ID ABHD3_HUMAN Reviewed; 409 AA. AC Q8WU67; B0YIV0; B7Z5C2; O43411; DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot. DT 20-MAR-2007, sequence version 2. DT 27-MAR-2024, entry version 148. DE RecName: Full=Phospholipase ABHD3 {ECO:0000305}; DE EC=3.1.1.32 {ECO:0000250|UniProtKB:Q91ZH7}; DE EC=3.1.1.4 {ECO:0000250|UniProtKB:Q91ZH7}; DE AltName: Full=Abhydrolase domain-containing protein 3 {ECO:0000305}; GN Name=ABHD3 {ECO:0000312|HGNC:HGNC:18718}; 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). RC TISSUE=Brain; RA Yu W., Sarginson J., Gibbs R.A.; RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). 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 [GENOMIC DNA]. RG NHLBI resequencing and genotyping service (RS&G); RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16177791; DOI=10.1038/nature03983; RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D., RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J., RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L., RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K., RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.; RT "DNA sequence and analysis of human chromosome 18."; RL Nature 437:551-555(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT CYS-3. RC TISSUE=Lung; 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). CC -!- FUNCTION: Phospholipase that may play a role in phospholipids CC remodeling. May selectively cleave myristate (C14)-containing CC phosphatidylcholines through its predominant phospholipase 1 activity, CC cleaving preferentially acyl groups in sn1 position. In parallel, may CC have a minor phospholipase 2 activity acting on acyl groups in position CC sn2. In addition to (C14)-containing phosphatidylcholines, may also act CC on other medium-chain-containing and oxidatively truncated CC phospholipids. {ECO:0000250|UniProtKB:Q91ZH7}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn- CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; CC Evidence={ECO:0000250|UniProtKB:Q91ZH7}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802; CC Evidence={ECO:0000250|UniProtKB:Q91ZH7}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn- CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, CC ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32; CC Evidence={ECO:0000250|UniProtKB:Q91ZH7}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18690; CC Evidence={ECO:0000250|UniProtKB:Q91ZH7}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-tetradecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3- CC phosphocholine + H2O = 2-(9Z,12Z-octadecadienoyl)-sn-glycero-3- CC phosphocholine + H(+) + tetradecanoate; Xref=Rhea:RHEA:54388, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807, CC ChEBI:CHEBI:76084, ChEBI:CHEBI:86094; CC Evidence={ECO:0000250|UniProtKB:Q91ZH7}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54389; CC Evidence={ECO:0000250|UniProtKB:Q91ZH7}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-tetradecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3- CC phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-tetradecanoyl- CC sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:54392, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, CC ChEBI:CHEBI:64489, ChEBI:CHEBI:86094; CC Evidence={ECO:0000250|UniProtKB:Q91ZH7}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54393; CC Evidence={ECO:0000250|UniProtKB:Q91ZH7}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-tetradecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero- CC 3-phosphocholine + H2O = 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn- CC glycero-3-phosphocholine + H(+) + tetradecanoate; CC Xref=Rhea:RHEA:54396, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30807, ChEBI:CHEBI:76079, ChEBI:CHEBI:86102; CC Evidence={ECO:0000250|UniProtKB:Q91ZH7}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54397; CC