ID A0A2T7PJ30_POMCA Unreviewed; 1464 AA.
AC A0A2T7PJ30;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=EGF-like domain-containing protein {ECO:0000259|PROSITE:PS01186};
GN ORFNames=C0Q70_04680 {ECO:0000313|EMBL:PVD33424.1};
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:PVD33424.1, ECO:0000313|Proteomes:UP000245119};
RN [1] {ECO:0000313|EMBL:PVD33424.1, ECO:0000313|Proteomes:UP000245119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD33424.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PVD33424.1};
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:PRU00124}.
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:PVD33424.1}.
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DR EMBL; PZQS01000003; PVD33424.1; -; Genomic_DNA.
DR STRING; 400727.A0A2T7PJ30; -.
DR Proteomes; UP000245119; Miscellaneous, Linkage group lg3.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd00112; LDLa; 2.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 2.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 5.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR000033; LDLR_classB_rpt.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR PANTHER; PTHR46513:SF13; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 4-LIKE PROTEIN; 1.
DR PANTHER; PTHR46513; VITELLOGENIN RECEPTOR-LIKE PROTEIN-RELATED-RELATED; 1.
DR Pfam; PF14670; FXa_inhibition; 4.
DR Pfam; PF00057; Ldl_recept_a; 2.
DR Pfam; PF00058; Ldl_recept_b; 7.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00192; LDLa; 2.
DR SMART; SM00135; LY; 17.
DR SUPFAM; SSF57196; EGF/Laminin; 3.
DR SUPFAM; SSF57424; LDL receptor-like module; 2.
DR SUPFAM; SSF63825; YWTD domain; 4.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50068; LDLRA_2; 2.
DR PROSITE; PS51120; LDLRB; 12.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000245119};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1220..1241
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 71..114
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 115..157
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 158..203
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 204..246
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 418..461
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 462..504
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 575..590
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS01186"
FT REPEAT 637..679
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 680..722
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 723..765
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 766..808
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 922..965
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 966..1008
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REGION 1256..1294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1309..1392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1416..1464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1272..1294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1310..1337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1344..1359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1360..1380
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1446..1464
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1120..1135
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1138..1150
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1145..1163
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1157..1172
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 1464 AA; 163312 MW; 9F5B6C238BC6DDA1 CRC64;
MHFSDANCEK KLCAKMFAVP TVVGKVGSPF LLFANRKDVR IIDATDPRPN SSVIISNLKD
AAAVDFIHSE GWIFWTDVSL EVIERTSINS SHTSVSVIST GIVSPDGLAC DWLGKKLYWT
DSETNRIEVS NLDGTFRKVL FWRRLDQPRA IALDPQNGYV YWTDWGEMPK IERAGMDGNQ
DSREIIVADN IFWPNGLTLD YEDSKIYWVD AKLHYIHSCD FDGSNRRAVV EGNLPHPFAL
TLFEETIYWT DWQTRSIHAC NKRTSAEMMV LHEDIFSPMD IHSFEAKRQP SGVNPCGNNN
GGCSHLCLMS PRPPFYSCAC PTGVRLLQDG KTCAQGAEKI LFLARRRDLR KISLDTLDYT
AVVLPLTDVR HAIAVDYDPV EDYVYWTDDE TRAIQRSRLD GSDQLDEPRA ICLDPQSGYM
YWSDWGKQPK IERANLDGTD RITLVDTNLG WPNGLAVDLS VGRLYWGDAK TDHIETSDLM
GGDRRILVSE NLPHIFGFTL IGDFIYWTDW QRRSIERVNK TTGLQREKII DQLPDLMGLK
AVDVHKREGT NPCASNNNGC SHLCLYRPPP KGPVCACPMG FELVSNGSTC IVPEAFLLFS
SQSNINRISL QTSHYNQPIP IQGVKQAVAI DFHFKENRIY VTDVSSKRIS RAFMNGSSLE
HIIEFGLNYA EGMAVDWVAN NIYWADTNKN RIEVARLDGS SRKVLIWRQL DNPRALALDP
PSGYMYWSMW GEEPQLVRAN LDGTQRRVLI TGQGRIQDLT IDYVDRRLYW ADIDQHNIQS
SDLLGGDKRL IVPSNLPHPM GITQYEDYIY WTDFDSKSIE RANKMTGKDR SLIQEGVDYA
LDISVIHASR QSGHNSCGSN NGGCSHLCLA HSVDHKDNRT HHCACPTHYH LNSDDKTCSV
GVVLQGPSNF KPRSLVLFPE RGYMFYTNMV KSPRIESARM DGSEKTELFI KGLVQPVSLT
IDKTEGKLYW VDAGKNRIEM SDLTGGNHRV LVDGHLVAPR GLAVHGQFLY WLDRDQQLLE
RCQKKTGAKR LWVRGRMQGL SDLIAVQHSL DVTSHPCAVG NGGCSHICMV DSDIKARCSC
PYNLVLKKDG LTCADPPTCP PDHFTCKSGG ITCIPLVWRC DNLSECEDSS DEQDCPICGP
TQFHCQSGEC VSKDNQCDGT ANCKDGSDER GCCAGVPCAS CESQGQGACA PGELRDCSEG
EAKCVHQPTV DKVHHNATHY AIAIVVGVIF LIVIIVVILF CRRKTRHVPF TDDDIQMAKK
PLNPQTSGEP PPPQSHTLSS RGGKTSASGG LSLGGTSLAS GLPPFYDRSH VTGASSSSST
GTQYPQETLN PPPSPVTERS VYTGGGHYCS SQSVGTVRSA RRQHKPHRSR HHHHHHHSHI
PPPPTTPCST DVCDDSEPYP AKRFRYYFNN SLVELSYDSD PYPPPPTPRR YFSDDVSCPP
SPSTERSYFN PYPPPPSPVG NSDC
//
