ID I3MQR7_ICTTR Unreviewed; 500 AA.
AC I3MQR7;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=phospholipase A1 {ECO:0000256|ARBA:ARBA00013179};
DE EC=3.1.1.32 {ECO:0000256|ARBA:ARBA00013179};
DE AltName: Full=Phospholipase A1 {ECO:0000256|ARBA:ARBA00031180};
GN Name=LIPG {ECO:0000313|Ensembl:ENSSTOP00000014330.3};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000014330.3, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000014330.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-
CC octadecenoate + di-(9Z)-octadecenoylglycerol + H(+);
CC Xref=Rhea:RHEA:38575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75945;
CC Evidence={ECO:0000256|ARBA:ARBA00000652};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576;
CC Evidence={ECO:0000256|ARBA:ARBA00000652};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tributanoylglycerol + H2O = butanoate +
CC dibutanoylglycerol + H(+); Xref=Rhea:RHEA:40475, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:35020,
CC ChEBI:CHEBI:76478; Evidence={ECO:0000256|ARBA:ARBA00001601};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476;
CC Evidence={ECO:0000256|ARBA:ARBA00001601};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) +
CC hexadecanoate + hexadecanoyl-sn-glycero-3-phosphocholine;
CC Xref=Rhea:RHEA:41384, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:64563, ChEBI:CHEBI:72999;
CC Evidence={ECO:0000256|ARBA:ARBA00000879};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41385;
CC Evidence={ECO:0000256|ARBA:ARBA00000879};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32;
CC Evidence={ECO:0000256|ARBA:ARBA00000111};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000256|ARBA:ARBA00010701, ECO:0000256|RuleBase:RU004262}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00152}.
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DR EMBL; AGTP01028662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005323130.1; XM_005323073.2.
DR AlphaFoldDB; I3MQR7; -.
DR STRING; 43179.ENSSTOP00000014330; -.
DR ESTHER; icttr-i3mqr7; Lipoprotein_Lipase.
DR Ensembl; ENSSTOT00000016014.3; ENSSTOP00000014330.3; ENSSTOG00000016012.3.
DR GeneID; 101965427; -.
DR CTD; 9388; -.
DR eggNOG; ENOG502QU8P; Eukaryota.
DR GeneTree; ENSGT00940000159394; -.
DR HOGENOM; CLU_027171_1_2_1; -.
DR InParanoid; I3MQR7; -.
DR OrthoDB; 3428256at2759; -.
DR TreeFam; TF324997; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005769; C:early endosome; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0004465; F:lipoprotein lipase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008970; F:phospholipase A1 activity; IEA:UniProtKB-EC.
DR GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; IEA:Ensembl.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0055091; P:phospholipid homeostasis; IEA:Ensembl.
DR GO; GO:0032376; P:positive regulation of cholesterol transport; IEA:Ensembl.
DR GO; GO:0010983; P:positive regulation of high-density lipoprotein particle clearance; IEA:Ensembl.
DR GO; GO:0050746; P:regulation of lipoprotein metabolic process; IEA:Ensembl.
DR GO; GO:0043691; P:reverse cholesterol transport; IEA:Ensembl.
DR CDD; cd00707; Pancreat_lipase_like; 1.
DR CDD; cd01758; PLAT_LPL; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.60.60.20; PLAT/LH2 domain; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013818; Lipase.
DR InterPro; IPR016272; Lipase_LIPH.
DR InterPro; IPR033906; Lipase_N.
DR InterPro; IPR002330; Lipo_Lipase.
DR InterPro; IPR001024; PLAT/LH2_dom.
DR InterPro; IPR036392; PLAT/LH2_dom_sf.
DR InterPro; IPR000734; TAG_lipase.
DR PANTHER; PTHR11610:SF13; ENDOTHELIAL LIPASE; 1.
DR PANTHER; PTHR11610; LIPASE; 1.
DR Pfam; PF00151; Lipase; 1.
DR Pfam; PF01477; PLAT; 1.
DR PIRSF; PIRSF000865; Lipoprotein_lipase_LIPH; 1.
DR PRINTS; PR00822; LIPOLIPASE.
DR PRINTS; PR00821; TAGLIPASE.
DR SMART; SM00308; LH2; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 1.
DR PROSITE; PS50095; PLAT; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|PIRSR:PIRSR000865-2};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Heparin-binding {ECO:0000256|ARBA:ARBA00022674};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000865-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..500
FT /note="phospholipase A1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030172864"
FT DOMAIN 347..482
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT ACT_SITE 169
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT ACT_SITE 193
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT ACT_SITE 274
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT BINDING 207
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-2"
FT BINDING 212
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-2"
SQ SEQUENCE 500 AA; 56689 MW; 1323CAA60D055BA6 CRC64;
MKNSVPLLCF WSAYCCFAAG SPTPFGPEGR LEGELHESRK VQAVSKPSVS FNLRTSKDPE
HEGCYLSPGH NQSLEDCGFD VTAKTFFIIH GWTTSGMLAN WLYKLVSALQ MREKDANVVV
VDWLPLAHQL YRDAVNNTRM VGHSVARMLD WLQEKDDFSL RNVHLIGYSL GAHVAGYAGN
FVKGTVGRIT GLDPAGPLFE GVDINKRLSP DDADFVDVLH THTGTFGLSI GIQMPVGHID
IYPNGGDFQP GCGFNDVLGS IAYGTITEVM KCEHERAVHL FVDSLVNQDK PSFAFQCTDS
NRFKKGICLS CRKNRCNSIG YNVKKMRNKR NSKMYLKTRA GMPFRVYHYQ MKIHIFSYKN
RGEIEPTFYV TLYGTNADSQ ILPLEIVEQI GLNATNTFLV YTEEDLGDLL KIKLTWEGTS
QSWYNLWKEL RSYLSQPSNT KWELHIRRIR VKSGETQRKL TFCTEDPENT SISPGQELWF
HKCRDGWRMK NETSPTMELV
//