Evidence={ECO:0000250|UniProtKB:Q91ZH7}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-tetradecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn- CC glycero-3-phosphocholine + H2O = 2-(4Z,7Z,10Z,13Z,16Z,19Z- CC docosahexaenoyl)-sn-glycero-3-phosphocholine + H(+) + tetradecanoate; CC Xref=Rhea:RHEA:54400, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30807, ChEBI:CHEBI:76085, ChEBI:CHEBI:86162; CC Evidence={ECO:0000250|UniProtKB:Q91ZH7}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54401; CC Evidence={ECO:0000250|UniProtKB:Q91ZH7}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2-ditetradecanoyl-sn-glycero-3-phosphocholine + H2O = 2- CC tetradecanoyl-sn-glycero-3-phosphocholine + H(+) + tetradecanoate; CC Xref=Rhea:RHEA:54404, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30807, ChEBI:CHEBI:45240, ChEBI:CHEBI:131738; CC Evidence={ECO:0000250|UniProtKB:Q91ZH7}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54405; CC Evidence={ECO:0000250|UniProtKB:Q91ZH7}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-octadecanoyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1- CC octadecanoyl-sn-glycero-3-phosphocholine + acetate + H(+); CC Xref=Rhea:RHEA:54408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30089, ChEBI:CHEBI:73858, ChEBI:CHEBI:75220; CC Evidence={ECO:0000250|UniProtKB:Q91ZH7}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54409; CC Evidence={ECO:0000250|UniProtKB:Q91ZH7}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2-ditetradecanoyl-sn-glycero-3-phosphocholine + H2O = 1- CC tetradecanoyl-sn-glycero-3-phosphocholine + H(+) + tetradecanoate; CC Xref=Rhea:RHEA:54456, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30807, ChEBI:CHEBI:45240, ChEBI:CHEBI:64489; CC Evidence={ECO:0000250|UniProtKB:Q91ZH7}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54457; CC Evidence={ECO:0000250|UniProtKB:Q91ZH7}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-octadecanoyl-2-pentanoyl-sn-glycero-3-phosphocholine + H2O = CC 1-octadecanoyl-sn-glycero-3-phosphocholine + H(+) + pentanoate; CC Xref=Rhea:RHEA:54460, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:31011, ChEBI:CHEBI:73858, ChEBI:CHEBI:138211; CC Evidence={ECO:0000250|UniProtKB:Q91ZH7}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54461; CC Evidence={ECO:0000250|UniProtKB:Q91ZH7}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-octadecanoyl-2-hexanoyl-sn-glycero-3-phosphocholine + H2O = CC 1-octadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexanoate; CC Xref=Rhea:RHEA:54464, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17120, ChEBI:CHEBI:73858, ChEBI:CHEBI:138212; CC Evidence={ECO:0000250|UniProtKB:Q91ZH7}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54465; CC Evidence={ECO:0000250|UniProtKB:Q91ZH7}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-octadecanoyl-2-octanoyl-sn-glycero-3-phosphocholine + H2O = CC 1-octadecanoyl-sn-glycero-3-phosphocholine + H(+) + octanoate; CC Xref=Rhea:RHEA:54468, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:25646, ChEBI:CHEBI:73858, ChEBI:CHEBI:138213; CC Evidence={ECO:0000250|UniProtKB:Q91ZH7}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54469; CC Evidence={ECO:0000250|UniProtKB:Q91ZH7}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-octadecanoyl-2-nonanoyl-sn-glycero-3-phosphocholine + H2O = CC 1-octadecanoyl-sn-glycero-3-phosphocholine + H(+) + nonanoate; CC Xref=Rhea:RHEA:54472, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:32361, ChEBI:CHEBI:73858, ChEBI:CHEBI:138214; CC Evidence={ECO:0000250|UniProtKB:Q91ZH7}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54473; CC Evidence={ECO:0000250|UniProtKB:Q91ZH7}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-O-hexadecyl-2-nonadioyl-sn-glycero-3-phosphocholine + H2O = CC 1-O-hexadecyl-sn-glycero-3-phosphocholine + H(+) + nonanedioate; CC Xref=Rhea:RHEA:54552, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:64496, ChEBI:CHEBI:78208, ChEBI:CHEBI:138269; CC