ID F1MSI2_BOVIN Unreviewed; 2062 AA.
AC F1MSI2;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 2.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=Agrin {ECO:0000256|ARBA:ARBA00016077};
GN Name=AGRN {ECO:0000313|Ensembl:ENSBTAP00000017563.5,
GN ECO:0000313|VGNC:VGNC:25742};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000017563.5, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000017563.5, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000017563.5,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000017563.5}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000017563.5};
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 PaxDb; 9913-ENSBTAP00000017563; -.
DR Ensembl; ENSBTAT00000017563.5; ENSBTAP00000017563.5; ENSBTAG00000013191.5.
DR VEuPathDB; HostDB:ENSBTAG00000013191; -.
DR VGNC; VGNC:25742; AGRN.
DR eggNOG; KOG3509; Eukaryota.
DR GeneTree; ENSGT00940000158337; -.
DR HOGENOM; CLU_001582_1_0_1; -.
DR TreeFam; TF326548; -.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000013191; Expressed in dorsal thalamus and 104 other cell types or tissues.
DR ExpressionAtlas; F1MSI2; baseline and differential.
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:0043113; P:receptor clustering; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd00055; EGF_Lam; 2.
DR CDD; cd00104; KAZAL_FS; 9.
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; -; 9.
DR Gene3D; 2.10.25.10; Laminin; 6.
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; IPR009030; Growth_fac_rcpt_cys_sf.
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; 2.
DR Pfam; PF00050; Kazal_1; 1.
DR Pfam; PF07648; Kazal_2; 8.
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; 4.
DR SMART; SM00180; EGF_Lam; 2.
DR SMART; SM00057; FIMAC; 2.
DR SMART; SM00274; FOLN; 5.
DR SMART; SM00280; KAZAL; 9.
DR SMART; SM00282; LamG; 3.
DR SMART; SM00200; SEA; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 9.
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; 9.
DR PROSITE; PS50025; LAM_G_DOMAIN; 3.
DR PROSITE; PS51121; NTA; 1.
DR PROSITE; PS50024; SEA; 1.
PE 1: Evidence at protein level;
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 Proteomics identification {ECO:0007829|PeptideAtlas:F1MSI2};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..2062
FT /note="Agrin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018772003"
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 484..538
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 543..603
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 610..668
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 706..754
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 795..848
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 849..895
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 924..973
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 1130..1252
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 1327..1365
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1370..1546
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1547..1584
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1586..1623
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1633..1816
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1812..1851
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1881..2059
