ID A0A2T7P196_POMCA Unreviewed; 1328 AA.
AC A0A2T7P196;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Ig-like domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=C0Q70_12330 {ECO:0000313|EMBL:PVD27176.1};
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:PVD27176.1, ECO:0000313|Proteomes:UP000245119};
RN [1] {ECO:0000313|EMBL:PVD27176.1, ECO:0000313|Proteomes:UP000245119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD27176.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PVD27176.1};
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:PVD27176.1}.
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DR EMBL; PZQS01000007; PVD27176.1; -; Genomic_DNA.
DR EnsemblMetazoa; XM_025244518.1; XP_025100303.1; LOC112567731.
DR Proteomes; UP000245119; Miscellaneous, Linkage group lg7.
DR CDD; cd00037; CLECT; 1.
DR CDD; cd00096; Ig; 1.
DR CDD; cd00112; LDLa; 3.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 3.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR013162; CD80_C2-set.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR PANTHER; PTHR24270:SF61; CD320 ANTIGEN; 1.
DR PANTHER; PTHR24270; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 1.
DR Pfam; PF08205; C2-set_2; 1.
DR Pfam; PF13927; Ig_3; 1.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00192; LDLa; 4.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 2.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 4.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS50835; IG_LIKE; 2.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 4.
DR PROSITE; PS51450; LRR; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000245119};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 338..421
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1006..1106
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1124..1209
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 558..573
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 584..602
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 669..684
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 689..701
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 708..723
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 1328 AA; 148413 MW; 37BD2E7299824887 CRC64;
MRESLNLTHL TTPESSQHDF DHSNQTDERN KSETVYEVRE DQCLRQTLIT VSGQGGVILV
SFSNISMPST TPSDCTIRVV VPEGKYVQTT LDYSTDMDKV QITTSEDPDF TDVLTTFSFQ
ARYLPLLMSG YNQIFFKIPV SQTSGELKLR FLANEEDLRM TLPIVRTSPT SGYVTTWGFD
DNRRHPCYMN ASRTIHVPLN HVIMVSFSYV DIHHEIKYTC KKAFIQIYEI ENNTRSNSLR
MEICFNSIAK TLVLNTSVEV RFYTIICLER GFKMIFSFHS VNETPARLSS GLWDCSVPHY
SSFKQHLECN LEPECQGGED EGPHCPFSSP ECNGSVSVRN KCFTFLKSTG YLSWFSASRQ
CRNRGGNLAN VKTKQERDAL STISQYQKSL SYNFIGLSTY DGTLPPQYKK VLVWSDGTVA
YNTPLKVVST YKISLNSLQT FCFMSDLYYT FDLVVHCAKD YQQNVYGKPM NTLCEFPVTS
FVPQMSVLMP LINSDHATNN SLYVACADGH FTFDFLSCDK ASHCGAQTFP LYCKTKSVVT
AMFVCLDNSN TLPYSLVCDF RLDCSDGSDE NFCTRDQTCA GFRCLNGQCI NSDKFCDADL
DCWDATDEKC SVFRLWEING SNFVDLPAVI EFDQNNNLIY KALDVTDACP DTHFRCPPDG
YCLPVYVRCN GVYDCPYHED EDDCASYTCP GFYRCRASTV CVHVDHMCDG RPQCPQHDDE
LFCELSCPQG CVCQGLAFVC SVTFNTQTFP AMRYLDASGS GMSTSDMAPS IYLVWLSLAA
CDLQVLSNMS LPSLQTLDLS NNLLTWLDMS YFMKFENLQS SSPVRKPFAV LVHKLHVIVT
TLVPLAALEL EPSYVTGDTV SPRLSCRDTP TSCDCHHDVR TASVNIESSV GVLGNYPHYM
KCSYSLAPGE TLLNLDMYQI VNGVQTALGT LYDSGNPVWD GNTPSDIRRR SLLIRFDPTT
LQLFYNDTVC SDEKNYTCSV AFRSAEGTRT RSSSTQVTIE ASPGAPTMTA VPGYNITENT
TVTFTCTGNV GKPPGQFQWY MYRGSTRENQ TDQAATQSNT LATPSCTYTG RSSINITMTR
MEQGIVMRCR VYHPTQGSNT NTDDCTNPNT GFCRNGERML VFYPVSISLS PQTPAITVDQ
GSDYSLTCNA EGYPQPVLRW YKNSDPNYTL GTNSTLKLQN LTLSDSGVYV CIGSNNINGA
QLNDSKQVEI TIESTLHVVD MLPPVKVSNL NLDKQLMSTL VPGDEGVFAA QHVVTALCVV
KFDDLGTLPV VGEQWPERRT RSAASLQRLK RYQKTKHELV LTSVIKRSSN DLNSGWGAIQ
DPIPPKLF
//
