Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

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_HUMAN             Reviewed;        2068 AA.
O00468; Q5SVA1; Q5SVA2; Q60FE1; Q7KYS8; Q8N4J5; Q96IC1; Q9BTD4;
25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
12-SEP-2018, sequence version 6.
07-NOV-2018, entry version 179.
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;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
TISSUE=Retinal pigment epithelium;
Kato S.;
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
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., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 20-2068 (ISOFORM 6), AND TISSUE
SPECIFICITY.
PubMed=9652404; DOI=10.1046/j.1432-1327.1998.2540123.x;
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.;
"Primary structure and high expression of human agrin in basement
membranes of adult lung and kidney.";
Eur. J. Biochem. 254:123-128(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 20-172 (ISOFORMS 1/3/4/5/6/7), AND
INTERACTION WITH LAMININ.
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1558-2068 (ISOFORM 6), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1869-2068 (ISOFORM 3).
TISSUE=Brain, Colon, and Kidney;
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).
[6]
IDENTIFICATION OF TRANSMEMBRANE ISOFORM (ISOFORM 2).
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).
[7]
IDENTIFICATION OF TRANSMEMBRANE ISOFORM (ISOFORM 2), ALTERNATIVE
SPLICING, AND TISSUE SPECIFICITY.
PubMed=16487930; DOI=10.1016/j.bbrc.2006.01.161;
Kumar P., Ferns M.J., Meizel S.;
"Identification of agrinSN isoform and muscle-specific receptor
tyrosine kinase (MuSK) in sperm.";
Biochem. Biophys. Res. Commun. 342:522-528(2006).
[8]
ERRATUM.
Kumar P., Ferns M.J., Meizel S.;
Biochem. Biophys. Res. Commun. 344:453-453(2006).
[9]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-135.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[10]
IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, AND
SUBCELLULAR LOCATION.
PubMed=20551380; DOI=10.1074/mcp.M110.001693;
Didangelos A., Yin X., Mandal K., Baumert M., Jahangiri M., Mayr M.;
"Proteomics characterization of extracellular space components in the
human aorta.";
Mol. Cell. Proteomics 9:2048-2062(2010).
[11]
INTERACTION WITH LRP4, AND FUNCTION.
PubMed=21969364; DOI=10.1074/jbc.M111.279307;
Zhang W., Coldefy A.S., Hubbard S.R., Burden S.J.;
"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).";
J. Biol. Chem. 286:40624-40630(2011).
[12]
POTENTIAL USAGE AS A BIOMARKER FOR SARCOPENIA.
PubMed=22683512; DOI=10.1016/j.exger.2012.05.021;
Drey M., Sieber C.C., Bauer J.M., Uter W., Dahinden P., Fariello R.G.,
Vrijbloed J.W.;
"C-terminal Agrin Fragment as a potential marker for sarcopenia caused
by degeneration of the neuromuscular junction.";
Exp. Gerontol. 48:76-80(2013).
[13]
INVOLVEMENT IN CMS8, VARIANT CMS8 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-2046,
FUNCTION, AND CHARACTERIZATION OF VARIANT CMS8 ARG-1709.
PubMed=19631309; DOI=10.1016/j.ajhg.2009.06.015;
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., Koenig J., Eymard B., Schaeffer L.,
Hantai D.;
"Identification of an agrin mutation that causes congenital myasthenia
and affects synapse function.";
Am. J. Hum. Genet. 85:155-167(2009).
[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., Koenig J., Eymard B., Schaeffer L.,
Hantai D.;
Am. J. Hum. Genet. 85:536-536(2009).
[15]
VARIANT CMS8 PHE-1727, INTERACTION WITH DAG1, AND CHARACTERIZATION OF
VARIANT CMS8 PHE-1727.
PubMed=22205389; DOI=10.1007/s00439-011-1132-4;
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.;
"LG2 agrin mutation causing severe congenital myasthenic syndrome
mimics functional characteristics of non-neural (z-) agrin.";
Hum. Genet. 131:1123-1135(2012).
