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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_CHICK             Reviewed;        2081 AA.
P31696; Q90609; Q90685;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
06-MAR-2013, sequence version 3.
22-NOV-2017, entry version 171.
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;
Flags: Precursor;
Name=AGRN; Synonyms=AGRIN;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 5), AND FUNCTION.
PubMed=7860635; DOI=10.1083/jcb.128.4.625;
Gesemann M., Denzer A.J., Ruegg M.A.;
"Acetylcholine receptor-aggregating activity of agrin isoforms and
mapping of the active site.";
J. Cell Biol. 128:625-636(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-221 (ISOFORMS 1 AND 9), GLYCOSYLATION,
INTERACTION WITH LAMININ, TISSUE SPECIFICITY, AND SUBCELLULAR
LOCATION.
TISSUE=Spinal cord;
PubMed=8522611; DOI=10.1083/jcb.131.6.1547;
Denzer A.J., Gesemann M., Schumacher B., Rueegg M.A.;
"An amino-terminal extension is required for the secretion of chick
agrin and its binding to extracellular matrix.";
J. Cell Biol. 131:1547-1560(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 94-2073 (ISOFORM 1).
TISSUE=Brain;
PubMed=1314620; DOI=10.1016/0896-6273(92)90089-V;
Tsim K.W.K., Rueegg M.A., Escher G., Kroeger S., McMahan U.J.;
"cDNA that encodes active agrin.";
Neuron 8:677-689(1992).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1901-1921 (ISOFORM 1).
STRAIN=White leghorn;
PubMed=8393816; DOI=10.1006/dbio.1993.1210;
Thomas W.S., O'Dowd D.K., Smith M.A.;
"Developmental expression and alternative splicing of chick agrin
RNA.";
Dev. Biol. 158:523-535(1993).
[5]
ALTERNATIVE SPLICING.
PubMed=1314621; DOI=10.1016/0896-6273(92)90090-Z;
Rueegg M.A., Tsim K.W.K., Horton S.E., Kroeger S., Escher G.,
Gensch E.M., McMahan U.J.;
"The agrin gene codes for a family of basal lamina proteins that
differ in function and distribution.";
Neuron 8:691-699(1992).
[6]
ALTERNATIVE SPLICING, INTERACTION WITH DAG1, AND HEPARIN BINDING.
PubMed=8607994; DOI=10.1016/S0896-6273(00)80096-3;
Gesemann M., Cavalli V., Denzer A.J., Brancaccio A., Schumacher B.,
Ruegg M.A.;
"Alternative splicing of agrin alters its binding to heparin,
dystroglycan, and the putative agrin receptor.";
Neuron 16:755-767(1996).
[7]
LAMININ BINDING.
PubMed=9151673; DOI=10.1083/jcb.137.3.671;
Denzer A.J., Brandenberger R., Gesemann M., Chiquet M., Ruegg M.A.;
"Agrin binds to the nerve-muscle basal lamina via laminin.";
J. Cell Biol. 137:671-683(1997).
[8]
FUNCTION.
PubMed=11425874; DOI=10.1083/jcb.153.7.1441;
Bezakova G., Helm J.P., Francolini M., Lomo T.;
"Effects of purified recombinant neural and muscle agrin on skeletal
muscle fibers in vivo.";
J. Cell Biol. 153:1441-1452(2001).
[9]
ALTERNATIVE SPLICING (ISOFORMS 1 AND 9), 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).
[10]
HEPARAN SULFATE BINDING, AND CHONDROITIN SULFATE BINDING.
PubMed=12773545; DOI=10.1074/jbc.M212676200;
Winzen U., Cole G.J., Halfter W.;
"Agrin is a chimeric proteoglycan with the attachment sites for
heparan sulfate/chondroitin sulfate located in two multiple serine-
glycine clusters.";
J. Biol. Chem. 278:30106-30114(2003).
[11]
HEPARAN SULFATE BINDING, CHONDROITIN SULFATE BINDING, AND FUNCTION.
