ID A0A087VXK8_ECHMU Unreviewed; 1680 AA.
AC A0A087VXK8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Agrin {ECO:0000313|EMBL:CDI96886.1};
GN ORFNames=EmuJ_000061400 {ECO:0000313|EMBL:CDI96886.1};
OS Echinococcus multilocularis (Fox tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus.
OX NCBI_TaxID=6211 {ECO:0000313|EMBL:CDI96886.1};
RN [1] {ECO:0000313|EMBL:CDI96886.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23485966; DOI=10.1038/nature12031;
RA Tsai I.J., Zarowiecki M., Holroyd N., Garciarrubio A., Sanchez-Flores A.,
RA Brooks K.L., Tracey A., Bobes R.J., Fragoso G., Sciutto E., Aslett M.,
RA Beasley H., Bennett H.M., Cai J., Camicia F., Clark R., Cucher M.,
RA De Silva N., Day T.A., Deplazes P., Estrada K., Fernandez C., Holland P.W.,
RA Hou J., Hu S., Huckvale T., Hung S.S., Kamenetzky L., Keane J.A., Kiss F.,
RA Koziol U., Lambert O., Liu K., Luo X., Luo Y., Macchiaroli N., Nichol S.,
RA Paps J., Parkinson J., Pouchkina-Stantcheva N., Riddiford N., Rosenzvit M.,
RA Salinas G., Wasmuth J.D., Zamanian M., Zheng Y., Cai X., Soberon X.,
RA Olson P.D., Laclette J.P., Brehm K., Berriman M., Garciarrubio A.,
RA Bobes R.J., Fragoso G., Sanchez-Flores A., Estrada K., Cevallos M.A.,
RA Morett E., Gonzalez V., Portillo T., Ochoa-Leyva A., Jose M.V., Sciutto E.,
RA Landa A., Jimenez L., Valdes V., Carrero J.C., Larralde C.,
RA Morales-Montor J., Limon-Lason J., Soberon X., Laclette J.P.;
RT "The genomes of four tapeworm species reveal adaptations to parasitism.";
RL Nature 496:57-63(2013).
RN [2] {ECO:0000313|EMBL:CDI96886.1}
RP NUCLEOTIDE SEQUENCE.
RA Zhang Y., Guo Z.;
RL Submitted (NOV-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; LN902843; CDI96886.1; -; Genomic_DNA.
DR STRING; 6211.A0A087VXK8; -.
DR eggNOG; KOG3509; Eukaryota.
DR OMA; ANDEWHK; -.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; 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; 2.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 3.30.60.30; -; 7.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
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; PTHR10913:SF82; -; 1.
DR PANTHER; PTHR10913; FOLLISTATIN-RELATED; 1.
DR Pfam; PF07648; Kazal_2; 7.
DR Pfam; PF00053; Laminin_EGF; 2.
DR Pfam; PF02210; Laminin_G_2; 2.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00180; EGF_Lam; 2.
DR SMART; SM00280; KAZAL; 7.
DR SMART; SM00282; LamG; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 7.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
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; 2.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Laminin EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00460};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1680
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001831601"
FT DOMAIN 267..322
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 374..424
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 455..502
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 536..592
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 599..662
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 679..726
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 752..799
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 800..847
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1090..1129
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1133..1363
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1488..1679
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 231..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 752..764
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 772..781
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 822..831
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1100..1117
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1119..1128
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1652..1679
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ SEQUENCE 1680 AA; 184998 MW; 2A327790445E1FA5 CRC64;
MLRIHSLLLA LLLLPLLNAS SDRNPRCFVE YADPRNTTFN GTAEFLTESY SDGVKVVIKV
EGILSDPTKA LRLRSSPIEG YLSSANCVSS VLIGKPQIWL GSHKFDGVKL KFIVQVVRHL
DSLEEDLCLQ KQCHPGAICE TWNDIALSKV TVCVCLSLYD LATSGRCQLT TGEVCASDGN
IYANTCHMLR TSCLQQTELS IVSWAAVNQK DCQQQAKSVR LRHFRPRSKE HYKAATHTSH
LTFEDEQQGE KPQQDSVHPN KREPIVPTKT PDCVHTCSLT TVQPVCGSDG NTYLNPCLLE
LRGCISLQPA ELHAVHWGYC PARPPEIEPI FCDHANYCQF GAICASNTQL PSAYNHDTFS
LMRRQAGIQS SICTCDHYRC SEKWYKEPIC GDDGVTYPGD CFLNQAACIQ QSPKHKLHNG
SCKTSNQGMN PCLEQSCPWP GEECRVDIQG RKMCVCPERC PAIVIPVCGS DGITYDSVCH
LLQMACLKKK HIWVIHAGQC LLPGNVCERQ GLYCRRYEIC SQQNNQVNRD MSLTYAAPSL
KCSCPICPES GLGGKVCGSD GKTYRSECHL RAAACQGESF ELEIKQRGAC DACQNKKCEF
YSMCQTDDAG RAFCACPTNC LMVNMPVCGS DGRTYNNECL LKVHACSIQK HIWVIDTKPC
ATCSKPCPLG MRCLGGQCVC RESCPKPSLA GEVCGTDGRI YPSACELRRQ ACVNKVTVKV
DGSGLACRKP TYTSNASTSI DIQADQVLEN VCGCNKVGSR DQFCDSKGRC RCHWGVEGTK
CDQCASGYWG ISNGKPCISC SCNPSGSIAV NTCDSYSGQC KCKPGIRGQQ CNICPNGELL
TGEYCKEPLS KMSAVKPEIR KAEEGALVSG INFTPLATAF ISFTQLISPP FTFTLKFTPS
PGVSDGDIAL LVIPRADKVG QYSFLKLGIS SGNLELSYVS KLGIGKTRYI MGKQKLEPRL
IKVSVEVTND EDLSLYVANS TSFGVYKGAT SRLIRSDEYG VMTSNRGMGL VLGCISPNRA
LVSRCGFSGC LTEAELVYYP TIGQVQRHVF VTDGKATGLN WKHLPRDGIR VCLSQVSGQE
VPKNLLSSEA LINCDLLNPC KNGGQCISMT DGSFKKCVCL PGWQGNYCQL EAAIIPEFSG
KAFIRLAGPT GAESLKKRKM SMEIIFLRKP YEGIIFAIPP SQTGSEFIVI RADSDECLKV
YLRVGRIVQF SHSYFYNWLL KRFGPRQRLA IAKICSVAND EWHKLSIEKT SHYMTVQLDD
KKSTRLRLLP QRLPKTNREL RKALTSFDLS NSPVYLGGIP DKESHFLDDF VLLKQSFVGA
IQKVVLNGAE LVLAGPSQNK EGFLREQGVE HWEGTVQWQG PPCGENYSLC AKDSKSLKRI
CRPLGSGYEC SCSTPLTHMS FVRHLTASLH GIDLLNNETA QQEISAKAEE MACDEVATRN
GMASNELQHD VPSKGSEIAV PFNRIRREEV DSVQSRVGQS NGNVVLDRNS VLLSGRTVIN
YRGFIEKENI LDNIRIQLKT ETPDGLIMMI PERGHHFEEF IAISLSNGRP EAYLSLKSSD
HSSLLKRDST YPDGRRVTTL KAAPFVANGE WHTIQLIRNK GYMSLIVDDQ MVSGELTDTD
GILNNEGDIW LGGSLEQVTT LPWQYQQNFT GCISALFFNE VSIGLLGDAD LLYGTVSACS
//