[16]
VARIANT VAL-745, VARIANTS CMS8 SER-76; ILE-105 AND ARG-1875, AND
CHARACTERIZATION OF VARIANTS CMS8 SER-76 AND ILE-105.
PubMed=24951643; DOI=10.1093/brain/awu160;
Nicole S., Chaouch A., Torbergsen T., Bauche S., de Bruyckere E.,
Fontenille M.J., Horn M.A., van Ghelue M., Loeseth S., Issop Y.,
Cox D., Mueller J.S., Evangelista T., Staalberg E., Ioos C.,
Barois A., Brochier G., Sternberg D., Fournier E., Hantai D.,
Abicht A., Dusl M., Laval S.H., Griffin H., Eymard B., Lochmueller H.;
"Agrin mutations lead to a congenital myasthenic syndrome with distal
muscle weakness and atrophy.";
Brain 137:2429-2443(2014).
-!- 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. This secreted isoform forms a bridge, after release from
motor neurons, to basal lamina through binding laminin via the NtA
domain.
-!- FUNCTION: 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.
-!- FUNCTION: 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.
-!- FUNCTION: Isoform 3 and isoform 6: lack any 'z' insert, are
muscle-specific and may be involved in endothelial cell
differentiation.
-!- FUNCTION: 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).
{ECO:0000250, ECO:0000269|PubMed:19631309,
ECO:0000269|PubMed:21969364}.
-!- 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 (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. {ECO:0000250,
ECO:0000269|PubMed:21969364, ECO:0000269|PubMed:22205389,
ECO:0000269|PubMed:9151673}.
-!- INTERACTION:
O15265:ATXN7; NbExp=2; IntAct=EBI-947482, EBI-708350;
-!- SUBCELLULAR LOCATION: Isoform 1: Secreted, extracellular space,
extracellular matrix {ECO:0000269|PubMed:20551380}. Note=Synaptic
basal lamina at the neuromuscular junction.
{ECO:0000250|UniProtKB:P31696}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cell junction, synapse
{ECO:0000250|UniProtKB:A2ASQ1}. Cell membrane
{ECO:0000250|UniProtKB:A2ASQ1}; Single-pass type II membrane
protein {ECO:0000250|UniProtKB:A2ASQ1}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Comment=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.;
Name=1; Synonyms=Secreted agrin, LN-agrin;
IsoId=O00468-1; Sequence=Displayed;
Name=2; Synonyms=Transmembrane agrin, TM-agrin;
IsoId=O00468-2; Sequence=VSP_045753, VSP_045754;
Note=Produced by usage of an alternative first exon.;
Name=3; Synonyms=Agrin z(0);
IsoId=O00468-3; Sequence=VSP_045756;
Name=4; Synonyms=Agrin z(+11);
IsoId=O00468-4; Sequence=VSP_045757;
Name=5; Synonyms=Agrin z(+8);
IsoId=O00468-5; Sequence=VSP_045758;
Name=6; Synonyms=Agrin y(0)z(0);
IsoId=O00468-6; Sequence=VSP_045755, VSP_045756;
Name=7; Synonyms=y(0);
IsoId=O00468-7; Sequence=VSP_045755;
-!- 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. {ECO:0000269|PubMed:16487930,
ECO:0000269|PubMed:20551380, ECO:0000269|PubMed:9652404}.
-!- 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/DAG1 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.
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). {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).
-!- DISEASE: Myasthenic syndrome, congenital, 8 (CMS8) [MIM:615120]: A
form of congenital myasthenic syndrome, a group of disorders
characterized by failure of neuromuscular transmission, including
pre-synaptic, synaptic, and post-synaptic disorders that are not
of autoimmune origin. Clinical features are easy fatigability and
muscle weakness. CMS8 is an autosomal recessive disease
characterized by prominent defects of both the pre- and
postsynaptic regions. Affected individuals have onset of muscle
weakness in early childhood; the severity of the weakness and
muscles affected is variable. {ECO:0000269|PubMed:19631309,
ECO:0000269|PubMed:22205389, ECO:0000269|PubMed:24951643}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- MISCELLANEOUS: Cleaved C-terminal fragments may be used as a
biomarker for sarcopenia, age-related progressive loss of skeletal
muscle. {ECO:0000305|PubMed:22683512}.
