ID H2MR84_ORYLA Unreviewed; 516 AA.
AC H2MR84;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Lipoprotein lipase {ECO:0000256|ARBA:ARBA00018617, ECO:0000256|RuleBase:RU362020};
DE Short=LPL {ECO:0000256|RuleBase:RU362020};
DE EC=3.1.1.34 {ECO:0000256|ARBA:ARBA00013181, ECO:0000256|RuleBase:RU362020};
GN Name=lpl {ECO:0000313|Ensembl:ENSORLP00000021263.2};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000021263.2, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000021263.2, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000021263.2,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000021263.2}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000021263.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Key enzyme in triglyceride metabolism. Catalyzes the
CC hydrolysis of triglycerides from circulating chylomicrons and very low
CC density lipoproteins (VLDL), and thereby plays an important role in
CC lipid clearance from the blood stream, lipid utilization and storage.
CC Mediates margination of triglyceride-rich lipoprotein particles in
CC capillaries. Recruited to its site of action on the luminal surface of
CC vascular endothelium by binding to GPIHBP1 and cell surface heparan
CC sulfate proteoglycans. {ECO:0000256|RuleBase:RU362020}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid +
CC H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.34;
CC Evidence={ECO:0000256|ARBA:ARBA00000137,
CC ECO:0000256|RuleBase:RU362020};
CC -!- SUBUNIT: Homodimer. Interacts with APOC2; the interaction activates LPL
CC activity in the presence of lipids. {ECO:0000256|RuleBase:RU362020}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362020};
CC Peripheral membrane protein {ECO:0000256|RuleBase:RU362020};
CC Extracellular side {ECO:0000256|RuleBase:RU362020}. Secreted
CC {ECO:0000256|RuleBase:RU362020}. Secreted, extracellular space,
CC extracellular matrix {ECO:0000256|ARBA:ARBA00004498,
CC ECO:0000256|RuleBase:RU362020}. Note=Newly synthesized LPL binds to
CC cell surface heparan proteoglycans and is then released by heparanase.
CC Subsequently, it becomes attached to heparan proteoglycan on
CC endothelial cells. Locates to the plasma membrane of microvilli of
CC hepatocytes with triglyceride-rich lipoproteins (TRL). Some of the
CC bound LPL is then internalized and located inside non-coated endocytic
CC vesicles. {ECO:0000256|RuleBase:RU362020}.
CC -!- PTM: Tyrosine nitration after lipopolysaccharide (LPS) challenge down-
CC regulates the lipase activity. {ECO:0000256|RuleBase:RU362020}.
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 AlphaFoldDB; H2MR84; -.
DR STRING; 8090.ENSORLP00000021263; -.
DR ESTHER; oryla-h2mr84; Lipoprotein_Lipase.
DR Ensembl; ENSORLT00000021264.2; ENSORLP00000021263.2; ENSORLG00000016997.2.
DR GeneTree; ENSGT00940000157178; -.
DR HOGENOM; CLU_1574356_0_0_1; -.
DR InParanoid; H2MR84; -.
DR Proteomes; UP000001038; Chromosome 4.
DR Bgee; ENSORLG00000016997; Expressed in liver and 14 other cell types or tissues.
DR GO; GO:0042627; C:chylomicron; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:UniProtKB-KW.
DR GO; GO:0034185; F:apolipoprotein binding; IBA:GO_Central.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004465; F:lipoprotein lipase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004620; F:phospholipase activity; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0019433; P:triglyceride catabolic process; IBA:GO_Central.
DR GO; GO:0034372; P:very-low-density lipoprotein particle remodeling; IBA:GO_Central.
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 NCBIfam; TIGR03230; lipo_lipase; 1.
DR PANTHER; PTHR11610; LIPASE; 1.
DR PANTHER; PTHR11610:SF3; LIPOPROTEIN 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 Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU362020};
KW Chylomicron {ECO:0000256|ARBA:ARBA00022513, ECO:0000256|RuleBase:RU362020};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|RuleBase:RU362020};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Heparin-binding {ECO:0000256|ARBA:ARBA00022674,
KW ECO:0000256|RuleBase:RU362020};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362020};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|RuleBase:RU362020};
KW Lipid metabolism {ECO:0000256|RuleBase:RU362020};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362020};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000865-2};
KW Nitration {ECO:0000256|ARBA:ARBA00023074, ECO:0000256|RuleBase:RU362020};
KW Reference proteome {ECO:0000313|Proteomes:UP000001038};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU362020};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU362020};
KW VLDL {ECO:0000256|ARBA:ARBA00023313, ECO:0000256|RuleBase:RU362020}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU362020"
FT CHAIN 21..516
FT /note="Lipoprotein lipase"
FT /evidence="ECO:0000256|RuleBase:RU362020"
FT /id="PRO_5017100210"
FT DOMAIN 364..487
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT ACT_SITE 179
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT ACT_SITE 203
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT ACT_SITE 291
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT BINDING 222
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-2"
SQ SEQUENCE 516 AA; 57994 MW; 3E908596AD575E54 CRC64;
MGKELLCFFT LWITLGNISA TFSSDLESNT TSLFVNSTTT AAPLPTTTEW MTDYADILSK
FSLRTADIPD EDMCYIQAGH PETIKDCQFN AEAQTFIVIH GWTVTGMFES WVPKLVSALY
ERVPNANVIV VDWLTRASQH YPTSASYTKL VGRDVAKFVT WLQNELQLPW DRIHVLGYSL
GAHVAGVAGH LTDNKISRIT GLDPAGPSFE HADDQSTLSR DDGQFVDVLH TNTRGSPDRS
IGIQRPVGHI DIYPNGGTFQ PGCDIQNTLL GIASAGIKGL QNMDQLVKCS HERSIHLFID
SLVNTQHQSM AYRCNSKEAF NKGVCLSCRK NRCNKLGYNI NKVRTARSTK MYLKTRGMMP
YKVFHYQVKA HFFSKSEQSF TEQPMKISLF GTHGETEDIA FVLPELSCNN TVSFLITTDV
DIGELMIVKL RWEKDAILSW SDWWGSSKFH IRKLRIKSGE TQSKVIFNAK EGEFADLVRG
GEDAVFVKSK EDNISRKERR MHRLKTEGSL FGKSEA
//
