ID H2N9J6_PONAB Unreviewed; 2044 AA.
AC H2N9J6;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 3.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Agrin {ECO:0000256|ARBA:ARBA00016077};
DE AltName: Full=Activin-binding protein {ECO:0000256|ARBA:ARBA00042260};
DE AltName: Full=Follistatin {ECO:0000256|ARBA:ARBA00039758};
GN Name=AGRN {ECO:0000313|Ensembl:ENSPPYP00000002342.2};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000002342.2, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000002342.2, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPPYP00000002342.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Binds directly to activin and functions as an activin
CC antagonist. Specific inhibitor of the biosynthesis and secretion of
CC pituitary follicle stimulating hormone (FSH).
CC {ECO:0000256|ARBA:ARBA00037743}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR Ensembl; ENSPPYT00000002413.2; ENSPPYP00000002342.2; ENSPPYG00000002025.2.
DR eggNOG; KOG3509; Eukaryota.
DR GeneTree; ENSGT00940000158337; -.
DR HOGENOM; CLU_001582_1_0_1; -.
DR InParanoid; H2N9J6; -.
DR OMA; AMEISPF; -.
DR TreeFam; TF326548; -.
DR Proteomes; UP000001595; Chromosome 1.
DR GO; GO:0005604; C:basement membrane; IEA:Ensembl.
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:Ensembl.
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; 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; PTHR10913:SF45; AGRIN; 1.
DR PANTHER; PTHR10913; FOLLISTATIN-RELATED; 1.
DR Pfam; PF00008; EGF; 1.
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; 2.
DR SMART; SM00180; EGF_Lam; 2.
DR SMART; SM00057; FIMAC; 4.
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; PS51257; PROKAR_LIPOPROTEIN; 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:UP000001595};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..2044
FT /note="Agrin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035151697"
FT DOMAIN 30..157
FT /note="NtA"
FT /evidence="ECO:0000259|PROSITE:PS51121"
FT DOMAIN 196..244
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 264..319
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 345..391
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 408..463
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 489..536
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 541..601
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 608..666
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 704..752
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 793..846
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 847..893
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 922..971
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 1129..1251
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 1328..1366
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1371..1547
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1548..1585
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1587..1624
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1634..1817
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1813..1852
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1863..2041
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 995..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1275..1333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1033
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1275..1301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1307..1332
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 31..103
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00443"
FT DISULFID 793..805
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 795..812
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 814..823
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 847..859
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 849..866
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 868..877
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1337..1354
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1356..1365
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1575..1584
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1614..1623
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1842..1851
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 2044 AA; 214957 MW; 797BD95B323C4AB1 CRC64;
MANPSRPGPL RLLLLLLVVA ACVLPGAGGT CPERALERRE EEANVVLTGT VEEILNVDPV
QHTYSCKVRV WRYLKGKDLV ARESLLDGGN KVVISGFGDP LICDNQVSTG DTRIFFVNPA
PPYLWPAHKN ELMLNSSLMR ITLRNLEEVE FCVEDKPGTH FTPVPPTPPD ACRGMLCGFG
AVCEPNAEGP GRASCVCKKS PCPSVVAPVC GSDASTYSNE CELQRAQCSQ QRRIRLLSRG
PCGSRDPCSN VNCSFGSTCA RSADGLTASC LCPATCRGAP EGTVCGSDGA DYAGECQLLR
RACARQENVF KKFDGPCDPC QGALPDPSRS CRVNPRTRRP EMLLRPESCP ARQAPVCGDD
GVTYENDCVM GRSGAARGLL LQKVRSGQCQ GRDQCPEPCQ FNAVCLSRRG RPRCSCDRVT
CDGAYRPVCA QDGRTYDSDC WRQQAECRQQ RAIPSKHQGP CDQAPSPCLG VQCAFGATCA
VKNGQAACEC LQACSSLYDP VCGSDGVTYG SACELEATAC TLGREIQVAH KGPCDRCGQC
RFGALCEAET GRCVCSSECV ALAQPVCGSD GHTYPSECML HVHACTRQIS LHVASAGPCE
TCGDAVCAFG AVCSAGQCVC PRCEHPPPGP VCGSDGVTYG SACELREAAC QQQTQIEEAR
AGPCEQAECG SGGSGSGEDG DCEQELCRQR GGIWDEDSED GPCVCDFSCQ SVPGSPVCGS
DGITYSTECE LKKARCESQR ELYVAAQGAC RGPTFTPLPP VAPLRCAQTP YGCCQDNITA
ARGVGLAGCP SACQCNPHGS YGGTCDPATG QCSCRPGVGG LRCDRCEPGF WNFRGIVTDG
RSGCTPCSCD PQGAVRDDCE QMTGLCSCKP GVAGPKCGQC PDGRALGPAG CEADASAPAT
CAEMHCEFGA LCVEESGSAH CVCPMLTCPE ASATKVCGSD GVTYGNECQL KTIACRQGLQ
ISIQSLGPCQ EAVAPSTHPT SASVTVTTPG LLLSQALPPP GALPLAPSST AHSRAAPPPS
SRPQTTASIP RTTVWPVLTV PPTAPSPAPS LVASAFGESG STDGSGDEEL SGDQEASGGG
SGGLEPFEGS SVATPGPPIE RASCYNSALG CCSDGKTPSL DAEGSNCPAT KVFQGVLELE
GVEGQELFYT PEMADPKSEL FGETARSIES TLDDLFRNSD VKKDFRSVRL RDLGPGKSVR
AIVDVHFDPT TAFRAPDVAR ALLRQIQVSR RRSLGLRRPL QEHVRFMDFD WFPAFFTGAT
SGAIAAVATA RATTASRLPS SAVTPRALHP SHTSQPVAKT TAAPPTRRPP TTAPSRVPGR
RPPVPQQPPK PCDSQPCFHG GTCQDWALGG GFTCSCPAGR GGAICEKVLG APVPAFEGHS
FLAFRTLRAY HTLRLALEFR ALEPQGLLLY NGNARGKDFL ALALLDGRVQ LRFDTGSGPA
VLTSAVPVEP GQWHRLELSR HWRRGTLSVD GETPVLGESP SGTDGLNLDT DLFVGGVPED
QAAVALERTF VGTGLRGCIR LLDVNNQRLE LGIGPGAATR GSGVGECGDH PCLPNPCRGG
APCQALEAGR FHCQCPPSRV GPTCADEKSS CQPNPCHGAA PCRVLPEGGA QCECPLGRGG
TLCQTASGQD GSGPFLADFN GFSHLELRGL HTFARDLGEK MALEVVFLAR GPSGLLLYNG
QKTDGKGDFV SLALQDRHLE FRYDLGKGAA VIRSREPVTL GAWTRVSLER NGRKGAMRVG
DGPRVLGESP VPHTVLNLKE PLYVGGAPDF SKLARAAAVS SGFNGAIQLV SLGGRQLLTP
EHVLRQVDVT SFADHPCTQA SGHPCLNGAS CIPREAAYVC LCPGGFSGPH CEKGLVEKSV
GDVDALSFDG RTFVEYLNAV TESEKALQSN HFELSLRTEA TQGLVLWSGK ATERADYVAL
AIVDGHLQLS YNLGSQPVVL RSTVPVNTNR WLRVVAHREQ REGSLQVGNE APVTGSSPLG
ATQLDTDGAL WLGGLPELPV GPALPKAYGT GFVGCLRDVV VGRRPLHLLE DAVTKPELRP
CPTP
//
