ID F7G810_CALJA Unreviewed; 2045 AA.
AC F7G810;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 3.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=Agrin {ECO:0000256|ARBA:ARBA00016077};
GN Name=AGRN {ECO:0000313|Ensembl:ENSCJAP00000020999.3};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000020999.3, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000020999.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000020999.3}
RP IDENTIFICATION.
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; 9483.ENSCJAP00000020999; -.
DR Ensembl; ENSCJAT00000022204.3; ENSCJAP00000020999.3; ENSCJAG00000011412.5.
DR eggNOG; KOG3509; Eukaryota.
DR GeneTree; ENSGT00940000158337; -.
DR InParanoid; F7G810; -.
DR OMA; AMEISPF; -.
DR TreeFam; TF326548; -.
DR Proteomes; UP000008225; Chromosome 7.
DR Bgee; ENSCJAG00000011412; Expressed in kidney and 6 other cell types or tissues.
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; 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; 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; 8.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00180; EGF_Lam; 2.
DR SMART; SM00057; FIMAC; 4.
DR SMART; SM00274; FOLN; 7.
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; 2.
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:UP000008225};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..2045
FT /note="Agrin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035189665"
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 924..973
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 1128..1250
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 1329..1367
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1372..1548
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1549..1586
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1588..1625
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1635..1818
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1814..1853
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1864..2042
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 997..1093
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1270..1334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1036
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1293..1311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1313..1331
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 1338..1355
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1357..1366
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1576..1585
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1615..1624
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1843..1852
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 2045 AA; 215431 MW; E9C7F6318C438141 CRC64;
MAGPGPSRPG ALRPLLLLLV VAARVLPGAG GTCPERALER REEEANVVLT GTVEEILNVD
PVQHTYSCKV RVWRYLKGKD LVARESLLDG GNKVVISGFG DPLICDNQVS TGDTRIFFVN
PAPPYLWPAH KNELMLNSSL MRITLRNLEE VEFCVEDKPG THFTPVPPTP PDACRGMLCG
FGAVCEPSAE GPGRASCVCK KSPCPSVVAP VCGSDASTYS NECELQRAQC SQQRRIRLLS
RGPCGSRDPC SNVTCSFGST CARSSDGLTA SCLCPETCRG APEGTVCGSD GADYPGECQL
LRRACAHQEN VFKKFDGPCD PCQGAVAELS RSCRVNPRTR RPEMLLRPES CPARRAPVCG
DDGVTYKNDC VMGRSGATRG LLLQKVRSGQ CQPQDQCPEP CPFNAVCLSR RGRPHCSCDR
VTCDGAYRPV CAQDGHTYDN DCWRQQAECR HQRAIPSKHQ GPCDQAPSPC VGVQCAFGAT
CSVKNGQAAC ECRQACSGLY DPVCGSDGVT YGSVCELEAM ACTLGREVRV VRKGPCDHCG
QCRFGALCEA ETGRCVCPSE CVALAQPVCG SDGHTYASEC MLHVHACTHQ ISLHVASAGP
CETCGHAVCA FGAVCSAGQC MCPRCEHPPP GPVCGSDGVT YDSACELREA ACRQQKQIEE
ARAGPCEQLE CGSGGSGSGE DGDCEQELCR QRGGIWDEDS EDGPCVCDFS CQSVPGSPVC
GSDGITYGTE CDLKKARCES QRELHVVAQG ACQGPTFAPL PPVAPSHCAQ TPYGCCQDNI
TMARGVGLAG CPSACQCNPH GSYGSTCDPA TGQCSCRPGV GGLRCDRCEP GFWNFRGIVT
DGHSGCTPCS CDPQGAVRDD CEQMSGLCSC KPGAAGPKCG QCPDGRALGP AGCEADASAP
ETCAEVRCKF GALCVEDSGS AHCVCPMLTC PEANASKVCG SDGVTYGNEC QLKTIACRQG
LHLSIQSLGP CQEAVAPSTH PTSASVIVTT PGLLSQGLPA PPSALPLAPS STTHSQTTPP
PSSRPRTTTS IPRTTVWPVP PTAPSPVPSL VASAFGESGS ADGSDDEELS GDQEASGGGS
GGLEPLEGSS VATPGLPIER ASCYNAPLGC CSDGKTPSLD VEGSNCPATR VFQGMLELEG
VEGQELFYTP EMADPKSELF GETARSIESV LDDLFRNSDV KKDFRSVHLR DLGPGRSVRA
IVDVHFDPTT AFRAPDVGRA LLRQLQVSRR RSLGVRRPLQ EHVRFMDFDW FPAFFTGATS
GAIAAVATAR ATTASRPPPS AVTPRAPHPG HTSRPISKTT AAPTTRRPPT TAPSHVPGYP
PLPPALQQPP KPCDSQPCLH GGTCQDGALG GDFTCSCPAG WGGAVCERVL HAPVPAFGGH
SFLAFPTLRA YHTLRLALEF RTLEPQGLLL YNGNARGKDF LALALLDGHV QLRFDTGSGP
AVLTSAVLVD LGRWHRLELS RHWRRGTLSV DGETPVLGES PSGTDGLNLD TDLFVGGVPE
DQAAVVLERI FVGTGLRGCI RLLDINNQLL ELSVGPGAAA QGSAVGECGD HPCLPNPCHG
RAPCQALEAG RFRCLCPPGH FGPTCAEEKN PCQPNPCHGA APCHVLPEGG VQCQCPLGQG
GTLCQTVSGQ DGSRPFLADF NGFSHLELRG LHTFARDLGE KMALEVVFLA RGPSGLLLYN
GQKTDGKGDF VSLALQDRHL EFRYDLGKGA AVIRSKEPVT LGTWTSVSLE RNGRKGAMRV
GDGPRMLGES PVPHTVLNLK EPLYVGGAPD FSKLARAAAV SSGFSGAIQL VSLGGLQLLT
PEHVLRQMDV TSFADHPCTR ASGHPCLNGA SCVPREAAYV CLCPGGFSGP HCEKGLVEKS
AGDLDALAFD GRTFIEYLNA VTESEKVLQS NHFELSLRTE ATQGLVLWSG KATEQADYVA
LAIVDGHLQL SYNLGSQPVV LRSTVPVNTS RWLRVVAHRE QREGSLQVGN EAPVTGSSPL
GATQLDTDGA LWLGGLPELP MGPALPKAYG TGFVGCLRDV MVGQHPLHLL EDAVTKPELR
PCPAA
//
