ID A0A093HSJ3_STRCA Unreviewed; 635 AA.
AC A0A093HSJ3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=sn-1-specific diacylglycerol lipase {ECO:0000256|ARBA:ARBA00026104};
DE EC=3.1.1.116 {ECO:0000256|ARBA:ARBA00026104};
DE Flags: Fragment;
GN ORFNames=N308_08858 {ECO:0000313|EMBL:KFV85658.1};
OS Struthio camelus australis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC Struthio.
OX NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV85658.1, ECO:0000313|Proteomes:UP000053584};
RN [1] {ECO:0000313|EMBL:KFV85658.1, ECO:0000313|Proteomes:UP000053584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV85658.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000256|ARBA:ARBA00010701}.
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DR EMBL; KL206788; KFV85658.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093HSJ3; -.
DR STRING; 441894.ENSSCUP00000020806; -.
DR Proteomes; UP000053584; 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 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000053584};
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..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 70..88
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 100..124
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 341..473
FT /note="Fungal lipase-like"
FT /evidence="ECO:0000259|Pfam:PF01764"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV85658.1"
FT NON_TER 635
FT /evidence="ECO:0000313|EMBL:KFV85658.1"
SQ SEQUENCE 635 AA; 70886 MW; 870822C737449C51 CRC64;
WIGILVLYTV HKGQFDCTGG GLLHSYLLVL LILLAAIICA LSAIVCVSMR GTISNPGPRK
SLPKLLYTRL LLYLPEFIWA IVGAVWVSDS SVHCERTVMN VIFGTVVASW IIIIFTIIGV
VIVFDPLGGK KTVYLTDGVN RNLESSQSGQ LLYNMKSTAT RVWEKRIRLL CCCIVQDDDH
RVAFTSIAEL FRAYFSDTDL VPSDIAAGLT LLHQEQDKME SCPKEPEEVL CHSPSSPVTD
DLDIELENAA HYMRFAAAAY GWPYYIYTNP FTALCKLNGD CCGNRPTDSD ITGSDRRNFH
FGSILKITGL QYRDFIHISF HNKIYEIPFF VALDHKKETI VVAVRGTLSF EDILTDLSAD
CEDLTLEDVL ENGFVHKGIT QAATYIYRKL INDGILNQAF TIAPEYKLVI VGHSLGGGTA
SILAIMLRNS FPTLKCFAFS PPGGLLSKSL ADYTKHFIVS VIVGKDLVAR LSMPNMEDLK
RRIVRMVANC NKPKYQILLR GCWYEVFGGD PDNFPTELDG RNQDDLTQPL LAEESLMVHR
SPSYNALEDE SHLNSPPQYP HLYLPGKIIH IVEESSSRRL CSSDIKYTAS WSKETVFSSI
LISPKMITDH MPDVVLKALN SLSQEHGSCM ACQTR
//