ID ABHGA_HUMAN Reviewed; 558 AA. AC O95870; A2BEY3; B7Z4R6; Q5SRR1; Q5SRR2; Q8WYH0; Q9NW33; DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 14-DEC-2022, entry version 185. DE RecName: Full=Phosphatidylserine lipase ABHD16A {ECO:0000305}; DE EC=3.1.-.- {ECO:0000250|UniProtKB:Q9Z1Q2}; DE AltName: Full=Alpha/beta hydrolase domain-containing protein 16A {ECO:0000305}; DE Short=Abhydrolase domain-containing protein 16A {ECO:0000305}; DE AltName: Full=HLA-B-associated transcript 5 {ECO:0000303|PubMed:25290914}; DE Short=hBAT5 {ECO:0000303|PubMed:25290914}; DE AltName: Full=Monoacylglycerol lipase ABHD16A {ECO:0000305}; DE EC=3.1.1.23 {ECO:0000269|PubMed:25290914}; DE AltName: Full=Protein G5; GN Name=ABHD16A {ECO:0000312|HGNC:HGNC:13921}; GN Synonyms=BAT5 {ECO:0000303|PubMed:25290914}, G5, NG26; ORFNames=PP199; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=15498874; DOI=10.1073/pnas.0404089101; RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X., RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.; RT "Large-scale cDNA transfection screening for genes related to cancer RT development and progression."; RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Teratocarcinoma; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14656967; DOI=10.1101/gr.1736803; RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., RA Hood L.; RT "Analysis of the gene-dense major histocompatibility complex class III RT region and its comparison to mouse."; RL Genome Res. 13:2621-2636(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Shiina S., Tamiya G., Oka A., Inoko H.; RT "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [7] RP PROTEIN SEQUENCE OF 2-12 (ISOFORM 1). RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., RA Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass spectrometric RT identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [9] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL RP PROPERTIES. RX PubMed=25290914; DOI=10.1371/journal.pone.0109869; RA Savinainen J.R., Patel J.Z., Parkkari T., Navia-Paldanius D., RA Marjamaa J.J., Laitinen T., Nevalainen T., Laitinen J.T.; RT "Biochemical and pharmacological characterization of the human lymphocyte RT antigen B-associated transcript 5 (BAT5/ABHD16A)."; RL PLoS ONE 9:E109869-E109869(2014). RN [10] RP VARIANTS SPG86 HIS-118; ILE-121; GLN-252; ARG-409 AND 445-ARG--LEU-558 DEL, RP AND INVOLVEMENT IN SPG86. RX PubMed=34587489; DOI=10.1016/j.ajhg.2021.09.005; RG Care4Rare Canada Consortium; RA Lemire G., Ito Y.A., Marshall A.E., Chrestian N., Stanley V., Brady L., RA Tarnopolsky M., Curry C.J., Hartley T., Mears W., Derksen A., Rioux N., RA Laflamme N., Hutchison H.T., Pais L.S., Zaki M.S., Sultan T., Dane A.D., RA Gleeson J.G., Vaz F.M., Kernohan K.D., Bernard G., Boycott K.M.; RT "ABHD16A deficiency causes a complicated form of hereditary spastic RT paraplegia associated with intellectual disability and cerebral RT anomalies."; RL Am. J. Hum. Genet. 108:2017-2023(2021). RN [11] RP VARIANTS SPG86 114-ARG--LEU-558 DEL AND GLN-457, CHARACTERIZATION OF RP VARIANTS SPG86 114-ARG--LEU-558 DEL AND GLN-457, AND INVOLVEMENT IN SPG86. RX PubMed=34489854; DOI=10.3389/fneur.2021.720201; RA Yahia A., Elsayed L.E.O., Valter R., Hamed A.A.A., Mohammed I.N., RA Elseed M.A., Salih M.A., Esteves T., Auger N., Abubaker R., Koko M., RA Abozar F., Malik H., Adil R., Emad S., Musallam M.A., Idris R., RA Eltazi I.Z.M., Babai A., Ahmed E.A.A., Abd Allah A.S.I., Mairey M., RA Ahmed A.K.M.A., Elbashir M.I., Brice A., Ibrahim M.E., Ahmed A.E., RA Lamari F., Stevanin G.; RT "Pathogenic variants in ABHD16A cause a novel psychomotor developmental RT disorder with spastic paraplegia."; RL Front. Neurol. 