ABHD3_HUMAN
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 03-AUG-2022, entry version 139.
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};
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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; Q8WU67; -.
DR PeptideAtlas; Q8WU67; -.
DR PRIDE; Q8WU67; -.
DR ProteomicsDB; 74636; -. [Q8WU67-1]
DR Antibodypedia; 2532; 127 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 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; RNDPFVP; -.
DR OrthoDB; 1162019at2759; -.
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 1080 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 190 other tissues.
DR ExpressionAtlas; Q8WU67; baseline and differential.
DR Genevisible; Q8WU67; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0034338; F:short-chain carboxylesterase activity; IBA:GO_Central.
DR GO; GO:0044255; P:cellular lipid metabolic process; IBA:GO_Central.
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; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR000952; AB_hydrolase_4_CS.
DR InterPro; IPR012020; ABHD4.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF005211; Ab_hydro_YheT; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS01133; UPF0017; 1.
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
