AGRIN_DIPOM
ID AGRIN_DIPOM Reviewed; 1328 AA.
AC Q90404;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Agrin;
DE Flags: Fragment;
GN Name=AGRN; Synonyms=AGRIN;
OS Diplobatis ommata (Ocellated electric ray) (Discopyge ommata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Batoidea; Torpediniformes; Narcinidae; Diplobatis.
OX NCBI_TaxID=1870830;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Smith M.A., Magill-Solc C., Rupp F., Yao Y.-M.M., Schilling J.W., Snow P.,
RA McMahan U.J.;
RT "Isolation and characterization of a cDNA that encodes an agrin homolog in
RT the marine ray.";
RL Mol. Cell. Neurosci. 3:406-417(1992).
CC -!- FUNCTION: Plays a central role in the formation and the maintenance of
CC the neuromuscular junction (NMJ), the synapse between motor neuron and
CC skeletal muscle. Ligand of the MUSK signaling complex that induces the
CC phosphorylation of MUSK, the kinase of the complex. The activation of
CC MUSK in myotubes induces the formation of NMJ by regulating different
CC processes including the transcription of specific genes and the
CC clustering of AChR in the postsynaptic membrane (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Note=Synaptic basal lamina at the neuromuscular
CC junction. {ECO:0000250|UniProtKB:P31696}.
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DR EMBL; L01423; AAA49224.1; -; mRNA.
DR PIR; T43060; T43060.
DR AlphaFoldDB; Q90404; -.
DR SMR; Q90404; -.
DR PRIDE; Q90404; -.
DR GO; GO:0071944; C:cell periphery; IEA:UniProt.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR CDD; cd00055; EGF_Lam; 2.
DR CDD; cd00110; LamG; 3.
DR Gene3D; 3.30.70.960; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR003884; FacI_MAC.
DR InterPro; IPR003645; Fol_N.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR000082; SEA_dom.
DR InterPro; IPR036364; SEA_dom_sf.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF07648; Kazal_2; 2.
DR Pfam; PF00053; Laminin_EGF; 2.
DR Pfam; PF00054; Laminin_G_1; 3.
DR Pfam; PF01390; SEA; 1.
DR SMART; SM00181; EGF; 6.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00180; EGF_Lam; 2.
DR SMART; SM00057; FIMAC; 1.
DR SMART; SM00274; FOLN; 2.
DR SMART; SM00280; KAZAL; 2.
DR SMART; SM00282; LamG; 3.
DR SMART; SM00200; SEA; 1.
DR SUPFAM; SSF100895; SSF100895; 2.
DR SUPFAM; SSF49899; SSF49899; 3.
DR SUPFAM; SSF82671; SSF82671; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00022; EGF_1; 5.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS01248; EGF_LAM_1; 1.
DR PROSITE; PS50027; EGF_LAM_2; 2.
DR PROSITE; PS51465; KAZAL_2; 2.
DR PROSITE; PS50025; LAM_G_DOMAIN; 3.
DR PROSITE; PS50024; SEA; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; Differentiation; Disulfide bond; EGF-like domain;
KW Glycoprotein; Laminin EGF-like domain; Repeat.
