ID A0A2T7PYB8_POMCA Unreviewed; 2623 AA.
AC A0A2T7PYB8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PVD38422.1};
GN ORFNames=C0Q70_01037 {ECO:0000313|EMBL:PVD38422.1};
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:PVD38422.1, ECO:0000313|Proteomes:UP000245119};
RN [1] {ECO:0000313|EMBL:PVD38422.1, ECO:0000313|Proteomes:UP000245119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD38422.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PVD38422.1};
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:PVD38422.1}.
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DR EMBL; PZQS01000001; PVD38422.1; -; Genomic_DNA.
DR STRING; 400727.A0A2T7PYB8; -.
DR Proteomes; UP000245119; Miscellaneous, Linkage group lg1.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProt.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd00033; CCP; 5.
DR CDD; cd00041; CUB; 1.
DR CDD; cd00054; EGF_CA; 9.
DR CDD; cd00112; LDLa; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 7.
DR Gene3D; 2.10.25.10; Laminin; 10.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 3.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR003410; HYR_dom.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR InterPro; IPR007527; Znf_SWIM.
DR PANTHER; PTHR45836:SF13; NEUROGENIC LOCUS NOTCH HOMOLOG PROTEIN 1; 1.
DR PANTHER; PTHR45836; SLIT HOMOLOG; 1.
DR Pfam; PF00008; EGF; 4.
DR Pfam; PF07645; EGF_CA; 2.
DR Pfam; PF12661; hEGF; 3.
DR Pfam; PF00057; Ldl_recept_a; 1.
DR Pfam; PF00084; Sushi; 5.
DR SMART; SM00032; CCP; 7.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00181; EGF; 16.
DR SMART; SM00179; EGF_CA; 10.
DR SMART; SM01411; Ephrin_rec_like; 3.
DR SMART; SM00192; LDLa; 1.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 6.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 3.
DR SUPFAM; SSF57184; Growth factor receptor domain; 4.
DR SUPFAM; SSF57424; LDL receptor-like module; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 5.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS00022; EGF_1; 10.
DR PROSITE; PS01186; EGF_2; 10.
DR PROSITE; PS50026; EGF_3; 13.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS50825; HYR; 1.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 1.
DR PROSITE; PS50923; SUSHI; 7.
DR PROSITE; PS50966; ZF_SWIM; 1.
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}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00325};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000245119};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Sushi {ECO:0000256|PROSITE-ProRule:PRU00302};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00325};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00325}.
FT DOMAIN 210..315
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 426..541
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 540..605
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 606..664
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 665..730
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 731..790
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 790..829
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 830..869
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 898..957
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 1023..1087
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 1088..1148
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 1147..1228
FT /note="HYR"
FT /evidence="ECO:0000259|PROSITE:PS50825"
FT DOMAIN 1645..1684
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1686..1722
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1725..1763
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1765..1802
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1804..1842
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1887..1925
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1927..1962
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1964..2001
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1974..2023
FT /note="SWIM-type"
FT /evidence="ECO:0000259|PROSITE:PS50966"
FT DOMAIN 2003..2041