PubMed=15198666; DOI=10.1111/j.1471-4159.2004.02454.x;
Baerwald-de la Torre K., Winzen U., Halfter W., Bixby J.L.;
"Glycosaminoglycan-dependent and -independent inhibition of neurite
outgrowth by agrin.";
J. Neurochem. 90:50-61(2004).
[12]
FUNCTION, ALTERNATIVE SPLICING, INTERACTION WITH DAG1, HEPARIN
BINDING, AND MUTAGENESIS OF ASN-1905; GLU-1906; ILE-1907;
1905-ASN--ILE-1907 AND 1902-HIS--PRO-1908.
PubMed=17012237; DOI=10.1074/jbc.M607887200;
Scotton P., Bleckmann D., Stebler M., Sciandra F., Brancaccio A.,
Meier T., Stetefeld J., Ruegg M.A.;
"Activation of muscle-specific receptor tyrosine kinase and binding to
dystroglycan are regulated by alternative mRNA splicing of agrin.";
J. Biol. Chem. 281:36835-36845(2006).
[13]
INTERACTION WITH DAG1, STRUCTURE OF CARBOHYDRATES, AND FUNCTION.
PubMed=17649979; DOI=10.1021/bi7006383;
Sallum C.O., Kammerer R.A., Alexandrescu A.T.;
"Thermodynamic and structural studies of carbohydrate binding by the
agrin-G3 domain.";
Biochemistry 46:9541-9550(2007).
[14]
INTERDOMAIN DISULFIDE BOND.
PubMed=19845005; DOI=10.1002/pro.276;
McFarlane A.A., Stetefeld J.;
"An interdomain disulfide bridge links the NtA and first FS domain in
agrin.";
Protein Sci. 18:2421-2428(2009).
[15]
FUNCTION OF ISOFORM 9.
PubMed=19940118; DOI=10.1074/jbc.M109.039420;
Porten E., Seliger B., Schneider V.A., Woll S., Stangel D.,
Ramseger R., Kroger S.;
"The process-inducing activity of transmembrane agrin requires
follistatin-like domains.";
J. Biol. Chem. 285:3114-3125(2010).
[16]
PROTEOLYTIC PROCESSING BY MMPS, AND FUNCTION.
PubMed=22984437; DOI=10.1371/journal.pone.0043669;
Patel T.R., Butler G., McFarlane A., Xie I., Overall C.M.,
Stetefeld J.;
"Site specific cleavage mediated by MMPs regulates function of
agrin.";
PLoS ONE 7:E43669-E43669(2012).
[17]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 26-156 IN COMPLEX WITH
LAMININ, AND DISULFIDE BOND.
PubMed=11473262; DOI=10.1038/90422;
Stetefeld J., Jenny M., Schulthess T., Landwehr R., Schumacher B.,
Frank S., Rueegg M.A., Engel J., Kammerer R.A.;
"The laminin-binding domain of agrin is structurally related to N-
TIMP-1.";
Nat. Struct. Biol. 8:705-709(2001).
[18]
STRUCTURE BY NMR OF 1870-2081 IN COMPLEX WITH CALCIUM IONS, X-RAY
CRYSTALLOGRAPHY (1.42 ANGSTROMS) OF 1870-2081 IN COMPLEX WITH CALCIUM
IONS, AND DISULFIDE BOND.
PubMed=15016366; DOI=10.1016/j.str.2004.02.001;
Stetefeld J., Alexandrescu A.T., Maciejewski M.W., Jenny M.,
Rathgeb-Szabo K., Schulthess T., Landwehr R., Frank S., Rueegg M.A.,
Kammerer R.A.;
"Modulation of agrin function by alternative splicing and Ca2+
binding.";
Structure 12:503-515(2004).
[19]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 26-156, INTERACTION WITH
LAMININ, AND DISULFIDE BOND.
PubMed=15694127; DOI=10.1016/j.matbio.2004.11.003;
Mascarenhas J.B., Rueegg M.A., Sasaki T., Eble J.A., Engel J.,
Stetefeld J.;
"Structure and laminin-binding specificity of the NtA domain expressed
in eukaryotic cells.";
Matrix Biol. 23:507-513(2005).
-!- 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 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.
-!- FUNCTION: 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.
-!- FUNCTION: 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.
-!- FUNCTION: 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.
-!- FUNCTION: 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.