-!- CAUTION: The unknown residue 'x' in the transmembrane isoform is
probably a proline residue by similarity to mouse and rat
sequences. {ECO:0000305}.
-!- WEB RESOURCE: Name=The Leiden Muscular Dystrophy pages, Agrin
(AGRN); Note=Leiden Open Variation Database (LOVD);
URL="http://www.lovd.nl/AGRN";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AB191264; BAD52440.1; -; mRNA.
EMBL; AL645608; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF016903; AAC39776.1; -; mRNA.
EMBL; U84406; AAB52917.1; -; mRNA.
EMBL; BC004220; AAH04220.2; -; mRNA.
EMBL; BC007649; AAH07649.1; -; mRNA.
EMBL; BC034009; AAH34009.1; -; mRNA.
EMBL; BC063620; AAH63620.1; -; mRNA.
CCDS; CCDS30551.1; -. [O00468-6]
RefSeq; NP_001292204.1; NM_001305275.1. [O00468-1]
RefSeq; NP_940978.2; NM_198576.3. [O00468-6]
RefSeq; XP_005244806.1; XM_005244749.3. [O00468-3]
UniGene; Hs.273330; -.
UniGene; Hs.602356; -.
ProteinModelPortal; O00468; -.
BioGrid; 132000; 19.
IntAct; O00468; 11.
MINT; O00468; -.
STRING; 9606.ENSP00000368678; -.
CarbonylDB; O00468; -.
GlyConnect; 998; -.
iPTMnet; O00468; -.
PhosphoSitePlus; O00468; -.
BioMuta; AGRN; -.
EPD; O00468; -.
MaxQB; O00468; -.
PaxDb; O00468; -.
PeptideAtlas; O00468; -.
PRIDE; O00468; -.
ProteomicsDB; 47914; -.
Ensembl; ENST00000379370; ENSP00000368678; ENSG00000188157. [O00468-6]
GeneID; 375790; -.
KEGG; hsa:375790; -.
UCSC; uc001ack.3; human. [O00468-1]
CTD; 375790; -.
DisGeNET; 375790; -.
EuPathDB; HostDB:ENSG00000188157.13; -.
GeneCards; AGRN; -.
GeneReviews; AGRN; -.
HGNC; HGNC:329; AGRN.
HPA; HPA040090; -.
MalaCards; AGRN; -.
MIM; 103320; gene.
MIM; 615120; phenotype.
neXtProt; NX_O00468; -.
OpenTargets; ENSG00000188157; -.
Orphanet; 98913; Postsynaptic congenital myasthenic syndromes.
Orphanet; 98914; Presynaptic congenital myasthenic syndromes.
PharmGKB; PA24626; -.
eggNOG; ENOG410ITSI; Eukaryota.
eggNOG; ENOG410YKSA; LUCA.
GeneTree; ENSGT00930000150942; -.
HOGENOM; HOG000033860; -.
HOVERGEN; HBG080471; -.
InParanoid; O00468; -.
KO; K06254; -.
OMA; FQGVLIL; -.
OrthoDB; EOG091G048M; -.
TreeFam; TF326548; -.
Reactome; R-HSA-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
Reactome; R-HSA-2022928; HS-GAG biosynthesis.
Reactome; R-HSA-2024096; HS-GAG degradation.
Reactome; R-HSA-216083; Integrin cell surface interactions.
Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions.
Reactome; R-HSA-3000178; ECM proteoglycans.
Reactome; R-HSA-3560783; Defective B4GALT7 causes EDS, progeroid type.
Reactome; R-HSA-3560801; Defective B3GAT3 causes JDSSDHD.
Reactome; R-HSA-3656237; Defective EXT2 causes exostoses 2.
Reactome; R-HSA-3656253; Defective EXT1 causes exostoses 1, TRPS2 and CHDS.
Reactome; R-HSA-419037; NCAM1 interactions.
