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Database: UniProt
Entry: A0A2T7PUH8_POMCA
LinkDB: A0A2T7PUH8_POMCA
Original site: A0A2T7PUH8_POMCA 
ID   A0A2T7PUH8_POMCA        Unreviewed;      1493 AA.
AC   A0A2T7PUH8;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=EGF-like domain-containing protein {ECO:0000259|PROSITE:PS50026};
GN   ORFNames=C0Q70_04043 {ECO:0000313|EMBL:PVD37050.1};
OS   Pomacea canaliculata (Golden apple snail).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Architaenioglossa; Ampullarioidea; Ampullariidae; Pomacea.
OX   NCBI_TaxID=400727 {ECO:0000313|EMBL:PVD37050.1, ECO:0000313|Proteomes:UP000245119};
RN   [1] {ECO:0000313|EMBL:PVD37050.1, ECO:0000313|Proteomes:UP000245119}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD37050.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:PVD37050.1};
RA   Liu C., Liu B., Ren Y., Zhang Y., Wang H., Li S., Jiang F., Yin L.,
RA   Zhang G., Qian W., Fan W.;
RT   "The genome of golden apple snail Pomacea canaliculata provides insight
RT   into stress tolerance and invasive adaptation.";
RL   Submitted (APR-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}.
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:PVD37050.1}.
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DR   EMBL; PZQS01000002; PVD37050.1; -; Genomic_DNA.
DR   STRING; 400727.A0A2T7PUH8; -.
DR   Proteomes; UP000245119; Miscellaneous, Linkage group lg2.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR   Gene3D; 2.10.25.10; Laminin; 10.
DR   Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 8.
DR   InterPro; IPR026823; cEGF.
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; IPR013111; EGF_extracell.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
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; PF12662; cEGF; 1.
DR   Pfam; PF07974; EGF_2; 1.
DR   Pfam; PF14670; FXa_inhibition; 6.
DR   Pfam; PF00053; Laminin_EGF; 5.
DR   PRINTS; PR00011; EGFLAMININ.
DR   SMART; SM00181; EGF; 31.
DR   SMART; SM00179; EGF_CA; 8.
DR   SMART; SM00180; EGF_Lam; 21.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 3.
DR   PROSITE; PS00010; ASX_HYDROXYL; 3.
DR   PROSITE; PS00022; EGF_1; 15.
DR   PROSITE; PS01186; EGF_2; 7.
DR   PROSITE; PS50026; EGF_3; 11.
DR   PROSITE; PS01187; EGF_CA; 4.
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}; Reference proteome {ECO:0000313|Proteomes:UP000245119};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..1493
FT                   /note="EGF-like domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015626413"
FT   DOMAIN          50..85
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          128..168
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          252..292
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          380..420
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          480..511
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          524..556
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          745..775
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          783..818
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          960..990
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1371..1401
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1451..1486
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DISULFID        75..84
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        501..510
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        527..537
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        546..555
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        765..774
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        808..817
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        980..989
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1391..1400
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1476..1485
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   1493 AA;  160367 MW;  5B4D88D0914E2725 CRC64;
     MLLLFLLEVF NCFTWRLQQS SMPPMSGNPP CDDQREGSHL TGPWQCLCGG RGQCNNAMCH
     NGGQCRGGYY PSCACPPGFQ GPQCQYDVNE CSNNNGGCER DCQNTVGSYK CRCSTGFELA
     EDMKACVDVD ECVDHNGGCQ HKCVNTYGGF HCECPKGQRL HADGRTCISV SGCSVSNGGC
     EHVCVDGYNG HYHCRCRSGY TLGDNGKTCH EADPCRENNG GCEHKCVNDR GRAICQCFSG
     FSLSADGRSC QDINECEQQN GMCLQTCINT KGSFVCTCTP GYQLGVDGRS CYRIEMEVVD
     FCAIGNGGCD HKCQHSREGP ICSCRRGYSL MADGKACRDI NECEEGEKCC SDYCNNNPGG
     YTCSCRQGFL LSRDGCTCDD IDECLGNNGG CEQICVNSQG SFSCVCNQGY TLSIDGQRCL
     PMESRLTDRG PQRGDLPKIR FETTPRPIIP ATDHNILSQE LLETESKYTC IPGTFGPDCG
     YMCTNCQNGA QCTEARDGCV CPAGWQGTLC DQPCSEGTFG EGCNRMCTRR CQNGGSCHPV
     TGRCKCPPGV KGENCEDGCP PGYYGEACDK LCLHQCSSGY CNRIFGICEC RLGWFGPSCN
     LPCPPFTYGS NCMEQCNCVT KNSKGCNSET GECQCKIGYH GDRCEDECPE GRYGDGCQHR
     CSCPVGTKCD PMSGYCLRDC PAGWTGSRCN EPCPHGKHGK NCKLSCRCHG NACDPETGKC
     VCEPGRMGKR CRRTCPEGSW GINCKNKCTC ENGATCDTVT GECLCRDGWY GPHCREECPE
     GRYGPQCLMR CMCENNASCN PADGRCTCKA GWTGQICDRA CPPGMYGENC VLRCNCLNSA
     ECDPVTGECL CAPGWRGTSC AQPCQDEMYG PGCSRKCRCQ NGAECDHISG ACTCAAGWRS
     IYCEKACPEG FYGIECQSIC NCGTGSTCDH VTGKCACPAG YMGILCDQRC PPGTWGQDCR
     RDCECDNDAN CEAISGQCIC PPGFRGARCE EPCPHGTYGQ NCLYRCFCMH DSTCNHIDGT
     CNCTNGWMGD ACERGCASGR WGPNCAMECE CVHAMSCDST NGQCYCDVGY TGLRCNRTCP
     VGSYGKDCKE TCMCANDAEC DHKSGKCTCK DGWVGDRCER ACSFGLYGKD CKDRCNCTLG
     DPCYHVTGQC SCPAGLTGSA CEESGFQLDS SVNLVNSDPE GCSEGSYGPN CDRVCNCENE
     GTCDVSTGNC VCPDGFVGPT CGQRCPENRY GENCTGICTC QNGARCNKGR ASASVSLATQ
     EKPAKTVRDG EGGWACPDGT FGLNCEEKCQ CSHGNCDHVT GACSCHLGWT GKTCSEGCPP
     ERFGPDCAHS CMCKNNGSCD SASGCCSCTP GFYGQVCEIE CPEGTHGTYC TDRCDCVNGA
     KCDPRTGQCK CPTGLTGDRC EKSCPKGRYG MNCRQECSCG ETDCDSVSGE CLCQPGFTGD
     HCMKACPEGR FGPNCEYQCN CDNNGLCDPQ SGTCLCPEGW VGARCQTAES EWL
//
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