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Database: UniProt
Entry: A0A0V0VIU9_9BILA
LinkDB: A0A0V0VIU9_9BILA
Original site: A0A0V0VIU9_9BILA 
ID   A0A0V0VIU9_9BILA        Unreviewed;       181 AA.
AC   A0A0V0VIU9;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   RecName: Full=MD-2-related lipid-recognition domain-containing protein {ECO:0000259|SMART:SM00737};
GN   ORFNames=T09_9277 {ECO:0000313|EMBL:KRX63364.1};
OS   Trichinella sp. T9.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX63364.1, ECO:0000313|Proteomes:UP000054681};
RN   [1] {ECO:0000313|EMBL:KRX63364.1, ECO:0000313|Proteomes:UP000054681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS409 {ECO:0000313|EMBL:KRX63364.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KRX63364.1}.
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DR   EMBL; JYDN01000032; KRX63364.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0VIU9; -.
DR   STRING; 181606.A0A0V0VIU9; -.
DR   Proteomes; UP000054681; Unassembled WGS sequence.
DR   GO; GO:0008047; F:enzyme activator activity; IEA:InterPro.
DR   GO; GO:0006689; P:ganglioside catabolic process; IEA:InterPro.
DR   Gene3D; 2.70.220.10; Ganglioside GM2 activator; 1.
DR   InterPro; IPR028996; GM2-AP.
DR   InterPro; IPR036846; GM2-AP_sf.
DR   InterPro; IPR003172; ML_dom.
DR   PANTHER; PTHR17357:SF0; GANGLIOSIDE GM2 ACTIVATOR; 1.
DR   PANTHER; PTHR17357; GM2 GANGLIOSIDE ACTIVATOR PROTEIN; 1.
DR   Pfam; PF02221; E1_DerP2_DerF2; 1.
DR   SMART; SM00737; ML; 1.
DR   SUPFAM; SSF63707; Ganglioside M2 (gm2) activator; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..181
FT                   /note="MD-2-related lipid-recognition domain-containing
FT                   protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006871042"
FT   DOMAIN          34..174
FT                   /note="MD-2-related lipid-recognition"
FT                   /evidence="ECO:0000259|SMART:SM00737"
SQ   SEQUENCE   181 AA;  20712 MW;  3DCF47C6E80B0B9E CRC64;
     MSSKCLALML FGSLVLMMVM GFDNKPALST SSHAYDCGNE NRIIRLYSFR LGPMPLVFPD
     VLQMHIDLEI MDKIPNQVDA HVRVEKQVTK TIWVRVPCML QFGSCDYYRI DACLLTEEMF
     GCPIEIGRHN HTETYLLDSP ETFNPNSLRG NYRTLVEINN SDTGEPLACF NFIYSINGSR
     W
//
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