ID ABD12_HUMAN Reviewed; 398 AA. AC Q8N2K0; A6NED4; A6NJ90; A8K450; B4DE71; Q5T710; Q5T711; Q96CR1; Q9BX05; AC Q9NPX7; Q9UFV6; DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 28-NOV-2003, sequence version 2. DT 27-MAR-2024, entry version 175. DE RecName: Full=Lysophosphatidylserine lipase ABHD12 {ECO:0000305}; DE EC=3.1.-.- {ECO:0000269|PubMed:30237167}; DE AltName: Full=2-arachidonoylglycerol hydrolase ABHD12 {ECO:0000305}; DE AltName: Full=Abhydrolase domain-containing protein 12 {ECO:0000305}; DE Short=hABHD12 {ECO:0000303|PubMed:30237167, ECO:0000303|PubMed:30643283}; DE AltName: Full=Monoacylglycerol lipase ABHD12 {ECO:0000305}; DE EC=3.1.1.23 {ECO:0000269|PubMed:22969151, ECO:0000269|PubMed:30237167}; DE AltName: Full=Oxidized phosphatidylserine lipase ABHD12 {ECO:0000305}; DE EC=3.1.-.- {ECO:0000269|PubMed:30643283}; GN Name=ABHD12 {ECO:0000303|PubMed:20797687, GN ECO:0000312|HGNC:HGNC:15868}; GN Synonyms=C20orf22 {ECO:0000312|HGNC:HGNC:15868}; 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] (ISOFORMS 1 AND 3). RC TISSUE=Cerebellum, Kidney, and Ovarian carcinoma; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [3] 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Pancreas; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 152-398 (ISOFORM 1). RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [6] RP INVOLVEMENT IN PHARC, AND VARIANT PHARC 352-ARG--HIS-398 DEL. RX PubMed=20797687; DOI=10.1016/j.ajhg.2010.08.002; RA Fiskerstrand T., H'mida-Ben Brahim D., Johansson S., M'zahem A., RA Haukanes B.I., Drouot N., Zimmermann J., Cole A.J., Vedeler C., Bredrup C., RA Assoum M., Tazir M., Klockgether T., Hamri A., Steen V.M., Boman H., RA Bindoff L.A., Koenig M., Knappskog P.M.; RT "Mutations in ABHD12 cause the neurodegenerative disease PHARC: An inborn RT error of endocannabinoid metabolism."; RL Am. J. Hum. Genet. 87:410-417(2010). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [8] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND RP MUTAGENESIS OF SER-246; ASP-333 AND HIS-372. RX PubMed=22969151; DOI=10.1194/jlr.m030411; RA Navia-Paldanius D., Savinainen J.R., Laitinen J.T.; RT "Biochemical and pharmacological characterization of human alpha/beta- RT hydrolase domain containing 6 (ABHD6) and 12 (ABHD12)."; RL J. Lipid Res. 53:2413-2424(2012). RN [9] RP INVOLVEMENT IN PHARC, AND VARIANT PHARC 65-ARG--HIS-398 DEL. RX PubMed=22938382; DOI=10.1186/1750-1172-7-59; RA Eisenberger T., Slim R., Mansour A., Nauck M., Nurnberg G., Nurnberg P., RA Decker C., Dafinger C., Ebermann I., Bergmann C., Bolz H.J.; RT "Targeted next-generation sequencing identifies a homozygous nonsense RT mutation in ABHD12, the gene underlying PHARC, in a family clinically RT diagnosed with Usher syndrome type 3."; RL Orphanet J. Rare Dis. 7:59-59(2012). RN [10] RP FUNCTION, INVOLVEMENT IN PHARC, AND VARIANT PHARC 377-LYS--HIS-398 DEL. RX PubMed=24027063; DOI=10.1002/humu.22437; RA Chen D.H., Naydenov A., Blankman J.L., Mefford H.C., Davis M., Sul Y., RA Barloon A.S., Bonkowski E., Wolff J., Matsushita M., Smith C., RA Cravatt B.F., Mackie K., Raskind W.H., Stella N., Bird T.D.; RT "Two novel mutations in ABHD12: expansion of the mutation spectrum in PHARC RT and assessment of their functional effects."; RL Hum. Mutat. 