{ECO:0000250, ECO:0000269|PubMed:11425874,
ECO:0000269|PubMed:15198666, ECO:0000269|PubMed:17012237,
ECO:0000269|PubMed:17649979, ECO:0000269|PubMed:19940118,
ECO:0000269|PubMed:22984437, ECO:0000269|PubMed:7860635}.
-!- 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 'B' splice variants 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. 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. {ECO:0000250, ECO:0000269|PubMed:11473262,
ECO:0000269|PubMed:15016366, ECO:0000269|PubMed:15694127,
ECO:0000269|PubMed:17012237, ECO:0000269|PubMed:17649979,
ECO:0000269|PubMed:8522611, ECO:0000269|PubMed:8607994}.
-!- INTERACTION:
P05067:APP (xeno); NbExp=3; IntAct=EBI-457650, EBI-2431589;
P02469:Lamb1 (xeno); NbExp=2; IntAct=EBI-457650, EBI-6662997;
-!- SUBCELLULAR LOCATION: Isoform 1: Secreted, extracellular space,
extracellular matrix {ECO:0000269|PubMed:11161480,
ECO:0000269|PubMed:8522611}. Note=Synaptic basal lamina at the
neuromuscular junction. {ECO:0000269|PubMed:11161480}.
-!- SUBCELLULAR LOCATION: Isoform 9: Cell junction, synapse
{ECO:0000269|PubMed:11161480}. Cell membrane
{ECO:0000269|PubMed:11161480}; Single-pass type II membrane
protein {ECO:0000269|PubMed:11161480}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=10;
Comment=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.;
Name=1; Synonyms=LN-agrin, agrin A4B19;
IsoId=P31696-1; Sequence=Displayed;
Name=2; Synonyms=Agrin-related protein 1, agrin A4B0;
IsoId=P31696-2; Sequence=VSP_045774;
Name=3; Synonyms=Agrin-related protein 2, agrin A4B8;
IsoId=P31696-3; Sequence=VSP_045776;
Name=4; Synonyms=Agrin A4B11;
IsoId=P31696-4; Sequence=VSP_045775;
Name=5; Synonyms=Muscle agrin, agrin A0B0;
IsoId=P31696-5; Sequence=VSP_045773, VSP_045774;
Name=6; Synonyms=Agrin A0B8;
IsoId=P31696-6; Sequence=VSP_045773, VSP_045776;
Name=7; Synonyms=Muscle agrin, agrin A0B11;
IsoId=P31696-7; Sequence=VSP_045773, VSP_045775;
Name=8; Synonyms=Agrin A0B19;
IsoId=P31696-8; Sequence=VSP_045773;
Name=9; Synonyms=TM-agrin, SN-agrin;
IsoId=P31696-9; Sequence=VSP_045770, VSP_045771;
Note=Transmembrane isoform produced by usage of an alternative
first exon.;
Name=10;
IsoId=P31696-10; Sequence=VSP_045772;
-!- TISSUE SPECIFICITY: Detected in embryonic brain, spinal cord,
skeletal muscle, vitreous humor and liver (at protein level).
{ECO:0000269|PubMed:8522611}.
-!- DOMAIN: The 4 amino acid insert at the 'A' site is required for
effecient binding of heparin.
-!- DOMAIN: The NtA domain, absent in TM-Agrin, is required for
binding laminin and connecting to basal lamina.
-!- 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.
-!- PTM: 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. {ECO:0000250, ECO:0000269|PubMed:8522611}.
-!- PTM: 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).
{ECO:0000250}.
-!- PTM: Proteolytically cleaved in vitro in both the N-terminal and
C-terminal by several matrix metaloproteinases (MMPs).
{ECO:0000269|PubMed:22984437}.
-!- SEQUENCE CAUTION:
Sequence=AAA48585.1; Type=Frameshift; Positions=110; Evidence={ECO:0000305};
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EMBL; U35613; AAC59740.1; -; mRNA.
EMBL; M94271; AAA48585.1; ALT_FRAME; mRNA.
EMBL; M97371; AAA48586.1; -; mRNA.
EMBL; M97372; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; U07271; AAA16788.1; -; mRNA.
PIR; JH0591; AGCH.
UniGene; Gga.4448; -.
