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Database: UniProt
Entry: A0A1I8GHG6_9PLAT
LinkDB: A0A1I8GHG6_9PLAT
Original site: A0A1I8GHG6_9PLAT 
ID   A0A1I8GHG6_9PLAT        Unreviewed;       168 AA.
AC   A0A1I8GHG6;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   08-NOV-2023, entry version 17.
DE   RecName: Full=lysoplasmalogenase {ECO:0000256|ARBA:ARBA00035673};
DE            EC=3.3.2.2 {ECO:0000256|ARBA:ARBA00035673};
OS   Macrostomum lignano.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC   Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX   NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0002040-snap-gene-0.7-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:maker-uti_cns_0002040-snap-gene-0.7-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-O-(1Z-alkenyl)-sn-glycero-3-phosphocholine + H2O = a 2,3-
CC         saturated aldehyde + sn-glycerol 3-phosphocholine;
CC         Xref=Rhea:RHEA:22544, ChEBI:CHEBI:15377, ChEBI:CHEBI:16870,
CC         ChEBI:CHEBI:73359, ChEBI:CHEBI:77287; EC=3.3.2.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00035598};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-O-(1Z-alkenyl)-sn-glycero-3-phosphoethanolamine + H2O = a
CC         2,3-saturated aldehyde + sn-glycero-3-phosphoethanolamine;
CC         Xref=Rhea:RHEA:16905, ChEBI:CHEBI:15377, ChEBI:CHEBI:73359,
CC         ChEBI:CHEBI:77288, ChEBI:CHEBI:143890; EC=3.3.2.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00035579};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the TMEM86 family.
CC       {ECO:0000256|ARBA:ARBA00007375}.
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DR   AlphaFoldDB; A0A1I8GHG6; -.
DR   WBParaSite; maker-uti_cns_0002040-snap-gene-0.7-mRNA-1; maker-uti_cns_0002040-snap-gene-0.7-mRNA-1; maker-uti_cns_0002040-snap-gene-0.7.
DR   Proteomes; UP000095280; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR012506; TMEM86B-like.
DR   PANTHER; PTHR31885; GH04784P; 1.
DR   PANTHER; PTHR31885:SF6; GH04784P; 1.
DR   Pfam; PF07947; YhhN; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        24..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        47..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        80..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   168 AA;  17905 MW;  C80ED5B4150C3A47 CRC64;
     MCLFAVAQVA YAWAFGMSPL RPRVGLSASL VAVAAYLSVF PRANSVLMRY VGLVYTTLIF
     VMFWRAIARV RFEKSLGGCT SLAGAVGAAL FVVSDFCIAV NKFVTPLPHA NAVIMSTYYG
     AQLGIAFSVL DSQLDRVVSL SAKGSDDDAQ KGLLKNGNGF PGKRVCAH
//
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