ID A0A0C2D275_9BILA Unreviewed; 907 AA.
AC A0A0C2D275;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=EGF-like domain protein {ECO:0000313|EMBL:KIH56132.1};
GN ORFNames=ANCDUO_13691 {ECO:0000313|EMBL:KIH56132.1};
OS Ancylostoma duodenale.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=51022 {ECO:0000313|EMBL:KIH56132.1, ECO:0000313|Proteomes:UP000054047};
RN [1] {ECO:0000313|EMBL:KIH56132.1, ECO:0000313|Proteomes:UP000054047}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zhejiang {ECO:0000313|EMBL:KIH56132.1,
RC ECO:0000313|Proteomes:UP000054047};
RA Mitreva M.;
RT "Draft genome of the parsitic nematode Ancylostoma duodenale.";
RL Submitted (DEC-2013) 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; KN736217; KIH56132.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2D275; -.
DR Proteomes; UP000054047; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
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 InterPro; IPR001759; Pentraxin-related.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR PANTHER; PTHR24044:SF496; METALLOENDOPEPTIDASE; 1.
DR PANTHER; PTHR24044; NOTCH LIGAND FAMILY MEMBER; 1.
DR Pfam; PF00008; EGF; 6.
DR Pfam; PF12661; hEGF; 2.
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; 5.
DR SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 6.
DR PROSITE; PS00022; EGF_1; 10.
DR PROSITE; PS01186; EGF_2; 7.
DR PROSITE; PS50026; EGF_3; 10.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS50825; HYR; 1.
DR PROSITE; PS51828; PTX_2; 1.
DR PROSITE; PS50923; SUSHI; 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:UP000054047};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Sushi {ECO:0000256|PROSITE-ProRule:PRU00302}.
FT DOMAIN 16..52
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 54..89
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 91..127
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 129..165
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 167..205
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 207..243
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 245..281
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 283..319
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 321..358
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 360..396
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 618..698
FT /note="HYR"
FT /evidence="ECO:0000259|PROSITE:PS50825"
FT DOMAIN 699..769
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DISULFID 42..51
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 58..68
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 79..88
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 117..126
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 155..164
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 176..193
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 195..204
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 233..242
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 271..280
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 309..318
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 348..357
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 386..395
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 907 AA; 99995 MW; 1EBFBD5AC613D9A9 CRC64;
MEAFLNVKEI NRILDKDDDC ADSPCALNAT CVDLVNDYEC QCPKGFKGKR CNVKEDLCAA
APCVHGLCVD TLFARRCICD EGWTGENCEV NIDDCASQPC QNGGTCTDEV AGFSCSCPAG
YRGVHCQHLV DHCSTSPCRN NATCTNLGAS YHCACPLGFD GTHCEHNKDE CLLGRCDKKG
TESCEDGINS FICLCKPGYS GEFCEVRIDQ CESSPCMNNG TCYDEGGSFR CECANGWTGE
TCEQETGSCD ARPCRNDGRC VNLVADYFCV CPEGVSGKDC EIAPNRCLGE PCLNGGVCGD
FGSRQECSCP KKFAGAGCQY LQDACTDNVC QNGGACSRNS DGGFRCTCKP GFTGLHCETN
VDDCARSPCP LGATCVDQIN AAYCRCPFNM TGSNCDKTID EDYDLHFYDP LRPASASLAL
PFQIAAKAIT VAMWVKFDQA QSKGTVFTMY NSKQANYSSD LTEVLRVDSD GLNIALFPNE
SALQLHFPVN QRINDGSWNH LVFTWSSERG TYSLIWNSVR IFAESGYGAS HEININALIT
LGSSEVGVAS FAGSLTRVHV WSRVLDFDSE IPMMVVSCHG TETVYDGLLL RFTGYTDMQG
KVERVPRSMC GREKRRRRDE AVVHVKSCPP DQYIMTSQRE INVTWPEPEF VGDNPLQKVE
RNFKQGQVFT WGEYDVLYVA WDNSSNTAEC SFKIHVSREH CPSLEDPVNG VQACESWGPH
LRYKACSIEC RDGYEFSKSP AIFYTCAADG MWRPRNRNQM VFRYPQCTKS VPATRVMLLR
VSYPGSSPCS EASRDALRSR LLASIQTINQ KWDMCTLTDQ TGCVGARVDV DCSEDFARVK
REAHSFKVRI ELPVKRDLVS HAVSGQKSKV ADALQNEIIN QGAFNLEKVF LPVCVTVGDR
LSLNMML
//
