ID A0A3Q2HRE0_HORSE Unreviewed; 1975 AA.
AC A0A3Q2HRE0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 2.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Agrin {ECO:0000256|ARBA:ARBA00016077};
GN Name=AGRN {ECO:0000313|Ensembl:ENSECAP00000035833.2,
GN ECO:0000313|VGNC:VGNC:111030};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000035833.2, ECO:0000313|Proteomes:UP000002281};
RN [1] {ECO:0000313|Ensembl:ENSECAP00000035833.2, ECO:0000313|Proteomes:UP000002281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000035833.2,
RC ECO:0000313|Proteomes:UP000002281};
RX PubMed=19892987; DOI=10.1126/science.1178158;
RG Broad Institute Genome Sequencing Platform;
RG Broad Institute Whole Genome Assembly Team;
RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT "Genome sequence, comparative analysis, and population genetics of the
RT domestic horse.";
RL Science 326:865-867(2009).
RN [2] {ECO:0000313|Ensembl:ENSECAP00000035833.2}
RP IDENTIFICATION.
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000035833.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR STRING; 9796.ENSECAP00000035833; -.
DR PaxDb; 9796-ENSECAP00000035833; -.
DR Ensembl; ENSECAT00000053590.3; ENSECAP00000035833.2; ENSECAG00000030432.3.
DR VGNC; VGNC:111030; AGRN.
DR GeneTree; ENSGT00940000158337; -.
DR InParanoid; A0A3Q2HRE0; -.
DR OMA; AMEISPF; -.
DR Proteomes; UP000002281; Chromosome 2.
DR Bgee; ENSECAG00000030432; Expressed in oviduct epithelium and 23 other cell types or tissues.
DR GO; GO:0005604; C:basement membrane; IEA:UniProt.
DR GO; GO:0005576; C:extracellular region; IEA:UniProt.
DR GO; GO:0005886; C:plasma membrane; IEA:GOC.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0043236; F:laminin binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007213; P:G protein-coupled acetylcholine receptor signaling pathway; IEA:InterPro.
DR GO; GO:0007528; P:neuromuscular junction development; IBA:GO_Central.
DR GO; GO:0043113; P:receptor clustering; IBA:GO_Central.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd00055; EGF_Lam; 2.
DR CDD; cd00104; KAZAL_FS; 8.
DR CDD; cd00110; LamG; 3.
DR Gene3D; 2.40.50.120; -; 1.
DR Gene3D; 2.60.120.200; -; 3.
DR Gene3D; 3.30.60.30; -; 8.
DR Gene3D; 2.10.25.10; Laminin; 5.
DR Gene3D; 3.30.70.960; SEA domain; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
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; IPR004850; NtA_dom.
DR InterPro; IPR000082; SEA_dom.
DR InterPro; IPR036364; SEA_dom_sf.
DR InterPro; IPR008993; TIMP-like_OB-fold.
DR PANTHER; PTHR15036:SF83; AGRIN; 1.
DR PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF00050; Kazal_1; 1.
DR Pfam; PF07648; Kazal_2; 7.
DR Pfam; PF00053; Laminin_EGF; 2.
DR Pfam; PF00054; Laminin_G_1; 3.
DR Pfam; PF03146; NtA; 1.
DR Pfam; PF01390; SEA; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 7.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00180; EGF_Lam; 2.
DR SMART; SM00057; FIMAC; 3.
DR SMART; SM00274; FOLN; 4.
DR SMART; SM00280; KAZAL; 8.
DR SMART; SM00282; LamG; 3.
DR SMART; SM00200; SEA; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR SUPFAM; SSF57196; EGF/Laminin; 3.
DR SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 8.
DR SUPFAM; SSF82671; SEA domain; 1.
DR SUPFAM; SSF50242; TIMP-like; 1.
DR PROSITE; PS00022; EGF_1; 4.
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; 8.
DR PROSITE; PS50025; LAM_G_DOMAIN; 3.
DR PROSITE; PS51121; NTA; 1.
DR PROSITE; PS50024; SEA; 1.