34:1672-1678(2013). RN [11] RP ACTIVITY REGULATION. RX PubMed=24879289; DOI=10.1371/journal.pone.0098286; RA Parkkari T., Haavikko R., Laitinen T., Navia-Paldanius D., Rytilahti R., RA Vaara M., Lehtonen M., Alakurtti S., Yli-Kauhaluoma J., Nevalainen T., RA Savinainen J.R., Laitinen J.T.; RT "Discovery of triterpenoids as reversible inhibitors of alpha/beta- RT hydrolase domain containing 12 (ABHD12)."; RL PLoS ONE 9:E98286-E98286(2014). RN [12] RP FUNCTION, AND CATALYTIC ACTIVITY. 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 [13] RP INVOLVEMENT IN PHARC. RX PubMed=25743180; DOI=10.1177/0003489415574513; RA Yoshimura H., Hashimoto T., Murata T., Fukushima K., Sugaya A., RA Nishio S.Y., Usami S.; RT "Novel ABHD12 mutations in PHARC patients: the differential diagnosis of RT deaf-blindness."; RL Ann. Otol. Rhinol. Laryngol. 124:77-83(2015). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [15] RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, GLYCOSYLATION, AND RP MUTAGENESIS OF SER-246. RX PubMed=30237167; DOI=10.1074/jbc.ra118.005640; RA Joshi A., Shaikh M., Singh S., Rajendran A., Mhetre A., Kamat S.S.; RT "Biochemical characterization of the PHARC-associated serine hydrolase RT ABHD12 reveals its preference for very-long-chain lipids."; RL J. Biol. Chem. 293:16953-16963(2018). RN [16] RP INVOLVEMENT IN PHARC. RX PubMed=29571850; DOI=10.1016/j.jns.2018.02.021; RA Frasquet M., Lupo V., Chumillas M.J., Vazquez-Costa J.F., Espinos C., RA Sevilla T.; RT "Phenotypical features of two patients diagnosed with PHARC syndrome and RT carriers of a new homozygous mutation in the ABHD12 gene."; RL J. Neurol. Sci. 387:134-138(2018). RN [17] RP FUNCTION, AND ACTIVITY REGULATION. RX PubMed=30420694; DOI=10.1038/s41589-018-0155-8; RA Ogasawara D., Ichu T.A., Vartabedian V.F., Benthuysen J., Jing H., Reed A., RA Ulanovskaya O.A., Hulce J.J., Roberts A., Brown S., Rosen H., Teijaro J.R., RA Cravatt B.F.; RT "Selective blockade of the lyso-PS lipase ABHD12 stimulates immune RT responses in vivo."; RL Nat. Chem. Biol. 14:1099-1108(2018). RN [18] RP FUNCTION, AND ACTIVITY REGULATION. RX PubMed=30720278; DOI=10.1021/acs.jmedchem.8b01958; RA Ogasawara D., Ichu T.A., Jing H., Hulce J.J., Reed A., Ulanovskaya O.A., RA Cravatt B.F.; RT "Discovery and optimization of selective and in vivo active inhibitors of RT the lysophosphatidylserine lipase alpha/beta-hydrolase domain-containing 12 RT (ABHD12)."; RL J. Med. Chem. 62:1643-1656(2019). RN [19] RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF SER-246. RX PubMed=30643283; DOI=10.1038/s41589-018-0195-0; RA Kelkar D.S., Ravikumar G., Mehendale N., Singh S., Joshi A., Sharma A.K., RA Mhetre A., Rajendran A., Chakrapani H., Kamat S.S.; RT "A chemical-genetic screen identifies ABHD12 as an oxidized- RT phosphatidylserine lipase."; RL Nat. Chem. Biol. 15:169-178(2019). RN [20] RP VARIANTS PHARC 159-TRP--HIS-398 DEL; PRO-186; ILE-202 AND GLN-372. RX PubMed=24697911; DOI=10.1016/j.ophtha.2014.02.008; RA Nishiguchi K.M., Avila-Fernandez A., van Huet R.A., Corton M., RA Perez-Carro R., Martin-Garrido E., Lopez-Molina M.I., Blanco-Kelly F., RA Hoefsloot L.H., van Zelst-Stams W.A., Garcia-Ruiz P.J., Del Val J., RA Di Gioia S.A., Klevering B.J., van de