ID A0A0L8IFM4_OCTBM Unreviewed; 1386 AA.
AC A0A0L8IFM4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Agrin {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=OCBIM_22005418mg {ECO:0000313|EMBL:KOG00302.1};
OS Octopus bimaculoides (California two-spotted octopus).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus.
OX NCBI_TaxID=37653 {ECO:0000313|EMBL:KOG00302.1};
RN [1] {ECO:0000313|EMBL:KOG00302.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOG00302.1};
RC TISSUE=Gonad {ECO:0000313|EMBL:KOG00302.1};
RA Tran T., Druce J.;
RT "MeaNS - Measles Nucleotide Surveillance Program.";
RL Submitted (JUL-2015) 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; KQ415816; KOG00302.1; -; Genomic_DNA.
DR EnsemblMetazoa; Ocbimv22005419m; Ocbimv22005419m.p; Ocbimv22005418m.g.
DR EnsemblMetazoa; XM_014913581.1; XP_014769067.1; LOC106868360.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00055; EGF_Lam; 2.
DR CDD; cd00104; KAZAL_FS; 6.
DR CDD; cd00110; LamG; 3.
DR Gene3D; 2.60.120.200; -; 3.
DR Gene3D; 3.30.60.30; -; 6.
DR Gene3D; 2.10.25.10; Laminin; 6.
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; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR15036:SF83; AGRIN; 1.
DR PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 1.
DR Pfam; PF00008; EGF; 2.
DR Pfam; PF07648; Kazal_2; 6.
DR Pfam; PF00053; Laminin_EGF; 2.
DR Pfam; PF00054; Laminin_G_1; 2.
DR Pfam; PF02210; Laminin_G_2; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 8.
DR SMART; SM00179; EGF_CA; 4.
DR SMART; SM00180; EGF_Lam; 2.
DR SMART; SM00057; FIMAC; 2.
DR SMART; SM00274; FOLN; 8.
DR SMART; SM00280; KAZAL; 6.
DR SMART; SM00282; LamG; 3.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 6.
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; 6.
DR PROSITE; PS50025; LAM_G_DOMAIN; 3.
PE 4: Predicted;
KW Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Laminin EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00460};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 26..73
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 98..144
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 159..213
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 231..278
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 316..363
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 414..466
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 467..513
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 540..587
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 686..723
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 728..913
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 914..951
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 952..989
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 996..1177
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1173..1209
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1215..1386
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DISULFID 414..426
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 416..433
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 435..444
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 467..479
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 469..486
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 488..497
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 713..722
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 941..950
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 979..988
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1199..1208
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KOG00302.1"
SQ SEQUENCE 1386 AA; 153006 MW; 509B3511E2C09963 CRC64;
GTNPCANKCR KYERCNINRQ GVAECVCPTS CEPVLRPICG SDGVTYDNEC QLQKDACQNE
LPIILKQRGP CGVKQPCLNH HCNFHGVCVV REGRAECDCP TCSEEFDPVC GMNGISYTNE
CKLRLENCQK RSDVKVKHKG LCNGCENQRC EFYAVCQSDG KNAKCVCPSA CVEVENKVCG
TNRISYQNEC ELKVASCRDQ KLIEVESRGD CNKCAKIRCP FGSTCENGMC VCPSECPADF
EVLCASNGQV YNNECEMKRY ACLKKTELYI VNNGPCDEIS GSGIVEGSGS GSICDETSCK
FGGTCELSEG SNYHCTCKNI CDAIRSIVCG SDGKTYGNDC MMKLESCYQQ QEITAVASEN
CEDLEEEPCD GNMPLVNPLT GQEYYCYDDK NICPAGSYCH KRATFAKCCR EGSCQCNPLG
SYGTSCDPHT RQCVCKPGVG GLRCDRCKPG NWGLLSIVKG SAGCIPCNCN RYGSVRDDCE
QNSGRCMCKN GITGMKCNVC PNRMQLGPQG CTEIPPKSCQ YLHCKYGAVC KRIDNQHQCV
CNINCSGYPD LVCGSDNQTY GSECQLKQFS CRLQQPISIE HKGICSFSTE SRMVTSPTPT
TRSRKTTRHI NHVSNEVTKI ILTKATERPP EVVGRIDDLC PSESDCDVPN SRCVLGICVC
KTGFIQTMDK KNCLEVVSVP PPSPTSNTTC TLNPCQNGGT CLMDKTLGYR CLCPLGTGGS
ICKDVVSFTV PSFSGTSYLR MPQIKNATTE MRIEVEFKSL NKDGIILFNS KEEDGSGDFV
SLTLNQGFVE LRYDLGNGLA IIRSAKPIRL NKYHHVIARR IGQDGFLQVD GQSNTAESSS
PGDLTSLNLE SPLYLGHIQN FTSLVKSRID VEVGLVGCIR KVIAGKRQSP YTYRLAYPDE
LSDVIDGVDI AECGNNPCSS MPCKNGGNCL MLDNVMVQCI CQEGFIGKYC ENEDMCINNP
CQGGGTCTPT DHGSYVCICP EDRKGRNCQE EVLQRLDVPE FNGTSYVELP LNDSDLLDTM
TIAVWFKTTK PDGMLFYASQ YSGGEGDFIA LNLENYYVEF SFNLGGGTTK VRSSQRISLD
SWHNVVIKRH HRTIEMIIDN EKSADGKSDG VVTKLNLAQR IFIGGFRDIF DVPSDTNIEK
GLNGAIQRVY INDKLYDNLI TDAIETKGVT KYKGPPCKKN PCLNGGICVP KLHIAECRCH
KQFTGHKCQN AIETKSQLKF EGDTFLAYLN GLDHKKTSQQ ANKFRLRFKS KKRSGLLFIM
NQGNTVRQDY FAVALVKGKM QLSYNLGAQT EENLHIIRST LKIKNNEWHV IEVERNQEEG
ILRVDDAVPV KRSSLSGATK LDTDGELWIG GKKNLPMGLP KDYYVGFEGC MDFVEVDDQR
LNLDFF
//