FT CHAIN <1..1328
FT /note="Agrin"
FT /id="PRO_0000055625"
FT DOMAIN <1..41
FT /note="Kazal-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 79..132
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 133..179
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 201..257
FT /note="Kazal-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 411..533
FT /note="SEA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT DOMAIN 608..644
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 649..825
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 865..902
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 914..1096
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1097..1135
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1146..1324
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 322..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 7..39
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 79..91
FT /evidence="ECO:0000250"
FT DISULFID 81..98
FT /evidence="ECO:0000250"
FT DISULFID 100..109
FT /evidence="ECO:0000250"
FT DISULFID 112..130
FT /evidence="ECO:0000250"
FT DISULFID 133..145
FT /evidence="ECO:0000250"
FT DISULFID 135..152
FT /evidence="ECO:0000250"
FT DISULFID 154..163
FT /evidence="ECO:0000250"
FT DISULFID 166..177
FT /evidence="ECO:0000250"
FT DISULFID 207..241
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 214..234
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 223..255
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 612..623
FT /evidence="ECO:0000250"
FT DISULFID 617..632
FT /evidence="ECO:0000250"
FT DISULFID 634..643
FT /evidence="ECO:0000250"
FT DISULFID 796..825
FT /evidence="ECO:0000250"
FT DISULFID 830..841
FT /evidence="ECO:0000250"
FT DISULFID 835..851
FT /evidence="ECO:0000250"
FT DISULFID 869..880
FT /evidence="ECO:0000250"
FT DISULFID 874..890
FT /evidence="ECO:0000250"
FT DISULFID 892..901
FT /evidence="ECO:0000250"
FT DISULFID 1101..1114
FT /evidence="ECO:0000250"
FT DISULFID 1108..1123
FT /evidence="ECO:0000250"
FT DISULFID 1125..1134
FT /evidence="ECO:0000250"
FT DISULFID 1298..1324
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 1328 AA; 144018 MW; 79D81C1AF2A71C18 CRC64;
VPLSPVCGSD GVTYDSECAL KLMRCMIQKD LHVVMLSPCK DASPSSVPEL HCSRSVYGCC
RDNVTAAQGV GLAGCPSTCE CNRYGSYSKT CSPSSGQCSC KPGVGGLKCD RCEPGFWNFR
GIVTDEKSGC TPCNCYPLGA VRDDCEQMSG LCSCKAGISG MKCNQCPNGS KLGPSGCDQD
PSVSRTCSDL HCQYGATCVQ SIGRAYCECP PSICPKNKQF KVCGSDGVTY ANECQLKTIA
CRQGSVINIL HQGPCQGTTP STGNIQTTDL TPSPKEHTNL SKIVSLETIP ILKAIFPVTD
NTTGPQVHKM YTVTASPGVI GHPTAGWPPS SLTSSEPPDL SGSGDFSGDT DLEASGNLEG
SGVEPMGFNE SSTGPPTPVP NERSTCDNTE FGCCSDGKTP SVDGEGSNCP PTKLFQGVLI
VEEVEGQELF YTPEMDDPKS ELFGETARSI ENALNELFGN SNVKKDFKSV RVHGLGPSDP
VRIIVEVHFD PRTSYNSHDV QRALLQQVKQ SRRKSIVVKK PEQDNVKIVD FDWAPLLFTT
TSTTAARTTV PITTASALPV TRRPPPATTR WPKVLPHAKV PSTTTKPATT RRPPFSRKVE
VRPATVKVHR PCDSQPCLHG GTCEDDGVSY TCSCPAGRGG AVCERTIVYF IPEFGGRSYL
AFKTMKAYYT VRISMEFRAS NLDGLPLVQW TEKGKGLHFY RPSEGYVELR FNHGVWDGVI
TSKTLIKPGN WHHVVGNRNR RSGMLSVDGE PHLIGESPPG TDGLNLDTDL FLGGTPEDEM
TLVTERTTAT KGLQGCIRLL DVNNLIYDLQ ERSNDVLYGS GVGECGNNPC SPNPCKNRGK
CHMKEAEMFH CESVGEFSGP TCADKHNPCD PNPCHQSANC MVLPEGGSKC ECPMGREGEL
CERVSEAEQD QGKAFIPEFN GLSYLEMNGI HTFVSDLLQK LSMEVIFLAK DPNGMIFYNG
QKTDGRGDFV SLNLRDGYLE FKYDLGKGAA VLRSKAPIPL NVWNVVTVER NGRKGLMKIN
KDELVSGESP KSRKAPHTAL NLKEAFYVGG APDFNKFARA AGIISGFTGA IQKLSLKSIP
LLKKENIRNA MEISNFRWHA CTKTRNPCQN GGVCSPRLRE YDCMCQRGFS GPQCEKALEE
KSASGSESVA FNGRTFIEYH NTVTRSEKAV QVNYFEMSIK TEATKGLILW SGKIAEKSDY
IALAVVDGFV QMTYDLGSKP VTLRSTIPVN TNQWVRIKAN RIHGYGTLQV GNEAPVTGSS
PFAATQLDTD GALWLGGIEK LAPGNRLPKA YSTGFIGCIK DVVIDRQELQ LVEDALNNPT
ILHCPAKK