Reactome; R-HSA-4420332; Defective B3GALT6 causes EDSP2 and SEMDJL1.
Reactome; R-HSA-975634; Retinoid metabolism and transport.
SignaLink; O00468; -.
ChiTaRS; AGRN; human.
GeneWiki; Agrin; -.
GenomeRNAi; 375790; -.
PRO; PR:O00468; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000188157; Expressed in 221 organ(s), highest expression level in right uterine tube.
CleanEx; HS_AGRN; -.
ExpressionAtlas; O00468; baseline and differential.
Genevisible; O00468; HS.
GO; GO:0005604; C:basement membrane; IDA:UniProtKB.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0045202; C:synapse; ISS:UniProtKB.
GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
GO; GO:0035374; F:chondroitin sulfate binding; ISS:UniProtKB.
GO; GO:0002162; F:dystroglycan binding; ISS:UniProtKB.
GO; GO:0005201; F:extracellular matrix structural constituent; HDA:BHF-UCL.
GO; GO:0043395; F:heparan sulfate proteoglycan binding; ISS:UniProtKB.
GO; GO:0043236; F:laminin binding; TAS:UniProtKB.
GO; GO:0033691; F:sialic acid binding; ISS:UniProtKB.
GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:UniProtKB.
GO; GO:0045162; P:clustering of voltage-gated sodium channels; TAS:UniProtKB.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0007213; P:G protein-coupled acetylcholine receptor signaling pathway; TAS:UniProtKB.
GO; GO:0006024; P:glycosaminoglycan biosynthetic process; TAS:Reactome.
GO; GO:0006027; P:glycosaminoglycan catabolic process; TAS:Reactome.
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 by RNA polymerase II; ISS:UniProtKB.
GO; GO:0043113; P:receptor clustering; IDA:UniProtKB.
GO; GO:0001523; P:retinoid metabolic process; TAS:Reactome.
GO; GO:0007165; P:signal transduction; TAS:UniProtKB.
GO; GO:0050808; P:synapse organization; TAS:UniProtKB.
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; IPR004850; NtA_dom.
InterPro; IPR000082; SEA_dom.
InterPro; IPR036364; SEA_dom_sf.
InterPro; IPR008993; TIMP-like_OB-fold.
Pfam; PF00008; EGF; 2.
Pfam; PF00050; Kazal_1; 1.
Pfam; PF07648; Kazal_2; 8.
Pfam; PF00053; Laminin_EGF; 2.
Pfam; PF00054; Laminin_G_1; 3.
Pfam; PF03146; NtA; 1.
Pfam; PF01390; SEA; 1.
SMART; SM00181; EGF; 7.
SMART; SM00179; EGF_CA; 3.
SMART; SM00180; EGF_Lam; 2.
SMART; SM00057; FIMAC; 4.
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; SSF50242; SSF50242; 1.
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; PS51121; NTA; 1.
PROSITE; PS50024; SEA; 1.
1: Evidence at protein level;
Alternative splicing; Calcium; Cell junction; Cell membrane;
Complete proteome; Congenital myasthenic syndrome;
Developmental protein; Differentiation; Disease mutation;
Disulfide bond; EGF-like domain; Extracellular matrix; Glycoprotein;
Heparan sulfate; Laminin EGF-like domain; Membrane; Phosphoprotein;
Polymorphism; Proteoglycan; Reference proteome; Repeat; Secreted;
Signal; Synapse; Transmembrane; Transmembrane helix.
SIGNAL 1 29 {ECO:0000255}.
CHAIN 30 2068 Agrin.
/FTId=PRO_0000007471.
CHAIN 30 1102 Agrin N-terminal 110 kDa subunit.
{ECO:0000250}.
/FTId=PRO_0000421613.
CHAIN 1103 2068 Agrin C-terminal 110 kDa subunit.
{ECO:0000250}.
/FTId=PRO_0000421614.
CHAIN 1103 1863 Agrin C-terminal 90 kDa fragment.
{ECO:0000250}.
/FTId=PRO_0000421615.
CHAIN 1864 2068 Agrin C-terminal 22 kDa fragment.