12:720201-720201(2021). RN [12] RP VARIANT SPG86 279-GLN--LEU-558 DEL, AND INVOLVEMENT IN SPG86. RX PubMed=34866177; DOI=10.1111/cge.14097; RA Miyake N., Silva S., Troncoso M., Okamoto N., Andachi Y., Kato M., RA Iwabuchi C., Hirose M., Fujita A., Uchiyama Y., Matsumoto N.; RT "A homozygous ABHD16A variant causes a complex hereditary spastic RT paraplegia with developmental delay, absent speech, and characteristic RT face."; RL Clin. Genet. 101:359-363(2022). CC -!- FUNCTION: Phosphatidylserine (PS) lipase that mediates the hydrolysis CC of phosphatidylserine to generate lysophosphatidylserine (LPS) (By CC similarity). LPS constitutes a class of signaling lipids that regulates CC immunological and neurological processes (By similarity). Has no CC activity towards diacylglycerol, triacylglycerol or CC lysophosphatidylserine lipase (PubMed:25290914). Also has CC monoacylglycerol lipase activity, with preference for 1-(9Z,12Z- CC octadecadienoyl)-glycerol (1-LG) and 2-glyceryl-15-deoxy-Delta(12,14)- CC prostaglandin J2 (15d-PGJ(2)-G) (PubMed:25290914). CC {ECO:0000250|UniProtKB:Q9Z1Q2, ECO:0000269|PubMed:25290914}. CC -!- CATALYTIC ACTIVITY: CC Reaction=1-heptadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero- CC 3-phosphoserine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1- CC heptadecanoyl-sn-glycero-3-phosphoserine + H(+); CC Xref=Rhea:RHEA:44500, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:32395, ChEBI:CHEBI:84461, ChEBI:CHEBI:84462; CC Evidence={ECO:0000250|UniProtKB:Q9Z1Q2}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L- CC serine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3- CC phospho-L-serine + H(+); Xref=Rhea:RHEA:41752, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:75020, CC ChEBI:CHEBI:75029; Evidence={ECO:0000250|UniProtKB:Q9Z1Q2}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-octadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3- CC phosphoserine + H2O = (9Z,12Z)-octadecadienoate + 1-octadecanoyl-sn- CC glycero-3-phosphoserine + H(+); Xref=Rhea:RHEA:44516, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, CC ChEBI:CHEBI:84466, ChEBI:CHEBI:84467; CC Evidence={ECO:0000250|UniProtKB:Q9Z1Q2}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-heptadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero- CC 3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1- CC heptadecanoyl-sn-glycero-3-phosphocholine + H(+); CC Xref=Rhea:RHEA:44520, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:32395, ChEBI:CHEBI:74340, ChEBI:CHEBI:84470; CC Evidence={ECO:0000250|UniProtKB:Q9Z1Q2}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho- CC glycerol + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3- CC phospho-glycerol + H(+); Xref=Rhea:RHEA:44524, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:84472, CC ChEBI:CHEBI:84475; Evidence={ECO:0000250|UniProtKB:Q9Z1Q2}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1D- CC myo-inositol) + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero- CC 3-phospho-(1D-myo-inositol) + H(+); Xref=Rhea:RHEA:44528, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, CC ChEBI:CHEBI:72833, ChEBI:CHEBI:72837; CC Evidence={ECO:0000250|UniProtKB:Q9Z1Q2}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-heptadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero- CC 3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1- CC heptadecanoyl-sn-glycero-3-phosphoethanolamine + H(+); CC