ID C9JBM3_HUMAN Unreviewed; 126 AA. AC C9JBM3; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 05-OCT-2016, sequence version 8. DT 27-MAR-2024, entry version 87. DE RecName: Full=1-acylglycerol-3-phosphate O-acyltransferase ABHD5 {ECO:0000256|ARBA:ARBA00040731}; DE EC=2.3.1.51 {ECO:0000256|ARBA:ARBA00013211}; DE AltName: Full=Abhydrolase domain-containing protein 5 {ECO:0000256|ARBA:ARBA00042413}; DE Flags: Fragment; GN Name=ABHD5 {ECO:0000313|Ensembl:ENSP00000391582.1}; 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 {ECO:0000313|Ensembl:ENSP00000391582.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000391582.1, ECO:0000313|Proteomes:UP000005640} 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., 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 [2] {ECO:0000313|Ensembl:ENSP00000391582.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (NOV-2023) to UniProtKB. 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:0000256|ARBA:ARBA00036590}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37444; CC Evidence={ECO:0000256|ARBA:ARBA00036590}; 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:0000256|ARBA:ARBA00035818}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37456; CC Evidence={ECO:0000256|ARBA:ARBA00035818}; 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:0000256|ARBA:ARBA00000045}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37132; CC Evidence={ECO:0000256|ARBA:ARBA00000045}; 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:0000256|ARBA:ARBA00001203}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33188; CC Evidence={ECO:0000256|ARBA:ARBA00001203}; 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:0000256|ARBA:ARBA00036294}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37164; CC Evidence={ECO:0000256|ARBA:ARBA00036294}; 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:0000256|ARBA:ARBA00036557}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37452; CC Evidence={ECO:0000256|ARBA:ARBA00036557}; 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:0000256|ARBA:ARBA00000816}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37144; CC Evidence={ECO:0000256|ARBA:ARBA00000816}; 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:0000256|ARBA:ARBA00036296}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37148; CC Evidence={ECO:0000256|ARBA:ARBA00036296}; 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:0000256|ARBA:ARBA00000300}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19710; CC Evidence={ECO:0000256|ARBA:ARBA00000300}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. CC -!- SIMILARITY: Belongs to the peptidase S33 family. ABHD4/ABHD5 subfamily. CC {ECO:0000256|ARBA:ARBA00038097}. 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; AC006055; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC105903; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; C9JBM3; -. DR SMR; C9JBM3; -. DR ESTHER; human-ABHD5; CGI-58_ABHD5_ABHD4. DR MassIVE; C9JBM3; -. DR PeptideAtlas; C9JBM3; -. DR ProteomicsDB; 9486; -. DR Antibodypedia; 29395; 364 antibodies from 33 providers. DR Ensembl; ENST00000456453.5; ENSP00000391582.1; ENSG00000011198.10. DR UCSC; uc062itx.1; human. DR HGNC; HGNC:21396; ABHD5. DR VEuPathDB; HostDB:ENSG00000011198; -. DR GeneTree; ENSGT00390000016277; -. DR HOGENOM; CLU_114579_0_0_1; -. DR OMA; DTTIRWC; -. DR ChiTaRS; ABHD5; human. DR Proteomes; UP000005640; Chromosome 3. DR Bgee; ENSG00000011198; Expressed in amniotic fluid and 196 other cell types or tissues. DR ExpressionAtlas; C9JBM3; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008233; F:peptidase activity; IEA:InterPro. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR000073; AB_hydrolase_1. DR InterPro; IPR002410; Peptidase_S33. DR PANTHER; PTHR42886:SF34; 1-ACYLGLYCEROL-3-PHOSPHATE O-ACYLTRANSFERASE ABHD5; 1. DR PANTHER; PTHR42886; RE40534P-RELATED; 1. DR Pfam; PF00561; Abhydrolase_1; 1. DR PRINTS; PR00111; ABHYDROLASE. DR PRINTS; PR00793; PROAMNOPTASE. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1. PE 1: Evidence at protein level; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098}; KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209}; KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264}; KW Proteomics identification {ECO:0007829|EPD:C9JBM3, KW ECO:0007829|MaxQB:C9JBM3}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 36..126 FT /note="AB hydrolase-1" FT /evidence="ECO:0000259|Pfam:PF00561" FT NON_TER 126 FT /evidence="ECO:0000313|Ensembl:ENSP00000391582.1" SQ SEQUENCE 126 AA; 14096 MW; 46CDD7FD60898B97 CRC64; MLKCVPCTYK KEPVRISNGN KIWTLKFSHN ISNKTPLVLL HGFGGGLGLW ALNFGDLCTN RPVYAFDLLG FGRSSRPRFD SDAEEVENQF VESIEEWRCA LGLDKMILLG HNLGGFLAAA YSLKYP //