{ECO:0000250}.
/FTId=PRO_0000421616.
DOMAIN 30 157 NtA. {ECO:0000255|PROSITE-
ProRule:PRU00443}.
DOMAIN 191 244 Kazal-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
DOMAIN 264 319 Kazal-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
DOMAIN 337 391 Kazal-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
DOMAIN 408 463 Kazal-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
DOMAIN 484 536 Kazal-like 5. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
DOMAIN 540 601 Kazal-like 6. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
DOMAIN 607 666 Kazal-like 7. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
DOMAIN 699 752 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 1130 1252 SEA. {ECO:0000255|PROSITE-
ProRule:PRU00188}.
DOMAIN 1329 1367 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1372 1548 Laminin G-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 1549 1586 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1588 1625 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1635 1822 Laminin G-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 1818 1857 EGF-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1868 2065 Laminin G-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
CA_BIND 1941 2009 {ECO:0000250}.
COMPBIAS 671 677 Gly/Ser-rich.
COMPBIAS 974 1099 Ser/Thr-rich.
COMPBIAS 1058 1097 Gly/Ser-rich.
COMPBIAS 1254 1324 Ser/Thr-rich.
SITE 1102 1103 Cleavage, alpha site; by neurotrypsin.
{ECO:0000250}.
SITE 1250 1250 Alternative splice site to produce 'x'
isoforms. {ECO:0000250}.
SITE 1751 1751 Alternative splice site to produce 'y'
isoforms. {ECO:0000250}.
SITE 1862 1862 Critical for cleavage by neurotrypsin.
{ECO:0000250}.
SITE 1863 1864 Cleavage, beta site; by neurotrypsin.
{ECO:0000250}.
SITE 1888 1888 Alternative splice site to produce 'z'
isoforms. {ECO:0000250}.
SITE 1892 1892 Highly important for the agrin receptor
complex activity of the 'z(8)' insert.
{ECO:0000250}.
MOD_RES 674 674 Phosphoserine.
{ECO:0000250|UniProtKB:A2ASQ1}.
MOD_RES 676 676 Phosphoserine.
{ECO:0000250|UniProtKB:A2ASQ1}.
CARBOHYD 135 135 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 250 250 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 777 777 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 932 932 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1835 1835 O-linked (Fuc...) serine.
{ECO:0000250|UniProtKB:P25304}.
DISULFID 31 103 {ECO:0000250}.
DISULFID 152 177 Or C-152 with C-183.
DISULFID 197 228 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 202 221 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 210 242 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 270 303 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 276 296 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 285 317 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 349 368 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 357 389 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 414 447 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 421 440 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 429 461 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 490 520 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 494 513 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 502 534 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 546 585 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 555 578 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 567 599 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 613 650 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 623 643 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 632 664 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 705 736 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 709 729 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 718 750 {ECO:0000255|PROSITE-ProRule:PRU00798}.
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 923 955 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 928 948 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 937 969 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 1333 1344 {ECO:0000250}.
DISULFID 1338 1355 {ECO:0000250}.
DISULFID 1357 1366 {ECO:0000250}.
DISULFID 1519 1548 {ECO:0000250}.
DISULFID 1553 1564 {ECO:0000250}.
DISULFID 1558 1574 {ECO:0000250}.
DISULFID 1576 1585 {ECO:0000250}.
DISULFID 1592 1603 {ECO:0000250}.
DISULFID 1597 1613 {ECO:0000250}.
DISULFID 1615 1624 {ECO:0000250}.
DISULFID 1822 1836 {ECO:0000250}.
DISULFID 1830 1845 {ECO:0000250}.
DISULFID 1847 1856 {ECO:0000250}.
DISULFID 2039 2065 {ECO:0000250}.
VAR_SEQ 1 104 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_045753.
VAR_SEQ 105 154 NQVSTGDTRIFFVNPAPPYLWPAHKNELMLNSSLMRITLRN
LEEVEFCVE -> MPXLAVARDTRQPAGASLLVRGFMVPCN
ACLILLATATLGFAVLLFLNNY (in isoform 2).