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 992..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1056..1101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1278..1333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1030
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1284..1310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1312..1328
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 33..105
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00443"
FT DISULFID 795..807
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 797..814
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 816..825
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 849..861
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 851..868
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 870..879
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1336..1353
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1355..1364
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1574..1583
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1613..1622
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1841..1850
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 2062 AA; 218428 MW; 22217D39A49798EB CRC64;
MASFRPFSRA LLQPLLLLLV VAVRALPSAD GTCPERALER REEEANVVLT GTVEEILNVD
PVQHTYSCKV RVWRYLKGKD VVAQESLLDG GNKVVIGGFG DPLICDNQVS TGDTRIFFVN
PAPPYLWPAH KNELMLNSSL MRITLRNLEE VEHCVEDKPG THFTPVPPTP PDACRGMLCG
FGAVCEPSAD EPGRASCVCK KSSCPSVVAP VCGSDASTYS NECELQRAQC SQQRRIRLLR
RGPCGTRDPC SNVTCSFGST CVPSADGLTA TCLCPATCLG APEGPVCGSD GSDYPSECQL
LRHACAHQEN IFKKFDGPCD PCQGFLSDLS RTCRVNPRTR RPEMLLRPES CPPRGTPVCG
DDGVTYDNDC VMGRTGAAQG ILLQKVRSGQ CQPRDQCPEP CRFNAVCLSR RGRPRCSCDR
VVCDGAYRPV CAHDGHTYDN DCWRQQAECQ QQRSIPMKHQ GPCDQSPSPC RGVQCPFGAM
CAVKNGEAEC ACPKACSGVY DPVCGSDGIT YGSACELEAT ACALGREIRV ARRGPCDRCG
QCRFGALCEA ETGRCVCPSE CVASAQPVCG SDGRTYASEC ELHVHACTHQ ISLHVASAGP
CQTCGDTVCA FGAVCSAGQC VCPRCERPPP GPVCGSDGVT YGSSCELREA ACQQQTQIEE
AWAGPCEQAE CGSGGSGSGE DGECEPELCR QRGGIWDEDS EDGPCVCGFS CQGVLRSPVC
GSDGVTYRTE CELKKARCES QPELYVVAQG ACRGPTLAPL PPAIPLHCAQ TPYGCCQDNI
TVAQGVGLAG CPSSCQCNPH GSYGGTCDPV TGQCSCRPGV GGLKCDRCEP GFWNFRGIVT
DGRSGCTPCS CDPRGAVRDD CEQMTGLCSC KPGVAGPKCG QCPDGRALGP AGCETDSSPP
KTCAEMLCEF GASCVEEAGS AHCVCPTPTC PGADATKVCG SDGVTYGNEC QLRTIACRQG
LEISIQSFGP CQEGITSGPR VTSASVAPSA LDLNKAPLPP PSALPLAPSS TRHSQPTSRA
SSQPWTMASI PRTTARPVLT MPPVAPSPAA SLVTSAFGES GSADGSGDEE LSGDLEASGA
GSGGLESPER DSAGTPGLPM ERASCYNSPM GCCSDGKTPS LDAEGSNCPA TKVFQGVLEL
EGVEGQELFY TPEMADPKSE LFGETARSIE SALDDLFRNS DVKKDFRSVR LRDLGPGSSV
RAIVEVHFDP TTAFRASDVG RALLRQLQAS RRRSLGVRRP LQEHVRFMDF DWFPAFFTGA
TPAAATARAT TVARLPPSAA TPRAHFPSHT SRPVSRTTPP ATTRQPPTTA PSRVPGRRPL
PPGTQQPRRP CDSQPCLHGG TCQDQGSGAD FTCSCPAGTG GAVCEKALHP SVPAFGGHSF
LAFPTLRAYH TLRLALEFRA LEPQGLLLYN GNARGKDFLG LVLLGGRVQF RFDTGSGPAV
LTSSVPVQPG RWHHLELSRH WRQGTLSVDG ETPVLGQSPS GTDGLNLDTD LFVGGVPEDQ
ASTVLERTSV SIGLRGCIRL LDVNNQRLEL SSWPESATRS SGVGKCGDHP CLPSPCLGGA
PCQALEAGRF HCQCPPGRFG PTCADEKDPC QPNPCHGAAP CRVLPQGEAK CECPHGREGS
LCQTVSEPED NQPFLADFSS FSYLELKGLH TFERDLGEKM ALEVVFLARS PSGLLLYNGQ
KTDGKGDFVS LALHNGLLEF RYDLGKGAAV IRSKEPVALG AWTRVSLERN GRKGAMRVGD
GPRVLGESPV PHTVLNLKEP LFVGGAPDFS KLARAAAVSS GFDGAIQLVS LNGRQLLTRE
NVVRAVDVSS FADHPCTQAE GQPCLHGASC LPREASYECL CPAGFSGLHC EKGLIEKSAG
DLDALAFDGR TYIEYLNAVT ESELTNEIPA PETLDSGAHP SEKALQSNHF ELSLRTEATQ
GLVLWSGKAT ERADYIALAI VDGRLQLAYD LGSQPVVLRS TVPVNTNRWL RVRAHRKQRE
GSLQVGNEAP VTGSSPLGAT QLDTDGALWL GGLEKLPTGQ ALPKAYGTGF VGCLRDVVVG
QRPVHLLEDA ITKPELRPCP AL
//
