ABHD5_HUMAN
ID ABHD5_HUMAN Reviewed; 349 AA.
AC Q8WTS1; B2R9K0; Q9Y369;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=1-acylglycerol-3-phosphate O-acyltransferase ABHD5 {ECO:0000305};
DE EC=2.3.1.51 {ECO:0000269|PubMed:18606822};
DE AltName: Full=Abhydrolase domain-containing protein 5;
DE AltName: Full=Lipid droplet-binding protein CGI-58;
GN Name=ABHD5 {ECO:0000312|HGNC:HGNC:21396}; Synonyms=NCIE2; ORFNames=CGI-58;
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 [GENOMIC DNA], TISSUE SPECIFICITY, AND VARIANTS CDS
RP LYS-7; PRO-130 AND LYS-260.
RX PubMed=11590543; DOI=10.1086/324121;
RA Lefevre C., Jobard F., Caux F., Bouadjar B., Karaduman A., Heilig R.,
RA Lakhdar H., Wollenberg A., Verret J.-L., Weissenbach J., Oezguec M.,
RA Lathrop M., Prud'homme J.-F., Fischer J.;
RT "Mutations in CGI-58, the gene encoding a new protein of the
RT esterase/lipase/thioesterase subfamily, in Chanarin-Dorfman syndrome.";
RL Am. J. Hum. Genet. 69:1002-1012(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Substantia nigra;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
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].
RC TISSUE=Skin;
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 FUNCTION, AND CHARACTERIZATION OF VARIANTS CDS PRO-130 AND LYS-260.
RX PubMed=16679289; DOI=10.1016/j.cmet.2006.03.005;
RA Lass A., Zimmermann R., Haemmerle G., Riederer M., Schoiswohl G.,
RA Schweiger M., Kienesberger P., Strauss J.G., Gorkiewicz G., Zechner R.;
RT "Adipose triglyceride lipase-mediated lipolysis of cellular fat stores is
RT activated by CGI-58 and defective in Chanarin-Dorfman Syndrome.";
RL Cell Metab. 3:309-319(2006).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND INDUCTION.
RX PubMed=18832586; DOI=10.2353/ajpath.2008.080005;
RA Akiyama M., Sakai K., Takayama C., Yanagi T., Yamanaka Y., McMillan J.R.,
RA Shimizu H.;
RT "CGI-58 is an alpha/beta-hydrolase within lipid transporting lamellar
RT granules of differentiated keratinocytes.";
RL Am. J. Pathol. 173:1349-1360(2008).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND CHARACTERIZATION OF VARIANTS CDS PRO-130
RP AND LYS-260.
RX PubMed=18606822; DOI=10.1074/jbc.m801783200;
RA Ghosh A.K., Ramakrishnan G., Chandramohan C., Rajasekharan R.;
RT "CGI-58, the causative gene for Chanarin-Dorfman syndrome, mediates
RT acylation of lysophosphatidic acid.";
RL J. Biol. Chem. 283:24525-24533(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP VARIANT ARG-82.
RX PubMed=15967942; DOI=10.1001/archderm.141.6.798;
RA Schleinitz N., Fischer J., Sanchez A., Veit V., Harle J.-R.,
RA Pelissier J.-F.;
RT "Two new mutations of the ABHD5 gene in a new adult case of Chanarin
RT Dorfman syndrome: an uncommon lipid storage disease.";
RL Arch. Dermatol. 141:798-800(2005).
RN [12]
RP VARIANT CDS GLY-115.
RX PubMed=17495960; DOI=10.1038/sj.jid.5700860;
RA Ben Selma Z., Yilmaz S., Schischmanoff P.O., Blom A., Ozogul C.,
RA Laroche L., Caux F.;
RT "A novel S115G mutation of CGI-58 in a Turkish patient with Dorfman-
RT Chanarin syndrome.";
RL J. Invest. Dermatol. 127:2273-2276(2007).