{ECO:0000305}.
/FTId=VSP_045754.
VAR_SEQ 1752 1755 Missing (in isoform 6 and isoform 7).
{ECO:0000305}.
/FTId=VSP_045755.
VAR_SEQ 1889 1907 Missing (in isoform 3 and isoform 6).
{ECO:0000303|PubMed:9652404,
ECO:0000303|Ref.1}.
/FTId=VSP_045756.
VAR_SEQ 1889 1896 Missing (in isoform 4). {ECO:0000305}.
/FTId=VSP_045757.
VAR_SEQ 1897 1907 Missing (in isoform 5). {ECO:0000305}.
/FTId=VSP_045758.
VARIANT 23 23 V -> L. {ECO:0000269|PubMed:19631309}.
/FTId=VAR_068724.
VARIANT 58 58 D -> N. {ECO:0000269|PubMed:19631309}.
/FTId=VAR_068725.
VARIANT 76 76 G -> S (in CMS8; results in decreased
AChR clustering).
{ECO:0000269|PubMed:24951643}.
/FTId=VAR_071367.
VARIANT 105 105 N -> I (in CMS8; results in decreased
AChR clustering).
{ECO:0000269|PubMed:19631309,
ECO:0000269|PubMed:24951643}.
/FTId=VAR_068726.
VARIANT 267 267 T -> M. {ECO:0000269|PubMed:19631309}.
/FTId=VAR_068727.
VARIANT 375 375 A -> S (in dbSNP:rs138031468).
{ECO:0000269|PubMed:19631309}.
/FTId=VAR_068728.
VARIANT 728 728 E -> V (in dbSNP:rs113288277).
{ECO:0000269|PubMed:19631309}.
/FTId=VAR_068729.
VARIANT 745 745 A -> V. {ECO:0000269|PubMed:24951643}.
/FTId=VAR_071368.
VARIANT 852 852 Q -> R (in dbSNP:rs9697293).
{ECO:0000269|PubMed:19631309}.
/FTId=VAR_068730.
VARIANT 984 984 V -> M. {ECO:0000269|PubMed:19631309}.
/FTId=VAR_068731.
VARIANT 1088 1088 L -> F (in dbSNP:rs150132566).
{ECO:0000269|PubMed:19631309}.
/FTId=VAR_068732.
VARIANT 1118 1118 T -> K (in dbSNP:rs149159118).
{ECO:0000269|PubMed:19631309}.
/FTId=VAR_068733.
VARIANT 1135 1135 Q -> R (in dbSNP:rs142416636).
{ECO:0000269|PubMed:19631309}.
/FTId=VAR_068734.
VARIANT 1240 1240 P -> L (in dbSNP:rs142620337).
{ECO:0000269|PubMed:19631309}.
/FTId=VAR_068735.
VARIANT 1341 1341 G -> R. {ECO:0000269|PubMed:19631309}.
/FTId=VAR_068736.
VARIANT 1451 1451 P -> L. {ECO:0000269|PubMed:19631309}.
/FTId=VAR_068737.
VARIANT 1514 1514 A -> T (in dbSNP:rs111818381).
{ECO:0000269|PubMed:19631309}.
/FTId=VAR_068738.
VARIANT 1565 1565 Q -> H (in dbSNP:rs199876002).
{ECO:0000269|PubMed:19631309}.
/FTId=VAR_068739.
VARIANT 1666 1666 V -> I (in dbSNP:rs17160775).
{ECO:0000269|PubMed:19631309}.
/FTId=VAR_048966.
VARIANT 1671 1671 R -> Q. {ECO:0000269|PubMed:19631309}.
/FTId=VAR_068740.
VARIANT 1698 1698 R -> P. {ECO:0000269|PubMed:19631309}.
/FTId=VAR_068741.
VARIANT 1709 1709 G -> R (in CMS8; results in disruption of
the neuromuscular junction architecture;
does not affect phosphorylation of MUSK;
does not affect AChR clustering).
{ECO:0000269|PubMed:19631309}.
/FTId=VAR_068742.
VARIANT 1727 1727 V -> F (in CMS8; 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).