UniGene; Gga.48948; -.
PDB; 1JB3; X-ray; 1.60 A; A=26-156.
PDB; 1JC7; X-ray; 2.73 A; A=26-154.
PDB; 1PXU; X-ray; 2.20 A; A=25-155.
PDB; 1PZ7; X-ray; 1.42 A; A/B=1870-2081.
PDB; 1PZ8; X-ray; 2.35 A; A/B/C/D=1870-2081.
PDB; 1PZ9; X-ray; 2.80 A; A/B=1870-2081.
PDB; 1Q56; NMR; -; A=1870-2081.
PDB; 3I70; X-ray; 2.30 A; A=26-153.
PDBsum; 1JB3; -.
PDBsum; 1JC7; -.
PDBsum; 1PXU; -.
PDBsum; 1PZ7; -.
PDBsum; 1PZ8; -.
PDBsum; 1PZ9; -.
PDBsum; 1Q56; -.
PDBsum; 3I70; -.
ProteinModelPortal; P31696; -.
SMR; P31696; -.
BioGrid; 676782; 1.
IntAct; P31696; 5.
STRING; 9031.ENSGALP00000039379; -.
PaxDb; P31696; -.
PRIDE; P31696; -.
eggNOG; ENOG410ITSI; Eukaryota.
eggNOG; ENOG410YKSA; LUCA.
HOGENOM; HOG000033860; -.
HOVERGEN; HBG080471; -.
InParanoid; P31696; -.
EvolutionaryTrace; P31696; -.
Proteomes; UP000000539; Unplaced.
GO; GO:0030424; C:axon; IDA:AgBase.
GO; GO:0005605; C:basal lamina; IDA:AgBase.
GO; GO:0045178; C:basal part of cell; IDA:AgBase.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0031012; C:extracellular matrix; TAS:AgBase.
GO; GO:0005576; C:extracellular region; IMP:AgBase.
GO; GO:0005615; C:extracellular space; IDA:AgBase.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0045121; C:membrane raft; IDA:AgBase.
GO; GO:0031594; C:neuromuscular junction; IDA:AgBase.
GO; GO:0005886; C:plasma membrane; IDA:AgBase.
GO; GO:0045202; C:synapse; IDA:AgBase.
GO; GO:0030548; F:acetylcholine receptor regulator activity; IDA:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0035374; F:chondroitin sulfate binding; IDA:UniProtKB.
GO; GO:0002162; F:dystroglycan binding; IDA:UniProtKB.
GO; GO:0050840; F:extracellular matrix binding; IMP:AgBase.
GO; GO:0005539; F:glycosaminoglycan binding; IMP:AgBase.
GO; GO:0043395; F:heparan sulfate proteoglycan binding; IDA:UniProtKB.
GO; GO:0008201; F:heparin binding; IDA:UniProtKB.
GO; GO:0043236; F:laminin binding; IDA:UniProtKB.
GO; GO:0043237; F:laminin-1 binding; IDA:AgBase.
GO; GO:0004872; F:receptor activity; TAS:AgBase.
GO; GO:0033691; F:sialic acid binding; IDA:UniProtKB.
GO; GO:0030297; F:transmembrane receptor protein tyrosine kinase activator activity; IDA:UniProtKB.
GO; GO:0031532; P:actin cytoskeleton reorganization; TAS:AgBase.
GO; GO:0007420; P:brain development; IMP:AgBase.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0046847; P:filopodium assembly; IDA:AgBase.
GO; GO:0007213; P:G-protein coupled acetylcholine receptor signaling pathway; IEA:InterPro.
GO; GO:0010977; P:negative regulation of neuron projection development; IDA:AgBase.
GO; GO:0007399; P:nervous system development; IDA:AgBase.
GO; GO:0007528; P:neuromuscular junction development; TAS:AgBase.
GO; GO:0007158; P:neuron cell-cell adhesion; TAS:AgBase.
GO; GO:0051491; P:positive regulation of filopodium assembly; ISS:UniProtKB.
GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
GO; GO:0045887; P:positive regulation of synaptic growth at neuromuscular junction; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0043113; P:receptor clustering; IDA:UniProtKB.