Evidence={ECO:0000250|UniProtKB:Q91ZH7}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54553; CC Evidence={ECO:0000250|UniProtKB:Q91ZH7}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-nonadioyl-sn-glycero-3-phosphocholine + H2O = CC 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + nonanedioate; CC Xref=Rhea:RHEA:41388, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:72998, ChEBI:CHEBI:78207, ChEBI:CHEBI:78208; CC Evidence={ECO:0000250|UniProtKB:Q91ZH7}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41389; CC Evidence={ECO:0000250|UniProtKB:Q91ZH7}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-(9-oxononanoyl)-sn-glycero-3-phosphocholine + CC H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + 9-oxononanoate + CC H(+); Xref=Rhea:RHEA:41179, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:61042, ChEBI:CHEBI:72998, ChEBI:CHEBI:77812; CC Evidence={ECO:0000250|UniProtKB:Q91ZH7}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41180; CC Evidence={ECO:0000250|UniProtKB:Q91ZH7}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-(5-oxopentanoyl)-sn-glycero-3-phosphocholine CC + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + 5-oxopentanoate CC + H(+); Xref=Rhea:RHEA:40483, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16120, ChEBI:CHEBI:72998, ChEBI:CHEBI:77890; CC Evidence={ECO:0000250|UniProtKB:Q91ZH7}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40484; CC Evidence={ECO:0000250|UniProtKB:Q91ZH7}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-glutaroyl-sn-glycero-3-phosphocholine + H2O = CC 1-hexadecanoyl-sn-glycero-3-phosphocholine + glutarate + H(+); CC Xref=Rhea:RHEA:41159, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30921, ChEBI:CHEBI:72998, ChEBI:CHEBI:77756; CC Evidence={ECO:0000250|UniProtKB:Q91ZH7}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41160; CC Evidence={ECO:0000250|UniProtKB:Q91ZH7}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1- CC O-hexadecyl-sn-glycero-3-phosphocholine + acetate + H(+); CC Xref=Rhea:RHEA:40479, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30089, ChEBI:CHEBI:44811, ChEBI:CHEBI:64496; CC Evidence={ECO:0000250|UniProtKB:Q91ZH7}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40480; CC Evidence={ECO:0000250|UniProtKB:Q91ZH7}; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II CC membrane protein {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8WU67-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8WU67-2; Sequence=VSP_056137, VSP_056138; CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase 4 CC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC19155.1; Type=Erroneous initiation; Evidence={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; AF007152; AAC19155.1; ALT_INIT; mRNA. DR EMBL; AK298728; BAH12858.1; -; mRNA. DR EMBL; EF444943; ACA05928.1; -; Genomic_DNA. DR EMBL; AC106037; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471088; EAX01131.1; -; Genomic_DNA. DR EMBL; BC021196; AAH21196.1; -; mRNA. DR CCDS; CCDS32802.1; -. [Q8WU67-1] DR RefSeq; NP_001295185.1; NM_001308256.1. DR RefSeq; NP_001295186.1; NM_001308257.1. DR RefSeq; NP_612213.2; NM_138340.4. [Q8WU67-1] DR AlphaFoldDB; Q8WU67; -. DR BioGRID; 128149; 28. DR IntAct; Q8WU67; 5. DR MINT; Q8WU67; -. DR STRING; 9606.ENSP00000289119; -. DR ESTHER; human-ABHD3; abh_upf0017. DR iPTMnet; Q8WU67; -. DR PhosphoSitePlus; Q8WU67; -. DR BioMuta; ABHD3; -. DR DMDM; 134035377; -. DR EPD; Q8WU67; -. DR jPOST; Q8WU67; -. DR MassIVE; Q8WU67; -. DR MaxQB; Q8WU67; -. DR PaxDb; 9606-ENSP00000289119; -. DR PeptideAtlas; Q8WU67; -. DR ProteomicsDB; 74636; -. [Q8WU67-1] DR Pumba; Q8WU67; -. DR Antibodypedia; 2532; 132 antibodies from 24 providers. DR DNASU; 171586; -. DR Ensembl; ENST00000289119.7; ENSP00000289119.2; ENSG00000158201.10. [Q8WU67-1] DR Ensembl; ENST00000577891.1; ENSP00000463365.1; ENSG00000158201.10. [Q8WU67-2] DR