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2043..2079
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2081..2118
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 94..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 191..206
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 928..955
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 1674..1683
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1712..1721
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1792..1801
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1832..1841
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1915..1924
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1931..1941
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1952..1961
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1972..1989
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1991..2000
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2012..2029
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2031..2040
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2069..2078
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2108..2117
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 2623 AA; 282536 MW; D1DD69892946142F CRC64;
MYSVVSTVHQ RDTLVVYEEN AGANSNCAGL KKNHPIVPLG NGAALNLEKK NLCVKCSGSK
LRTWLPGRRL EVNARRRDRN VCVELILKQV NKGAQDDGRT DSDKKNRNNG SSSHSCVLDD
SKPCNFELED KGAGLLPHSD DASNIHVCSG HVLKPVYLLK CQAQYDKAKV CFPGTFRCMD
GSQCLNNAWK CDGLYDCPDQ SDEADCAASC TSYIQKPSGS LNVTYEANRP CTWVIEGVVG
QTLSVTFHTV DLECDVDFIE VWSGGPTIET STQKALFTGS VRDRIVYGDN NFLIIRLISD
NSVEGPGFTA TWQTDPELSS EERMVEATDS WTEVTSPHYH NSQRPSVYFR LFTVNTTDGS
HITMEIMDNQ LMVNDFVYNP QELSSIVSSS NSSPLVFVSL GSSFTFQISS KGNSTRAFRA
RVKRGCSPDL TLTSGVIESP GPTPTGPYPS SLTCTYTIRA PRDHPRGFMI SFVSFKMADD
KDEIMVYNVT DSVSNQMYTN SRYTLSSQLP QHLYSGSVFV IQFTSSLAQS DGYFALNFSR
DCPAVADATN MTLSTTLSHA FTFVSISCNQ GYSFAQEEFV SSIMVSLTCS QDGNWDKPRM
PTCRQTYCGV PQTIANGEIY SGSGNARYGA IVQYRCFPGF RVNGSSTSTC QENGQWTLPP
ECLSATCPPP PTIVNGNLTF ITGNSSSSAD RQYFGAIVMY TCHPGYDLIG SMYSLCYSAI
WSMPPPVCQA IKCPVPEVDR ATLSTQSPVE LGESLIITCN PGYTNNGTDS FQSTCTSSGM
FEVPRNVCQD KNECETVGIC GAHQTCHNTD GNFTCVCEKG FTLTSGKCED IDECANNTSG
CDVTNGYCNN TSGGFTCVCN SGYTMYTQNG TTGKNIPLPE DGLRQGDVYY INHTCVPVTC
PSLPSIPHGT LLSASTSYFY NETAGYRCDR GYTLTGSAVV TCQSNGQWSA LPPTCNPRYC
AALSPTGIVS AVIPPNPTVI GDKVTLVCRS QVGPEYNKTL YCAYDPLTDN MTLQGDSHNC
PAIDCGSPSL VATGGSVNVS TSSGLGESFE FSCEPGFVVT GESTLGNRTV RCGEDGRWGF
GTLYCEDQRC TDPGTPVGMD MTSASFDVNG TVTYTCLRPG YVARPDVRTC VYENDQVTWD
GSTPVCVDIE RPVFSNCPSE VIYRNIYTSA AFPMPSATDN SGLVLPLKVS PPGFRLDMPL
SQSFNVNFTA SDVTGNTATC QVAIIVRDTV SPDLTCPDYL QFNVNSNTSY TVDLQTEGNI
TGANLTFYPD RVVQVGPTTV GVAPYHVTTI DGYGFERQCA FIVDIRPTAC LSDYLTPGGA
TKQCTSQAGG SLTCTVTCGA GMAFQDGSTT KTYSCSGQNE WSPTLPARSC TPTVVPRYIY
MVAINYTWDG TGSISSCLNQ SAEELVAAIP TRNAPCPIDG DPFSLITFNA SVFSLDNNAT
NLVLELTVTN LTSISSVDYD YCQSILSNLN STVAKAFFKI QTTSCVGQTV QCEPGYMENG
NQCIECPSGQ YQNQTGQTEC KTCAGNFSSS PRVSASQCVE SCPLGFANGQ GIVANRSPCY
ACPVDTYLNT SYTANCTACP SSSTTFGTRG ASSSAQCKAC PPGQYPVNST SCSPCPKGYY
KTSTGYTKCT ECPANTTTNT TGSSASTSCI SPTSPACGNG GIPVIYFHES GCTCPEGYYG
TTCENPINPC DSSPCYNNGI CTRQGVNYTC SCPSGFTGNQ CQVDSQNNCQ NNTCSDISFC
RDKINSADCV CPSGGNYTGP QCAVPQDLCS SSPCKNGATC QNFPAVRYTC QCQPGYTGST
CETLIDQCAL NSHGCLYGGQ CTNGINNYTC SCQQSYQGSH CQQTPDYCNL SNPCPGGVCY
NDYNMSKALC ACSYPYRLNV NSGRCEEIDV CSERRPCQNN ATCQSVSPGQ FHCACPQGYE
GSLCQHIVRS CTNSSCVHGQ CVDVLNNYTC VCDTGYTGRS CEINVNDCPG QCVMSNTLTC
IDGVNQYTCS CEAGFTGVHC ETNINECASL PCKHNGACVE SVTPGDYNCT CRDGWTGKNC
DTLPVFCRND SCQNGGVCYS LQDRLFCSCQ AGTHGNACNE TTNICSIVSP CVNPNQCQSR
NKTASCNCPQ NYIGGSCQLV KDFCIPNPCP TGQCVTTDVG YSCQCQAADN CTTTDHSCAS
LTCPSGSKCV ETASGPLCLC HPGYLLGGGV CKNTSSDFDI YFTRRSNTAV RALQPFTVTG
QALSLTFWIS FLDDSSSFPV RLISDRMDRV LLVSQSGVTF GGTFAVNFTE YNGSPQSLSA
EHKWTFCAIT WSVTGQYKIY IDSVDCQAQW NSQRLFPLLR KVVPWLHLTF VILEGAIAIY
ISQLLMADVS QTCVDSLLYP YIGEDFVGYI SQLNVWNGTL TSQAALALYA NSDAAPSSLA
PAYRWAEYQF NSWVKVISPS TVKRDKAMCQ MRNYGNECAN DTGTLLTFGA YHVVYASRDT
AGNVAMCRFN VYVQREGHVC NSGEADSGDS TLTSCAAQPS FWVRLTSGNV TYTVTELLKV
SAIEQDTFVI SFVANSVLIR DEVTVTTQTT CSQGYGRFGA GCVQCVAGSF LNSATNMCEQ
WQSAPTPTHL VRLNVTPCST ESDDALEWAS TSCVGQFDED KCQ
//
