ID C9J1D1_HUMAN Unreviewed; 308 AA. AC C9J1D1; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 20-JUN-2018, sequence version 2. DT 27-MAR-2024, entry version 85. 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}; GN Name=ABHD5 {ECO:0000313|Ensembl:ENSP00000412014.2}; 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:ENSP00000412014.2, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000412014.2, 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:ENSP00000412014.2} 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 RefSeq; XP_011532081.1; XM_011533779.2. DR ESTHER; human-ABHD5; CGI-58_ABHD5_ABHD4. DR ProteomicsDB; 8066; -. DR Antibodypedia; 29395; 364 antibodies from 33 providers. DR Ensembl; ENST00000454293.2; ENSP00000412014.2; ENSG00000011198.10. DR Ensembl; ENST00000642351.1; ENSP00000494478.1; ENSG00000011198.10. DR UCSC; uc062iua.1; human. DR HGNC; HGNC:21396; ABHD5. DR VEuPathDB; HostDB:ENSG00000011198; -. DR GeneTree; ENSGT00390000016277; -. DR HOGENOM; CLU_3210087_0_0_1; -. DR ChiTaRS; ABHD5; human. DR Proteomes; UP000005640; Chromosome 3. DR Bgee; ENSG00000011198; Expressed in amniotic fluid and 196 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR000073; AB_hydrolase_1. 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 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:C9J1D1, KW ECO:0007829|MaxQB:C9J1D1}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 36..291 FT /note="AB hydrolase-1" FT /evidence="ECO:0000259|Pfam:PF00561" SQ SEQUENCE 308 AA; 34536 MW; 48FC898C8F36806B CRC64; MLKCVPCTYK KEPVRISNGN KIWTLKFSHN ISNKTPLVLL HGFGGGLGLW ALNFGDLCTN RPVYAFDLLG FGRSSRPRFD SDAEEVENQF VESIEEWRCA LGLDKMILLG HNLGGFLAAA YSLKYPSRVN HLILVEPWGF PERPDLADQD RPIPVWIRAL GAALTPFNPL AGLRIAGPFG LSLVQRLRPD FKRKYSSMFE DDTVTEYIYH CNVQTPSGET AFKNMTIPYG WAKRPMLQRI GKMHPDIPVS VIFGARSCID GNSGTSIQSL RPHSYVKTIA ILGAGHYVYA DQPEEFNQKV KEICDTVD //