Agrn
entrez
11603
canonical
uniprot
A2ASQ1
canonical
ensembl
ENSMUSG00000041936
resolver
ensp
ENSMUSP00000101200
resolver
ensp
ENSMUSP00000137931
resolver
ensp
ENSMUSP00000255225
resolver
ensp
ENSMUSP00000255226
resolver
ensp
ENSMUSP00000255227
resolver
enst
ENSMUST00000180572
resolver
genesymbol
Agrn
resolver
genesymbol_syn
Agrin
resolver
uniprot
A2ASP9
resolver
uniprot
A2ASQ0
resolver
uniprot
B2RWU1
resolver
uniprot
M0QWP1
resolver
uniprot_entry
AGRIN_MOUSE
resolver
uniprot_entry
M0QWP1_MOUSE
resolver
uniprot_sec
A2ASP9
resolver
uniprot_sec
A2ASQ0
resolver
uniprot_sec
B2RWU1
resolver
amino_acid_sequence
MPPLPLEHRPRQQPGASVLVRYFMIPCNICLILLATSTLGFAVLLFLSNYKPGIHFTAAPSMPPDVCRGMLCGFGAVCEPSVEDPGRASCVCKKNVCPAMVAPVCGSDASTYSNECELQRAQCNQQRRIRLLRQGPCGSRDPCANVTCSFGSTCVPSADGQTASCLCPTTCFGAPDGTVCGSDGVDYPSECQLLRHACANQEHIFKKFDGPCDPCQGSMSDLNHICRVNPRTRHPEMLLRPENCPAQHTPICGDDGVTYENDCVMSRIGAARGLLLQKVRSGQCQTRDQCPETCQFNSVCLSRRGRPHCSCDRVTCDGAYRPVCAQDGHTYDNDCWRQQAECRQQQTIPPKHQGPCDQTPSPCRGAQCAFGATCTVKNGKAVCECQRVCSGGYDPVCGSDGVTYGSVCELESMACTLGREIRVARRGPCDRCGQCRFGSLCEVETGRCVCPSECVESAQPVCGSDGHTYASECELHVHACTHQISLYVASAGHCQTCGETVCTFGAVCSAGQCVCPRCEHPPPGPVCGSDGVTYLSACELREAACQQQVQIEEARAGPCEPAECGSGGSGSGEDNACEQELCRQHGGVWDEDSEDGPCVCDFSCQSVLKSPVCGSDGVTYSTECHLKKARCEARQELYVAAQGACRGPTLAPLLPMASPHCAQTPYGCCQDNVTAAQGVGLAGCPSTCHCNPHGSYSGTCDPVTGQCSCRPGVGGLRCDRCEPGFWNFRGIVTDGHSGCTPCSCDPRGAVRDDCEQMTGLCSCRPGVAGPKCGQCPDGQALGHLGCEADPTTPVTCVEMHCEFGASCVEEAGFAQCVCPTLTCPEANSTKVCGSDGVTYGNECQLKTIACRQRLDISIQSLGPCRESVAPGVSPTSASMTTPRHILSRTLASPHSSLPLSPSTTAHDWPTPLPTSPQTVVGTPRSTAATPSDVASLATAIFRESGSTNGSGDEELSGDEEASGGGSGGLEPPVGSVVVTHGPPIERASCYNSPLGCCSDGKTPSLDSEGSNCPATKAFQGVLELEGVEGQELFYTPEMADPKSELFGETARSIESTLDDLFRNSDVKKDFWSIRLRELGPGKLVRAIVDVHFDPTTAFQAPDVGQALLQQIQVSRPWALAVRRPLREHVRFLDFDWFPTFFTGAATGTTAAVATARATTVSRLSASSVTPRVYPSYTSRPVGRTTAPLTTRRPPTTTASIDRPRTPGPQRPPKSCDSQPCLHGGTCQDLDSGKGFSCSCTAGRAGTVCEKVQLPSVPAFKGHSFLAFPTLRAYHTLRLALEFRALETEGLLLYNGNARGKDFLALALLDGHVQFRFDTGSGPAVLTSLVPVEPGRWHRLELSRHWRQGTLSVDGEAPVVGESPSGTDGLNLDTKLYVGGLPEEQVATVLDRTSVGIGLKGCIRMLDINNQQLELSDWQRAVVQSSGVGECGDHPCSPNPCHGGALCQALEAGVFLCQCPPGRFGPTCADEKNPCQPNPCHGSAPCHVLSRGGAKCACPLGRSGSFCETVLENAGSRPFLADFNGFSYLELKGLHTFERDLGEKMALEMVFLARGPSGLLLYNGQKTDGKGDFVSLALHNRHLEFRYDLGKGAAIIRSKEPIALGTWVRVFLERNGRKGALQVGDGPRVLGESPKSRKVPHTMLNLKEPLYVGGAPDFSKLARGAAVASGFDGAIQLVSLRGHQLLTQEHVLRAVDVAPFAGHPCTQAVDNPCLNGGSCIPREATYECLCPGGFSGLHCEKGIVEKSVGDLETLAFDGRTYIEYLNAVTESELTNEIPAPETLDSRALFSEKALQSNHFELSLRTEATQGLVLWIGKVGERADYMALAIVDGHLQLSYDLGSQPVVLRSTVKVNTNRWLRVRAHREHREGSLQVGNEAPVTGSSPLGATQLDTDGALWLGGLQKLPVGQALPKAYGTGFVGCLRDVVVGHRQLHLLEDAVTKPELRPCPTL
uniprot
proteins
function
FUNCTION: Depending on alternative splicing and post-translational modifications, it has a role in different processes, including neuromuscular junction formation and maintenance, and regulation of neurite outgrowth (PubMed:10402191, PubMed:11018052, PubMed:12796478, PubMed:17611272, PubMed:19303856, PubMed:21885656, PubMed:8653787). Involved in the positive regulation of cartilage formation through alpha-dystroglycan binding and up-regulation of SOX9 (By similarity). {ECO:0000250|UniProtKB:O00468, 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: [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 (PubMed:8653787, PubMed:10402191). 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 (PubMed:17611272, PubMed:19303856). {ECO:0000269|PubMed:10402191, ECO:0000269|PubMed:17611272, ECO:0000269|PubMed:19303856, ECO:0000269|PubMed:8653787}.; 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. {ECO:0000269|PubMed:12796478}.
uniprot
proteins
mass_dalton
207539
uniprot
proteins
post_translational_modification
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}.
uniprot
proteins
pubmed
10402191
uniprot
proteins
pubmed
10581249
uniprot
proteins
pubmed
11018052
uniprot
proteins
pubmed
11161480
uniprot
proteins
pubmed
12796478
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16452087
uniprot
proteins
pubmed
17611272
uniprot
proteins
pubmed
18230682
uniprot
proteins
pubmed
19221030
uniprot
proteins
pubmed
19303856
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21037280
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21885656
uniprot
proteins
pubmed
21890498
uniprot
proteins
pubmed
8653787
uniprot
proteins
pubmed
9188458
uniprot
proteins
sequence_length
1950
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: 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}.
uniprot
proteins
transmembrane_region
TRANSMEM 27..47; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins