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Database: UniProt
Entry: H9G5M1_ANOCA
LinkDB: H9G5M1_ANOCA
Original site: H9G5M1_ANOCA 
ID   H9G5M1_ANOCA            Unreviewed;      1508 AA.
AC   H9G5M1;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 2.
DT   24-JAN-2024, entry version 74.
DE   RecName: Full=Agrin {ECO:0000256|ARBA:ARBA00016077};
OS   Anolis carolinensis (Green anole) (American chameleon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Iguania; Dactyloidae; Anolis.
OX   NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000001759.3, ECO:0000313|Proteomes:UP000001646};
RN   [1] {ECO:0000313|Ensembl:ENSACAP00000001759.3}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000001759.3};
RG   The Genome Sequencing Platform;
RA   Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA   Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSACAP00000001759.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-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; 28377.ENSACAP00000001759; -.
DR   Ensembl; ENSACAT00000001800.3; ENSACAP00000001759.3; ENSACAG00000001639.3.
DR   eggNOG; KOG3509; Eukaryota.
DR   GeneTree; ENSGT00940000158337; -.
DR   HOGENOM; CLU_001582_1_0_1; -.
DR   TreeFam; TF326548; -.
DR   Proteomes; UP000001646; Unplaced.
DR   Bgee; ENSACAG00000001639; Expressed in hemipenis and 11 other cell types or tissues.
DR   GO; GO:0005886; C:plasma membrane; IEA:GOC.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007528; P:neuromuscular junction development; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0043113; P:receptor clustering; IBA:GO_Central.
DR   CDD; cd00053; EGF; 1.
DR   CDD; cd00054; EGF_CA; 3.
DR   CDD; cd00055; EGF_Lam; 2.
DR   CDD; cd00104; KAZAL_FS; 4.
DR   CDD; cd00110; LamG; 3.
DR   Gene3D; 2.60.120.200; -; 3.
DR   Gene3D; 3.30.60.30; -; 4.
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; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
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; IPR000082; SEA_dom.
DR   InterPro; IPR036364; SEA_dom_sf.
DR   PANTHER; PTHR15036:SF83; AGRIN; 1.
DR   PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 1.
DR   Pfam; PF00008; EGF; 4.
DR   Pfam; PF07648; Kazal_2; 4.
DR   Pfam; PF00053; Laminin_EGF; 2.
DR   Pfam; PF00054; Laminin_G_1; 3.
DR   Pfam; PF01390; SEA; 1.
DR   PRINTS; PR00011; EGFLAMININ.
DR   SMART; SM00181; EGF; 5.
DR   SMART; SM00179; EGF_CA; 4.
DR   SMART; SM00180; EGF_Lam; 2.
DR   SMART; SM00274; FOLN; 4.
DR   SMART; SM00280; KAZAL; 4.
DR   SMART; SM00282; LamG; 3.
DR   SMART; SM00200; SEA; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR   SUPFAM; SSF57196; EGF/Laminin; 4.
DR   SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 4.
DR   SUPFAM; SSF82671; SEA domain; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00022; EGF_1; 3.
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; 4.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 3.
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:ARBA00023207};
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:UP000001646}.
FT   DOMAIN          1..50
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51465"
FT   DOMAIN          68..115
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51465"
FT   DOMAIN          153..201
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51465"
FT   DOMAIN          241..294
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          295..341
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          372..419
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51465"
FT   DOMAIN          591..713
FT                   /note="SEA"
FT                   /evidence="ECO:0000259|PROSITE:PS50024"
FT   DOMAIN          789..827
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          825..1001
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          1002..1039
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1041..1078
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1088..1271
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          1267..1305
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1316..1505
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   REGION          440..461
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          505..558
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          746..793
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        505..520
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        532..546
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        756..775
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        241..253
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        243..260
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        262..271
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        295..307
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        297..314
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        316..325
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1029..1038
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1068..1077
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1295..1304
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   1508 AA;  162432 MW;  5B87C8FBF19E54AC CRC64;
     RCVCPTECIP SSQPVCGTDG ITYQNECELH VRACTQQTNI EVAAQGDCKT CGGVVCSFGA
     QCVDGQCVCP RCEKQPLGRV CGSNDVTYEN ACELRVAACQ QKKDIEITRT GPCEEECGSG
     GGSGSGDLNE CDRDSCRQFG GSWDEDVEDD RCVCDYTCGS VPRNPVCGSD GVTYANECEL
     KKTRCEKHQD IYVMSQGACR GVTSLPPPLE VLHCSQTVYG CCPDNVTLAL GVGSAGCPST
     CHCNPYGSYG GGCDPATGQC SCKPGVGGLK CDRCEPGFWN FRGIVTDGKS GCTPCHCDPV
     GSVRDDCEQM TGLCSCKTGI TGMKCNQCPN GSKLGMSGCE KGEDGASEEL PTIGLNPFGA
     SCVEINGSAH CECPICTEEN MGKVCGSDGV TYGDQCQLRT IACRQGQVIE VKHFGQCQES
     ITHAGHTTLP TTIRPLDSLI IPPPPQTTPQ APEQPKTAAG ARHFEDKASR LGHPVTRRTT
     TTPHPATTAW TTHSVRQTTI RPLSTAPVVP GTTQPAYVES GSAEGSGEPE MGTSGDQESS
     GMGSAGDEET EETRVTGTPV IERATCYNTP LGCCSDGKTA AVDSEGSNCP ATKVFQGVLI
     LEEVEGQELF YTPEMADPKS ELFGETARSI ESALDELFRN SDIKKDFKSI RVRDLSQSNP
     VRVIVEAHFD PATTFAATDI QRALLKQIKA SKKRTILVKK PQQENIRFMD FDWIPQLFTT
     TTTTTTATTM APAATTRHFT TTAVPRALYP GRPNGKTSGP ITTKRPVTTA PATTSRKKPF
     RLPPTTKKPA RPCDSHPCLH GGTCEDDGRD FTCSCPAGKE DTIRYFIPSF GGKSYLAFKM
     MKAYHTVRIA MEFRASELSG LLLYNGQNRG KDFISLALVN GFVELRFNTG SGTGIITSRV
     PIEPGRWHQL VVNRNRRSGM LSVDGEPHVN GESPSGTDGL NLDTDLFIGG APEDQIAAVA
     ERTSVPSGLK GCIRLLDVNN QMYDLREKGS DVLYGSGVGE CGNNPCHPNP CHHGGLCHVK
     EAEMFHCECL HGYTGPTCAD ERNPCDPNPC HISATCLVLP EGGAKCECPM GREGEFCESV
     TELDQTVPFL PEFNGFSYLE LNGLQTFVTD LQDKMSMEVV FLAKNPSGMI FYNGQKTDGK
     GDFISLSLHD GYLEYRYDLG KGAAVIKSKE PIPLNTWTSV LLERSARKGV MRINNGERIM
     GESPLPHTSL NLKEPLYVGG APDFSKLARA AAMSTSFDGA IQKISIKGIP VLKEENIRSA
     IEISTFRSHP CTQKPSPCQN GGMCNPRLES YECACQRGFF GAHCEKVIIE KAAGDSEAIA
     FNGRTYIEYH NAVTKSPDAL DYPLDISEKA LQSNHFELSI KTEATQGLIL WSGKALDRSD
     YIALAIVDGR VQMTYDLGSK PVVLHSTVLV NTNQWVQIKA YRVHREGSLQ VGNEAPITGS
     SPLGATQLDT DGALWLGGLE KLSVAHKLPK AYSTGFIGCI RDVVVDRQEL HLVEDALNNP
     TILQCSAK
//
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