ID A0A2Y9QFI3_DELLE Unreviewed; 2038 AA.
AC A0A2Y9QFI3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Agrin {ECO:0000256|ARBA:ARBA00016077};
GN Name=AGRN {ECO:0000313|RefSeq:XP_022454107.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022454107.1};
RN [1] {ECO:0000313|RefSeq:XP_022454107.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022454107.1};
RG RefSeq;
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 RefSeq; XP_022454107.1; XM_022598399.2.
DR Proteomes; UP000248483; Unplaced.
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; 1.
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; 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; 3.
DR SMART; SM00180; EGF_Lam; 2.
DR SMART; SM00057; FIMAC; 3.
DR SMART; SM00274; FOLN; 6.
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; 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 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:UP000248483};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..2038
FT /note="Agrin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016111017"
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 491..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 917..973
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 1121..1243
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 1318..1356
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1361..1537
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1538..1575
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1577..1614
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1624..1811
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1807..1846
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1857..2035
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 1005..1093
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1292..1323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1005..1024
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1295..1320
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 1327..1344
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1346..1355
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1565..1574
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1604..1613
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1836..1845
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 2038 AA; 216189 MW; 35AF128834A21000 CRC64;
MARLRPSGQA PLQPLLLLLV VAARALPGAD GTCPERALER REEEANVVLT GTVEEILNVD
PVQHTYSCKV RVWRYLKGKD VVAQESLLDG GNKVVIGGFG DPLICDNQVS TGDTRIFFVN
PAPPYLWPAH KNELMLNSSL MRITLRNLEE VEHCVEDKPG THFMPVPPTP PDACRGMLCG
FGAVCEPSAE EPGQASCVCK KSVCPSVVAP VCGSDASTYS NECELQRAQC SQQRRIRLLR
RGPCGTRDPC SNVTCSFGST CARSADGLTA TCLCPATCLG APEGPVCGSD GTDYPSECQL
LRQACAHQEN VFKKFDGPCD PCQGALNDLS LICRVDPRTR RPEMLLRPES CPPRQAPVCG
DDGVTYSNDC VMGRTGATRG LLLQKVRSGQ CQPRDQCPEA CKFSAVCLSR RGRPRCSCDR
VICDGAYKPV CAHDGHTYDN DCWRQQAECQ QQRSIPAKRQ GPCDQPPSPC RGVQCPFGAM
CAVKNGEAEC ACQRACSGIY DPVCGSDGVT YGSTCELEAT ACALGREIRV ARRGPCDRCG
QCRFGALCEA ETGRCVCPSE CVASAQPVCG SDGRTYASEC ELHVHACTRQ IGLHVASAGP
CETCGDTVCA FGAVCSAGRC VCPRCERPPP GPVCGSDGVT YRSSCELREA ACQQQMQIEE
ARVGPCEQAE CGSGGSGSGE HGECGQELCR QRGGIWDEDS EDGPCVCDFS CQSVLRSPVC
GSDGVTYRTE CELKKARCES RPELYVVAQG ACSAPTLAPL LPAVPLHCAQ SPYGCCLDNI
TAARGVGLAG CPSSCQCNPH GSYGGTCDPA TGQCSCRPGV GGLKCDRCEP GFWNFRGIVT
DGRSGCTPCS CDPQGAVRDD CEQMTGLCSC KPRVAGPRCG QCPDGRALGP AGCETDSPAP
KTCAEMPCEF GASCVEEAGS AHCMCPTPAC PGANATKVCG SDGVTYGDEC QLRTIACRQG
LDISIQSLGP CQEDITSGPR PTSASVALSG LDLSKALLPP PSALSLAPSS TARPASQPWT
TASVPRTAAR PVLTMPPTAA SPAASLVTSA FGSADGSGDE ELSGDLEASA AGSGGLEPPE
RDSAGTPGPP MERASCYNSP MGCCSDGKTP SLDAEGSNCP ATKVFQGVLE LEGVEGQELF
YTPEMADPKS ELFGETARSI ESALDDLFRN SDLKKDFRSV RLRDLGPGNS VRAIVDVHFD
PTTAFRAPDV CQALVRQIQA SRRRSLGVRR PLQEHVRFMD FDWFPAFFTG ATPAAATARA
TTVARLPPSA VTPRALYPSH TSRPVSRITV PFTARQPPTP APSRMPAHRP SPPGIQQPPR
PCDSQPCLHG GTCQDQGSGG DFTCRCTAGR GGAVCEQAPR PSVPAFGGHS FLAFPTLRAY
HTLRLALEFR ALEPQGLLLY NGNVRGKDFL ALALLGGRVQ LRFDTGSGPA VLTSSVPVQP
GRWHHLELSR HWRQGTLSVD GETPVLGQSP SGTDGLNLDM DLFVGGVPED QASVVLERTS
VGVGLRGCIR LLDVNNQQLE LSNWQGSATR SSGVGECGDH PCVPNPCLGG APCQALEAGM
FHCRCLPGRF GPTCADEKDP CQPNPCHGAA PCRVLPQGEA KCECPRGREG SLCQTVSERE
NSQPFLADFS SFSYLELKGL HTFERDLGEK MELEVVFLAR GPSGLLLYNG QKTDGKGDFV
SLALHDRVLE FRYDLGKGAA VIRSKEPVAL GAWTRVSLER NGRKGAMRVD DGPRVLGESP
KSRKVPHTVL NLKEPLYVGG APDFSKLARA AAVSSGLDGA IQLVSLNGRQ LLTREHVVRA
VGVSSFADHP CTQAEGHPCL NGASCLPREA SYECLCPGGF SGLHCEKGLI EKSAGDLDTL
AFDGRTYIEY LNAVAESEKA LQSNYFELSL RTEATQGLVL WSGKAAERAD YIALAIVDGR
LQLAYDLGSQ PMVLRSTVPV STNRWLRVRA HREQREGSLQ VGNEAPVTGS SPLGATQLDT
DGALWLGGLE KLPVGQALPK AYGTGFVGCL RDVVVGRRPL NLLEDAVTKP DLRPCPAP
//
