TM86B_MOUSE
ID TM86B_MOUSE Reviewed; 226 AA.
AC Q497J1;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Lysoplasmalogenase;
DE EC=3.3.2.2 {ECO:0000250|UniProtKB:B0BNF0};
DE AltName: Full=Transmembrane protein 86B;
GN Name=Tmem86b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=21515882; DOI=10.1074/jbc.m111.247163;
RA Wu L.C., Pfeiffer D.R., Calhoon E.A., Madiai F., Marcucci G., Liu S.,
RA Jurkowitz M.S.;
RT "Purification, identification, and cloning of lysoplasmalogenase, the
RT enzyme that catalyzes hydrolysis of the vinyl ether bond of
RT lysoplasmalogen.";
RL J. Biol. Chem. 286:24916-24930(2011).
CC -!- FUNCTION: Enzyme catalyzing the degradation of lysoplasmalogen.
CC Lysoplasmalogens are formed by the hydrolysis of the abundant membrane
CC glycerophospholipids plasmalogens. May control the respective levels of
CC plasmalogens and lysoplasmalogens in cells and modulate cell membrane
CC properties. {ECO:0000250|UniProtKB:B0BNF0}.
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:0000250|UniProtKB:B0BNF0};
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:0000250|UniProtKB:B0BNF0};
CC -!- ACTIVITY REGULATION: Competitively inhibited by lysophosphatidic acid.
CC {ECO:0000250|UniProtKB:Q8N661}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:Q8N661}.
CC -!- TISSUE SPECIFICITY: Enriched in liver. Also detected in brain and
CC testis. {ECO:0000269|PubMed:21515882}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryo.
CC {ECO:0000269|PubMed:21515882}.
CC -!- SIMILARITY: Belongs to the TMEM86 family. {ECO:0000305}.
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DR EMBL; BC100527; AAI00528.1; -; mRNA.
DR CCDS; CCDS20739.1; -.
DR RefSeq; NP_075929.1; NM_023440.2.
DR AlphaFoldDB; Q497J1; -.
DR STRING; 10090.ENSMUSP00000060237; -.
DR iPTMnet; Q497J1; -.
DR PhosphoSitePlus; Q497J1; -.
DR MaxQB; Q497J1; -.
DR PaxDb; Q497J1; -.
DR PRIDE; Q497J1; -.
DR ProteomicsDB; 259568; -.
DR Antibodypedia; 33044; 13 antibodies from 7 providers.
DR Ensembl; ENSMUST00000055085; ENSMUSP00000060237; ENSMUSG00000045282.
DR GeneID; 68255; -.
DR KEGG; mmu:68255; -.
DR UCSC; uc009eya.1; mouse.
DR CTD; 255043; -.
DR MGI; MGI:1915505; Tmem86b.
DR VEuPathDB; HostDB:ENSMUSG00000045282; -.
DR eggNOG; KOG4804; Eukaryota.
DR GeneTree; ENSGT00390000007101; -.
DR HOGENOM; CLU_079086_1_0_1; -.
DR InParanoid; Q497J1; -.
DR OMA; YVSAFGW; -.
DR OrthoDB; 1516092at2759; -.
DR PhylomeDB; Q497J1; -.
DR TreeFam; TF324663; -.
DR Reactome; R-MMU-1482788; Acyl chain remodelling of PC.
DR BioGRID-ORCS; 68255; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Tmem86b; mouse.
DR PRO; PR:Q497J1; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q497J1; protein.
DR Bgee; ENSMUSG00000045282; Expressed in bone marrow and 59 other tissues.
DR ExpressionAtlas; Q497J1; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0047408; F:alkenylglycerophosphocholine hydrolase activity; ISS:UniProtKB.
DR GO; GO:0047409; F:alkenylglycerophosphoethanolamine hydrolase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046485; P:ether lipid metabolic process; ISS:UniProtKB.
DR InterPro; IPR012506; YhhN.
DR PANTHER; PTHR31885; PTHR31885; 1.
DR Pfam; PF07947; YhhN; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Lipid metabolism; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..226
FT /note="Lysoplasmalogenase"
FT /id="PRO_0000201842"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 226 AA; 24989 MW; 66EA65B05D329800 CRC64;
MDARKEGLPL ETLFSDQYPQ VRRWLAPFIL ACSLYFLLWI PVDQPSWVSA LIKCQPILCL
VVFLWAVAPG GSSTWLLQGA LVCSAVGDAC LIWPEAFFYG TAAFSVAHLF YLGAFGLTPL
QPGLLLCTTL ASLTYYSFLL LHLEQGMVLP VMAYGLILNS MLWRSLVWGG SASWGAVLFT
FSDGVLAWDT FVYSLPFARL VTMSTYYAAQ LLLILSALRN PGLKTH
