ID A0A2B4R2G9_STYPI Unreviewed; 197 AA.
AC A0A2B4R2G9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Latrophilin Cirl {ECO:0000313|EMBL:PFX11023.1};
DE Flags: Fragment;
GN Name=Cirl {ECO:0000313|EMBL:PFX11023.1};
GN ORFNames=AWC38_SpisGene25564 {ECO:0000313|EMBL:PFX11023.1};
OS Stylophora pistillata (Smooth cauliflower coral).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC Astrocoeniina; Pocilloporidae; Stylophora.
OX NCBI_TaxID=50429 {ECO:0000313|EMBL:PFX11023.1, ECO:0000313|Proteomes:UP000225706};
RN [1] {ECO:0000313|Proteomes:UP000225706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Voolstra C.R., Li Y., Liew Y.J., Baumgarten S., Zoccola D., Flot J.-F.,
RA Tambutte S., Allemand D., Aranda M.;
RT "Comparative analysis of the genomes of Stylophora pistillata and Acropora
RT digitifera provides evidence for extensive differences between species of
RT corals.";
RL bioRxiv 0:0-0(2017).
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:PFX11023.1}.
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DR EMBL; LSMT01004352; PFX11023.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B4R2G9; -.
DR STRING; 50429.A0A2B4R2G9; -.
DR Proteomes; UP000225706; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd22827; Gal_Rha_Lectin_SUL-I-like; 1.
DR Gene3D; 2.60.120.740; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR024731; EGF_dom.
DR InterPro; IPR000922; Lectin_gal-bd_dom.
DR InterPro; IPR043159; Lectin_gal-bd_sf.
DR PANTHER; PTHR46780:SF23; L-RHAMNOSE-BINDING LECTIN CSL2-RELATED; 1.
DR PANTHER; PTHR46780; PROTEIN EVA-1; 1.
DR Pfam; PF12947; EGF_3; 1.
DR Pfam; PF02140; Gal_Lectin; 1.
DR SMART; SM00179; EGF_CA; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS50228; SUEL_LECTIN; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Reference proteome {ECO:0000313|Proteomes:UP000225706}.
FT DOMAIN 60..100
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 117..196
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
FT NON_TER 197
FT /evidence="ECO:0000313|EMBL:PFX11023.1"
SQ SEQUENCE 197 AA; 21830 MW; 516C9B1BDE3F1E6B CRC64;
MPSVTIPWDL TTARVKMGFM EMELAAQKQT TLKTAHMVVK HTWGKREAFQ INLTHFDALD
LDECASGTHG CDVNAECNNI LGSYNCTCIY GFNGNGTNCT EKVWSITICE RKPNRIISCE
NERKIDAVYA NFGRLDRVTC VHGVMSNTNC RAVNSLSTVQ TKCNGKVSCE LAATNSDFGD
PCAGTYKYLE VKFKCVL
//