Warrenburg B.P., Vazquez C., RA Cremers F.P., Garcia-Sandoval B., Hoyng C.B., Collin R.W., Rivolta C., RA Ayuso C.; RT "Exome sequencing extends the phenotypic spectrum for ABHD12 mutations: RT from syndromic to nonsyndromic retinal degeneration."; RL Ophthalmology 121:1620-1627(2014). RN [21] RP VARIANT PHARC ARG-253, AND CHARACTERIZATION OF VARIANTS PHARC ILE-202; RP ARG-253 AND 352-ARG--HIS-398 DEL. RX PubMed=27890673; DOI=10.1016/j.nbd.2016.11.008; RA Tingaud-Sequeira A., Raldua D., Lavie J., Mathieu G., Bordier M., RA Knoll-Gellida A., Rambeau P., Coupry I., Andre M., Malm E., Moeller C., RA Andreasson S., Rendtorff N.D., Tranebjaerg L., Koenig M., Lacombe D., RA Goizet C., Babin P.J.; RT "Functional validation of ABHD12 mutations in the neurodegenerative disease RT PHARC."; RL Neurobiol. Dis. 98:36-51(2017). CC -!- FUNCTION: Lysophosphatidylserine (LPS) lipase that mediates the CC hydrolysis of lysophosphatidylserine, a class of signaling lipids that CC regulates immunological and neurological processes (PubMed:25290914, CC PubMed:30237167, PubMed:30420694, PubMed:30720278, PubMed:30643283). CC Represents a major lysophosphatidylserine lipase in the brain, thereby CC playing a key role in the central nervous system (By similarity). Also CC able to hydrolyze oxidized phosphatidylserine; oxidized CC phosphatidylserine is produced in response to severe inflammatory CC stress and constitutes a proapoptotic 'eat me' signal CC (PubMed:30643283). Also has monoacylglycerol (MAG) lipase activity: CC hydrolyzes 2-arachidonoylglycerol (2-AG), thereby acting as a regulator CC of endocannabinoid signaling pathways (PubMed:22969151, CC PubMed:24027063). Has a strong preference for very-long-chain lipid CC substrates; substrate specificity is likely due to improved catalysis CC and not improved substrate binding (PubMed:30237167). CC {ECO:0000250|UniProtKB:Q99LR1, ECO:0000269|PubMed:22969151, CC ECO:0000269|PubMed:24027063, ECO:0000269|PubMed:25290914, CC ECO:0000269|PubMed:30237167, ECO:0000269|PubMed:30420694, CC ECO:0000269|PubMed:30643283, ECO:0000269|PubMed:30720278}. CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O = CC (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-L-serine; CC Xref=Rhea:RHEA:40499, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30823, ChEBI:CHEBI:64765, ChEBI:CHEBI:74617; CC Evidence={ECO:0000269|PubMed:25290914, ECO:0000269|PubMed:30237167}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40500; CC Evidence={ECO:0000269|PubMed:25290914, ECO:0000269|PubMed:30237167}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) + CC H2O = (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-(1'-sn- CC glycerol); Xref=Rhea:RHEA:44584, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:64717, CC ChEBI:CHEBI:72828; Evidence={ECO:0000250|UniProtKB:Q99LR1}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1D-myo-inositol) + CC H2O = (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-1D-myo- CC inositol; Xref=Rhea:RHEA:44588, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30823, ChEBI:CHEBI:58444, ChEBI:CHEBI:78762; CC Evidence={ECO:0000250|UniProtKB:Q99LR1}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + H2O = CC (9Z)-octadecenoate + H(+) + sn-glycero-3-phosphoethanolamine; CC