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Database: UniProt
Entry: A7RV84_NEMVE
LinkDB: A7RV84_NEMVE
Original site: A7RV84_NEMVE 
ID   A7RV84_NEMVE            Unreviewed;       280 AA.
AC   A7RV84;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=sn-1-specific diacylglycerol lipase ABHD11 {ECO:0000256|ARBA:ARBA00044064};
DE            EC=3.1.1.116 {ECO:0000256|ARBA:ARBA00026104};
DE   AltName: Full=Alpha/beta hydrolase domain-containing protein 11 {ECO:0000256|ARBA:ARBA00042703};
DE   Flags: Fragment;
GN   ORFNames=NEMVEDRAFT_v1g94848 {ECO:0000313|EMBL:EDO44599.1};
OS   Nematostella vectensis (Starlet sea anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Edwardsiidae; Nematostella.
OX   NCBI_TaxID=45351 {ECO:0000313|EMBL:EDO44599.1, ECO:0000313|Proteomes:UP000001593};
RN   [1] {ECO:0000313|EMBL:EDO44599.1, ECO:0000313|Proteomes:UP000001593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593};
RX   PubMed=17615350; DOI=10.1126/science.1139158;
RA   Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA   Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA   Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA   Technau U., Martindale M.Q., Rokhsar D.S.;
RT   "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT   genomic organization.";
RL   Science 317:86-94(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-didecanoylglycerol + H2O = decanoate + decanoylglycerol +
CC         H(+); Xref=Rhea:RHEA:48596, ChEBI:CHEBI:11152, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:27689, ChEBI:CHEBI:90605;
CC         Evidence={ECO:0000256|ARBA:ARBA00043771};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-octadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-
CC         glycerol + H2O = 2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-glycerol +
CC         H(+) + octadecanoate; Xref=Rhea:RHEA:77107, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:77129,
CC         ChEBI:CHEBI:186738; Evidence={ECO:0000256|ARBA:ARBA00043706};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol
CC         + H2O = 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H(+) +
CC         octadecanoate; Xref=Rhea:RHEA:38507, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:52392,
CC         ChEBI:CHEBI:75728; Evidence={ECO:0000256|ARBA:ARBA00043768};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + H2O = 2-(9Z-
CC         octadecenoyl)-glycerol + H(+) + octadecanoate; Xref=Rhea:RHEA:77103,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629,
CC         ChEBI:CHEBI:73990, ChEBI:CHEBI:75468;
CC         Evidence={ECO:0000256|ARBA:ARBA00043740};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycerol + H2O = a 2-acylglycerol + a fatty
CC         acid + H(+); Xref=Rhea:RHEA:33275, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17389, ChEBI:CHEBI:17815,
CC         ChEBI:CHEBI:28868; EC=3.1.1.116;
CC         Evidence={ECO:0000256|ARBA:ARBA00043667};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,3-diacyl-sn-glycerol + H2O = a 1-acyl-sn-glycerol + a
CC         fatty acid + H(+); Xref=Rhea:RHEA:38503, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:64683,
CC         ChEBI:CHEBI:77272; Evidence={ECO:0000256|ARBA:ARBA00043742};
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily.
CC       {ECO:0000256|ARBA:ARBA00008645}.
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DR   EMBL; DS469543; EDO44599.1; -; Genomic_DNA.
DR   RefSeq; XP_001636662.1; XM_001636612.1.
DR   AlphaFoldDB; A7RV84; -.
DR   STRING; 45351.A7RV84; -.
DR   eggNOG; KOG2382; Eukaryota.
DR   HOGENOM; CLU_020336_53_0_1; -.
DR   InParanoid; A7RV84; -.
DR   OMA; VHFEQPQ; -.
DR   PhylomeDB; A7RV84; -.
DR   Proteomes; UP000001593; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
DR   GO; GO:0044255; P:cellular lipid metabolic process; IBA:GO_Central.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   PANTHER; PTHR46118; PROTEIN ABHD11; 1.
DR   PANTHER; PTHR46118:SF4; PROTEIN ABHD11; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001593}.
FT   DOMAIN          25..153
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         280
FT                   /evidence="ECO:0000313|EMBL:EDO44599.1"
SQ   SEQUENCE   280 AA;  32069 MW;  7F306BC2AB439416 CRC64;
     SNSSPVQLTY SRVEGVDRDP DPPDPPLFIM HGLFGNKKNW RTIALTMNEK TGREIVTIDA
     RNHGKSEHHD RMNYTLQALD ARQLMYELEI PKAVLVGHSM GGKVGMTFAL TYPEMVDKLI
     VVDVSPSRSV SEDDIQRYLN TKLQMDLGKV RSKQDAEKML EGAVKVCIVH LVPMLRQFFL
     TNLVATSTGF QWRVNLEAID RNLEEIMTFP EEFPYPTFEG DVLFIGGAKS NYIQRSDYAR
     IYKLFPRAEI TYIPDCGHWV HVDKPNELMD IILEFLSRDT
//
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