Reviewed, UniProtKB/Swiss-Prot O00468 (AGRIN_HUMAN)

Names and origin

Protein names

Recommended name:
    Agrin

Gene names

Name:	AGRN
Synonyms:	AGRIN

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	2045 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Component of the basal lamina that causes the aggregation of acetylcholine receptors and acetylcholine-esterase on the surface of muscle fibers of the neuromuscular junction By similarity.
Subunit structure	Binds to laminin. Ref.4
Subcellular location	Secreted › extracellular space › extracellular matrix. Note: Synaptic basal lamina at the neuromuscular junction By similarity.
Post-translational modification	Contains heparan sulfate chains as well as N-linked and O-linked oligosaccharides By similarity.
Sequence similarities	Contains 4 EGF-like domains. Contains 9 Kazal-like domains. Contains 2 laminin EGF-like domains. Contains 3 laminin G-like domains. Contains 1 NtA (N-terminal agrin) domain. Contains 1 SEA domain.

Ontologies

Keywords
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Polymorphism
Domain	EGF-like domain Laminin EGF-like domain Repeat Signal
PTM	Disulfide bond Glycoprotein Heparan sulfate Proteoglycan
Gene Ontology (GO)
Biological process	clustering of voltage-gated sodium channels Traceable author statement. Source: UniProtKB muscarinic acetylcholine receptor signaling pathway Traceable author statement. Source: UniProtKB receptor clustering Ref.4 Inferred from direct assay. Source: UniProtKB synapse organization Ref.1 Traceable author statement. Source: UniProtKB
Cellular component	basal lamina Inferred from direct assay. Source: UniProtKB extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	laminin binding Ref.1 Traceable author statement. Source: UniProtKB structural constituent of cytoskeleton Ref.1 Traceable author statement. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 29	29	Potential
	Chain	30 – 2045	2016	Agrin		PRO_0000007471
Regions
	Domain	30 – 157	128	NtA
	Domain	170 – 242	73	Kazal-like 1
	Domain	246 – 317	72	Kazal-like 2
	Domain	318 – 389	72	Kazal-like 3
	Domain	392 – 461	70	Kazal-like 4
	Domain	466 – 534	69	Kazal-like 5
	Domain	535 – 599	65	Kazal-like 6
	Domain	600 – 664	65	Kazal-like 7
	Domain	668 – 750	83	Kazal-like 8
	Domain	793 – 846	54	Laminin EGF-like 1
	Domain	847 – 893	47	Laminin EGF-like 2
	Domain	899 – 969	71	Kazal-like 9
	Domain	1130 – 1252	123	SEA
	Domain	1329 – 1367	39	EGF-like 1
	Domain	1372 – 1548	177	Laminin G-like 1
	Domain	1549 – 1586	38	EGF-like 2
	Domain	1588 – 1625	38	EGF-like 3
	Domain	1635 – 1818	184	Laminin G-like 2
	Domain	1814 – 1853	40	EGF-like 4
	Domain	1864 – 2042	179	Laminin G-like 3
	Compositional bias	974 – 1099	126	Ser/Thr-rich
	Compositional bias	1254 – 1324	71	Ser/Thr-rich
Amino acid modifications
	Glycosylation	135	1	N-linked (GlcNAc...)
	Glycosylation	250	1	N-linked (GlcNAc...) Potential
	Glycosylation	777	1	N-linked (GlcNAc...) Potential
	Glycosylation	932	1	N-linked (GlcNAc...) Potential
	Disulfide bond	31 ↔ 103		By similarity
	Disulfide bond	793 ↔ 805		By similarity
	Disulfide bond	795 ↔ 812		By similarity
	Disulfide bond	814 ↔ 823		By similarity
	Disulfide bond	826 ↔ 844		By similarity
	Disulfide bond	847 ↔ 859		By similarity
	Disulfide bond	849 ↔ 866		By similarity
	Disulfide bond	868 ↔ 877		By similarity
	Disulfide bond	880 ↔ 891		By similarity
	Disulfide bond	1333 ↔ 1344		By similarity
	Disulfide bond	1338 ↔ 1355		By similarity
	Disulfide bond	1357 ↔ 1366		By similarity
	Disulfide bond	1519 ↔ 1548		By similarity
	Disulfide bond	1553 ↔ 1564		By similarity
	Disulfide bond	1558 ↔ 1574		By similarity
