ID A0A2T7PEB3_POMCA Unreviewed; 1821 AA.
AC A0A2T7PEB3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PVD31755.1};
GN ORFNames=C0Q70_07173 {ECO:0000313|EMBL:PVD31755.1};
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:PVD31755.1, ECO:0000313|Proteomes:UP000245119};
RN [1] {ECO:0000313|EMBL:PVD31755.1, ECO:0000313|Proteomes:UP000245119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD31755.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PVD31755.1};
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
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:PVD31755.1}.
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DR EMBL; PZQS01000004; PVD31755.1; -; Genomic_DNA.
DR STRING; 400727.A0A2T7PEB3; -.
DR Proteomes; UP000245119; Miscellaneous, Linkage group lg4.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07066; CRD_FZ; 3.
DR CDD; cd00112; LDLa; 8.
DR CDD; cd06263; MAM; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.60.120.200; -; 3.
DR Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 3.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 8.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR000998; MAM_dom.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR PANTHER; PTHR24252:SF7; HYALIN; 1.
DR Pfam; PF01392; Fz; 3.
DR Pfam; PF00057; Ldl_recept_a; 6.
DR Pfam; PF00629; MAM; 3.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00063; FRI; 2.
DR SMART; SM00192; LDLa; 8.
DR SMART; SM00137; MAM; 2.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR SUPFAM; SSF63501; Frizzled cysteine-rich domain; 3.
DR SUPFAM; SSF57424; LDL receptor-like module; 8.
DR SUPFAM; SSF56487; SRCR-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50038; FZ; 3.
DR PROSITE; PS01209; LDLRA_1; 4.
DR PROSITE; PS50068; LDLRA_2; 8.
DR PROSITE; PS50060; MAM_2; 3.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Protease {ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000245119};
KW Serine protease {ECO:0000256|RuleBase:RU363034}.
FT DOMAIN 320..423
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 436..583
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 575..709
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 939..1174
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 1212..1360
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 1406..1566
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 1647..1815
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 441..502
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 449..495
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 486..524
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 694..706
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 713..728
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 738..756
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 750..765
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 768..780
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 775..793
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 787..802
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 805..817
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 812..830
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 824..839
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1386..1401
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1589..1604
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1606..1618
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1613..1631
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 1821 AA; 200861 MW; 7AEBD1395C448847 CRC64;
MADSVSWQGE GESFRKRYST STEPRTPTPS SPNGHVGGVG RVPSLPESGE ADDVFVDEKL
KAESEAESSP IHQTSTSYLT STMETPIITY GGNLLLISQW PGTREQLETS LSQDFISIVN
NSQLEAFYLG LSVEDFQPET QNVTFQLDFR QNVTELTAQE PVQHLKVFLQ QEIYHLLRNG
QTVIGIIPES FVLYDIPQLS STSAPPWTTV TSRHLTSTSS STVSSSSIAV SLPLSSPTSS
TPSASSVSAA VTAAASSTPS TSSAAPSTSS ASTTASVTSS SSSSEFVSSS EKSLMSSTKI
QTTTQTATSQ TSTATVPEEC LELTFDPCLD LGYSHFSLPN LMGHESVEEA EEDFYMFNNS
LATACTNDFT FFCAFAFPPC DVTLSNWMPC LETCQDTVSR CNDQLPWPLD CVGFPHEQPC
LQSIFLPPST STSPPPPSSL CVSQNYQPCR SLGFTSTMYP TWFAEDEAAN IRAFETWGMP
TIQSGCSRVA EYFMCAMFFP SCNAEHNNVT RPCRSTCEEV EEACYSQAKF NPYCPLFNTD
PNTCLLPPVM TTPLGTISNR KSSITEVTTT PPTTPTPHQC LPISIEACRH FGHLNGSVPS
TWGATDVETI QKQYLYLVDP VVSSGCSEVA LFYACAMLFP RCDDGVFLYP CRSVCEEYDR
KCRNAPRFFP QNCSLLPDKA TDGECLQPPR PVDCGDQFRC EGAPLCVPKS AVCNQANDCG
DWSDERNCTC NSDFEFKCDM GMCIRNYRRC DYQINCPDAS DEANCTNCTR NQFTCRDGRC
LMAEWVCDGD MDCSDGEDEA DCGTCDLPSF ACTSGECLSS DARCDGVVQC KDQTDEKNCM
EVFDDILFLF VDGGAHAVCA DGFTKQHADL ACQYLRYPGA ITMEVKIYPH LMYYKVSTNG
TFKTVISRGE PVDFCDDRVI SLTCAPAECG ENNMMGNFII NGQDANPGNA PWQVSIQEFG
KHFCGGSLIH QYFVVTAAHC VDQYITLTNL DVVVGAVDLS KPEASRKQVR VKRIIKHPQY
QPLNGYDVAL VELATPVNFT AYVGPLCLPR AEHQFSRFSR CFTTGWGRMD PSISSMATRL
QMLKMSLWDT NKCNSSYAWD GGIRPTEICA GYYSGIRAPC QGDSGGPLFC LSLSYNWVLV
GVASYVHDGC NKPEKPVVFS DVSLYNGWIH NNTECRFQCG TGRCLYDSSM VCNKVNDCGD
NSDEIDLCEI SANCTFEDGY LCGYNSGQWL WVSETVINNR YPLYDYNQGR YPGMFLIGPF
RGLTLHTPRI DLTSPHCFRF RYHMRGMVVQ GLSVHVHALE TVGWKMVWSR NITNIGWGED
IWQLGQFNLG KGHFDIAIMP YDDGVVSVDD VRLLSGTCAA TAGCTDDEFS CKTNGEMNCL
PSKLRCNVVA DCDDASDEVG CKEPLYICNM EDGVQCGLRQ NSSDSNSGEW RLVNGSRVDM
RDVTFNTSKG HLMHLGTERM LSTDAVYMYH ELYLGGRPHC LSFSFFSTST VRVEVEFLPT
TSSAPQVIWF MADRRTIGWS RTQAQIPAAV KGQLRYVVYG NRLDRSILHP MFALDDMRID
RNDCPTFTCP ADQQACSSEA FCLTPAQMCD RVVDCRGGED ERPCNCTTAE FKCPNAQCIP
KVSTCDTIRD CPDGSDEGAI CDHLVSVTCD FEDPFICGYS QNASSEEKAY RWSREKGGPL
NFGTGPDRDR TGNSSAYYMM ANGENGKAHD YVALQSRSFL SNGSTSLAFY YHAYNIFHQF
DITGTLALVT KDHVTGSEVV QWQLRADGNS TWRSACVQLP ASNSLSVTFV ASRGKAQRAD
LALDDVTLLD KSCDEFSKSE L
//
