ID A0A2G5TYV9_9PELO Unreviewed; 1228 AA.
AC A0A2G5TYV9;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 13-SEP-2023, entry version 16.
DE RecName: Full=EGF-like domain-containing protein {ECO:0000259|PROSITE:PS50026};
GN Name=Cni-Y64G10A.7 {ECO:0000313|EMBL:PIC32116.1};
GN Synonyms=Cnig_chr_IV.g12573 {ECO:0000313|EMBL:PIC32116.1};
GN ORFNames=B9Z55_012573 {ECO:0000313|EMBL:PIC32116.1};
OS Caenorhabditis nigoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC32116.1, ECO:0000313|Proteomes:UP000230233};
RN [1] {ECO:0000313|Proteomes:UP000230233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT competition proteins.";
RL Submitted (OCT-2017) 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:PIC32116.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PDUG01000004; PIC32116.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5TYV9; -.
DR Proteomes; UP000230233; Chromosome iv.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR CDD; cd00055; EGF_Lam; 1.
DR Gene3D; 2.10.25.10; Laminin; 4.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 6.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR042635; MEGF10/SREC1/2-like.
DR PANTHER; PTHR24043; SCAVENGER RECEPTOR CLASS F; 1.
DR Pfam; PF14670; FXa_inhibition; 3.
DR Pfam; PF00053; Laminin_EGF; 6.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 21.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00180; EGF_Lam; 17.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR PROSITE; PS00022; EGF_1; 12.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 8.
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 Reference proteome {ECO:0000313|Proteomes:UP000230233}.
FT DOMAIN 155..195
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 424..459
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 472..502
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 558..588
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 649..684
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 955..990
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1083..1118
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1173..1203
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 166..183
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 185..194
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 449..458
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 492..501
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 578..587
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 674..683
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 980..989
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1108..1117
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1193..1202
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1228 AA; 131897 MW; 37348828A9FE3522 CRC64;
MQLDSGHVQC FCDEGYELID SKWCQDQNEC NNNNGDCDQI CVNLAGSHEC QCKPGFRLMM
DGRGCEDISE CSSNNGGCEQ ICSNQEGGYM CSCEPGFELS EDGHSCHDIN ECLINNGGCA
QLCKNRKGSR RCQCFAGYVL AHDEKSCVEC PNGFFGSTCQ LSCSDCQNGG KCSMRGAGLL
SKCDCPSGYT GEKCEQICPN GLWGVDCAHK CSCKLCDPTT GSCRCEDPER CSDGPCPDGY
YGSQCNLKCR MDCPNGKCDP IFGYCTCPDG LYGQNCEKSC PNFTFGKNCR FPCKCAREHS
EGCDEITGKC RCKPGYYGHH CKRMCSPGLY GPGCARKCSC SAGVRCDPVT GDCTKKCPAG
YQGNLCDQPC PAGYFGYDCD RKCQCDDVES PHRTKVCHHV TGTCTCLPGK TGPLCDQSCA
MNTYGPNCAH TCACVNGAKC DERDGSCHCT PGFYGATCSE VCPTGRFGID CMQLCKCQNG
AICDPKDGSC ECSPGWSGKK CDKACAPGTF GKDCSRKCDC ADGMHCDPSD GECICPPGKK
GHKCEETCEH GLFGAGCKGI CSCQNGGVCD SITGSCECRA GWRGKKCDRP CPDGRFGEGC
NAICDCTTSN DTSTYNPFVA RCDHVTGECR CPAGWTGPDC QTSCPLGRHG EGCRHSCQCS
NGASCDRVTG FCDCPSGFMG KNCESECPAG LWGSNCMKHC LCMHGGECNK ETGDCECVDG
WTGPSCEFCK SKCAHSANLG VTVHNDAIVK MERVVIGKPV DVNVYLAGVV NIVKSLVPVD
TMDRNAKRLV NVRMERFVIR SVDIAHANQD GGERSVIDLV SKATTVNTAL KVAVVRIASP
VTISQVVVNV PKDMQVTLAQ NSVPKAHTEK IVPINAIVVI TRFVMQFLEN ASANRDILDR
TAKVVVYKEG LVPIAINYAL VRMEGCVIHR VALVFARQDI LGPSVKLLVS RIDLDQRNCE
KICNCENGGT CDRLTGQCRC LPGFTGMTCN QVCPDGRYGA GCKEKCRCTN GHCNPTNGEC
KCNLGFTGPS CEQSCPSGKY GLNCTLDCEC HGQARCDPVQ GCCDCPPGRY GSRCQFACPN
GFYGWYCSQS CSCQNGAHCD GADGRCLCPA GFQGDKCEQK CTEGTFGPAC SQNCNCGKFK
CDSTNGKCIC PVGRHGPLCE EECRAGRYGE SCMNKCQCFN GASCDPKTGQ CTCSPGWLGP
TCQVEMLDPN NIANRGDLPE DWEWRKKR
//