Xref=Rhea:RHEA:40895, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30823, ChEBI:CHEBI:74971, ChEBI:CHEBI:143890; CC Evidence={ECO:0000250|UniProtKB:Q99LR1}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = 1-(9Z- CC octadecenoyl)-sn-glycerol + H(+) + phosphocholine; CC Xref=Rhea:RHEA:41091, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:28610, ChEBI:CHEBI:75757, ChEBI:CHEBI:295975; CC Evidence={ECO:0000250|UniProtKB:Q99LR1}; 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:22969151, CC ECO:0000269|PubMed:30237167}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38492; CC Evidence={ECO:0000269|PubMed:22969151, ECO:0000269|PubMed:30237167}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-sn-glycero-3-phospho-L-serine + H2O = H(+) + CC hexadecanoate + sn-glycero-3-phospho-L-serine; Xref=Rhea:RHEA:44552, CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:64765, ChEBI:CHEBI:75020; CC Evidence={ECO:0000269|PubMed:30237167}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44553; CC Evidence={ECO:0000269|PubMed:30237167}; 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:22969151, ECO:0000269|PubMed:30237167}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26133; CC Evidence={ECO:0000269|PubMed:22969151, ECO:0000269|PubMed:30237167}; CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolyzes glycerol monoesters of long-chain fatty acids.; CC EC=3.1.1.23; Evidence={ECO:0000269|PubMed:22969151, CC ECO:0000269|PubMed:30237167}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-decanoylglycerol + H2O = decanoate + glycerol + H(+); CC Xref=Rhea:RHEA:44320, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17754, ChEBI:CHEBI:27689, ChEBI:CHEBI:75547; CC Evidence={ECO:0000269|PubMed:22969151}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44321; CC Evidence={ECO:0000269|PubMed:22969151}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-dodecanoylglycerol + H2O = dodecanoate + glycerol + H(+); CC Xref=Rhea:RHEA:44316, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17754, ChEBI:CHEBI:18262, ChEBI:CHEBI:75539; CC Evidence={ECO:0000269|PubMed:22969151}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44317; CC Evidence={ECO:0000269|PubMed:22969151}; 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:22969151}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44313; CC Evidence={ECO:0000269|PubMed:22969151}; 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:22969151, CC ECO:0000269|PubMed:30237167}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39964; CC Evidence={ECO:0000269|PubMed:22969151, ECO:0000269|PubMed:30237167}; 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:22969151, CC ECO:0000269|PubMed:30237167}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38488; CC Evidence={ECO:0000269|PubMed:22969151, ECO:0000269|PubMed:30237167}; 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:22969151}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44733; CC Evidence={ECO:0000269|PubMed:22969151}; 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:22969151, ECO:0000269|PubMed:25290914, CC ECO:0000269|PubMed:30237167}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44729; CC Evidence={ECO:0000269|PubMed:22969151, ECO:0000269|PubMed:25290914, CC