Xref=Rhea:RHEA:44540, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:32395, ChEBI:CHEBI:84489, ChEBI:CHEBI:84490; CC Evidence={ECO:0000250|UniProtKB:Q9Z1Q2}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'- CC sn-glycerol) + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero- CC 3-phospho-(1'-sn-glycerol) + H(+); Xref=Rhea:RHEA:40919, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, CC ChEBI:CHEBI:72841, ChEBI:CHEBI:75158; CC Evidence={ECO:0000250|UniProtKB:Q9Z1Q2}; CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolyzes glycerol monoesters of long-chain fatty acids.; CC EC=3.1.1.23; Evidence={ECO:0000269|PubMed:25290914}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-tetradecanoylglycerol + H2O = glycerol + H(+) + CC tetradecanoate; Xref=Rhea:RHEA:44312, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30807, CC ChEBI:CHEBI:75562; Evidence={ECO:0000269|PubMed:25290914}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44313; CC Evidence={ECO:0000269|PubMed:25290914}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-hexadecanoylglycerol + H2O = glycerol + H(+) + CC hexadecanoate; Xref=Rhea:RHEA:39963, ChEBI:CHEBI:7896, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, CC ChEBI:CHEBI:75455; Evidence={ECO:0000269|PubMed:25290914}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39964; CC Evidence={ECO:0000269|PubMed:25290914}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + CC glycerol + H(+); Xref=Rhea:RHEA:38487, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823, CC ChEBI:CHEBI:75342; Evidence={ECO:0000269|PubMed:25290914}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38488; CC Evidence={ECO:0000269|PubMed:25290914}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + CC glycerol + H(+); Xref=Rhea:RHEA:38491, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823, CC ChEBI:CHEBI:73990; Evidence={ECO:0000269|PubMed:25290914}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38492; CC Evidence={ECO:0000269|PubMed:25290914}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-(9Z,12Z-octadecadienoyl)-glycerol + H2O = (9Z,12Z)- CC octadecadienoate + glycerol + H(+); Xref=Rhea:RHEA:44732, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, CC ChEBI:CHEBI:30245, ChEBI:CHEBI:75457; CC Evidence={ECO:0000269|PubMed:25290914}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44733; CC Evidence={ECO:0000269|PubMed:25290914}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O = CC (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+); CC Xref=Rhea:RHEA:44728, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17754, ChEBI:CHEBI:32395, ChEBI:CHEBI:75612; CC Evidence={ECO:0000269|PubMed:25290914}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44729; CC Evidence={ECO:0000269|PubMed:25290914}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O = CC (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+); CC Xref=Rhea:RHEA:26132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17754, ChEBI:CHEBI:32395, ChEBI:CHEBI:52392; CC Evidence={ECO:0000269|PubMed:25290914}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26133; CC Evidence={ECO:0000269|PubMed:25290914}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + prostaglandin D2-1-glycerol ester = glycerol + H(+) + CC prostaglandin D2; Xref=Rhea:RHEA:45412, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:57406, CC ChEBI:CHEBI:85232; Evidence={ECO:0000269|PubMed:25290914}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45413; CC Evidence={ECO:0000269|PubMed:25290914}; CC -!