GeneID; 171586; -. DR KEGG; hsa:171586; -. DR MANE-Select; ENST00000289119.7; ENSP00000289119.2; NM_138340.5; NP_612213.2. DR UCSC; uc002ktl.2; human. [Q8WU67-1] DR AGR; HGNC:18718; -. DR CTD; 171586; -. DR DisGeNET; 171586; -. DR GeneCards; ABHD3; -. DR HGNC; HGNC:18718; ABHD3. DR HPA; ENSG00000158201; Low tissue specificity. DR MIM; 612197; gene. DR neXtProt; NX_Q8WU67; -. DR OpenTargets; ENSG00000158201; -. DR PharmGKB; PA38659; -. DR VEuPathDB; HostDB:ENSG00000158201; -. DR eggNOG; KOG1838; Eukaryota. DR GeneTree; ENSGT00950000182902; -. DR HOGENOM; CLU_032487_4_0_1; -. DR InParanoid; Q8WU67; -. DR OMA; LDWHGPH; -. DR OrthoDB; 3665677at2759; -. DR PhylomeDB; Q8WU67; -. DR TreeFam; TF313195; -. DR PathwayCommons; Q8WU67; -. DR Reactome; R-HSA-1483191; Synthesis of PC. DR SignaLink; Q8WU67; -. DR BioGRID-ORCS; 171586; 24 hits in 1158 CRISPR screens. DR ChiTaRS; ABHD3; human. DR GenomeRNAi; 171586; -. DR Pharos; Q8WU67; Tbio. DR PRO; PR:Q8WU67; -. DR Proteomes; UP000005640; Chromosome 18. DR RNAct; Q8WU67; Protein. DR Bgee; ENSG00000158201; Expressed in jejunal mucosa and 191 other cell types or tissues. DR ExpressionAtlas; Q8WU67; baseline and differential. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC. DR GO; GO:0008126; F:acetylesterase activity; IBA:GO_Central. DR GO; GO:0047372; F:acylglycerol lipase activity; IBA:GO_Central. DR GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC. DR GO; GO:0008970; F:phospholipase A1 activity; IMP:UniProtKB. DR GO; GO:0004623; F:phospholipase A2 activity; IMP:UniProtKB. DR GO; GO:0051792; P:medium-chain fatty acid biosynthetic process; IBA:GO_Central. DR GO; GO:0051793; P:medium-chain fatty acid catabolic process; IBA:GO_Central. DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; TAS:Reactome. DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IMP:UniProtKB. DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR000073; AB_hydrolase_1. DR InterPro; IPR000952; AB_hydrolase_4_CS. DR InterPro; IPR012020; ABHD4. DR PANTHER; PTHR10794; ABHYDROLASE DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR10794:SF50; PHOSPHOLIPASE ABHD3; 1. DR Pfam; PF00561; Abhydrolase_1; 1. DR PIRSF; PIRSF005211; Ab_hydro_YheT; 1. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1. DR PROSITE; PS01133; UPF0017; 1. DR Genevisible; Q8WU67; HS. PE 2: Evidence at transcript level; KW Alternative splicing; Hydrolase; Lipid metabolism; Membrane; KW Phospholipid metabolism; Reference proteome; Serine esterase; KW Signal-anchor; Transmembrane; Transmembrane helix. FT CHAIN 1..409 FT /note="Phospholipase ABHD3" FT /id="PRO_0000280208" FT TRANSMEM 26..46 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT DOMAIN 140..233 FT /note="AB hydrolase-1" FT /evidence="ECO:0000255" FT ACT_SITE 220 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT ACT_SITE 346 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT ACT_SITE 375 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT VAR_SEQ 56..136 FT /note="PQLVTGGESFSRFLQDHCPVVTETYYPTVWCWEGRGQTLLRPFITSKPPVQY FT RNELIKTADGGQISLDWFDNDNSTCYMDA -> RTTRRSGAGRVEDRPCLDLSSLRSPR FT CSTGMNLLKLQMEDRFHWTGLIMITVRVIWMPAPDLLSYCCLASREQARSHISFI (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056137" FT VAR_SEQ 137..409 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056138" FT VARIANT 3 FT /note="R -> C (in dbSNP:rs17851878)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_031089" SQ SEQUENCE 409 AA; 46009 MW; 9A3920EB7528273B CRC64; MQRLAMDLRM LSRELSLYLE HQVRVGFFGS GVGLSLILGF SVAYAFYYLS SIAKKPQLVT GGESFSRFLQ DHCPVVTETY YPTVWCWEGR GQTLLRPFIT SKPPVQYRNE LIKTADGGQI SLDWFDNDNS TCYMDASTRP TILLLPGLTG TSKESYILHM IHLSEELGYR CVVFNNRGVA GENLLTPRTY CCANTEDLET VIHHVHSLYP SAPFLAAGVS MGGMLLLNYL GKIGSKTPLM AAATFSVGWN TFACSESLEK PLNWLLFNYY LTTCLQSSVN KHRHMFVKQV DMDHVMKAKS IREFDKRFTS VMFGYQTIDD YYTDASPSPR LKSVGIPVLC LNSVDDVFSP SHAIPIETAK QNPNVALVLT SYGGHIGFLE GIWPRQSTYM DRVFKQFVQA MVEHGHELS //