GO; GO:0071340; P:skeletal muscle acetylcholine-gated channel clustering; IDA:AgBase.
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; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
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; IPR004850; NtA_dom.
InterPro; IPR000082; SEA_dom.
InterPro; IPR036364; SEA_dom_sf.
InterPro; IPR008993; TIMP-like_OB-fold.
Pfam; PF00008; EGF; 4.
Pfam; PF00050; Kazal_1; 2.
Pfam; PF07648; Kazal_2; 7.
Pfam; PF00053; Laminin_EGF; 2.
Pfam; PF00054; Laminin_G_1; 3.
Pfam; PF03146; NtA; 1.
Pfam; PF01390; SEA; 1.
SMART; SM00181; EGF; 8.
SMART; SM00179; EGF_CA; 3.
SMART; SM00180; EGF_Lam; 2.
SMART; SM00057; FIMAC; 2.
SMART; SM00274; FOLN; 6.
SMART; SM00280; KAZAL; 9.
SMART; SM00282; LamG; 3.
SMART; SM00200; SEA; 1.
SUPFAM; SSF100895; SSF100895; 9.
SUPFAM; SSF49899; SSF49899; 3.
SUPFAM; SSF50242; SSF50242; 1.
SUPFAM; SSF82671; SSF82671; 1.
PROSITE; PS00010; ASX_HYDROXYL; 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; PS51121; NTA; 1.
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;
Extracellular matrix; Glycoprotein; Heparan sulfate;
Laminin EGF-like domain; Membrane; Metal-binding; Proteoglycan;
Reference proteome; Repeat; Secreted; Signal; Synapse; Transmembrane.
SIGNAL 1 24 {ECO:0000255}.
CHAIN 25 2081 Agrin.
/FTId=PRO_0000055624.
CHAIN 25 1116 Agrin N-terminal 110 kDa subunit.
/FTId=PRO_0000421629.
CHAIN 1117 2081 Agrin C-terminal 110 kDa subunit.
/FTId=PRO_0000421630.
CHAIN 1117 1876 Agrin C-terminal 90 kDa fragment.
/FTId=PRO_0000421631.
CHAIN 1877 2081 Agrin C-terminal 22 kDa fragment.
/FTId=PRO_0000421632.
DOMAIN 25 159 NtA. {ECO:0000255|PROSITE-
ProRule:PRU00443}.
DOMAIN 193 246 Kazal-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
DOMAIN 268 321 Kazal-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
DOMAIN 339 393 Kazal-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
DOMAIN 409 464 Kazal-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
DOMAIN 486 538 Kazal-like 5. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
DOMAIN 551 603 Kazal-like 6. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
DOMAIN 616 668 Kazal-like 7. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
DOMAIN 700 753 Kazal-like 8. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
DOMAIN 793 846 Laminin EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00460}.
DOMAIN 847 893 Laminin EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00460}.
DOMAIN 917 971 Kazal-like 9. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
DOMAIN 1144 1266 SEA. {ECO:0000255|PROSITE-
ProRule:PRU00188}.
DOMAIN 1347 1383 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1388 1563 Laminin G-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 1564 1601 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1603 1640 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1650 1831 Laminin G-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 1832 1870 EGF-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1894 2078 Laminin G-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
CA_BIND 1953 2022
COMPBIAS 671 678 Gly/Ser-rich.
COMPBIAS 974 1113 Ser/Thr-rich.
COMPBIAS 1072 1099 Gly/Ser-rich.
COMPBIAS 1268 1337 Ser/Thr-rich.
SITE 140 141 Cleavage; by MMP1.
SITE 153 154 Cleavage; by MMP7.
SITE 161 162 Cleavage; by MMP12.
SITE 1116 1117 Cleavage, alpha site; by neurotrypsin.
{ECO:0000250}.
SITE 1765 1765 Alternative splice site to produce 'A'
isoform. {ECO:0000250}.
SITE 1821 1822 Cleavage; by MMP1.
SITE 1830 1831 Cleavage; by MMP7.
SITE 1875 1875 Critical for cleavage by neurotrypsin.
{ECO:0000250}.
SITE 1876 1877 Cleavage, beta site; by neurotrypsin.