- CATALYTIC ACTIVITY: CC Reaction=11-oxo-5Z,9,12E,14E-prostatetraenoate + H2O = 15-deoxy- CC Delta(12,14)-prostaglandin J2 + glycerol + H(+); CC Xref=Rhea:RHEA:45416, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17754, ChEBI:CHEBI:85236, ChEBI:CHEBI:85238; CC Evidence={ECO:0000269|PubMed:25290914}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45417; CC Evidence={ECO:0000269|PubMed:25290914}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(9Z,12Z-octadecadienoyl)-glycerol + H2O = (9Z,12Z)- CC octadecadienoate + glycerol + H(+); Xref=Rhea:RHEA:48428, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, CC ChEBI:CHEBI:30245, ChEBI:CHEBI:75568; CC Evidence={ECO:0000269|PubMed:25290914}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48429; CC Evidence={ECO:0000269|PubMed:25290914}; CC -!- ACTIVITY REGULATION: Inhibited by beta-lactone-based lipid inhibitors, CC such as beta-lactone palmostatin-B. {ECO:0000269|PubMed:25290914}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=6.9 uM for 1-(9Z,12Z-octadecadienoyl)-glycerol (1-LG) (in absence CC of BSA) {ECO:0000269|PubMed:25290914}; CC KM=137.8 uM for 1-(9Z,12Z-octadecadienoyl)-glycerol (1-LG) (in CC presence of BSA) {ECO:0000269|PubMed:25290914}; CC KM=20.9 uM for 2-glyceryl-15-deoxy-Delta(12,14)-prostaglandin J2 CC (15d-PGJ(2)-G) (in presence of BSA) {ECO:0000269|PubMed:25290914}; CC Vmax=7.3 nmol/min/mg enzyme with 1-(9Z,12Z-octadecadienoyl)-glycerol CC (1-LG) as substrate (in absence of BSA) CC {ECO:0000269|PubMed:25290914}; CC Vmax=13.2 nmol/min/mg enzyme with 1-(9Z,12Z-octadecadienoyl)-glycerol CC (1-LG) as substrate (in presence of BSA) CC {ECO:0000269|PubMed:25290914}; CC pH dependence: CC Optimum pH is 7.2-8.0. {ECO:0000269|PubMed:25290914}; CC -!- INTERACTION: CC O95870; Q9NRZ7: AGPAT3; NbExp=3; IntAct=EBI-348517, EBI-2803601; CC O95870; Q13520: AQP6; NbExp=3; IntAct=EBI-348517, EBI-13059134; CC O95870; Q6P5T0: AQP7; NbExp=3; IntAct=EBI-348517, EBI-10489564; CC O95870; P18859: ATP5PF; NbExp=3; IntAct=EBI-348517, EBI-2606700; CC O95870; O95415: BRI3; NbExp=3; IntAct=EBI-348517, EBI-2874789; CC O95870; Q8N350-4: CBARP; NbExp=3; IntAct=EBI-348517, EBI-19051169; CC O95870; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-348517, EBI-7062247; CC O95870; P05177: CYP1A2; NbExp=3; IntAct=EBI-348517, EBI-17183330; CC O95870; Q86UW9: DTX2; NbExp=7; IntAct=EBI-348517, EBI-740376; CC O95870; Q15125: EBP; NbExp=3; IntAct=EBI-348517, EBI-3915253; CC O95870; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-348517, EBI-781551; CC O95870; P14324: FDPS; NbExp=3; IntAct=EBI-348517, EBI-948245; CC O95870; Q9Y680: FKBP7; NbExp=3; IntAct=EBI-348517, EBI-3918971; CC O95870; Q8TB36: GDAP1; NbExp=3; IntAct=EBI-348517, EBI-11110431; CC O95870; P36382: GJA5; NbExp=3; IntAct=EBI-348517, EBI-750433; CC O95870; Q6ZVE7: GOLT1A; NbExp=3; IntAct=EBI-348517, EBI-17231387; CC O95870; Q5T7V8: GORAB; NbExp=3; IntAct=EBI-348517, EBI-3917143; CC O95870; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-348517, EBI-13345167; CC O95870; P04921: GYPC; NbExp=3; IntAct=EBI-348517, EBI-7797098; CC O95870; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-348517, EBI-18053395; CC O95870; Q01628: IFITM3; NbExp=3; IntAct=EBI-348517, EBI-7932862; CC O95870; P11215: ITGAM; NbExp=3; IntAct=EBI-348517, EBI-2568251; CC O95870; P01374: LTA; NbExp=3; IntAct=EBI-348517, EBI-524105; CC O95870; Q96FX8: PERP; NbExp=3; IntAct=EBI-348517, EBI-17183069; CC O95870; Q99640-2: PKMYT1; NbExp=3; IntAct=EBI-348517, EBI-12257782; CC O95870; Q07864: POLE; NbExp=3; IntAct=EBI-348517, EBI-348526; CC O95870; O60831: PRAF2; NbExp=3; IntAct=EBI-348517, EBI-2506064; CC