ID A0A016VKX2_9BILA Unreviewed; 721 AA.
AC A0A016VKX2;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=sn-1-specific diacylglycerol lipase {ECO:0000256|ARBA:ARBA00026104};
DE EC=3.1.1.116 {ECO:0000256|ARBA:ARBA00026104};
GN Name=Acey_s0008.g115 {ECO:0000313|EMBL:EYC27662.1};
GN Synonyms=Acey-F42G9.6 {ECO:0000313|EMBL:EYC27662.1};
GN ORFNames=Y032_0008g115 {ECO:0000313|EMBL:EYC27662.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC27662.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
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:ARBA00024531};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33276;
CC Evidence={ECO:0000256|ARBA:ARBA00024531};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EYC27662.1}.
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; JARK01001344; EYC27662.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016VKX2; -.
DR Proteomes; UP000024635; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR CDD; cd00519; Lipase_3; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002921; Fungal_lipase-like.
DR PANTHER; PTHR45792; DIACYLGLYCEROL LIPASE HOMOLOG-RELATED; 1.
DR PANTHER; PTHR45792:SF2; DIACYLGLYCEROL LIPASE-BETA; 1.
DR Pfam; PF01764; Lipase_3; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000024635};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 26..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 97..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 372..517
FT /note="Fungal lipase-like"
FT /evidence="ECO:0000259|Pfam:PF01764"
FT REGION 681..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..721
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 721 AA; 79614 MW; F785507CFA5BC13A CRC64;
MPSLIAFGRK WNIASDDFVF PELTEALVRL SWMAFAFAVF ILHFPLSCSG KDMTVSLLTL
LFVNGITVAL AFLTVGISSK GSIMNPYPRR HVATLLYIRL PVFVLEIALT IISTINAFQP
DPPDSVCHFS NILKVTIALE WALIVSVFFG VLIVFNPVDE DDVEDSTIIA RRVWSRRFKI
FTIRQDAHMR AAMDDLANLM SSFFSDVDIV FSDVLAGLFL VVHSPSNVYP PLIKTDTEPP
AWMTVENALH FQHFSSCVYG WPTYLLHNFG IRPAYKLFRK LQCCGRLRCD QKENSDVPMR
NISNDSRVHD RSHYKPSTKV LVIEDNCCFC NTAAFTLSNE QKNIDLFFVS FRNELYEVPF
VVLADHETRS IVITIRGSCS LVDLVTDLCL DDEVLSVDVD ADPLLRTDTT LDAEGEVRVH
RGMLMSARYV FDTLRKHQVL EDLAVLNTGY QLVVCGHSLG AGVASLLTLL LKQEYPDVRC
FAFAPPGCVI SENGLHEMEQ HVMGIVAGDD VVSRISFHAL QRLRVKVAAE LDACTKAKYE
ILIRGIFRIF FSPAWESGPL SGNGTVTDRL NLIPEGATMN GGSYGTTNAP PNTATAVTIS
TNQRLASRVE LFAPGKLLYI AEDESREDGV ACDWIDPKCL SDVKLTASAV TDHLPKNIER
MLEKVIAAKG AAVIIPPATA NEGSPTAAAA STANAPANNN TSARTTPPRL VVTDQPRTSS
R
//