{ECO:0000250}.
SITE 1901 1901 Alternative splice site to produce 'B'
isoforms. {ECO:0000250}.
SITE 1905 1905 Highly important for the agrin receptor
complex activity of the 'B8' insert.
{ECO:0000250}.
CARBOHYD 130 130 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 508 508 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 777 777 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 882 882 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 932 932 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 26 98
DISULFID 147 179 Or C-147 with C-185.
DISULFID 204 223 {ECO:0000255}.
DISULFID 212 244 {ECO:0000255}.
DISULFID 278 298 {ECO:0000255}.
DISULFID 287 319 {ECO:0000255}.
DISULFID 351 370 {ECO:0000255}.
DISULFID 359 391 {ECO:0000255}.
DISULFID 422 441 {ECO:0000255}.
DISULFID 430 462 {ECO:0000255}.
DISULFID 496 515 {ECO:0000255}.
DISULFID 504 536 {ECO:0000255}.
DISULFID 561 580 {ECO:0000255}.
DISULFID 569 601 {ECO:0000255}.
DISULFID 625 645 {ECO:0000255}.
DISULFID 634 666 {ECO:0000255}.
DISULFID 710 730 {ECO:0000255}.
DISULFID 719 751 {ECO:0000255}.
DISULFID 793 805 {ECO:0000250}.
DISULFID 795 812 {ECO:0000250}.
DISULFID 814 823 {ECO:0000250}.
DISULFID 826 844 {ECO:0000250}.
DISULFID 847 859 {ECO:0000250}.
DISULFID 849 866 {ECO:0000250}.
DISULFID 868 877 {ECO:0000250}.
DISULFID 880 891 {ECO:0000250}.
DISULFID 928 948 {ECO:0000255}.
DISULFID 937 969 {ECO:0000255}.
DISULFID 1351 1362 {ECO:0000250}.
DISULFID 1356 1371 {ECO:0000250}.
DISULFID 1373 1382 {ECO:0000250}.
DISULFID 1568 1579 {ECO:0000250}.
DISULFID 1573 1589 {ECO:0000250}.
DISULFID 1591 1600 {ECO:0000250}.
DISULFID 1607 1618 {ECO:0000250}.
DISULFID 1612 1628 {ECO:0000250}.
DISULFID 1630 1639 {ECO:0000250}.
DISULFID 1836 1849 {ECO:0000250}.
DISULFID 1843 1858 {ECO:0000250}.
DISULFID 1860 1869 {ECO:0000250}.
DISULFID 2052 2078
VAR_SEQ 1 60 MGGSGAAATLALGLALGLALGGWANCPERELQRREEEANVV
LTGTVEEIMNVDPVHHTYS -> MTACQYPMAPGALERDRL
YQHKVSLVVRYFMIPCNICLILLATSTLGFAVLLFLNNY
(in isoform 9).
{ECO:0000303|PubMed:8522611}.
/FTId=VSP_045770.
VAR_SEQ 61 157 Missing (in isoform 9).
{ECO:0000303|PubMed:8522611}.
/FTId=VSP_045771.
VAR_SEQ 150 156 Missing (in isoform 10). {ECO:0000305}.
/FTId=VSP_045772.
VAR_SEQ 1766 1769 Missing (in isoform 5, isoform 6, isoform
7 and isoform 8).
{ECO:0000303|PubMed:7860635}.
/FTId=VSP_045773.
VAR_SEQ 1902 1920 Missing (in isoform 2 and isoform 5).
{ECO:0000303|PubMed:7860635}.
/FTId=VSP_045774.
VAR_SEQ 1902 1909 Missing (in isoform 4 and isoform 7).
{ECO:0000303|PubMed:7860635}.
/FTId=VSP_045775.
VAR_SEQ 1910 1920 Missing (in isoform 3 and isoform 6).
{ECO:0000303|PubMed:7860635}.
/FTId=VSP_045776.
MUTAGEN 1902 1908 HLSNEIP->AAANEIA: No reduction in AGRN-
induced MUSK phosphorylation.
{ECO:0000269|PubMed:17012237}.
MUTAGEN 1905 1907 NEI->AAA,AES: Large reduction in AGRN-
induced MUSK phosphorylation.