{ECO:0000269|PubMed:22205389}.
/FTId=VAR_069066.
VARIANT 1734 1734 R -> H (in dbSNP:rs145444272).
{ECO:0000269|PubMed:19631309}.
/FTId=VAR_068743.
VARIANT 1789 1789 D -> N. {ECO:0000269|PubMed:19631309}.
/FTId=VAR_068744.
VARIANT 1875 1875 G -> R (in CMS8).
{ECO:0000269|PubMed:24951643}.
/FTId=VAR_071369.
VARIANT 2046 2046 G -> V. {ECO:0000269|PubMed:19631309}.
/FTId=VAR_068745.
CONFLICT 343 343 L -> R (in Ref. 3; AAC39776).
{ECO:0000305}.
SEQUENCE 2068 AA; 217320 MW; 8B3E3D0FF65517F0 CRC64;
MAGRSHPGPL RPLLPLLVVA ACVLPGAGGT CPERALERRE EEANVVLTGT VEEILNVDPV
QHTYSCKVRV WRYLKGKDLV ARESLLDGGN KVVISGFGDP LICDNQVSTG DTRIFFVNPA
PPYLWPAHKN ELMLNSSLMR ITLRNLEEVE FCVEDKPGTH FTPVPPTPPD ACRGMLCGFG
AVCEPNAEGP GRASCVCKKS PCPSVVAPVC GSDASTYSNE CELQRAQCSQ QRRIRLLSRG
PCGSRDPCSN VTCSFGSTCA RSADGLTASC LCPATCRGAP EGTVCGSDGA DYPGECQLLR
RACARQENVF KKFDGPCDPC QGALPDPSRS CRVNPRTRRP EMLLRPESCP ARQAPVCGDD
GVTYENDCVM GRSGAARGLL LQKVRSGQCQ GRDQCPEPCR FNAVCLSRRG RPRCSCDRVT
CDGAYRPVCA QDGRTYDSDC WRQQAECRQQ RAIPSKHQGP CDQAPSPCLG VQCAFGATCA
VKNGQAACEC LQACSSLYDP VCGSDGVTYG SACELEATAC TLGREIQVAR KGPCDRCGQC
RFGALCEAET GRCVCPSECV ALAQPVCGSD GHTYPSECML HVHACTHQIS LHVASAGPCE
TCGDAVCAFG AVCSAGQCVC PRCEHPPPGP VCGSDGVTYG SACELREAAC LQQTQIEEAR
AGPCEQAECG SGGSGSGEDG DCEQELCRQR GGIWDEDSED GPCVCDFSCQ SVPGSPVCGS
DGVTYSTECE LKKARCESQR GLYVAAQGAC RGPTFAPLPP VAPLHCAQTP YGCCQDNITA
ARGVGLAGCP SACQCNPHGS YGGTCDPATG QCSCRPGVGG LRCDRCEPGF WNFRGIVTDG
RSGCTPCSCD PQGAVRDDCE QMTGLCSCKP GVAGPKCGQC PDGRALGPAG CEADASAPAT
CAEMRCEFGA RCVEESGSAH CVCPMLTCPE ANATKVCGSD GVTYGNECQL KTIACRQGLQ
ISIQSLGPCQ EAVAPSTHPT SASVTVTTPG LLLSQALPAP PGALPLAPSS TAHSQTTPPP
SSRPRTTASV PRTTVWPVLT VPPTAPSPAP SLVASAFGES GSTDGSSDEE LSGDQEASGG
GSGGLEPLEG SSVATPGPPV ERASCYNSAL GCCSDGKTPS LDAEGSNCPA TKVFQGVLEL
EGVEGQELFY TPEMADPKSE LFGETARSIE STLDDLFRNS DVKKDFRSVR LRDLGPGKSV
RAIVDVHFDP TTAFRAPDVA RALLRQIQVS RRRSLGVRRP LQEHVRFMDF DWFPAFITGA
TSGAIAAGAT ARATTASRLP SSAVTPRAPH PSHTSQPVAK TTAAPTTRRP PTTAPSRVPG
RRPPAPQQPP KPCDSQPCFH GGTCQDWALG GGFTCSCPAG RGGAVCEKVL GAPVPAFEGR
SFLAFPTLRA YHTLRLALEF RALEPQGLLL YNGNARGKDF LALALLDGRV QLRFDTGSGP
