ABHGA_HUMAN
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 03-AUG-2022, entry version 183.
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).
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 -!- SIMILARITY: Belongs to the AB hydrolase superfamily. ABHD16 family.
CC {ECO:0000305}.
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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 PRIDE; 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 CTD; 7920; -.
DR DisGeNET; 7920; -.
DR GeneCards; ABHD16A; -.
DR HGNC; HGNC:13921; ABHD16A.
DR HPA; ENSG00000204427; Low tissue specificity.
DR MIM; 142620; gene.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; PTHR12277:SF54; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Hydrolase;
KW Lipid metabolism; Membrane; Reference proteome; Transmembrane;
KW 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 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