{ECO:0000269|PubMed:17012237}.
MUTAGEN 1905 1906 NE->AA: Some reduction in AGRN-induced
MUSK phosphorylation.
MUTAGEN 1905 1905 N->A: No effect on AGRN-induced MUSK
phosphorylation.
{ECO:0000269|PubMed:17012237}.
MUTAGEN 1906 1906 E->A: No effect on AGRN-induced MUSK
phosphorylation.
{ECO:0000269|PubMed:17012237}.
MUTAGEN 1907 1907 I->A: No effect on AGRN-induced MUSK
phosphorylation.
{ECO:0000269|PubMed:17012237}.
CONFLICT 1247 1249 RTI -> SIL (in Ref. 3; AAA48586).
{ECO:0000305}.
HELIX 31 36 {ECO:0000244|PDB:1JB3}.
STRAND 39 53 {ECO:0000244|PDB:1JB3}.
TURN 54 57 {ECO:0000244|PDB:1JB3}.
STRAND 58 70 {ECO:0000244|PDB:1JB3}.
HELIX 72 78 {ECO:0000244|PDB:1JB3}.
TURN 83 85 {ECO:0000244|PDB:1JB3}.
STRAND 86 92 {ECO:0000244|PDB:1JB3}.
STRAND 97 99 {ECO:0000244|PDB:1PXU}.
STRAND 107 114 {ECO:0000244|PDB:1JB3}.
HELIX 117 119 {ECO:0000244|PDB:1JB3}.
TURN 120 125 {ECO:0000244|PDB:1JB3}.
STRAND 126 129 {ECO:0000244|PDB:1JB3}.
HELIX 138 152 {ECO:0000244|PDB:1JB3}.
STRAND 1879 1881 {ECO:0000244|PDB:1PZ7}.
STRAND 1884 1889 {ECO:0000244|PDB:1PZ7}.
STRAND 1892 1895 {ECO:0000244|PDB:1PZ7}.
STRAND 1922 1935 {ECO:0000244|PDB:1PZ7}.
STRAND 1938 1946 {ECO:0000244|PDB:1PZ7}.
STRAND 1954 1960 {ECO:0000244|PDB:1PZ7}.
STRAND 1963 1972 {ECO:0000244|PDB:1PZ7}.
STRAND 1975 1982 {ECO:0000244|PDB:1PZ7}.
STRAND 1985 1987 {ECO:0000244|PDB:1PZ7}.
STRAND 1989 1996 {ECO:0000244|PDB:1PZ7}.
STRAND 1999 2004 {ECO:0000244|PDB:1PZ7}.
STRAND 2010 2013 {ECO:0000244|PDB:1PZ7}.
STRAND 2021 2023 {ECO:0000244|PDB:1PZ7}.
STRAND 2026 2031 {ECO:0000244|PDB:1PZ7}.
TURN 2037 2040 {ECO:0000244|PDB:1PZ7}.
HELIX 2043 2046 {ECO:0000244|PDB:1PZ7}.
STRAND 2050 2058 {ECO:0000244|PDB:1PZ7}.
TURN 2065 2067 {ECO:0000244|PDB:1PZ7}.