ECO:0000269|PubMed:30237167}; 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:22969151, ECO:0000269|PubMed:25290914}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48429; CC Evidence={ECO:0000269|PubMed:22969151, ECO:0000269|PubMed:25290914}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoylglycerol + H2O = glycerol + H(+) + CC hexadecanoate; Xref=Rhea:RHEA:39959, ChEBI:CHEBI:7896, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, CC ChEBI:CHEBI:69081; Evidence={ECO:0000269|PubMed:30237167}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39960; CC Evidence={ECO:0000269|PubMed:30237167}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-octadecanoylglycerol + H2O = glycerol + H(+) + CC octadecanoate; Xref=Rhea:RHEA:38363, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:25629, CC ChEBI:CHEBI:75555; Evidence={ECO:0000269|PubMed:30237167}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38364; CC Evidence={ECO:0000269|PubMed:30237167}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-octadecanoyl-2-(9,10-epoxyoctadecanoyl)-sn-glycero-3- CC phospho-L-serine + H2O = 1-octadecanoyl-sn-glycero-3-phosphoserine + CC 9,10-epoxyoctadecanoate + H(+); Xref=Rhea:RHEA:59364, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:84467, CC ChEBI:CHEBI:85195, ChEBI:CHEBI:143087; CC Evidence={ECO:0000269|PubMed:30643283}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59365; CC Evidence={ECO:0000269|PubMed:30643283}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-octadecanoyl-2-(10-hydroxyoctadecanoyl)-sn-glycero-3- CC phospho-L-serine + H2O = 1-octadecanoyl-sn-glycero-3-phosphoserine + CC 10-hydroxyoctadecanoate + H(+); Xref=Rhea:RHEA:59368, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:84467, CC ChEBI:CHEBI:143088, ChEBI:CHEBI:143089; CC Evidence={ECO:0000269|PubMed:30643283}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59369; CC Evidence={ECO:0000269|PubMed:30643283}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-(10-hydroxyoctadecanoyl)-sn-glycero-3- CC phospho-L-serine + H2O = 1-hexadecanoyl-sn-glycero-3-phospho-L-serine CC + 10-hydroxyoctadecanoate + H(+); Xref=Rhea:RHEA:59372, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:75020, CC ChEBI:CHEBI:143089, ChEBI:CHEBI:143094; CC Evidence={ECO:0000269|PubMed:30643283}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59373; CC Evidence={ECO:0000269|PubMed:30643283}; CC -!- ACTIVITY REGULATION: Selectively inhibited by DO264 (N-3-pyridyl-N'-(1- CC [3-chloro-4-{2-chloro-4-(trifluoromethoxy)phenoxy}pyridine-2- CC yl]piperidin-4-yl)thiourea) (PubMed:30420694, PubMed:30720278). CC Reversibly inhibited by triterpenoids, but with rather low potency CC (PubMed:24879289). {ECO:0000269|PubMed:24879289, CC ECO:0000269|PubMed:30420694, ECO:0000269|PubMed:30720278}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=117 uM for 2-arachidonoyglycerol {ECO:0000269|PubMed:22969151}; CC Vmax=42 nmol/min/mg enzyme toward 2-arachidonoyglycerol CC {ECO:0000269|PubMed:22969151}; CC pH dependence: CC Optimum pH is 7.2-9 with 2-arachidonoyglycerol as substrate. CC {ECO:0000269|PubMed:22969151}; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:30237167}; Single-pass membrane protein CC {ECO:0000255}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q8N2K0-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8N2K0-2; Sequence=VSP_009097; CC Name=3; CC IsoId=Q8N2K0-3; Sequence=VSP_037372; CC -!