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Database: UniProt
Entry: A0A091V7V3_OPIHO
LinkDB: A0A091V7V3_OPIHO
Original site: A0A091V7V3_OPIHO 
ID   A0A091V7V3_OPIHO        Unreviewed;       462 AA.
AC   A0A091V7V3;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   25-APR-2018, entry version 25.
DE   RecName: Full=Lipoprotein lipase {ECO:0000256|RuleBase:RU362020};
DE            Short=LPL {ECO:0000256|RuleBase:RU362020};
DE            EC=3.1.1.34 {ECO:0000256|RuleBase:RU362020};
DE   Flags: Fragment;
GN   ORFNames=N306_08959 {ECO:0000313|EMBL:KFQ99391.1};
OS   Opisthocomus hoazin (Hoatzin) (Phasianus hoazin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Opisthocomiformes; Opisthocomidae;
OC   Opisthocomus.
OX   NCBI_TaxID=30419 {ECO:0000313|EMBL:KFQ99391.1, ECO:0000313|Proteomes:UP000053605};
RN   [1] {ECO:0000313|EMBL:KFQ99391.1, ECO:0000313|Proteomes:UP000053605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N306 {ECO:0000313|EMBL:KFQ99391.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The primary function of this lipase is the hydrolysis of
CC       triglycerides of circulating chylomicrons and very low density
CC       lipoproteins (VLDL). Binding to heparin sulfate proteogylcans at
CC       the cell surface is vital to the function. The apolipoprotein,
CC       APOC2, acts as a coactivator of LPL activity in the presence of
CC       lipids on the luminal surface of vascular endothelium.
CC       {ECO:0000256|RuleBase:RU362020}.
CC   -!- CATALYTIC ACTIVITY: Triacylglycerol + H(2)O = diacylglycerol + a
CC       carboxylate. {ECO:0000256|RuleBase:RU362020}.
CC   -!- SUBUNIT: Homodimer. Interacts with APOC2; the interaction
CC       activates LPL activity in the presence of lipids.
CC       {ECO:0000256|RuleBase:RU362020}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000256|RuleBase:RU362020}; Lipid-anchor, GPI-anchor
CC       {ECO:0000256|RuleBase:RU362020}. Secreted
CC       {ECO:0000256|RuleBase:RU362020, ECO:0000256|SAAS:SAAS00553472}.
CC       Note=Locates to the plasma membrane of microvilli of hepatocytes
CC       with triacyl-glycerol-rich lipoproteins (TRL). Some of the bound
CC       LPL is then internalized and located inside non-coated endocytic
CC       vesicles. {ECO:0000256|RuleBase:RU362020}.
CC   -!- PTM: Tyrosine nitration after lipopolysaccharide (LPS) challenge
CC       down-regulates the lipase activity.
CC       {ECO:0000256|RuleBase:RU362020}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase
CC       family. {ECO:0000256|RuleBase:RU004262,
CC       ECO:0000256|SAAS:SAAS00591292}.
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DR   EMBL; KK733782; KFQ99391.1; -; Genomic_DNA.
DR   PhylomeDB; A0A091V7V3; -.
DR   Proteomes; UP000053605; Unassembled WGS sequence.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0042627; C:chylomicron; IEA:UniProtKB-UniRule.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:UniProtKB-UniRule.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004465; F:lipoprotein lipase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00707; Pancreat_lipase_like; 1.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR013818; Lipase/vitellogenin.
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; PTHR11610; 1.
DR   PANTHER; PTHR11610:SF3; PTHR11610:SF3; 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; SSF49723; SSF49723; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   TIGRFAMs; TIGR03230; lipo_lipase; 1.
DR   PROSITE; PS50095; PLAT; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|RuleBase:RU362020};
KW   Chylomicron {ECO:0000256|RuleBase:RU362020};
KW   Complete proteome {ECO:0000313|Proteomes:UP000053605};
KW   Disulfide bond {ECO:0000256|RuleBase:RU362020};
KW   Glycoprotein {ECO:0000256|RuleBase:RU362020};
KW   GPI-anchor {ECO:0000256|RuleBase:RU362020};
KW   Heparin-binding {ECO:0000256|RuleBase:RU362020};
KW   Hydrolase {ECO:0000256|RuleBase:RU362020};
KW   Lipid degradation {ECO:0000256|RuleBase:RU362020};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU362020};
KW   Lipoprotein {ECO:0000313|EMBL:KFQ99391.1};
KW   Membrane {ECO:0000256|RuleBase:RU362020};
KW   Nitration {ECO:0000256|RuleBase:RU362020};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053605};
KW   Secreted {ECO:0000256|RuleBase:RU362020,
KW   ECO:0000256|SAAS:SAAS00439306}; VLDL {ECO:0000256|RuleBase:RU362020}.
FT   DOMAIN      313    436       PLAT. {ECO:0000259|PROSITE:PS50095}.
FT   ACT_SITE    131    131       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR000865-1}.
FT   ACT_SITE    155    155       Charge relay system. {ECO:0000256|PIRSR:
FT                                PIRSR000865-1}.
FT   ACT_SITE    240    240       Charge relay system. {ECO:0000256|PIRSR:
FT                                PIRSR000865-1}.
FT   NON_TER       1      1       {ECO:0000313|EMBL:KFQ99391.1}.
FT   NON_TER     462    462       {ECO:0000313|EMBL:KFQ99391.1}.
SQ   SEQUENCE   462 AA;  52307 MW;  1FDBAD30A84D08F2 CRC64;
     EAETGFEGIE SKFSLRTPAE PDEDVCYLVP GQVDSLARCN FNHTSKTFVV IHGWTVTGMY
     ESWVPKLVDA LYKREPDSNV VVVDWLVRAQ QHYPVSAAYT KLVGKDVAMF IDWMEEKFNY
     PLNNVHLLGY SLGAHAAGIA GSLTKKKVNR ITGLDPAGPT FEYADALTRL SPDDADFVDV
     LHTYTRGSPD RSIGIQKPVG HIDIYPNGGG FQPGCNLGEA LRLIAEKGFA DVDQLVKCSH
     ERSIHLFIDS LLFEEKPSMA YRCNTKEAFE KGLCLSCRKN RCNNLGYKVN RVRTKRNTKM
     YLKTRAQMPY KVFHYQVKIH FFGKTNTTKT NQPFLISLYG TLDQSENIAF TLPEVSSNKT
     FSFLIYTEVD IGDLLMLKLQ WEKDSFFSWS DWWTPFTFDI QRVRVKSGET QKKVVFCSRD
     GTSRLSKGEE AAIFVKCLEQ PVNRKRGGAK KAFKENSAHE SA
//
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