ID A0A094KSM8_ANTCR Unreviewed; 1166 AA.
AC A0A094KSM8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Agrin {ECO:0000256|ARBA:ARBA00016077};
DE Flags: Fragment;
GN ORFNames=N321_02997 {ECO:0000313|EMBL:KFZ53808.1};
OS Antrostomus carolinensis (Chuck-will's-widow) (Caprimulgus carolinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Caprimulgiformes;
OC Caprimulgidae; Antrostomus.
OX NCBI_TaxID=279965 {ECO:0000313|EMBL:KFZ53808.1, ECO:0000313|Proteomes:UP000053620};
RN [1] {ECO:0000313|EMBL:KFZ53808.1, ECO:0000313|Proteomes:UP000053620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N321 {ECO:0000313|EMBL:KFZ53808.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; KL342559; KFZ53808.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094KSM8; -.
DR Proteomes; UP000053620; Unassembled WGS sequence.
DR GO; GO:0005604; C:basement membrane; IEA:UniProt.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 3.
DR CDD; cd00104; KAZAL_FS; 1.
DR CDD; cd00110; LamG; 3.
DR Gene3D; 2.60.120.200; -; 3.
DR Gene3D; 3.30.60.30; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 4.
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; 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; 1.
DR Pfam; PF00054; Laminin_G_1; 3.
DR Pfam; PF01390; SEA; 1.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00274; FOLN; 2.
DR SMART; SM00280; KAZAL; 1.
DR SMART; SM00282; LamG; 3.
DR SMART; SM00200; SEA; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 1.
DR SUPFAM; SSF82671; SEA domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00022; EGF_1; 4.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS51465; KAZAL_2; 1.
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 Proteoglycan {ECO:0000256|ARBA:ARBA00023207};
KW Reference proteome {ECO:0000313|Proteomes:UP000053620}.
FT DOMAIN 29..78
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 251..373
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 453..489
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 494..670
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 671..708
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 710..747
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 757..940
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 936..974
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 985..1163
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 178..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 479..488
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 698..707
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 737..746
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 964..973
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFZ53808.1"
FT NON_TER 1166
FT /evidence="ECO:0000313|EMBL:KFZ53808.1"
SQ SEQUENCE 1166 AA; 126026 MW; D8F3F98AF7A7B87F CRC64;
DPSAPKSCEE MSCEFGASCV EVNGFAHCEC PSPLCSEANM TKVCGSDGVT YGDQCQLKTI
ACRQGQVITV KHVGQCHESI THTSHTSPPT PLPTLPLDKL ILPPPLRLTT RAPEPTELAT
SSLLLEARPT ERGHPTTRRI TTARPATTPW MTHGVYKTTV RPLSTAPVVL ATTQPAYAES
GSAEGSGDQE MGISGDQESS GAGSAGEEEV EENQVTSTPA IERATCYNTP LGCCSDGKTA
AADAEGSNCP ATKVFQGVLI LEEVEGQELF YTPEMADPKS ELFGETARSI ESALDELFRN
SDVKKDFKSI RVRDLGQSSA VRVIVESHFD PATSYTAPDI QGALLKQIKA SKKKTILVKK
PQQEHVKFMD FDWIPRLFTT TVTTTTATTM APATTRRYTT AAAATTVHVL RPDAAGRPST
KLAGAVSTKR PTSTLPATTR RKPTRQPPTT KKPSRPCDSH PCLHGGTCED DGKEFTCSCP
AGKGGAVCEK PIRYFIPSFG GKSYLAFKMM KAYHTVRIAM EFRTVELSGL LLYNGQNRGK
DFISLALVGG FVELRFNTGS GTGVITSKVR VEPGKWHQLV VNRNRRSGTL SVDGEPHVSG
ESPTGTDGLN LDTDLFIGGA PEDQMAAVAD RTAATTGLKG CIRLLDVNNQ MYDLREKGSD
VLYGSGVGEC GNDPCHPNPC HHGGICHVKE AEMFHCECLH TYTGPTCADE RNPCDPTPCH
VSATCLVLPE GGALCACPMG REGDFCELVT EQDHTMPFLP EFNGFSYLEL NGLQTFVPDL
QDKMSMEVVF LAKNPSGMIF YNGQKTDGKG DFVSLALHDG YLEYRYDLGK GAAVLRSKEP
VPLNTWISVL LERNGRKGVM RINNGERVMG ESPVPHTFLN LKEPFYVGGA PDFSKLARAA
AISTSFDGAV QRISIKGVPV LKEQNIRSAI EISPFRGHPC TQKPNPCQNG GTCSPRLESY
ECACQRGFSG AHCEKVIIEK AAGDAEAIAF DGRTYMEYHN AVTKSEKALQ SNHFELSIKT
EATQGLILWS GKGLERSDYI ALAIVDGFVQ MTYDLGSKPV ILRSTVPVNT NQWIHIKAYR
VQREGSLQVG NEAPIAGSSP LGATQLDTDG ALWLGGMEKL NVAHKLPKAY STGFIGCIRD
VIVDRQELHL VEDALNNPTI LHCSAK
//