CC -!- FUNCTION: Coenzyme A-dependent lysophosphatidic acid acyltransferase
CC that catalyzes the transfert of an acyl group on a lysophosphatidic
CC acid (PubMed:18606822). Functions preferentially with 1-oleoyl-
CC lysophosphatidic acid followed by 1-palmitoyl-lysophosphatidic acid, 1-
CC stearoyl-lysophosphatidic acid and 1-arachidonoyl-lysophosphatidic acid
CC as lipid acceptor. Functions preferentially with arachidonoyl-CoA
CC followed by oleoyl-CoA as acyl group donors (By similarity). Functions
CC in phosphatidic acid biosynthesis (PubMed:18606822). May regulate the
CC cellular storage of triacylglycerol through activation of the
CC phospholipase PNPLA2 (PubMed:16679289). Involved in keratinocyte
CC differentiation (PubMed:18832586). Regulates lipid droplet fusion (By
CC similarity). {ECO:0000250|UniProtKB:Q9DBL9,
CC ECO:0000269|PubMed:16679289, ECO:0000269|PubMed:18606822,
CC ECO:0000269|PubMed:18832586}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:58608; EC=2.3.1.51;
CC Evidence={ECO:0000269|PubMed:18606822};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19710;
CC Evidence={ECO:0000305|PubMed:18606822};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + hexadecanoyl-CoA
CC = 1-(9Z)-octadecenoyl-2-hexadecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37143, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74551;
CC Evidence={ECO:0000269|PubMed:18606822};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37144;
CC Evidence={ECO:0000305|PubMed:18606822};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + octadecanoyl-CoA
CC = 1-(9Z-octadecenoyl)-2-octadecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37147, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74552;
CC Evidence={ECO:0000269|PubMed:18606822};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37148;
CC Evidence={ECO:0000305|PubMed:18606822};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphate = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37131, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74546;
CC Evidence={ECO:0000269|PubMed:18606822};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37132;
CC Evidence={ECO:0000305|PubMed:18606822};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-(9Z-octadecenoyl)-sn-
CC glycero-3-phosphate = 1-(9Z)-octadecenoyl-2-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37443,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:74544,
CC ChEBI:CHEBI:74928; Evidence={ECO:0000250|UniProtKB:Q9DBL9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37444;
CC Evidence={ECO:0000250|UniProtKB:Q9DBL9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + eicosanoyl-CoA =
CC 1-(9Z)-octadecenoyl-2-eicosanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37451, ChEBI:CHEBI:57287, ChEBI:CHEBI:57380,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74937;
CC Evidence={ECO:0000250|UniProtKB:Q9DBL9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37452;
CC Evidence={ECO:0000250|UniProtKB:Q9DBL9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-phosphate
CC = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:33187, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:57518, ChEBI:CHEBI:64839;
CC Evidence={ECO:0000250|UniProtKB:Q9DBL9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33188;
CC Evidence={ECO:0000250|UniProtKB:Q9DBL9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-octadecanoyl-sn-glycero-3-phosphate
CC = 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37163, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:74560, ChEBI:CHEBI:74565;
CC Evidence={ECO:0000250|UniProtKB:Q9DBL9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37164;
CC Evidence={ECO:0000250|UniProtKB:Q9DBL9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-
CC glycero-3-phosphate = 1-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-2-(9Z)-
CC octadecenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37455,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:74938,
CC ChEBI:CHEBI:74941; Evidence={ECO:0000250|UniProtKB:Q9DBL9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37456;
CC Evidence={ECO:0000250|UniProtKB:Q9DBL9};
CC -!- ACTIVITY REGULATION: Acyltransferase activity is inhibited by
CC detergents such as Triton X-100 and 3-[(3-
CC cholamidopropyl)dimethylammonio]-1-propanesulfonate (CHAPS).
CC Acyltransferase activity is inhibited by the presence of magnesium and
CC calcium. {ECO:0000250|UniProtKB:Q9DBL9}.
