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Database: UniProt
Entry: A0A1U7R9R8_MESAU
LinkDB: A0A1U7R9R8_MESAU
Original site: A0A1U7R9R8_MESAU 
ID   A0A1U7R9R8_MESAU        Unreviewed;       226 AA.
AC   A0A1U7R9R8;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Lysoplasmalogenase TMEM86B {ECO:0000256|ARBA:ARBA00039876};
DE            EC=3.3.2.2 {ECO:0000256|ARBA:ARBA00035673};
DE   AltName: Full=Transmembrane protein 86B {ECO:0000256|ARBA:ARBA00042674};
GN   Name=Tmem86b {ECO:0000313|RefSeq:XP_005084184.1,
GN   ECO:0000313|RefSeq:XP_021091022.1, ECO:0000313|RefSeq:XP_021091023.1};
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036 {ECO:0000313|RefSeq:XP_005084184.1};
RN   [1] {ECO:0000313|RefSeq:XP_005084184.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (APR-2022) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the hydrolysis of the vinyl ether bond of choline
CC       or ethanolamine lysoplasmalogens, forming fatty aldehyde and
CC       glycerophosphocholine or glycerophosphoethanolamine, respectively and
CC       is specific for the sn-2-deacylated (lyso) form of plasmalogen.
CC       {ECO:0000256|ARBA:ARBA00037660}.
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   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the TMEM86 family.
CC       {ECO:0000256|ARBA:ARBA00007375}.
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DR   RefSeq; XP_005084184.1; XM_005084127.3.
DR   RefSeq; XP_021091022.1; XM_021235363.1.
DR   RefSeq; XP_021091023.1; XM_021235364.1.
DR   STRING; 10036.ENSMAUP00000001952; -.
DR   GeneID; 101829923; -.
DR   KEGG; maua:101829923; -.
DR   CTD; 255043; -.
DR   eggNOG; KOG4804; Eukaryota.
DR   OrthoDB; 3030862at2759; -.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0047408; F:alkenylglycerophosphocholine hydrolase activity; IEA:Ensembl.
DR   GO; GO:0047409; F:alkenylglycerophosphoethanolamine hydrolase activity; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0046485; P:ether lipid metabolic process; IEA:Ensembl.
DR   InterPro; IPR012506; TMEM86B-like.
DR   PANTHER; PTHR31885; GH04784P; 1.
DR   PANTHER; PTHR31885:SF7; LYSOPLASMALOGENASE; 1.
DR   Pfam; PF07947; YhhN; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        47..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        89..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        120..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        147..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        172..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   226 AA;  24726 MW;  5EAD37D49421CFF9 CRC64;
     MDPGKEGLLL KILFSDQHPQ VRRWLIPFFV SCVVYFVLWI PEDQPSWFSA LVKCLPILCL
     VVFLWAVTPG GSYPWLLQGG LVCSAVGDAC LIWPGAFLYG MAAFFATHVL YVWAFGLSPL
     RPGVLASVIP CALVYGSFLL PHLESGMVLP VSAYGLILFS MLWRSLARGG SAAWGGTLFT
     ISDSVLAWNA FIQPLGFARQ VTMTTYYAAQ LCLALSALRN PGLKTN
//
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