502 561 Kazal-like 7. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
DOMAIN 594 647 Kazal-like 8. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
DOMAIN 688 741 Laminin EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00460}.
DOMAIN 742 788 Laminin EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00460}.
DOMAIN 812 866 Kazal-like 9. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
DOMAIN 1014 1136 SEA. {ECO:0000255|PROSITE-
ProRule:PRU00188}.
DOMAIN 1211 1249 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1254 1430 Laminin G-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 1431 1468 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1470 1507 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1517 1699 Laminin G-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 1700 1739 EGF-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1775 1947 Laminin G-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
CA_BIND 1811 1880 {ECO:0000250}.
CA_BIND 1822 1891 {ECO:0000250}.
COMPBIAS 565 572 Gly/Ser-rich.
COMPBIAS 900 950 Ser/Thr-rich.
COMPBIAS 962 968 Gly/Ser-rich.
COMPBIAS 1138 1206 Ser/Thr-rich.
SITE 986 987 Cleavage, alpha site; by neurotrypsin.
{ECO:0000250}.
SITE 1134 1134 Alternative splice site to produce 'x'
isoforms.
SITE 1633 1633 Alternative splice site to produce 'y'
isoforms.
SITE 1744 1744 Critical for cleavage by neurotrypsin.
{ECO:0000250}.
SITE 1745 1746 Cleavage, beta site; by neurotrypsin.
{ECO:0000250}.
SITE 1770 1770 Alternative splice site to produce 'z'
isoforms.
SITE 1774 1774 Highly important for the agrin receptor
complex activity of the 'z' insert.
{ECO:0000250}.
MOD_RES 569 569 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 571 571 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CARBOHYD 145 145 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 672 672 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 827 827 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 948 948 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1717 1717 O-linked (Fuc...) serine.
{ECO:0000250|UniProtKB:P25304}.
DISULFID 97 116 {ECO:0000250}.
DISULFID 105 137 {ECO:0000250}.
DISULFID 171 191 {ECO:0000250}.
DISULFID 180 212 {ECO:0000250}.
DISULFID 244 263 {ECO:0000250}.
DISULFID 252 284 {ECO:0000250}.
DISULFID 316 335 {ECO:0000250}.
DISULFID 324 356 {ECO:0000250}.
DISULFID 389 408 {ECO:0000250}.
DISULFID 397 429 {ECO:0000250}.
DISULFID 454 473 {ECO:0000250}.
DISULFID 462 494 {ECO:0000250}.
DISULFID 518 538 {ECO:0000250}.
DISULFID 527 559 {ECO:0000250}.
DISULFID 604 624 {ECO:0000250}.
DISULFID 613 645 {ECO:0000250}.
DISULFID 688 700 {ECO:0000250}.
DISULFID 690 707 {ECO:0000250}.
DISULFID 709 718 {ECO:0000250}.
DISULFID 721 739 {ECO:0000250}.
DISULFID 742 754 {ECO:0000250}.
DISULFID 744 761 {ECO:0000250}.
DISULFID 763 772 {ECO:0000250}.
DISULFID 775 786 {ECO:0000250}.
DISULFID 823 843 {ECO:0000250}.
DISULFID 832 864 {ECO:0000250}.
DISULFID 1215 1226 {ECO:0000250}.
DISULFID 1220 1237 {ECO:0000250}.
DISULFID 1239 1248 {ECO:0000250}.
DISULFID 1401 1430 {ECO:0000250}.
DISULFID 1435 1446 {ECO:0000250}.
DISULFID 1440 1456 {ECO:0000250}.
DISULFID 1458 1467 {ECO:0000250}.
DISULFID 1474 1485 {ECO:0000250}.
DISULFID 1479 1495 {ECO:0000250}.
DISULFID 1497 1506 {ECO:0000250}.
DISULFID 1704 1718 {ECO:0000250}.
DISULFID 1712 1727 {ECO:0000250}.
DISULFID 1729 1738 {ECO:0000250}.
DISULFID 1921 1947 {ECO:0000250}.
VAR_SEQ 1 61 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_035995.
VAR_SEQ 1634 1637 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_035996.
VAR_SEQ 1771 1788 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_035997.
VARIANT 1061 1061 F -> S (in a mutant strain; shows
symptoms similar to the motor neuron
disease, agrin-associated congenital
myasthenic syndrome (CMS) with
progressive degradation of the
neuromuscular junction, decreased
acetylcholine receptor (AChR) density and
increased subsynaptic reticulum. Synapses
eventually denervate and muscles atrophy.
There is decreased glycosylation and
proteolytic processing is altered due to
changes in sensitivity to neurotrypsin).
{ECO:0000269|PubMed:21890498}.
CONFLICT 1212 1212 P -> T (in Ref. 2; AAI50704).
{ECO:0000305}.
STRAND 1520 1525 {ECO:0000244|PDB:3PVE}.
STRAND 1527 1530 {ECO:0000244|PDB:3PVE}.
HELIX 1533 1535 {ECO:0000244|PDB:3PVE}.
STRAND 1545 1555 {ECO:0000244|PDB:3PVE}.
STRAND 1557 1564 {ECO:0000244|PDB:3PVE}.
STRAND 1572 1578 {ECO:0000244|PDB:3PVE}.
STRAND 1581 1590 {ECO:0000244|PDB:3PVE}.
STRAND 1592 1596 {ECO:0000244|PDB:3PVE}.
STRAND 1605 1614 {ECO:0000244|PDB:3PVE}.
