ID A0A2T7NUU6_POMCA Unreviewed; 935 AA.
AC A0A2T7NUU6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=EGF-like domain-containing protein {ECO:0000259|PROSITE:PS50026};
GN ORFNames=C0Q70_15418 {ECO:0000313|EMBL:PVD24924.1};
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:PVD24924.1, ECO:0000313|Proteomes:UP000245119};
RN [1] {ECO:0000313|EMBL:PVD24924.1, ECO:0000313|Proteomes:UP000245119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD24924.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PVD24924.1};
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:PVD24924.1}.
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DR EMBL; PZQS01000009; PVD24924.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7NUU6; -.
DR STRING; 400727.A0A2T7NUU6; -.
DR EnsemblMetazoa; XM_025252179.1; XP_025107964.1; LOC112572477.
DR EnsemblMetazoa; XM_025252343.1; XP_025108128.1; LOC112572600.
DR Proteomes; UP000245119; Miscellaneous, Linkage group lg9.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007154; P:cell communication; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 6.
DR Gene3D; 2.10.25.140; -; 1.
DR Gene3D; 2.60.40.3510; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 8.
DR InterPro; IPR001774; DSL.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR PANTHER; PTHR24044:SF420; NEUROGENIC LOCUS PROTEIN DELTA; 1.
DR PANTHER; PTHR24044; NOTCH LIGAND FAMILY MEMBER; 1.
DR Pfam; PF00008; EGF; 4.
DR SMART; SM00051; DSL; 1.
DR SMART; SM00181; EGF; 8.
DR SMART; SM00179; EGF_CA; 8.
DR SUPFAM; SSF57196; EGF/Laminin; 8.
DR PROSITE; PS00022; EGF_1; 8.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 8.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000245119};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..935
FT /note="EGF-like domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015594747"
FT TRANSMEM 646..672
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 312..348
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 350..387
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 389..426
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 428..465
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 467..504
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 506..543
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 545..582
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 584..621
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 707..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 865..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..903
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 338..347
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 377..386
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 416..425
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 455..464
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 494..503
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 533..542
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 572..581
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 611..620
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 935 AA; 101795 MW; 4A97B079A6C06CA0 CRC64;
MDRKVHSAST ATLATLLVIV FGLACFQVVE GKGVVQVKAM SYSSSCSDNG FLRTQCDTFF
QFCLKKPQSP SDSLNRCDYG SYGPTSEYED QNNIDFSQAV TFAGGIANPM EFQVERFEGS
ELKLVIRVMD DEFWNPDEHL AWLTKVLSHT PAVSQQASQW SSIFTVSSGS YSFRFKFRSF
CATNFYSPSC DVYCVAQDND SGHYTCNQAT GAKAGQARDA ARTWMSALKG SVVTALPAPT
YPVPTRVHAR SILAGRTVSR YPPCATADRV NTEEAAQGFR VFHLRLPARL DRRQVPDNDA
MPQVEPGETV RRVDFCQSSP CLHGSTCNAH FGGYSCNCTK GWTGNRCEVE VDDCASAPCL
NGGTCDKKAG GGYSCRCHPD YGGTNCENFL DPCLSSPCLN SGTCVRLTPT DFKCNCSSDF
RGPTCTQYVD LCDSSPCQNA GTCTRLAHDA FRCTCTVDYV GPTCEEYIDP CVSRPCLNGA
SCVRVDYDNY TCVCRADYTG DLCDEYIDPC LSRPCLNSGT CARKTFDEFG CNCTDDFTGT
VCDEYVDPCT SNPCHHSGTC VRLAYDDFRC HCTDEYEGVV CEEYTNPCSI NPCLNSGLCE
PLNPKGYKCI CGKNFEGTNC SELTVPRTAR RTDGDTASKG GKVKDVLLPV GLGVSIGLLV
AAAIFALMFV MLRRKRDLIW CRGQDPEPSL NRRGTAMASA EREYPLSAKR NCSRRPRRPR
GPRGSRQKTL YEADNRPVPA VIVEPVPVIP GTIFNVFGYS LSAFGGCGCT TSCVMSYLGY
GPAAPCLHGT RTDSATNTED SESDTADSDS LVEIEDTTIS PSPNKYLFTP PAPPTSRLQG
RRGRRYRHVP HTPDIFRELK GIKAIGQRGP TPNIPTSPGA TTAPVCNNSK PPALNTSNDN
SSRRVQLLPG VSSAPVSVVH VAPSVHPEWA HPLNI
//