CC -!- SUBUNIT: Interacts with ADRP, PLIN and PNPLA2. Interacts with PLIN5;
CC promotes interaction with PNPLA2 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q8WTS1; Q5T4B2: CERCAM; NbExp=3; IntAct=EBI-2813554, EBI-12261896;
CC Q8WTS1; P51793: CLCN4; NbExp=3; IntAct=EBI-2813554, EBI-22754239;
CC Q8WTS1; Q8NI60: COQ8A; NbExp=3; IntAct=EBI-2813554, EBI-745535;
CC Q8WTS1; Q6ZPD8: DGAT2L6; NbExp=3; IntAct=EBI-2813554, EBI-12831978;
CC Q8WTS1; Q05329: GAD2; NbExp=3; IntAct=EBI-2813554, EBI-9304251;
CC Q8WTS1; O00258: GET1; NbExp=3; IntAct=EBI-2813554, EBI-18908258;
CC Q8WTS1; P48058-2: GRIA4; NbExp=3; IntAct=EBI-2813554, EBI-17517256;
CC Q8WTS1; Q9NQG6: MIEF1; NbExp=5; IntAct=EBI-2813554, EBI-740987;
CC Q8WTS1; A6NKB5-5: PCNX2; NbExp=3; IntAct=EBI-2813554, EBI-17616589;
CC Q8WTS1; Q99541: PLIN2; NbExp=3; IntAct=EBI-2813554, EBI-2115275;
CC Q8WTS1; O60664: PLIN3; NbExp=3; IntAct=EBI-2813554, EBI-725795;
CC Q8WTS1; Q00G26: PLIN5; NbExp=3; IntAct=EBI-2813554, EBI-21732470;
CC Q8WTS1; Q8N0V3: RBFA; NbExp=3; IntAct=EBI-2813554, EBI-3232108;
CC Q8WTS1; Q9Y225-2: RNF24; NbExp=3; IntAct=EBI-2813554, EBI-13044680;
CC Q8WTS1; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-2813554, EBI-6257312;
CC Q8WTS1; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-2813554, EBI-2623095;
CC Q8WTS1; Q8N4M1-3: SLC44A3; NbExp=3; IntAct=EBI-2813554, EBI-12056955;
CC Q8WTS1; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-2813554, EBI-8638294;
CC Q8WTS1; O43399: TPD52L2; NbExp=3; IntAct=EBI-2813554, EBI-782604;
CC Q8WTS1; Q6PEW1: ZCCHC12; NbExp=3; IntAct=EBI-2813554, EBI-748373;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18832586}. Lipid
CC droplet {ECO:0000250|UniProtKB:Q9DBL9}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9DBL9}. Note=Colocalized with PLIN and ADRP on
CC the surface of lipid droplets. The localization is dependent upon the
CC metabolic status of the adipocytes and the activity of PKA (By
CC similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed in various tissues, including
CC lymphocytes, liver, skeletal muscle and brain. Expressed by upper
CC epidermal layers and dermal fibroblasts in skin, hepatocytes and
CC neurons (at protein level). {ECO:0000269|PubMed:11590543,
CC ECO:0000269|PubMed:18832586}.
CC -!- DEVELOPMENTAL STAGE: Detected in fetal epidermis from 49 to 135 days
CC estimated gestational age (at protein level).
CC {ECO:0000269|PubMed:18832586}.
CC -!- INDUCTION: Up-regulated upon keratinocyte differentiation (at protein
CC level). {ECO:0000269|PubMed:18832586}.
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity and
CC may constitute the binding site for the phosphate moiety of the
CC glycerol-3-phosphate. {ECO:0000250}.