- PTM: Glycosylated; glycosylation is required for optimal activity. CC {ECO:0000269|PubMed:30237167}. CC -!- DISEASE: Polyneuropathy, hearing loss, ataxia, retinitis pigmentosa, CC and cataract (PHARC) [MIM:612674]: A slowly progressive neurologic CC disorder with a variable phenotype resembling Refsum disease. Clinical CC features include sensorineural hearing loss, visual problems related to CC cataracts, retinitis pigmentosa, pes cavus, ataxic and/or spastic gait CC disturbances with a progressive sensorimotor peripheral neuropathy. CC Other features include hyporeflexia, hyperreflexia, extensor plantar CC responses. {ECO:0000269|PubMed:20797687, ECO:0000269|PubMed:22938382, CC ECO:0000269|PubMed:24027063, ECO:0000269|PubMed:24697911, CC ECO:0000269|PubMed:25743180, ECO:0000269|PubMed:27890673, CC ECO:0000269|PubMed:29571850}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the serine esterase family. {ECO:0000305}. CC -!- CAUTION: A family suffering from Polyneuropathy, hearing loss, ataxia, CC retinitis pigmentosa, and cataract (PHARC) was initially clinically CC diagnosed with Usher syndrome type 3 (PubMed:22938382). Reexamination CC of one affected member of this family revealed ataxia but not CC polyneuropathy, demonstrating the phenotypic heterogeneity in PHARC and CC the need for careful neurological assessments to distinguish this CC disease from other neuropathic disorders (PubMed:22938382). CC {ECO:0000269|PubMed:22938382}. 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; AK075023; BAC11357.1; -; mRNA. DR EMBL; AK290815; BAF83504.1; -; mRNA. DR EMBL; AK293495; BAG56982.1; -; mRNA. DR EMBL; AL121772; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL353812; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471133; EAX10089.1; -; Genomic_DNA. DR EMBL; BC014049; AAH14049.1; -; mRNA. DR EMBL; AL117442; CAB55927.1; -; mRNA. DR CCDS; CCDS13172.1; -. [Q8N2K0-2] DR CCDS; CCDS42857.1; -. [Q8N2K0-1] DR PIR; T17237; T17237. DR RefSeq; NP_001035937.1; NM_001042472.2. [Q8N2K0-1] DR RefSeq; NP_056415.1; NM_015600.4. [Q8N2K0-2] DR AlphaFoldDB; Q8N2K0; -. DR SMR; Q8N2K0; -. DR BioGRID; 117541; 121. DR IntAct; Q8N2K0; 33. DR MINT; Q8N2K0; -. DR STRING; 9606.ENSP00000365725; -. DR BindingDB; Q8N2K0; -. DR ChEMBL; CHEMBL5516; -. DR DrugCentral; Q8N2K0; -. DR GuidetoPHARMACOLOGY; 3070; -. DR SwissLipids; SLP:000001043; -. DR ESTHER; human-ABHD12; ABHD12-PHARC. DR MEROPS; S09.939; -. DR GlyConnect; 1517; 3 N-Linked glycans (1 site). DR GlyCosmos; Q8N2K0; 2 sites, 4 glycans. DR GlyGen; Q8N2K0; 2 sites, 3 N-linked glycans (1 site), 1 O-linked glycan (1 site). DR iPTMnet; Q8N2K0; -. DR PhosphoSitePlus; Q8N2K0; -. DR SwissPalm; Q8N2K0; -. DR BioMuta; ABHD12; -. DR DMDM; 38604894; -. DR EPD; Q8N2K0; -. DR jPOST; Q8N2K0; -. DR MassIVE; Q8N2K0; -. DR MaxQB; Q8N2K0; -. DR PaxDb; 9606-ENSP00000365725; -. DR PeptideAtlas; Q8N2K0; -. DR ProteomicsDB; 71711; -. [Q8N2K0-1] DR ProteomicsDB; 71712; -. [Q8N2K0-2] DR ProteomicsDB; 71713; -. [Q8N2K0-3] DR Pumba; Q8N2K0; -. DR Antibodypedia; 10033; 200 antibodies