O95870; Q86VR2: RETREG3; NbExp=7; IntAct=EBI-348517, EBI-10192441; CC O95870; Q6NTF9-3: RHBDD2; NbExp=3; IntAct=EBI-348517, EBI-17589229; CC O95870; O75783: RHBDL1; NbExp=3; IntAct=EBI-348517, EBI-12104986; CC O95870; Q99942: RNF5; NbExp=9; IntAct=EBI-348517, EBI-348482; CC O95870; O75396: SEC22B; NbExp=3; IntAct=EBI-348517, EBI-1058865; CC O95870; O75920: SERF1B; NbExp=3; IntAct=EBI-348517, EBI-2115181; CC O95870; Q14973: SLC10A1; NbExp=3; IntAct=EBI-348517, EBI-3923031; CC O95870; Q9BRI3: SLC30A2; NbExp=3; IntAct=EBI-348517, EBI-8644112; CC O95870; Q9UHI5: SLC7A8; NbExp=3; IntAct=EBI-348517, EBI-13292283; CC O95870; Q9NPE6: SPAG4; NbExp=3; IntAct=EBI-348517, EBI-10819434; CC O95870; Q9H169-2: STMN4; NbExp=3; IntAct=EBI-348517, EBI-20117546; CC O95870; P61266: STX1B; NbExp=3; IntAct=EBI-348517, EBI-9071709; CC O95870; Q96DZ7: TM4SF19; NbExp=3; IntAct=EBI-348517, EBI-6448756; CC O95870; Q8IV31: TMEM139; NbExp=3; IntAct=EBI-348517, EBI-7238458; CC O95870; Q96AN5: TMEM143; NbExp=3; IntAct=EBI-348517, EBI-13342951; CC O95870; Q9BVK8: TMEM147; NbExp=4; IntAct=EBI-348517, EBI-348587; CC O95870; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-348517, EBI-8638294; CC O95870; Q96Q45-2: TMEM237; NbExp=5; IntAct=EBI-348517, EBI-10982110; CC O95870; Q6PI78: TMEM65; NbExp=3; IntAct=EBI-348517, EBI-6656213; CC O95870; O60636: TSPAN2; NbExp=3; IntAct=EBI-348517, EBI-3914288; CC O95870; Q86WB7-2: UNC93A; NbExp=3; IntAct=EBI-348517, EBI-13356252; CC O95870; O95183: VAMP5; NbExp=3; IntAct=EBI-348517, EBI-10191195; CC O95870; Q3ZAQ7: VMA21; NbExp=3; IntAct=EBI-348517, EBI-1055364; CC O95870; Q9NX94: WBP1L; NbExp=3; IntAct=EBI-348517, EBI-10316321; CC O95870; P0DTC6: 6; Xeno; NbExp=3; IntAct=EBI-348517, EBI-25475897; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9Z1Q2}; Multi- CC pass membrane protein {ECO:0000255}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O95870-1; Sequence=Displayed; CC Name=2; CC IsoId=O95870-2; Sequence=VSP_043825; CC -!- DISEASE: Spastic paraplegia 86, autosomal recessive (SPG86) CC [MIM:619735]: A form of spastic paraplegia, a neurodegenerative CC disorder characterized by a slow, gradual, progressive weakness and CC spasticity of the lower limbs. Rate of progression and the severity of CC symptoms are quite variable. Initial symptoms may include difficulty CC with balance, weakness and stiffness in the legs, muscle spasms, and CC dragging the toes when walking. In some forms of the disorder, bladder CC symptoms (such as incontinence) may appear, or the weakness and CC stiffness may spread to other parts of the body. SPG86 is an autosomal CC recessive form associated with impaired intellectual development, poor CC or absent speech, and behavioral abnormalities. Brain imaging shows CC thin corpus callosum and white matter abnormalities. Rare patients may CC have seizures. {ECO:0000269|PubMed:34489854, CC ECO:0000269|PubMed:34587489, ECO:0000269|PubMed:34866177}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. ABHD16 family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF193047; AAG22475.1; -; mRNA. DR EMBL; AK001207; BAA91553.1; -; mRNA. DR EMBL; AK023194; BAB14455.1; -; mRNA. DR EMBL; AK297712; BAH12652.1; -; mRNA. DR EMBL; AF129756; AAD18079.1; -; Genomic_DNA. DR EMBL; BA000025; BAB63383.1; -; Genomic_DNA. DR