CC -!- DISEASE: Chanarin-Dorfman syndrome (CDS) [MIM:275630]: An autosomal
CC recessive inborn error of lipid metabolism with multisystemic
CC accumulation of triglycerides although plasma concentrations are
CC normal. Clinical characteristics are congenital generalized ichthyosis,
CC vacuolated leukocytes, hepatomegaly, myopathy, cataracts, neurosensory
CC hearing loss and developmental delay. The disorder presents at birth
CC with generalized, fine, white scaling of the skin and a variable degree
CC of erythema resembling non-bullous congenital ichthyosiform
CC erythroderma. {ECO:0000269|PubMed:11590543,
CC ECO:0000269|PubMed:16679289, ECO:0000269|PubMed:17495960,
CC ECO:0000269|PubMed:18606822}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the peptidase S33 family. ABHD4/ABHD5 subfamily.
CC {ECO:0000305}.
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DR EMBL; AL606838; CAD12731.1; -; Genomic_DNA.
DR EMBL; AF151816; AAD34053.1; -; mRNA.
DR EMBL; AK313811; BAG36547.1; -; mRNA.
DR EMBL; AC105903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471055; EAW64699.1; -; Genomic_DNA.
DR EMBL; BC021958; AAH21958.1; -; mRNA.
DR CCDS; CCDS2711.1; -.
DR RefSeq; NP_057090.2; NM_016006.4.
DR AlphaFoldDB; Q8WTS1; -.
DR SMR; Q8WTS1; -.
DR BioGRID; 119288; 37.
DR IntAct; Q8WTS1; 35.
DR MINT; Q8WTS1; -.
DR STRING; 9606.ENSP00000390849; -.
DR SwissLipids; SLP:000000098; -.
DR ESTHER; human-ABHD5; CGI-58_ABHD5_ABHD4.
DR MEROPS; S33.975; -.
DR GlyGen; Q8WTS1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8WTS1; -.
DR PhosphoSitePlus; Q8WTS1; -.
DR BioMuta; ABHD5; -.
DR DMDM; 73921640; -.
DR EPD; Q8WTS1; -.
DR jPOST; Q8WTS1; -.
DR MassIVE; Q8WTS1; -.
DR MaxQB; Q8WTS1; -.
DR PaxDb; Q8WTS1; -.
DR PeptideAtlas; Q8WTS1; -.
DR PRIDE; Q8WTS1; -.
DR ProteomicsDB; 74594; -.
DR Antibodypedia; 29395; 348 antibodies from 33 providers.
DR DNASU; 51099; -.
DR Ensembl; ENST00000644371.2; ENSP00000495778.1; ENSG00000011198.10.
DR Ensembl; ENST00000649763.1; ENSP00000497701.1; ENSG00000011198.10.
DR GeneID; 51099; -.
DR KEGG; hsa:51099; -.
DR MANE-Select; ENST00000644371.2; ENSP00000495778.1; NM_016006.6; NP_057090.2.
DR UCSC; uc003cmx.4; human.
DR CTD; 51099; -.
DR DisGeNET; 51099; -.
DR GeneCards; ABHD5; -.
DR HGNC; HGNC:21396; ABHD5.
DR HPA; ENSG00000011198; Low tissue specificity.
DR MalaCards; ABHD5; -.
DR MIM; 275630; phenotype.
DR MIM; 604780; gene.
DR neXtProt; NX_Q8WTS1; -.
DR OpenTargets; ENSG00000011198; -.
DR Orphanet; 98907; Neutral lipid storage disease with ichthyosis.
DR PharmGKB; PA134891622; -.
DR VEuPathDB; HostDB:ENSG00000011198; -.
DR eggNOG; KOG4409; Eukaryota.
DR GeneTree; ENSGT00390000016277; -.
DR HOGENOM; CLU_017361_0_0_1; -.
DR InParanoid; Q8WTS1; -.
DR OMA; EQWRIDN; -.
DR OrthoDB; 1555935at2759; -.
DR PhylomeDB; Q8WTS1; -.
DR TreeFam; TF314196; -.
DR PathwayCommons; Q8WTS1; -.
DR Reactome; R-HSA-163560; Triglyceride catabolism.
DR SignaLink; Q8WTS1; -.
DR BioGRID-ORCS; 51099; 8 hits in 1074 CRISPR screens.