	Disulfide bond	1576 ↔ 1585		By similarity
	Disulfide bond	1592 ↔ 1603		By similarity
	Disulfide bond	1597 ↔ 1613		By similarity
	Disulfide bond	1615 ↔ 1624		By similarity
	Disulfide bond	1818 ↔ 1832		By similarity
	Disulfide bond	1826 ↔ 1841		By similarity
	Disulfide bond	1843 ↔ 1852		By similarity
	Disulfide bond	2016 ↔ 2042		By similarity
Natural variations
	Natural variant	1666	1	V → I: dbSNP rs17160775.		VAR_048966
Experimental info
	Sequence conflict	343	1	L → R in AAB52917. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O00468-1 [UniParc]. Last modified September 5, 2006. Version 4. Checksum: 108BDA7146ECB94D	FASTA	2,045	214,846
	10 20 30 40 50 60 MAGRSHPGPL RPLLPLLVVA ACVLPGAGGT CPERALERRE EEANVVLTGT VEEILNVDPV 70 80 90 100 110 120 QHTYSCKVRV WRYLKGKDLV ARESLLDGGN KVVISGFGDP LICDNQVSTG DTRIFFVNPA 130 140 150 160 170 180 PPYLWPAHKN ELMLNSSLMR ITLRNLEEVE FCVEDKPGTH FTPVPPTPPD ACRGMLCGFG 190 200 210 220 230 240 AVCEPNAEGP GRASCVCKKS PCPSVVAPVC GSDASTYSNE CELQRAQCSQ QRRIRLLSRG 250 260 270 280 290 300 PCGSRDPCSN VTCSFGSTCA RSADGLTASC LCPATCRGAP EGTVCGSDGA DYPGECQLLR 310 320 330 340 350 360 RACARQENVF KKFDGPCDPC QGALPDPSRS CRVNPRTRRP EMLLRPESCP ARQAPVCGDD 370 380 390 400 410 420 GVTYENDCVM GRSGAARGLL LQKVRSGQCQ GRDQCPEPCR FNAVCLSRRG RPRCSCDRVT 430 440 450 460 470 480 CDGAYRPVCA QDGRTYDSDC WRQQAECRQQ RAIPSKHQGP CDQAPSPCLG VQCAFGATCA 490 500 510 520 530 540 VKNGQAACEC LQACSSLYDP VCGSDGVTYG SACELEATAC TLGREIQVAR KGPCDRCGQC 550 560 570 580 590 600 RFGALCEAET GRCVCPSECV ALAQPVCGSD GHTYPSECML HVHACTHQIS LHVASAGPCE 610 620 630 640 650 660 TCGDAVCAFG AVCSAGQCVC PRCEHPPPGP VCGSDGVTYG SACELREAAC LQQTQIEEAR 670 680 690 700 710 720 AGPCEQAECG SGGSGSGEDG DCEQELCRQR GGIWDEDSED GPCVCDFSCQ SVPGSPVCGS 730 740 750 760 770 780 DGVTYSTECE LKKARCESQR GLYVAAQGAC RGPTFAPLPP VAPLHCAQTP YGCCQDNITA 790 800 810 820 830 840 ARGVGLAGCP SACQCNPHGS YGGTCDPATG QCSCRPGVGG LRCDRCEPGF WNFRGIVTDG 850 860 870 880 890 900 RSGCTPCSCD PQGAVRDDCE QMTGLCSCKP GVAGPKCGQC PDGRALGPAG CEADASAPAT 910 920 930 940 950 960 CAEMRCEFGA RCVEESGSAH CVCPMLTCPE ANATKVCGSD GVTYGNECQL KTIACRQGLQ 970 980 990 1000 1010 1020 ISIQSLGPCQ EAVAPSTHPT SASVTVTTPG LLLSQALPAP PGALPLAPSS TAHSQTTPPP 1030 1040 1050 1060 1070 1080 SSRPRTTASV PRTTVWPVLT VPPTAPSPAP SLVASAFGES GSTDGSSDEE LSGDQEASGG 1090 1100 1110 1120 1130 1140 GSGGLEPLEG SSVATPGPPV ERASCYNSAL GCCSDGKTPS LDAEGSNCPA TKVFQGVLEL 1150 1160 1170 1180 1190 1200 EGVEGQELFY TPEMADPKSE LFGETARSIE STLDDLFRNS DVKKDFRSVR LRDLGPGKSV 1210 1220 1230 1240 1250 1260 RAIVDVHFDP TTAFRAPDVA RALLRQIQVS RRRSLGVRRP LQEHVRFMDF DWFPAFITGA 1270 1280 1290 1300 1310 1320 TSGAIAAGAT ARATTASRLP SSAVTPRAPH PSHTSQPVAK TTAAPTTRRP PTTAPSRVPG 1330 1340 1350 1360 1370 1380 RRPPAPQQPP KPCDSQPCFH GGTCQDWALG GGFTCSCPAG RGGAVCEKVL GAPVPAFEGR 1390 1400 1410 1420 1430 1440 SFLAFPTLRA YHTLRLALEF RALEPQGLLL YNGNARGKDF LALALLDGRV QLRFDTGSGP 1450 1460 1470 1480 1490 1500 AVLTSAVPVE PGQWHRLELS RHWRRGTLSV DGETPVLGES PSGTDGLNLD TDLFVGGVPE 1510 1520 1530 1540 1550 1560 DQAAVALERT FVGAGLRGCI RLLDVNNQRL ELGIGPGAAT RGSGVGECGD HPCLPNPCHG 1570 1580 1590 1600 1610 1620 GAPCQNLEAG RFHCQCPPGR VGPTCADEKS PCQPNPCHGA APCRVLPEGG AQCECPLGRE 1630 1640 1650 1660 1670 1680 GTFCQTASGQ DGSGPFLADF NGFSHLELRG LHTFARDLGE KMALEVVFLA RGPSGLLLYN 1690 1700 1710 1720 1730 1740 GQKTDGKGDF VSLALRDRRL EFRYDLGKGA AVIRSREPVT LGAWTRVSLE RNGRKGALRV 1750 1760 1770 1780 1790 1800 GDGPRVLGES PVPHTVLNLK EPLYVGGAPD FSKLARAAAV SSGFDGAIQL VSLGGRQLLT 1810 1820 1830 1840 1850 1860 PEHVLRQVDV TSFAGHPCTR ASGHPCLNGA SCVPREAAYV CLCPGGFSGP HCEKGLVEKS 1870 1880 1890 1900 1910 1920 AGDVDTLAFD GRTFVEYLNA VTESEKALQS NHFELSLRTE ATQGLVLWSG KATERADYVA 1930 1940 1950 1960 1970 1980 LAIVDGHLQL SYNLGSQPVV LRSTVPVNTN RWLRVVAHRE QREGSLQVGN EAPVTGSSPL 1990 2000 2010 2020 2030 2040 GATQLDTDGA LWLGGLPELP VGPALPKAYG TGFVGCLRDV VVGRHPLHLL EDAVTKPELR PCPTP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structure and high expression of human agrin in basement membranes of adult lung and kidney." 