ABHD12

Lysophosphatidylserine lipase ABHD12

398 amino acids

Lysophosphatidylserine (LPS) lipase that mediates the hydrolysis of lysophosphatidylserine, a class of signaling lipids that regulates immunological and neurological processes (By similarity). Represents a major lysophosphatidylserine lipase in the brain, thereby playing a key role in the central nervous system (By similarity). Also able to hydrolyze oxidized phosphatidylserine; oxidized phosphatidylserine is produced in response to severe inflammatory stress and constitutes a proapoptotic 'eat me' signal. Also has monoacylglycerol (MAG) lipase activity: hydrolyzes 2-arachidonoylglycerol (2-AG), thereby acting as a regulator of endocannabinoid signaling pathways. Has a strong preference for very-long-chain lipid substrates; substrate specificity is likely due to improved catalysis and not improved substrate binding (By similarity).

Belongs to the serine esterase family.

45.22 kDa

MRKRTEPVALEHERRTASGSPSAGPAAAALDADCRLKQNLCLAGPGPAEPRCAADAGMKRALGRRKGLCFRLRKILFFVLGLYVAIPFLIKLCPGIQAKLIFLNFVRVPYFIDLKRPQDQGLNHTCNYYLQPEEDVTIGVWHTVPTVWWKNAQGKDQMWYEDALSSSHPIILYLHGNAGTRGGDHRVELYKVLSSLGYHVVTFDYRGWGDSVGTPSERGMTYDALHVFDWIKVRSGDNPVYIWGHSLGTGVATNLVRRLCERETPPDALILESPFTNIREEAKSHPFSVIYRYFPGFDWFFLDPITSSGIQFANDENVKHISCSLLILHAEDDPVVPFQLGRKLYNIAAPSRSFRDFKVQFIPFHSDLGYRHKYIYKSPELPRILREFLGKSEPGRQH

ABHD12

Lysophosphatidylserine lipase ABHD12

398 amino acids

Lysophosphatidylserine (LPS) lipase that mediates the hydrolysis of lysophosphatidylserine, a class of signaling lipids that regulates immunological and neurological processes (PubMed:25290914, PubMed:30237167, PubMed:30420694, PubMed:30720278, PubMed:30643283). Represents a major lysophosphatidylserine lipase in the brain, thereby playing a key role in the central nervous system (By similarity). Also able to hydrolyze oxidized phosphatidylserine; oxidized phosphatidylserine is produced in response to severe inflammatory stress and constitutes a proapoptotic 'eat me' signal (PubMed:30643283). Also has monoacylglycerol (MAG) lipase activity: hydrolyzes 2-arachidonoylglycerol (2-AG), thereby acting as a regulator of endocannabinoid signaling pathways (PubMed:22969151, PubMed:24027063). Has a strong preference for very-long-chain lipid substrates; substrate specificity is likely due to improved catalysis and not improved substrate binding (PubMed:30237167).

Belongs to the serine esterase family.

45.097 kDa

MRKRTEPVALEHERCAAAGSSSSGSAAAALDADCRLKQNLRLTGPAAAEPRCAADAGMKRALGRRKGVWLRLRKILFCVLGLYIAIPFLIKLCPGIQAKLIFLNFVRVPYFIDLKKPQDQGLNHTCNYYLQPEEDVTIGVWHTVPAVWWKNAQGKDQMWYEDALASSHPIILYLHGNAGTRGGDHRVELYKVLSSLGYHVVTFDYRGWGDSVGTPSERGMTYDALHVFDWIKARSGDNPVYIWGHSLGTGVATNLVRRLCERETPPDALILESPFTNIREEAKSHPFSVIYRYFPGFDWFFLDPITSSGIKFANDENVKHISCPLLILHAEDDPVVPFQLGRKLYSIAAPARSFRDFKVQFVPFHSDLGYRHKYIYKSPELPRILREFLGKSEPEHQH

ABHD12

Lysophosphatidylserine lipase ABHD12

398 amino acids

Lysophosphatidylserine (LPS) lipase that mediates the hydrolysis of lysophosphatidylserine, a class of signaling lipids that regulates immunological and neurological processes (By similarity). Represents a major lysophosphatidylserine lipase in the brain, thereby playing a key role in the central nervous system (By similarity). Also able to hydrolyze oxidized phosphatidylserine; oxidized phosphatidylserine is produced in response to severe inflammatory stress and constitutes a proapoptotic 'eat me' signal. Also has monoacylglycerol (MAG) lipase activity: hydrolyzes 2-arachidonoylglycerol (2-AG), thereby acting as a regulator of endocannabinoid signaling pathways. Has a strong preference for very-long-chain lipid substrates; substrate specificity is likely due to improved catalysis and not improved substrate binding (By similarity).

Belongs to the serine esterase family.

