ID A0A0M3JX24_ANISI Unreviewed; 683 AA.
AC A0A0M3JX24;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Protein crumbs {ECO:0000313|WBParaSite:ASIM_0001287701-mRNA-1};
GN ORFNames=ASIM_LOCUS12343 {ECO:0000313|EMBL:VDK47141.1};
OS Anisakis simplex (Herring worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Anisakidae; Anisakis;
OC Anisakis simplex complex.
OX NCBI_TaxID=6269 {ECO:0000313|Proteomes:UP000036680, ECO:0000313|WBParaSite:ASIM_0001287701-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ASIM_0001287701-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDK47141.1, ECO:0000313|Proteomes:UP000267096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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; UYRR01031172; VDK47141.1; -; Genomic_DNA.
DR WBParaSite; ASIM_0001287701-mRNA-1; ASIM_0001287701-mRNA-1; ASIM_0001287701.
DR Proteomes; UP000036680; Unplaced.
DR Proteomes; UP000267096; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 8.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 10.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR003410; HYR_dom.
DR PANTHER; PTHR24033; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24033:SF151; PROTEIN EYES SHUT; 1.
DR Pfam; PF00008; EGF; 5.
DR Pfam; PF12661; hEGF; 4.
DR Pfam; PF02494; HYR; 1.
DR Pfam; PF13385; Laminin_G_3; 1.
DR PRINTS; PR00010; EGFBLOOD.
DR SMART; SM00181; EGF; 10.
DR SMART; SM00179; EGF_CA; 9.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 7.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 7.
DR PROSITE; PS00022; EGF_1; 10.
DR PROSITE; PS01186; EGF_2; 7.
DR PROSITE; PS50026; EGF_3; 10.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS50825; HYR; 1.
PE 4: Predicted;
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 Reference proteome {ECO:0000313|Proteomes:UP000267096};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 2..38
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 40..75
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 77..113
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 115..151
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 153..192
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 194..230
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 232..268
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 270..306
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 308..345
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 347..383
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 608..683
FT /note="HYR"
FT /evidence="ECO:0000259|PROSITE:PS50825"
FT DISULFID 28..37
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 44..54
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 65..74
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 103..112
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 141..150
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 163..180
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 182..191
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 220..229
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 258..267
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 296..305
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 335..344
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 373..382
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 683 AA; 75589 MW; 5AA01A370CDCBC0D CRC64;
MLTDDCADNP CALNATCTDL VNDFHCDCPP GFGGKRCHEK EDLCAHDPCV NGLCVDALYS
QKCICEPGWT GPVCDVNIDE CADRPCFNGA TCKDQVDGFL CQCAPGFHGS VCQHMMDHCA
TSPCRNNATC VNQGAQYHCE CPLGFEGTHC EHNINECDLL HKCSQEGTEL CEDLINGFKC
NCRQGYTGEL CEIHIDQCAS EPCMNNGTCI DGGAMFRCEC PRGWKGTRCE EDDGSCALDP
CHNDAHCVNL VADYFCVCPE GVNGKNCEIA PNRCIGEPCH NGGVCGDFGS RLECTCPKDY
VGPGCQFELN ACQEGACRND GRCIVTEHGG YKCICEPGFT GRNCETNIND CSPSPCPLAA
TCIDQVNNYF CQCPFNMTGV NCDKAIDVDY DLHFYDALMT ASAALSVPFK FDSNAFSISL
WVKFDMPLSH GTVLTLYNSK EPNYPAKLSQ LLHVSADNVH LNMFADETPL SLHFPSNQRL
NDGHWNNLVI TWKSDDGAYS LIWNAVRIYA DVGYGTHKHL DINAWISLGD PISDTSTDSK
FVGSVTRVNM WKRVIDFENE VPDIVQQCQQ SQEIYDGLVL RFAGYNRMSG KVERIVRSTC
GRERTDLRST STVHVDRCPS DVFVVTQQKE VNVTWQEPRF SSKYGIQNIE RNLKPGQMFT
WGEYLVVYVA KDNTSQADCV FKA
//