AVLTSAVPVE PGQWHRLELS RHWRRGTLSV DGETPVLGES PSGTDGLNLD TDLFVGGVPE
DQAAVALERT FVGAGLRGCI RLLDVNNQRL ELGIGPGAAT RGSGVGECGD HPCLPNPCHG
GAPCQNLEAG RFHCQCPPGR VGPTCADEKS PCQPNPCHGA APCRVLPEGG AQCECPLGRE
GTFCQTASGQ DGSGPFLADF NGFSHLELRG LHTFARDLGE KMALEVVFLA RGPSGLLLYN
GQKTDGKGDF VSLALRDRRL EFRYDLGKGA AVIRSREPVT LGAWTRVSLE RNGRKGALRV
GDGPRVLGES PKSRKVPHTV LNLKEPLYVG GAPDFSKLAR AAAVSSGFDG AIQLVSLGGR
QLLTPEHVLR QVDVTSFAGH PCTRASGHPC LNGASCVPRE AAYVCLCPGG FSGPHCEKGL
VEKSAGDVDT LAFDGRTFVE YLNAVTESEL ANEIPVPETL DSGALHSEKA LQSNHFELSL
RTEATQGLVL WSGKATERAD YVALAIVDGH LQLSYNLGSQ PVVLRSTVPV NTNRWLRVVA
HREQREGSLQ VGNEAPVTGS SPLGATQLDT DGALWLGGLP ELPVGPALPK AYGTGFVGCL
RDVVVGRHPL HLLEDAVTKP ELRPCPTP


Related products :

Catalog number Product name Quantity
E1303h ELISA Agrin,AGRIN,AGRN,Homo sapiens,Human 96T
U1303h CLIA Agrin,AGRIN,AGRN,Homo sapiens,Human 96T
E1303h ELISA kit Agrin,AGRIN,AGRN,Homo sapiens,Human 96T
E1303r ELISA kit Agrin,Agrin,Agrn,Rat,Rattus norvegicus 96T
U1303r CLIA Agrin,Agrin,Agrn,Rat,Rattus norvegicus 96T
E1303m ELISA kit Agrin,Agrin,Agrn,Mouse,Mus musculus 96T
E1303r ELISA Agrin,Agrin,Agrn,Rat,Rattus norvegicus 96T
E1303m ELISA Agrin,Agrin,Agrn,Mouse,Mus musculus 96T
U1303m CLIA Agrin,Agrin,Agrn,Mouse,Mus musculus 96T
E09A0401 Monkey Agrin ELISA , Agrin 96 Tests/kit
E01A0401 Human Agrin ELISA , Agrin 96 Tests/kit
E03A0401 Mouse Agrin ELISA , Agrin
E05A0401 Guinea pig Agrin ELISA , Agrin
E03A0401 Mouse Agrin ELISA ,Agrin 96 Tests/kit
E01A0401 Human Agrin ELISA , Agrin
E12A0401 Chicken Agrin ELISA , Agrin 96 Tests/kit
ELR-Agrin-001 Custom Rat Agrin ELISA Kit available on demand 1 X 96 well strip plate
E07A0401 Porcine Agrin ELISA , Agrin 96 Tests/kit
E09A0401 Monkey Agrin ELISA , Agrin
E14A0401 Sheep Agrin ELISA , Agrin 96 Tests/kit
E04A0401 Rabbit Agrin ELISA , Agrin 96 Tests/kit
E11A0401 Bovine Agrin ELISA , Agrin 96 Tests/kit
E08A0401 Canine Agrin ELISA , Agrin 96 Tests/kit
E12A0401 Chicken Agrin ELISA , Agrin
E07A0401 Porcine Agrin ELISA , Agrin


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur | Gentaur





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur | Gentaur