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Database: UniProt
Entry: A0A368HF01_ANCCA
LinkDB: A0A368HF01_ANCCA
Original site: A0A368HF01_ANCCA 
ID   A0A368HF01_ANCCA        Unreviewed;       530 AA.
AC   A0A368HF01;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=EGF-like domain protein {ECO:0000313|EMBL:RCN53795.1};
GN   ORFNames=ANCCAN_00289 {ECO:0000313|EMBL:RCN53795.1};
OS   Ancylostoma caninum (Dog hookworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=29170 {ECO:0000313|EMBL:RCN53795.1, ECO:0000313|Proteomes:UP000252519};
RN   [1] {ECO:0000313|EMBL:RCN53795.1, ECO:0000313|Proteomes:UP000252519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Baltimore {ECO:0000313|EMBL:RCN53795.1,
RC   ECO:0000313|Proteomes:UP000252519};
RA   Mitreva M.;
RT   "Draft genome of the hookworm Ancylostoma caninum.";
RL   Submitted (OCT-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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RCN53795.1}.
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DR   EMBL; JOJR01000001; RCN53795.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A368HF01; -.
DR   STRING; 29170.A0A368HF01; -.
DR   Proteomes; UP000252519; Unassembled WGS sequence.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProt.
DR   CDD; cd00054; EGF_CA; 4.
DR   CDD; cd00110; LamG; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 2.10.25.10; Laminin; 6.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000483; Cys-rich_flank_reg_C.
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; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   PANTHER; PTHR45836:SF4; PROTEIN SLIT; 1.
DR   PANTHER; PTHR45836; SLIT HOMOLOG; 1.
DR   Pfam; PF00008; EGF; 5.
DR   Pfam; PF02210; Laminin_G_2; 1.
DR   Pfam; PF13855; LRR_8; 1.
DR   SMART; SM00181; EGF; 6.
DR   SMART; SM00179; EGF_CA; 5.
DR   SMART; SM00282; LamG; 1.
DR   SMART; SM00369; LRR_TYP; 2.
DR   SMART; SM00082; LRRCT; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 6.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 2.
DR   PROSITE; PS00022; EGF_1; 6.
DR   PROSITE; PS01186; EGF_2; 5.
DR   PROSITE; PS50026; EGF_3; 6.
DR   PROSITE; PS01187; EGF_CA; 2.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 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}; Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Reference proteome {ECO:0000313|Proteomes:UP000252519};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          141..176
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          178..215
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          217..253
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          255..293
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          295..331
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          342..379
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          382..530
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DISULFID        166..175
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        205..214
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        243..252
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        283..292
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        321..330
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        346..356
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        369..378
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   530 AA;  58612 MW;  A5985295C2976D32 CRC64;
     MFRDMSHNRV ESIEDGTFAN LTKLSTLILS YNKLRCLQPR SFAGLHSLRI LSLHGNDISL
     LPETAFESLG NITHIAVGSN SLYCDCRMEW FSRWIKSKFV EAGIARCVAP ANVANQLLLT
     ARSHQFQCGG VVPASVSAKC DACVTAPCKN GARCETTSGR DYRCHCAAGF HGKDCENEID
     ACYGHPCLNN AVCKVIQEGR FTCVCPKGFR GDYCEVNIDD CEKNKCQNGA RCIDLVNSYR
     CECGPMFRGK YCEEKLEYCS KRLNPCENGA KCHRMGSDYK CECLPGFTGR NCSTNIDDCG
     DHQCINGGIC VDGITTYSCQ CVMGFSGQFC EIPPMGNALY PNTAQCHSLL CGHGSCYTNE
     DMSEYECRCH EGYAGDKCDK IRSIGLHHPS AYVALEPWAV ESGNLSFAIR TSNESGLIAY
     YGDDSFISVE LYDGRIKIAF YIGNYPASHM YSYVTVNDGL AHRIEILVQG KKCSLSIDNQ
     TLQSIENDGK LENFSIDTKQ YLYIGGLPAD RAARVKSMFH VKESHSFKGN
//
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