45.075 kDa

MRKRTEPVALEHERCAAAGSSSSGSAAAALDADCRLKQNLRLTGTGAAEPRCAADAGMKRALGRRKGLWLRLRKILFCVLGLYIAIPFLIKLCPGIQAKLIFLNFVRVPYFIDLKKPQDQGLNHTCNYYLQPEEDVTIGVWHTVPAVWWKNAQGKDQMWYEDALASSHAIILYLHGNAGTRGGDHRVELYKVLSSLGYHVVTFDYRGWGDSVGTPSERGMTYDALHVFDWIKARSGDNPVYIWGHSLGTGVATNLVRRLCERETPPDALILESPFTNIREEAKSHPFSVIYRYFPGFDWFFLDPITSSGIKFANDENVKHISCPLLILHAEDDPVVPFQLGRKLYSIAAPARSFRDFKVQFVPFHSDLGYRHKYIYKSPELPRILREFLGKSEPEHQH

Abhd12

Lysophosphatidylserine lipase ABHD12

398 amino acids

Lysophosphatidylserine (LPS) lipase that mediates the hydrolysis of lysophosphatidylserine, a class of signaling lipids that regulates immunological and neurological processes (PubMed:23297193, PubMed:25580854, PubMed:30420694). Represents a major lysophosphatidylserine lipase in the brain, thereby playing a key role in the central nervous system (PubMed:23297193). Also able to hydrolyze oxidized phosphatidylserine; oxidized phosphatidylserine is produced in response to severe inflammatory stress and constitutes a proapoptotic 'eat me' signal (PubMed:30643283). Also has monoacylglycerol (MAG) lipase activity: hydrolyzes 2-arachidonoylglycerol (2-AG), thereby acting as a regulator of endocannabinoid signaling pathways (PubMed:18096503). Has a strong preference for very-long-chain lipid substrates; substrate specificity is likely due to improved catalysis and not improved substrate binding (PubMed:30237167).

Belongs to the serine esterase family.

45.27 kDa

MRKRTEPVTLEHERCAASGSSSSGSAAAALDADCSLKQNLRLAGKGTAEPHSASDAGMKRALGRRKSLWFRLRKILLCVLGFYIAIPFLVKLCPGIQAKLIFLNFVRVPYFIDLKKPQDQGLNHTCNYYLQPEDDVTIGVWHTIPSVWWKNAQGKDQMWYEDALASNHAIILYLHGNAGTRGGDHRVELYKVLSSLGYHVVTFDYRGWGDSVGTPSERGMTYDALHVFDWIKARSGDNPVYIWGHSLGTGVATNLVRRLCERETPPDALILESPFTNIREEAKSHPFSVIYRYFPGFDWFFLDPITSSGIKFANDENMKHISCPLLILHAEDDPVVPFHLGRKLYNIAAPSRSFRDFKVQFIPFHSDLGYRHKYIYKSPELPRILREFLGKSEPERQH

Abhd12

Lysophosphatidylserine lipase ABHD12

398 amino acids

Lysophosphatidylserine (LPS) lipase that mediates the hydrolysis of lysophosphatidylserine, a class of signaling lipids that regulates immunological and neurological processes (By similarity). Represents a major lysophosphatidylserine lipase in the brain, thereby playing a key role in the central nervous system (By similarity). Also able to hydrolyze oxidized phosphatidylserine; oxidized phosphatidylserine is produced in response to severe inflammatory stress and constitutes a proapoptotic 'eat me' signal. Also has monoacylglycerol (MAG) lipase activity: hydrolyzes 2-arachidonoylglycerol (2-AG), thereby acting as a regulator of endocannabinoid signaling pathways. Has a strong preference for very-long-chain lipid substrates; substrate specificity is likely due to improved catalysis and not improved substrate binding (By similarity).

Belongs to the serine esterase family.

45.296 kDa

MRKRTEPVTLEHERCAASGSSSSGSAAAALDADCSLKQNLRLAGKGTAEPHSASDAGMKRALGRRKSLWFRLRKILLCVLGFYIAIPFLVKLCPGIQAKLIFLNFVRVPYFIDLKKPQDQGLNHTCNYYLQPEDDVTIGVWHTIPSVWWKNAQGKDQMWYEDALASNHPIILYLHGNAGTRGGDHRVELYKVLSSLGYHVVTFDYRGWGDSVGTPSERGMTYDALHVFDWIKARSGDNPVYIWGHSLGTGVATNLVRRLCERETPPDALILESPFTNIREEAKSHPFSVIYRYFPGFDWFFLDPITSSGIKFANDENMKHISCPLLILHAEDDPVVPFHLGRKLYNIAAPSRSFRDFKVQFIPFHSDLGYRHKYIYKSPELPRILREFLGKSEPERQH

abhd12

Lysophosphatidylserine lipase ABHD12

386 amino acids

Lysophosphatidylserine (LPS) lipase that mediates the hydrolysis of lysophosphatidylserine, a class of signaling lipids that regulates immunological and neurological processes (By similarity). Represents a major lysophosphatidylserine lipase in the brain, thereby playing a key role in the central nervous system (By similarity). Also able to hydrolyze oxidized phosphatidylserine; oxidized phosphatidylserine is produced in response to severe inflammatory stress and constitutes a proapoptotic 'eat me' signal. Also has monoacylglycerol (MAG) lipase activity: hydrolyzes 2-arachidonoylglycerol (2-AG), thereby acting as a regulator of endocannabinoid signaling pathways. Has a strong preference for very-long-chain lipid substrates; substrate specificity is likely due to improved catalysis and not improved substrate binding (By similarity).

