TM86B_RAT
ID TM86B_RAT Reviewed; 233 AA.
AC B0BNF0;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Lysoplasmalogenase;
DE EC=3.3.2.2 {ECO:0000269|PubMed:21515882};
DE AltName: Full=Transmembrane protein 86B;
GN Name=Tmem86b;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
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:0000269|PubMed:21515882}.
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:0000269|PubMed:21515882};
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:0000269|PubMed:21515882};
CC -!- ACTIVITY REGULATION: Competitively inhibited by lysophosphatidic acid.
CC {ECO:0000250|UniProtKB:Q8N661}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=50 uM for lysoplasmenyl-choline {ECO:0000269|PubMed:21515882};
CC KM=50 uM for lysoplasmenyl-ethanolamine
CC {ECO:0000269|PubMed:21515882};
CC Vmax=24.5 umol/min/mg enzyme with lysoplasmenyl-choline as substrate
CC {ECO:0000269|PubMed:21515882};
CC Vmax=17.5 umol/min/mg enzyme with lysoplasmenyl-ethanolamine as
CC substrate {ECO:0000269|PubMed:21515882};
CC pH dependence:
CC Optimum pH is 7.0 with both ethanolamine and choline as substrates.
CC Fifty percent of maximal velocity occurs at pH 5.5 and pH 8.
CC {ECO:0000269|PubMed:21515882};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:Q8N661}.
CC -!- SIMILARITY: Belongs to the TMEM86 family. {ECO:0000305}.
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DR EMBL; BC158795; AAI58796.1; -; mRNA.
DR RefSeq; XP_006228351.1; XM_006228289.3.
DR AlphaFoldDB; B0BNF0; -.
DR STRING; 10116.ENSRNOP00000040879; -.
DR SwissLipids; SLP:000000631; -.
DR PaxDb; B0BNF0; -.
DR PeptideAtlas; B0BNF0; -.
DR GeneID; 690610; -.
DR UCSC; RGD:1593455; rat.
DR CTD; 255043; -.
DR RGD; 1593455; Tmem86b.
DR eggNOG; KOG4804; Eukaryota.
DR InParanoid; B0BNF0; -.
DR OMA; YVSAFGW; -.
DR OrthoDB; 1516092at2759; -.
DR PhylomeDB; B0BNF0; -.
DR Reactome; R-RNO-1482788; Acyl chain remodelling of PC.
DR SABIO-RK; B0BNF0; -.
DR PRO; PR:B0BNF0; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000038607; Expressed in liver and 19 other tissues.
DR ExpressionAtlas; B0BNF0; 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; IDA:RGD.
DR GO; GO:0047409; F:alkenylglycerophosphoethanolamine hydrolase activity; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
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 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Lipid metabolism; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..233
FT /note="Lysoplasmalogenase"
FT /id="PRO_0000410971"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..225
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 233 AA; 25912 MW; E96E6A5863B66F17 CRC64;
MPCCDPYPWI GLNVGRLSSF PLLKYPQVRR WLAPFIVACS LYFLLWIPED QPSWVSALVK
CQPILCLVLF LWAVAPGGSY TWLLQGALTC SAVGDACLIW PEAFFYGMAV FSVAHLLYLW
AFGLSPLQPG LLLCTTLASL TYYSFLLLHL EPNMVLPVAA YGLILNTMLW RGLVLGRSAG
WGAVLFIFSD GVLAWDTFVY TLPFARLVTM STYYAAQLLL TLSALRSPGL KTH
