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ABHD5_PIG
ID   ABHD5_PIG               Reviewed;         349 AA.
AC   Q5EE05;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=1-acylglycerol-3-phosphate O-acyltransferase ABHD5 {ECO:0000250|UniProtKB:Q8WTS1};
DE            EC=2.3.1.51 {ECO:0000250|UniProtKB:Q8WTS1};
DE   AltName: Full=Abhydrolase domain-containing protein 5;
GN   Name=ABHD5 {ECO:0000250|UniProtKB:Q8WTS1};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Xia T., Yang Z.Q.;
RT   "Mapping of porcine CGI-58 gene.";
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Coenzyme A-dependent lysophosphatidic acid acyltransferase
CC       that catalyzes the transfert of an acyl group on a lysophosphatidic
CC       acid. Functions preferentially with 1-oleoyl-lysophosphatidic acid
CC       followed by 1-palmitoyl-lysophosphatidic acid, 1-stearoyl-
CC       lysophosphatidic acid and 1-arachidonoyl-lysophosphatidic acid as lipid
CC       acceptor. Functions preferentially with arachidonoyl-CoA followed by
CC       oleoyl-CoA as acyl group donors (By similarity). Functions in
CC       phosphatidic acid biosynthesis (By similarity). May regulate the
CC       cellular storage of triacylglycerol through activation of the
CC       phospholipase PNPLA2 (By similarity). Involved in keratinocyte
CC       differentiation (By similarity). Regulates lipid droplet fusion (By
CC       similarity). {ECO:0000250|UniProtKB:Q8WTS1,
CC       ECO:0000250|UniProtKB:Q9DBL9}.
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:0000250|UniProtKB:Q8WTS1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19710;
CC         Evidence={ECO:0000250|UniProtKB:Q8WTS1};
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:0000250|UniProtKB:Q9DBL9};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37132;
CC         Evidence={ECO:0000250|UniProtKB:Q9DBL9};
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:0000250|UniProtKB:Q9DBL9};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37144;
CC         Evidence={ECO:0000250|UniProtKB:Q9DBL9};
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:0000250|UniProtKB:Q9DBL9};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37148;
CC         Evidence={ECO:0000250|UniProtKB:Q9DBL9};
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Lipid droplet
CC       {ECO:0000250}. Note=Colocalized with PLIN and ADRP on the surface of
CC       lipid droplets. The localization is dependent upon the metabolic status
CC       of the adipocytes and the activity of PKA (By similarity).
CC       {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the peptidase S33 family. ABHD4/ABHD5 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AY902463; AAW82452.1; -; mRNA.
DR   RefSeq; NP_001012407.1; NM_001012407.1.
DR   AlphaFoldDB; Q5EE05; -.
DR   SMR; Q5EE05; -.
DR   STRING; 9823.ENSSSCP00000012044; -.
DR   ESTHER; pig-abhd5; CGI-58_ABHD5_ABHD4.
DR   MEROPS; S33.975; -.
DR   PaxDb; Q5EE05; -.
DR   PeptideAtlas; Q5EE05; -.
DR   PRIDE; Q5EE05; -.
DR   Ensembl; ENSSSCT00005064321; ENSSSCP00005039743; ENSSSCG00005039875.
DR   GeneID; 497624; -.
DR   KEGG; ssc:497624; -.
DR   CTD; 51099; -.
DR   eggNOG; KOG4409; Eukaryota.
DR   InParanoid; Q5EE05; -.
DR   OrthoDB; 1555935at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005811; C:lipid droplet; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
DR   GO; GO:0042171; F:lysophosphatidic acid acyltransferase activity; IBA:GO_Central.
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; ISS:UniProtKB.
DR   GO; GO:0006654; P:phosphatidic acid biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0010898; P:positive regulation of triglyceride catabolic process; ISS: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   2: Evidence at transcript level;
KW   Acetylation; Acyltransferase; Cytoplasm; Differentiation;
KW   Fatty acid metabolism; Lipid biosynthesis; Lipid droplet; Lipid metabolism;
KW   Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW   Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WTS1"
FT   CHAIN           2..349
FT                   /note="1-acylglycerol-3-phosphate O-acyltransferase ABHD5"
FT                   /id="PRO_0000080868"
FT   DOMAIN          77..185
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:0000250|UniProtKB:Q8WTS1"
SQ   SEQUENCE   349 AA;  39004 MW;  DE85BD529EE16854 CRC64;
     MAAEEEEMDS TDACERSGWL TGWLPTWCPT STSHLKEAEE KILKCVPCIY KKGPVRISNG
     NKIWTLKLSH NISNKIPLVL LHGFGGGLGL WALNFGDLCT NRPVYAFDLL GFGRSSRPRF
     DTDAEEVENQ FVESIEEWRC ALGLDKVILL GHNLGGFLAA AYSLKYPSRV SHLILVEPWG
     FPERPDLADQ ERPIPVWIRA LGAALTPFNP LAGLRIAGPF GLSLVQRLRP DFKRKYSSMF
     EDDTVTEYIY HCNVQTPSGE TAFKNMTIPY GWAKRPMLHR IGKMNPDIPV SVIYGARSCI
     DGNSGTSIQS LRPHSYVKTI AILGAGHYVY ADQPEDFNLK VKEICDTVD
 
 
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