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. Eur. J. Biochem. 254:123-128(1998) [PubMed: 9652404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	Kato S. Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Retinal pigment epithelium.
[3]	"The DNA sequence and biological annotation of human chromosome 1." 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. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"Agrin binds to the nerve-muscle basal lamina via laminin." Denzer A.J., Brandenberger R., Gesemann M., Chiquet M., Ruegg M.A. J. Cell Biol. 137:671-683(1997) [PubMed: 9151673] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-172, INTERACTION WITH LAMIN.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1558-2045. Tissue: Brain, Colon and Kidney.
[6]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-135, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U84406 mRNA. Translation: AAB52917.1. AB191264 mRNA. Translation: BAD52440.1. AL645608 Genomic DNA. Translation: CAI15575.2. AF016903 mRNA. Translation: AAC39776.1. BC004220 mRNA. Translation: AAH04220.2. BC007649 mRNA. Translation: AAH07649.1. BC034009 mRNA. Translation: AAH34009.1. BC063620 mRNA. Translation: AAH63620.1.
IPI	IPI00374563.
RefSeq	NP_940978.2.
UniGene	Hs.273330
3D structure databases
SMR	O00468. Positions 36-146.
ModBase	Search...
Protein-protein interaction databases
IntAct	O00468. 2 interactions.
Proteomic databases
PRIDE	O00468.
Genome annotation databases
Ensembl	ENSG00000188157. Homo sapiens. [Contig view]
GeneID	375790.
KEGG	hsa:375790.
Organism-specific databases
GeneCards	GC01P000946.
HGNC	HGNC:329. AGRN.
MIM	103320. gene.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	O00468.
OMA	O00468. DWFPAFF.
Gene expression databases
ArrayExpress	O00468.
Bgee	O00468.
CleanEx	HS_AGRN.
GermOnline	ENSG00000188157. Homo sapiens.
Family and domain databases
InterPro	IPR004850. Agrin_NtA. IPR013320. ConA-like_subgrp. IPR006209. EGF. IPR006210. EGF-like. IPR013032. EGF-like_reg_CS. IPR000742. EGF_3. IPR002049. EGF_laminin. IPR003645. Fol_N. IPR001791. Laminin_G. IPR012679. Laminin_G_1. IPR002350. Prot_inh_Kazal. IPR000082. SEA. [Graphical view]
Gene3D	G3DSA:2.60.120.200. ConA_like_subgrp. 3 hits.
Pfam	PF00008. EGF. 4 hits. PF00050. Kazal_1. 9 hits. PF00053. Laminin_EGF. 2 hits. PF00054. Laminin_G_1. 3 hits. PF03146. NtA. 1 hit. PF01390. SEA. 1 hit. [Graphical view]
PRINTS	PR00011. EGFLAMININ.
SMART	SM00181. EGF. 4 hits. SM00180. EGF_Lam. 2 hits. SM00274. FOLN. 5 hits. SM00280. KAZAL. 9 hits. SM00282. LamG. 3 hits. SM00200. SEA. 1 hit. [Graphical view]
PROSITE	PS00022. EGF_1. 6 hits. PS01186. EGF_2. 1 hit. PS50026. EGF_3. 4 hits. PS01248. EGF_LAM_1. 1 hit. PS50027. EGF_LAM_2. 2 hits. PS50025. LAM_G_DOMAIN. 3 hits. PS51121. NTA. 1 hit. PS50024. SEA. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	100617.
SOURCE	Search...

Entry information

Entry name

AGRIN_HUMAN

Accession

Primary (citable) accession number: O00468
Secondary accession number(s): Q5SVA2 , Q60FE1, Q7KYS8, Q8N4J5, Q96IC1, Q9BTD4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2004
Last sequence update:	September 5, 2006
Last modified:	June 16, 2009
This is version 80 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)