Belongs to the serine esterase family.

44.608 kDa

MRKRAEPVPPEHESFGRAPLDRECSIKQKLRIPGTKGHYPHDSDCDSKGMKRFGRRYGLWSRLRMFLIFLLGLYIAIPFLVKICPAIQTQLVFLNLVRFPYFIDLKRPEDQGLNHTCNFYLQPEEDVSIGVWHTVPAVLWKDAQGKDLEWYEEVLSTSYPVILYLHGNAGTRGGDHRVQLYKVLSSMGYHVISFDYRGWGDSVGSPSESGMTYDALHVFDWIKARSGDNPVYIWGHSLGTGVATNLVRRLCERETPPDSLILESPFTNIREEAKSHPFSVIYRYFPGFDWFFLDPITASGIKFANDDNVKYISCPLLILHAEDDPVIPFHLGKKLYNIAAPARSLRDYKVQFVPFHKDLGYRHKYIYRSPELRQILRDFLGNTEQQ

abhd12

Lysophosphatidylserine lipase ABHD12

382 amino acids

Lysophosphatidylserine (LPS) lipase that mediates the hydrolysis of lysophosphatidylserine, a class of signaling lipids that regulates immunological and neurological processes (By similarity). Represents a major lysophosphatidylserine lipase in the brain, thereby playing a key role in the central nervous system (By similarity). Also able to hydrolyze oxidized phosphatidylserine; oxidized phosphatidylserine is produced in response to severe inflammatory stress and constitutes a proapoptotic 'eat me' signal. Also has monoacylglycerol (MAG) lipase activity: hydrolyzes 2-arachidonoylglycerol (2-AG), thereby acting as a regulator of endocannabinoid signaling pathways. Has a strong preference for very-long-chain lipid substrates; substrate specificity is likely due to improved catalysis and not improved substrate binding (By similarity).

Belongs to the serine esterase family.

43.285 kDa

MRKRKGSADHDSSFTATLTDGSSDLKQCHKGTDADTDPGGSGKEMGRRCRRGGLMWRLRRILIWLLGIYIAIPVIIKVCPSIQAKLVFLNFVRVPYFIDLKRPQDQGMNHTHNFYLQPEEGINIGVWHTVPAGMWREAQAKDAEWYEKSFQSSHPVILYLHGNAGTRGGDHRVQLYKVLSSLGYHVVTFDYRGWGDSEGSPSERGMTSDALFLYQWIKQRIGPKPLYIWGHSLGTGVATNLVRRLCDRGTPPDALILESPFTNIREEAKSHPFSMVYRYLPGFDWFFLDAISANDIRFASDENVNHISCPVLILHAEDDTVVPFQLGKKLYDLAAQSKSLNGHKVQFIPFSSSLGYRHKFIYKSPQLPNILSDFLRAPHPHG

ABHD12

Lysophosphatidylserine lipase ABHD12

381 amino acids

Lysophosphatidylserine (LPS) lipase that mediates the hydrolysis of lysophosphatidylserine, a class of signaling lipids that regulates immunological and neurological processes (By similarity). Represents a major lysophosphatidylserine lipase in the brain, thereby playing a key role in the central nervous system (By similarity). Also able to hydrolyze oxidized phosphatidylserine; oxidized phosphatidylserine is produced in response to severe inflammatory stress and constitutes a proapoptotic 'eat me' signal. Also has monoacylglycerol (MAG) lipase activity: hydrolyzes 2-arachidonoylglycerol (2-AG), thereby acting as a regulator of endocannabinoid signaling pathways. Has a strong preference for very-long-chain lipid substrates; substrate specificity is likely due to improved catalysis and not improved substrate binding (By similarity).

Belongs to the serine esterase family.

43.855 kDa

MRKRNESVTVEHERAAAAPAPLDKGCSLRHSLRLPAADTGMKRPLGRRHGLWFRLRRLIIWLLGVYIAIPFLVKLCPAIQAKLVFLNFVRVPYFIDLKRPQDQGLNHTCNYYLQPEEDVTIGVWHTVPAALWKNARGKDQLWFEDALGSSHPVILYLHGNAGTRGGDHRVELYKVLSSLGYHVVTFDYRGWGDSVGSPSERGMTYDALHVFDWIKARSGDNPVYIWGHSLGTGVATNLVRRLCERETPPEALILESPFTNIREEARSHPFSVIYRYFPGFDWFFLDPITTSGIKFANDENVKYISCSLLILHAEDDPVVPFHLGKKLYNIAATSRSFRDYKVQFVPFHTDLGYRHKYIYRSPELPRILREFLGIPEHEHHH