DR ChiTaRS; ABHD5; human.
DR GeneWiki; ABHD5; -.
DR GenomeRNAi; 51099; -.
DR Pharos; Q8WTS1; Tbio.
DR PRO; PR:Q8WTS1; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q8WTS1; protein.
DR Bgee; ENSG00000011198; Expressed in amniotic fluid and 195 other tissues.
DR ExpressionAtlas; Q8WTS1; baseline and differential.
DR Genevisible; Q8WTS1; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
DR GO; GO:0042171; F:lysophosphatidic acid acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
DR GO; GO:0010891; P:negative regulation of sequestering of triglyceride; IDA:UniProtKB.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0051006; P:positive regulation of lipoprotein lipase activity; IEA:Ensembl.
DR GO; GO:0010898; P:positive regulation of triglyceride catabolic process; IDA:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Cataract; Cytoplasm; Deafness;
KW Differentiation; Disease variant; Fatty acid metabolism; Ichthyosis;
KW Lipid biosynthesis; Lipid droplet; Lipid metabolism;
KW Phospholipid biosynthesis; Phospholipid metabolism; Phosphoprotein;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..349
FT /note="1-acylglycerol-3-phosphate O-acyltransferase ABHD5"
FT /id="PRO_0000080866"
FT DOMAIN 77..184
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT MOTIF 327..332
FT /note="HXXXXD motif"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6QA69"
FT VARIANT 7
FT /note="E -> K (in CDS; dbSNP:rs104893676)"
FT /evidence="ECO:0000269|PubMed:11590543"
FT /id="VAR_023387"
FT VARIANT 72
FT /note="I -> T (in dbSNP:rs2302349)"
FT /id="VAR_037574"
FT VARIANT 82
FT /note="H -> R (found in a patient with CDS but without
FT evidence it may cause the disease; dbSNP:rs145548259)"
FT /evidence="ECO:0000269|PubMed:15967942"
FT /id="VAR_057953"
FT VARIANT 115
FT /note="S -> G (in CDS)"
FT /evidence="ECO:0000269|PubMed:17495960"
FT /id="VAR_057954"
FT VARIANT 130
FT /note="Q -> P (in CDS; loss of PNPLA2-dependent
FT triacylclycerol hydrolysis but no effect on LPA
FT acyltransferase activity; dbSNP:rs28939077)"
FT /evidence="ECO:0000269|PubMed:11590543,
FT ECO:0000269|PubMed:16679289, ECO:0000269|PubMed:18606822"
FT /id="VAR_023388"
FT VARIANT 260
FT /note="E -> K (in CDS; loss of PNPLA2-dependent
FT triacylclycerol hydrolysis but no effect on LPA
FT acyltransferase activity; dbSNP:rs28939078)"
FT /evidence="ECO:0000269|PubMed:11590543,
FT ECO:0000269|PubMed:16679289, ECO:0000269|PubMed:18606822"
FT /id="VAR_023389"
FT CONFLICT 263
FT /note="F -> S (in Ref. 2; AAD34053)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 349 AA; 39096 MW; 85958A2DEC169C82 CRC64;
MAAEEEEVDS ADTGERSGWL TGWLPTWCPT SISHLKEAEE KMLKCVPCTY KKEPVRISNG
NKIWTLKFSH NISNKTPLVL LHGFGGGLGL WALNFGDLCT NRPVYAFDLL GFGRSSRPRF
DSDAEEVENQ FVESIEEWRC ALGLDKMILL GHNLGGFLAA AYSLKYPSRV NHLILVEPWG
FPERPDLADQ DRPIPVWIRA LGAALTPFNP LAGLRIAGPF GLSLVQRLRP DFKRKYSSMF
EDDTVTEYIY HCNVQTPSGE TAFKNMTIPY GWAKRPMLQR IGKMHPDIPV SVIFGARSCI
DGNSGTSIQS LRPHSYVKTI AILGAGHYVY ADQPEEFNQK VKEICDTVD