SEQUENCE 2081 AA; 224980 MW; 87FEFE1A11664F0E CRC64;
MGGSGAAATL ALGLALGLAL GGWANCPERE LQRREEEANV VLTGTVEEIM NVDPVHHTYS
CKVRVWRYLK GKDIVTHEIL LDGGNKVVIG GFGDPLICDN QVSTGDTRIF FVNPAPQYMW
PAHRNELMLN SSLMRITLRN LEEVEHCVEE HRKLLADKPN SYFTQTPPTP RDACRGMLCG
FGAVCERSPT DPSQASCVCK KTACPVVVAP VCGSDYSTYS NECELEKAQC NQQRRIKVIS
KGPCGSKDPC AEVTCSFGST CVRSADGQTA GCVCPASCSG VAESIVCGSD GKDYRSECDL
NKHACDKQEN VFKKFDGACD PCKGILNDMN RVCRVNPRTR RVELLSRPEN CPSKREPVCG
DDGVTYASEC VMGRTGAIRG LEIQKVRSGQ CQHQDKCKDE CKFNAVCLKR WHARCSCDRI
TCDGTYRPVC ARDSRTYSND CERQKAECHQ KAAIPVKHSG PCDLGTPSPC LSVECTFGAT
CVVKNREPVC ECQQVCQGRY DPVCGSDNRT YGNPCELNAM ACVLKREIRV KHKGPCDRCG
KCQFGAICEA ETGRCVCPTE CVPSSQPVCG TDGNTYGSEC ELHVRACTQQ KNILVAAQGD
CKSCGTTVCS FGSTCVGGQC VCPRCEQQPL AQVCGTDGLT YDNRCELRAA SCQQQKSIEV
AKMGPCEDEC GSGGSGSGDG SECEQDRCRH YGGWWDEDAE DDRCVCDFTC LAVPRSPVCG
SDDVTYANEC ELKKTRCEKR QNLYVTSQGA CRALTTTPPP LPVVHCSQTI YGCCPDNMTL
ALGVGAAGCP STCQCNPYGS YGGTCDPATG QCSCKPGVGG LKCDRCEPGF WNFRGIVTDS
KSGCTPCNCD PVGSVRDDCE QMTGLCSCKT GITGMKCNQC PNGSKMGMAG CEKDPSAPKS
CEEMSCEFGA TCVEVNGFAH CECPSPLCSE ANMTKVCGSD GVTYGDQCQL KTIACRQGQL
ITVKHVGQCH ESITHTSHTM PPTPLPTLPL DKLIVPPPLQ LTTQAPEPTE LATTSLLMEA
SPTTRSHPTT RRVTTTRPVT TPWMTHGVLK TTVRPLSTSP VVLATTQPPY AESGSAEGSG
DQEMSISGDQ ESSGAGSAGE EEVEESQVTP TPAIERATCY NTPLGCCSDG KTAAADAEGS
NCPATKVFQG VLILEEVEGQ ELFYTPEMAD PKSELFGETA RSIESALDEL FRNSDVKNDF
KSIRVRDLGQ SSAVRVIVES HFDPATSYTA ADVQAASLKQ IRASKKRTIL VKKPQQEHVK
FMDFDWIPRI FTTTITTTTA TTMAPATTRR HTTASAATTA HILRQDTVGH PSAKLAAPAS
TRRPTSTLPT TARRKPTRQP PSTTKKPSRP CDSHPCLHGG TCEDDGREFT CRCPAGKGGA
VCEKPIRYFI PSFGGKSYLA FKMMKAYHTV RIAMEFRATE LSGLLLYNGQ NRGKDFISLA
LVGGFVELRF NTGSGTGVIT SKVRVEPGKW HQLVVNRNRR SGMLAVDGEH VSGESPTGTD
GLNLDTDLFV GGAPEDQMAV VAERTAATVG LKGSIRLLDV NNQMYDLREK GSDVLYGSGV
GECGNDPCHP NPCHHGASCH VKEAEMFHCE CLHSYTGPTC ADERNPCDPT PCHISATCLV
LPEGGAMCAC PMGREGEFCE RVTEQDHTMP FLPEFNGFSY LELNGLQTLF LTCRQMSMEV
VFLAKSPSGM IFYNGQKTDG KGDFVSLALH DGYLEYRYDL GKGAAVLRSK EPVPLNTWIS
VLLERSGRKG VMRINNGERV MGESPKSRKV PHAFLNLKEP FYVGGAPDFS KLARAAAIST
SFYGAVQRIS IKGVPLLKEQ HIRSAVEIST FRAHPCTQKP NPCQNGGTCS PRLESYECAC
QRGFSGAHCE KVIIEKAAGD AEAIAFDGRT YMEYHNAVTK SHLSNEIPAP DALDYPAEPS
EKALQSNHFE LSIKTEATQG LILWSGKGLE RSDYIALAIV DGFVQMMYDL GSKPVVLRST
VPINTNHWTH IKAYRVQREG SLQVGNEAPI TGSSPLGATQ LDTDGALWLG GMERLSVAHK
LPKAYSTGFI GCIRDVIVDR QELHLVEDAL NNPTILHCSA K


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