ID A0A087YCA6_POEFO Unreviewed; 496 AA.
AC A0A087YCA6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Lipase G, endothelial type {ECO:0000313|Ensembl:ENSPFOP00000015659.2};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000015659.2, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000015659.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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; AYCK01009776; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007563618.1; XM_007563556.2.
DR AlphaFoldDB; A0A087YCA6; -.
DR STRING; 48698.ENSPFOP00000015659; -.
DR ESTHER; poefo-a0a087yca6; Lipoprotein_Lipase.
DR Ensembl; ENSPFOT00000015681.2; ENSPFOP00000015659.2; ENSPFOG00000015561.2.
DR GeneID; 103145900; -.
DR KEGG; pfor:103145900; -.
DR CTD; 9388; -.
DR eggNOG; ENOG502QU8P; Eukaryota.
DR GeneTree; ENSGT00940000159394; -.
DR OMA; QMPVGHV; -.
DR OrthoDB; 3428256at2759; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00707; Pancreat_lipase_like; 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 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:UP000028760};
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..496
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001834294"
FT DOMAIN 341..481
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT ACT_SITE 164
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT ACT_SITE 188
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT ACT_SITE 268
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT BINDING 199
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-2"
FT BINDING 202
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-2"
FT BINDING 207
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-2"
SQ SEQUENCE 496 AA; 56085 MW; C2A698E314C8BB85 CRC64;
MNLKIFLLWT FLQYVSSALG ENGVLKGEDE GFESTDTEAV HGRIKYNMRK SLDLDQEGCY
LQTGKKACLE ECGFNSTSKT IFIIHGWTMS GIFETWMHKL VSAVMQRENE ANVVVVDWMP
LAQQLYPDAV NHTLAVGVDI AKMFDWLQEE HKLPLENVHL IGYSLGAHVA GFAGTYVKGT
LGRITGLDPA GPMFEGVEEQ KRLSPDDADF VDVLHTYTRE ALGVSIGIQQ PIGDIDIYPN
GGDVQPGCAL GEMLAAAGNF MEVMKCEHER AVHLFVDSLM NKEHMSYAYQ CTGPDRFKKG
ICLSCRKNRC NNIGYNARKM RKRRNSKMYL KTRAKTPFGG YHYQMKMHVF NRKQFDNADP
TFYVKLYGGH NDTGNIFVVH ADPIGLNFTN TFLVFTEEDI GDLLKIRLSW EGDSESLSSV
FKYIKNSFWN WNAKAAKPAK PVLEIRRIRV KAGESQKKFA FCAQDPSKTE ISPGESITFV
KCRDGWEVKP RKRLPM
//