from 29 providers. DR DNASU; 26090; -. DR Ensembl; ENST00000339157.10; ENSP00000341408.5; ENSG00000100997.20. [Q8N2K0-1] DR Ensembl; ENST00000376542.8; ENSP00000365725.3; ENSG00000100997.20. [Q8N2K0-2] DR GeneID; 26090; -. DR KEGG; hsa:26090; -. DR MANE-Select; ENST00000339157.10; ENSP00000341408.5; NM_001042472.3; NP_001035937.1. DR UCSC; uc002wuq.4; human. [Q8N2K0-1] DR AGR; HGNC:15868; -. DR CTD; 26090; -. DR DisGeNET; 26090; -. DR GeneCards; ABHD12; -. DR GeneReviews; ABHD12; -. DR HGNC; HGNC:15868; ABHD12. DR HPA; ENSG00000100997; Low tissue specificity. DR MalaCards; ABHD12; -. DR MIM; 612674; phenotype. DR MIM; 613599; gene. DR neXtProt; NX_Q8N2K0; -. DR OpenTargets; ENSG00000100997; -. DR Orphanet; 171848; Polyneuropathy-hearing loss-ataxia-retinitis pigmentosa-cataract syndrome. DR PharmGKB; PA25738; -. DR VEuPathDB; HostDB:ENSG00000100997; -. DR eggNOG; KOG1552; Eukaryota. DR GeneTree; ENSGT00940000160517; -. DR HOGENOM; CLU_029375_1_0_1; -. DR InParanoid; Q8N2K0; -. DR OMA; VEFHRFE; -. DR OrthoDB; 47056at2759; -. DR PhylomeDB; Q8N2K0; -. DR TreeFam; TF315122; -. DR PathwayCommons; Q8N2K0; -. DR Reactome; R-HSA-426048; Arachidonate production from DAG. DR SignaLink; Q8N2K0; -. DR BioGRID-ORCS; 26090; 18 hits in 1159 CRISPR screens. DR ChiTaRS; ABHD12; human. DR GenomeRNAi; 26090; -. DR Pharos; Q8N2K0; Tchem. DR PRO; PR:Q8N2K0; -. DR Proteomes; UP000005640; Chromosome 20. DR RNAct; Q8N2K0; Protein. DR Bgee; ENSG00000100997; Expressed in C1 segment of cervical spinal cord and 184 other cell types or tissues. DR ExpressionAtlas; Q8N2K0; baseline and differential. DR GO; GO:0032281; C:AMPA glutamate receptor complex; IEA:Ensembl. DR GO; GO:0032839; C:dendrite cytoplasm; IEA:Ensembl. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0047372; F:acylglycerol lipase activity; IDA:UniProtKB. DR GO; GO:0004622; F:lysophospholipase activity; IDA:UniProtKB. DR GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; IEA:Ensembl. DR GO; GO:0004620; F:phospholipase activity; IDA:UniProtKB. DR GO; GO:0046464; P:acylglycerol catabolic process; IDA:UniProtKB. DR GO; GO:0007628; P:adult walking behavior; IEA:Ensembl. DR GO; GO:0019369; P:arachidonic acid metabolic process; TAS:Reactome. DR GO; GO:0046475; P:glycerophospholipid catabolic process; IDA:BHF-UCL. DR GO; GO:0052651; P:monoacylglycerol catabolic process; IDA:UniProtKB. DR GO; GO:0006660; P:phosphatidylserine catabolic process; IDA:UniProtKB. DR GO; GO:0009395; P:phospholipid catabolic process; IDA:UniProtKB. DR GO; GO:0050727; P:regulation of inflammatory response; IEA:Ensembl. DR GO; GO:0010996; P:response to auditory stimulus; IEA:Ensembl. DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR000073; AB_hydrolase_1. DR PANTHER; PTHR12277; ALPHA/BETA HYDROLASE DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR12277:SF61; LYSOPHOSPHATIDYLSERINE LIPASE ABHD12; 1. DR Pfam; PF00561; Abhydrolase_1; 1. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1. DR Genevisible; Q8N2K0; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cataract; Deafness; Disease variant; KW Endoplasmic reticulum; Glycoprotein; Hydrolase; Lipid metabolism; Membrane; KW Neuropathy; Reference proteome; Retinitis pigmentosa; Transmembrane; KW Transmembrane helix. FT CHAIN 1..398 FT /note="Lysophosphatidylserine lipase ABHD12" FT /id="PRO_0000079413" FT TOPO_DOM 1..74 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:Q99LR1" FT TRANSMEM 75..95 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:Q99LR1" FT TOPO_DOM 96..398 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:Q99LR1" FT ACT_SITE 246 FT /note="Nucleophile" FT /evidence="ECO:0000305|PubMed:22969151, FT ECO:0000305|PubMed:30237167" FT ACT_SITE 333 FT /note="Charge relay system" FT /evidence="ECO:0000305|PubMed:22969151" FT ACT_SITE 372 FT /note="Charge relay system" FT /evidence="ECO:0000305|PubMed:22969151" FT CARBOHYD 123 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 11..48 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_037372" FT VAR_SEQ 387..398 FT /note="EFLGKSEPEHQH -> PQQGPGSSPDPSMWSELV (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_009097" FT VARIANT 65..398 FT /note="Missing (in PHARC)" FT /evidence="ECO:0000269|PubMed:22938382" FT /id="VAR_081587" FT VARIANT 159..398 FT /note="Missing (in PHARC; uncertain significance)" FT /evidence="ECO:0000269|PubMed:24697911" FT /id="VAR_081588" FT VARIANT 186 FT /note="R -> P (in PHARC; uncertain significance; FT dbSNP:rs587777604)" FT /evidence="ECO:0000269|PubMed:24697911" FT /id="VAR_081589" FT VARIANT 202 FT /note="T -> I (in PHARC; uncertain significance; abolished FT monoacyglycerol lipase activity)" FT /evidence="ECO:0000269|PubMed:24697911, FT ECO:0000269|PubMed:27890673" FT /id="VAR_081590" FT VARIANT 253 FT /note="T -> R (in PHARC; abolished monoacyglycerol lipase FT activity; dbSNP:rs772987424)" FT /evidence="ECO:0000269|PubMed:27890673" FT /id="VAR_081591" FT VARIANT 349 FT /note="A -> T (in dbSNP:rs746748)" FT /id="VAR_050630" FT VARIANT 352..398 FT /note="Missing (in PHARC; abolished monoacyglycerol lipase FT activity)" FT /evidence="ECO:0000269|PubMed:20797687, FT ECO:0000269|PubMed:27890673" FT /id="VAR_081592" FT VARIANT 372 FT /note="H -> Q (in PHARC; uncertain significance; FT dbSNP:rs587777602)" FT /evidence="ECO:0000269|PubMed:24697911" FT /id="VAR_081593" FT VARIANT 377..398 FT /note="Missing (in PHARC)" FT /evidence="ECO:0000269|PubMed:24027063" FT /id="VAR_081594" FT MUTAGEN 246 FT /note="S->A: Loss of lipase activity." FT /evidence="ECO:0000269|PubMed:22969151, FT ECO:0000269|PubMed:30237167, ECO:0000269|PubMed:30643283" FT MUTAGEN 333 FT /note="D->N: Loss of 2-arachidonoyglycerol hydrolase FT activity." FT /evidence="ECO:0000269|PubMed:22969151" FT MUTAGEN 372 FT /note="H->A: Loss of 2-arachidonoyglycerol hydrolase FT activity." FT /evidence="ECO:0000269|PubMed:22969151" FT CONFLICT 359 FT /note="V -> I (in Ref. 1; BAF83504)" FT /evidence="ECO:0000305" FT CONFLICT 376 FT /note="Y -> C (in Ref. 1; BAC11357)" FT /evidence="ECO:0000305" SQ SEQUENCE 398 AA; 45097 MW; E21425C1412B5607 CRC64; MRKRTEPVAL EHERCAAAGS SSSGSAAAAL DADCRLKQNL RLTGPAAAEP RCAADAGMKR ALGRRKGVWL RLRKILFCVL GLYIAIPFLI KLCPGIQAKL IFLNFVRVPY FIDLKKPQDQ GLNHTCNYYL QPEEDVTIGV WHTVPAVWWK NAQGKDQMWY EDALASSHPI ILYLHGNAGT RGGDHRVELY KVLSSLGYHV VTFDYRGWGD SVGTPSERGM TYDALHVFDW IKARSGDNPV YIWGHSLGTG VATNLVRRLC ERETPPDALI LESPFTNIRE EAKSHPFSVI YRYFPGFDWF FLDPITSSGI KFANDENVKH ISCPLLILHA EDDPVVPFQL GRKLYSIAAP ARSFRDFKVQ FVPFHSDLGY RHKYIYKSPE LPRILREFLG KSEPEHQH //