ID A0A2T7Q1I1_POMCA Unreviewed; 330 AA.
AC A0A2T7Q1I1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=SRCR domain-containing protein {ECO:0000259|PROSITE:PS50287};
GN ORFNames=C0Q70_02144 {ECO:0000313|EMBL:PVD39510.1};
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:PVD39510.1, ECO:0000313|Proteomes:UP000245119};
RN [1] {ECO:0000313|EMBL:PVD39510.1, ECO:0000313|Proteomes:UP000245119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD39510.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PVD39510.1};
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:PRU00196}.
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:PVD39510.1}.
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DR EMBL; PZQS01000001; PVD39510.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7Q1I1; -.
DR EnsemblMetazoa; XM_025247180.1; XP_025102965.1; LOC112569354.
DR Proteomes; UP000245119; Miscellaneous, Linkage group lg1.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.10.250.10; SRCR-like domain; 1.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR PANTHER; PTHR48071:SF18; LCCL_LECTIN ADHESIVE-LIKE PROTEIN 1; 1.
DR PANTHER; PTHR48071; SRCR DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00530; SRCR; 1.
DR PRINTS; PR00258; SPERACTRCPTR.
DR SMART; SM00202; SR; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR SUPFAM; SSF56487; SRCR-like; 1.
DR PROSITE; PS50287; SRCR_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00196}; Reference proteome {ECO:0000313|Proteomes:UP000245119}.
FT DOMAIN 220..324
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DISULFID 294..304
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ SEQUENCE 330 AA; 36688 MW; FD503C3E4FFF203D CRC64;
MEWYFAPNVY DPETIATYVD GRFLVPQSTH QRLYFAENVG LTISNLTHED FGTYSVRVDI
RSGSSFVSEV IYATLHQPVP PTTEDELLHA RMLPNAAFSS GEWHVQLACG RFISVFSTFF
SVNWKTPSGR LLPTDQITGS DYILKLTNPI EEGNYSCFID IHEPAARCAH VPSTMLVSNE
IHVDDCSVQT VKNNAAKHQM EDIASAFKQL VMTGSESGNV RLVNGNRPWN GRIELKSPNG
TWGAMCSTFV GLNTAPVVCR MLGLTPDPRY SPYISYANQY GISKLPALTG YVSCTGNEDS
IFNCSISYNG QSCDRYYDLG VDCWPTFTTD
//