PE 4: Predicted;
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Heparan sulfate {ECO:0000256|ARBA:ARBA00023207};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00023207};
KW Reference proteome {ECO:0000313|Proteomes:UP000002281};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..1975
FT /note="Agrin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040372042"
FT DOMAIN 32..159
FT /note="NtA"
FT /evidence="ECO:0000259|PROSITE:PS51121"
FT DOMAIN 198..246
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 266..321
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 347..393
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 410..465
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 470..530
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 548..595
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 633..681
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 722..775
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 776..822
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 851..900
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 1057..1179
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 1257..1295
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1302..1478
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1479..1516
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1518..1555
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1565..1748
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1744..1783
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1794..1972
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 902..1023
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1207..1262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..917
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..952
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 974..988
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1214..1235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 33..105
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00443"
FT DISULFID 722..734
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 724..741
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 743..752
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 776..788
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 778..795
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 797..806
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1266..1283
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1285..1294
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1506..1515
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1545..1554
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1773..1782
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1975 AA; 209349 MW; BF70249B669150C4 CRC64;
MASLRRSGLA QLQPLLLLLV VAARALPGAD GTCPERALER REEEANVVLT GTVEEILNVD
PVQHTYSCKV RVWRYLKGRD VVTQESLLDG GNKVVIGGFG DPLICDNQVS TGDTRIFFVN
PAPPYLWPAH KNELMLNSSL MRITLRNLEE VEHCVEDKPG THFTPAPPTP PDACRGMLCG
FGAVCEPSAE GPGRASCVCK KSACPSVVAP VCGSDASTYS NECELQRAQC SQQRRIRLLS
RGPCGSQDPC SNVTCSFGST CARSADGQMA TCLCPTTCQG APQGPVCGSD GIDYPSECQL
LRSACARQKN IFKKFDGPCD PCQGALDDLS RICRVNPRTR RPEMLLRPES CPPRQAPVCG
DDGVTYDSDC VMGRTGAARG LLLQKVRSGQ CQPQDQCPDA CRFNAVCLSR RGRPRCSCDR
VVCDGAYRPV CAHDGHTYDN DCWRQQAECR QQRTIPTKHP GPCDRCGQCR FGALCEAETG
RCVCPSECVA SAQPVCGSDG HTYASECELH VHACTHQISL HVASAGHCQT CGDTLCTFGA
VCLAGQCVCP RCERPMPGPV CGSDGVTYGS TCELREAACR QQTQIEEARA GPCEQAECGS
GGSGSGEDGE CEQELCRGRG GIWDEDSEDG LCVCDFSCQS VLRSPVCGSD GVTYGSECEL
KKTRCESGRE LYVAVQGACQ GPTLAPLPPA VPPHCAQTPY GCCQDNITAA RGVGLAGCPS
SCQCNPHGAY GSTCDPALGQ CSCRPGVGGL RCDRCEPGFW NFRGIVTDGR SGCTPCSCDP
RGAVRDDCEQ MTGLCSCKPG VAGPKCGQCP DGRALGPAGC ETVSSVPETC AEIRCEFGAS
CVEEAGSAHC VCPTPTCLGA NATKVCGSDG VTYGNECQLR TIACRQGLDI SIQSLGPCQE
VVTPGTRPTS TSVATVGLDP SRALPLPPSA LPLAPSSTPH SRPTPRPSPR PWTTASIPRT
TERPVLTMPP TASLPAASLA SSAFGESGSA DGSGDEELSG DLEASGASSG GLEPPEGGSA
VSPGLPVERA SCYNSPLGCC SDGKTPSLDA EGSNCPATKA FQGVLELESV EGQELFYTPE
MADPKSELFG ETARSIESAL DDLFRNSDVK KDFRSVRLRD LGPGNSVRAI VDVHFDPTTA
FRAPDVGRAL LRQIQVSRRR SLGVRRPLQE HVRFLDLDWF PAFFTGATTG ATPAAATARA
TTVARLPSAV TPRAFHPSHT SRPSSRTTAH TPTRRPPTSA PRRGPGHLPL SPGSQQPPRP
CDSQPCFHGG TCQDLGSGGD FTCSCPVGRG GTICEKVLGP SRSAPAFGGH SFLAFPTLRA
YHTLRLALEF RALEPQGLLL YNGNDRGKDF LALALLGGRV QLRFDTGSGP AVLTSSVPVE
PGRWHRLELS RHWRRGTLSV DGETPVLGQS PSGTDGLNLD TDLFVGGVPE DQASVVLERT
SVGLGLRGCI RLLDINNQRL ELSGWQGAAT RSSGVGECGD HPCLPSPCLG GAPCQALEAG
AFHCQCPPGH FGPTCAEEKN PCQPNPCHGA APCRVLPEGQ AKCECPLGRG GPLCQTVSER
ENSRPFLADF HGFSYLELKG LHTFDRDLGE KMALEVVFLA RSPSGLLLYN GQKTDGKGDF
VSLALHDHRL EFRYDLGKGA AVIRSKEPVA LGTWTRVSLE RSGRKGAMRV DDGPRVLGES
PVPHTVLNLK EPLYVGGAPD FSKLARAAAV SSGFDGAIQL VSLKGQQLLT QEHVVRAVDV
SSFADHPCTR ASGYPCLNGA SCLPREASYV CLCPGGFSGL HCEKGLIEKS AGDLDTLAFD
GRTYIEYLNA VTESEKALQS NHFELSLRTE ATQGLVLWSG KATERADYVA LAIVDGRLQL
AYDLGSQPMV LRSTVPVNTN RWLRVRAHRE QREGSLQVGN EAPVTGSSPL GATQLDTDGA
LWLGGLEKLP VGQALPKAYG TGFVGCLRDV VVGRRPLHLL EDAVSRPELR PCPTP
//
