ID A0A0N5CSC1_THECL Unreviewed; 560 AA.
AC A0A0N5CSC1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Multiple epidermal growth factor-like domains protein 10 {ECO:0000313|WBParaSite:TCLT_0000312201-mRNA-1};
GN ORFNames=TCLT_LOCUS3122 {ECO:0000313|EMBL:VDM99432.1};
OS Thelazia callipaeda (Oriental eyeworm) (Parasitic nematode).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Thelazioidea; Thelaziidae; Thelazia.
OX NCBI_TaxID=103827 {ECO:0000313|Proteomes:UP000046394, ECO:0000313|WBParaSite:TCLT_0000312201-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:TCLT_0000312201-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDM99432.1, ECO:0000313|Proteomes:UP000276776}
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; UYYF01001015; VDM99432.1; -; Genomic_DNA.
DR STRING; 103827.A0A0N5CSC1; -.
DR WBParaSite; TCLT_0000312201-mRNA-1; TCLT_0000312201-mRNA-1; TCLT_0000312201.
DR OMA; PWQTGEV; -.
DR Proteomes; UP000046394; Unplaced.
DR Proteomes; UP000276776; Unassembled WGS sequence.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 4.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR042635; MEGF10/SREC1/2-like.
DR PANTHER; PTHR24043:SF8; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24043; SCAVENGER RECEPTOR CLASS F; 1.
DR Pfam; PF07974; EGF_2; 1.
DR Pfam; PF12661; hEGF; 3.
DR Pfam; PF00053; Laminin_EGF; 4.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 13.
DR SMART; SM00180; EGF_Lam; 13.
DR PROSITE; PS00022; EGF_1; 11.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 7.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Reference proteome {ECO:0000313|Proteomes:UP000276776}.
FT DOMAIN 1..25
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 38..68
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 76..111
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 119..154
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 253..283
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 420..455
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 505..540
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 15..24
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 58..67
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 101..110
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 144..153
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 273..282
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 445..454
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 530..539
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 560 AA; 60391 MW; 6B121F527C0E59A6 CRC64;
MNGGKCDPKT GHCDCAAGFM GRHCEEECPP GFYGTNCNNY CLCMHNGTCD SKNGTCKCAA
GWSGPSCEFT CPFGRYGVNC QEKCDCEHGA RCSTTDGTCY CLAGFTGERC EERCPYGFYG
DKCQELCSCE NGASCDSVTG YCHCAPGWRG RKCNRPCLKG YYGEHCASAC QCPNQRACNH
ITGRCHCPKG YAGHYCTELC PLGKFGENCA QQCDCAPNAD CDPLTGKCFC KPGYAGLDCA
QGCIQGRYGM NCENICQCEN SGTCNSATGQ CACPPGFVGA KCEVPCPPNR YGQKCAELCQ
CENNGTCDRV TGQCHCEAGF VGIRCRQRCS EGRFGPGCRE KCRCANQAHC DPVTGDCRCS
LGYTGETCDL PCPEGKYGLN CTLDCECEGN AKCDPVQGCC DCPSGRFGTR CQYTCPPGFY
GWYCSQSCDC QNGALCDPYA GRCQCPPGYF GEKCEQLCTN NTFGLQCQLK CNCGEFRCDP
KTGLCDCPLG FSGANCKQAC RPGRYGKHCE QRCECYNGAV CDRVSGQCTC APGYLGATCQ
QEQLDMESVA RRGDLPEYDF
//