STRAND 1617 1622 {ECO:0000244|PDB:3PVE}.
STRAND 1628 1631 {ECO:0000244|PDB:3PVE}.
STRAND 1649 1652 {ECO:0000244|PDB:3PVE}.
HELIX 1657 1659 {ECO:0000244|PDB:3PVE}.
HELIX 1662 1664 {ECO:0000244|PDB:3PVE}.
STRAND 1671 1679 {ECO:0000244|PDB:3PVE}.
HELIX 1687 1689 {ECO:0000244|PDB:3PVE}.
STRAND 1690 1695 {ECO:0000244|PDB:3PVE}.
SEQUENCE 1950 AA; 207539 MW; 0679A3F6D8BD1286 CRC64;
MPPLPLEHRP RQQPGASVLV RYFMIPCNIC LILLATSTLG FAVLLFLSNY KPGIHFTAAP
SMPPDVCRGM LCGFGAVCEP SVEDPGRASC VCKKNVCPAM VAPVCGSDAS TYSNECELQR
AQCNQQRRIR LLRQGPCGSR DPCANVTCSF GSTCVPSADG QTASCLCPTT CFGAPDGTVC
GSDGVDYPSE CQLLRHACAN QEHIFKKFDG PCDPCQGSMS DLNHICRVNP RTRHPEMLLR
PENCPAQHTP ICGDDGVTYE NDCVMSRIGA ARGLLLQKVR SGQCQTRDQC PETCQFNSVC
LSRRGRPHCS CDRVTCDGAY RPVCAQDGHT YDNDCWRQQA ECRQQQTIPP KHQGPCDQTP
SPCRGAQCAF GATCTVKNGK AVCECQRVCS GGYDPVCGSD GVTYGSVCEL ESMACTLGRE
IRVARRGPCD RCGQCRFGSL CEVETGRCVC PSECVESAQP VCGSDGHTYA SECELHVHAC
THQISLYVAS AGHCQTCGET VCTFGAVCSA GQCVCPRCEH PPPGPVCGSD GVTYLSACEL
REAACQQQVQ IEEARAGPCE PAECGSGGSG SGEDNACEQE LCRQHGGVWD EDSEDGPCVC
DFSCQSVLKS PVCGSDGVTY STECHLKKAR CEARQELYVA AQGACRGPTL APLLPMASPH
CAQTPYGCCQ DNVTAAQGVG LAGCPSTCHC NPHGSYSGTC DPVTGQCSCR PGVGGLRCDR
CEPGFWNFRG IVTDGHSGCT PCSCDPRGAV RDDCEQMTGL CSCRPGVAGP KCGQCPDGQA
LGHLGCEADP TTPVTCVEMH CEFGASCVEE AGFAQCVCPT LTCPEANSTK VCGSDGVTYG
NECQLKTIAC RQRLDISIQS LGPCRESVAP GVSPTSASMT TPRHILSRTL ASPHSSLPLS
PSTTAHDWPT PLPTSPQTVV GTPRSTAATP SDVASLATAI FRESGSTNGS GDEELSGDEE
ASGGGSGGLE PPVGSVVVTH GPPIERASCY NSPLGCCSDG KTPSLDSEGS NCPATKAFQG
VLELEGVEGQ ELFYTPEMAD PKSELFGETA RSIESTLDDL FRNSDVKKDF WSIRLRELGP
GKLVRAIVDV HFDPTTAFQA PDVGQALLQQ IQVSRPWALA VRRPLREHVR FLDFDWFPTF
FTGAATGTTA AVATARATTV SRLSASSVTP RVYPSYTSRP VGRTTAPLTT RRPPTTTASI
DRPRTPGPQR PPKSCDSQPC LHGGTCQDLD SGKGFSCSCT AGRAGTVCEK VQLPSVPAFK
GHSFLAFPTL RAYHTLRLAL EFRALETEGL LLYNGNARGK DFLALALLDG HVQFRFDTGS
GPAVLTSLVP VEPGRWHRLE LSRHWRQGTL SVDGEAPVVG ESPSGTDGLN LDTKLYVGGL
PEEQVATVLD RTSVGIGLKG CIRMLDINNQ QLELSDWQRA VVQSSGVGEC GDHPCSPNPC
HGGALCQALE AGVFLCQCPP GRFGPTCADE KNPCQPNPCH GSAPCHVLSR GGAKCACPLG
RSGSFCETVL ENAGSRPFLA DFNGFSYLEL KGLHTFERDL GEKMALEMVF LARGPSGLLL
YNGQKTDGKG DFVSLALHNR HLEFRYDLGK GAAIIRSKEP IALGTWVRVF LERNGRKGAL
QVGDGPRVLG ESPKSRKVPH TMLNLKEPLY VGGAPDFSKL ARGAAVASGF DGAIQLVSLR
GHQLLTQEHV LRAVDVAPFA GHPCTQAVDN PCLNGGSCIP REATYECLCP GGFSGLHCEK
GIVEKSVGDL ETLAFDGRTY IEYLNAVTES ELTNEIPAPE TLDSRALFSE KALQSNHFEL
SLRTEATQGL VLWIGKVGER ADYMALAIVD GHLQLSYDLG SQPVVLRSTV KVNTNRWLRV
RAHREHREGS LQVGNEAPVT GSSPLGATQL DTDGALWLGG LQKLPVGQAL PKAYGTGFVG
CLRDVVVGHR QLHLLEDAVT KPELRPCPTL


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