EMBL; AL662899; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL670886; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL805934; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX248244; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX511262; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR354443; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR753842; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR759761; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR759787; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC031839; AAH31839.1; -; mRNA. DR CCDS; CCDS4713.1; -. [O95870-1] DR CCDS; CCDS54988.1; -. [O95870-2] DR RefSeq; NP_001170986.1; NM_001177515.1. [O95870-2] DR RefSeq; NP_066983.1; NM_021160.2. [O95870-1] DR AlphaFoldDB; O95870; -. DR SMR; O95870; -. DR BioGRID; 113650; 86. DR IntAct; O95870; 74. DR MINT; O95870; -. DR STRING; 9606.ENSP00000379282; -. DR BindingDB; O95870; -. DR ChEMBL; CHEMBL6168; -. DR DrugCentral; O95870; -. DR SwissLipids; SLP:000001120; -. DR ESTHER; human-ABHD16A; ABHD16. DR MEROPS; S09.065; -. DR iPTMnet; O95870; -. DR PhosphoSitePlus; O95870; -. DR SwissPalm; O95870; -. DR BioMuta; ABHD16A; -. DR EPD; O95870; -. DR jPOST; O95870; -. DR MassIVE; O95870; -. DR MaxQB; O95870; -. DR PaxDb; O95870; -. DR PeptideAtlas; O95870; -. DR ProteomicsDB; 51110; -. [O95870-1] DR ProteomicsDB; 51111; -. [O95870-2] DR Antibodypedia; 27504; 96 antibodies from 19 providers. DR DNASU; 7920; -. DR Ensembl; ENST00000395952.8; ENSP00000379282.3; ENSG00000204427.12. [O95870-1] DR Ensembl; ENST00000440843.2; ENSP00000410347.2; ENSG00000204427.12. [O95870-2] DR Ensembl; ENST00000446529.6; ENSP00000395665.2; ENSG00000206403.11. [O95870-1] DR Ensembl; ENST00000548592.1; ENSP00000448431.1; ENSG00000206403.11. [O95870-2] DR Ensembl; ENST00000549722.1; ENSP00000447549.1; ENSG00000230475.9. [O95870-2] DR Ensembl; ENST00000549853.1; ENSP00000447846.1; ENSG00000236063.9. [O95870-2] DR Ensembl; ENST00000550556.1; ENSP00000447498.1; ENSG00000235676.9. [O95870-2] DR Ensembl; ENST00000551038.1; ENSP00000449579.1; ENSG00000231488.9. [O95870-2] DR Ensembl; ENST00000552042.1; ENSP00000448451.1; ENSG00000224552.9. [O95870-2] DR GeneID; 7920; -. DR KEGG; hsa:7920; -. DR MANE-Select; ENST00000395952.8; ENSP00000379282.3; NM_021160.3; NP_066983.1. DR UCSC; uc003nvy.3; human. [O95870-1] DR AGR; HGNC:13921; -. DR CTD; 7920; -. DR DisGeNET; 7920; -. DR GeneCards; ABHD16A; -. DR HGNC; HGNC:13921; ABHD16A. DR HPA; ENSG00000204427; Low tissue specificity. DR MalaCards; ABHD16A; -. DR MIM; 142620; gene. DR MIM; 619735; phenotype. DR neXtProt; NX_O95870; -. DR OpenTargets; ENSG00000204427; -. DR PharmGKB; PA25266; -. DR VEuPathDB; HostDB:ENSG00000204427; -. DR eggNOG; KOG1553; Eukaryota. DR GeneTree; ENSGT00940000160908; -. DR HOGENOM; CLU_040705_2_0_1; -. DR InParanoid; O95870; -. DR OMA; THCTQLP; -. DR PhylomeDB; O95870; -. DR TreeFam; TF314267; -. DR PathwayCommons; O95870; -. DR SignaLink; O95870; -. DR BioGRID-ORCS; 7920; 23 hits in 1069 CRISPR screens. DR ChiTaRS; ABHD16A; human. DR GeneWiki; BAT5; -. DR GenomeRNAi; 7920; -. DR Pharos; O95870; Tchem. DR PRO; PR:O95870; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; O95870; protein. DR Bgee; ENSG00000204427; Expressed in pituitary gland and 96 other tissues. DR ExpressionAtlas; O95870; baseline and differential. DR Genevisible; O95870; HS. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0047372; F:acylglycerol lipase activity; IDA:UniProtKB. DR GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; IBA:GO_Central. DR GO; GO:0004620; F:phospholipase activity; ISS:UniProtKB. DR GO; GO:0052651; P:monoacylglycerol catabolic process; IDA:UniProtKB. DR GO; GO:0006660; P:phosphatidylserine catabolic process; ISS:UniProtKB. DR GO; GO:1905344; P:prostaglandin catabolic process; IDA:BHF-UCL. DR Gene3D; 3.40.50.1820; -; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR000073; AB_hydrolase_1. DR InterPro; IPR026604; ABHD16A. DR PANTHER; PTHR12277:SF54; PHOSPHATIDYLSERINE LIPASE ABHD16A; 1. DR Pfam; PF00561; Abhydrolase_1; 1. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1. PE 1: Evidence at protein level; KW Alternative splicing; Direct protein sequencing; Disease variant; KW Hereditary spastic paraplegia; Hydrolase; Lipid metabolism; Membrane; KW Neurodegeneration; Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1..558 FT /note="Phosphatidylserine lipase ABHD16A" FT /id="PRO_0000064833" FT TRANSMEM 60..80 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 93..113 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 114..558 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:Q9Z1Q2" FT DOMAIN 281..407 FT /note="AB hydrolase-1" FT /evidence="ECO:0000255" FT ACT_SITE 355 FT /note="Charge relay system" FT /evidence="ECO:0000250|UniProtKB:Q8N2K0" FT ACT_SITE 430 FT /note="Charge relay system" FT /evidence="ECO:0000250|UniProtKB:Q8N2K0" FT ACT_SITE 507 FT /note="Charge relay system" FT /evidence="ECO:0000250|UniProtKB:Q8N2K0" FT VAR_SEQ 1..85 FT /note="MAKLLSCVLGPRLYKIYRERDSERAPASVPETPTAVTAPHSSSWDTYYQPRA FT LEKHADSILALASVFWSISYYSSPFAFFYLYRK -> MPPPALFLSSLYPRLEFQNDFY FT RSCIRRSSPQPPPNLAWRPESLYSGELAGG (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043825" FT VARIANT 114..558 FT /note="Missing (in SPG86; no protein detected in homozygous FT patient cells; increased levels of phosphatidylserine and FT decreased levels of lysophosphatidylserine in homozygous FT patient cells, indicating loss of function in FT phosphatidylserine catabolism)" FT /evidence="ECO:0000269|PubMed:34489854" FT /id="VAR_086886" FT VARIANT 118 FT /note="R -> H (in SPG86)" FT /evidence="ECO:0000269|PubMed:34587489" FT /id="VAR_086887" FT VARIANT 121 FT /note="N -> I (in SPG86; unknown pathological FT significance)" FT /evidence="ECO:0000269|PubMed:34587489" FT /id="VAR_086888" FT VARIANT 252 FT /note="R -> Q (in SPG86; unknown pathological FT significance)" FT /evidence="ECO:0000269|PubMed:34587489" FT /id="VAR_086889" FT VARIANT 279..558 FT /note="Missing (in SPG86)" FT /evidence="ECO:0000269|PubMed:34866177" FT /id="VAR_086890" FT VARIANT 409 FT /note="L -> R (in SPG86; unknown pathological FT significance)" FT /evidence="ECO:0000269|PubMed:34587489" FT /id="VAR_086891" FT VARIANT 445..558 FT /note="Missing (in SPG86)" FT /evidence="ECO:0000269|PubMed:34587489" FT /id="VAR_086892" FT VARIANT 457 FT /note="R -> Q (in SPG86; no protein detected in homozygous FT patient cells; increased levels of phosphatidylserine and FT decreased levels of lysophosphatidylserine in homozygous FT patient cells, indicating loss of function in FT phosphatidylserine catabolism)" FT /evidence="ECO:0000269|PubMed:34489854" FT /id="VAR_086893" FT CONFLICT 27 FT /note="A -> V (in Ref. 1; AAG22475)" FT /evidence="ECO:0000305" SQ SEQUENCE 558 AA; 63243 MW; BC46EDA0725D44EA CRC64; MAKLLSCVLG PRLYKIYRER DSERAPASVP ETPTAVTAPH SSSWDTYYQP RALEKHADSI LALASVFWSI SYYSSPFAFF YLYRKGYLSL SKVVPFSHYA GTLLLLLAGV ACLRGIGRWT NPQYRQFITI LEATHRNQSS ENKRQLANYN FDFRSWPVDF HWEEPSSRKE SRGGPSRRGV ALLRPEPLHR GTADTLLNRV KKLPCQITSY LVAHTLGRRM LYPGSVYLLQ KALMPVLLQG QARLVEECNG RRAKLLACDG NEIDTMFVDR RGTAEPQGQK LVICCEGNAG FYEVGCVSTP LEAGYSVLGW NHPGFAGSTG VPFPQNEANA MDVVVQFAIH RLGFQPQDII IYAWSIGGFT ATWAAMSYPD VSAMILDASF DDLVPLALKV MPDSWRGLVT RTVRQHLNLN NAEQLCRYQG PVLLIRRTKD EIITTTVPED IMSNRGNDLL LKLLQHRYPR VMAEEGLRVV RQWLEASSQL EEASIYSRWE VEEDWCLSVL RSYQAEHGPD FPWSVGEDMS ADGRRQLALF LARKHLHNFE ATHCTPLPAQ NFQMPWHL //