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Database: UniProt
Entry: H2L8Y7_ORYLA
LinkDB: H2L8Y7_ORYLA
Original site: H2L8Y7_ORYLA 
ID   H2L8Y7_ORYLA            Unreviewed;       507 AA.
AC   H2L8Y7;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Lipase, endothelial {ECO:0000313|Ensembl:ENSORLP00000002320.2};
GN   Name=lipg {ECO:0000313|Ensembl:ENSORLP00000002320.2};
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:ENSORLP00000002320.2, ECO:0000313|Proteomes:UP000001038};
RN   [1] {ECO:0000313|Ensembl:ENSORLP00000002320.2, ECO:0000313|Proteomes:UP000001038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000002320.2,
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:ENSORLP00000002320.2}
RP   IDENTIFICATION.
RC   STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000002320.2};
RG   Ensembl;
RL   Submitted (NOV-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   RefSeq; XP_011477165.1; XM_011478863.1.
DR   AlphaFoldDB; H2L8Y7; -.
DR   STRING; 8090.ENSORLP00000002320; -.
DR   ESTHER; oryla-h2l8y7; Lipoprotein_Lipase.
DR   Ensembl; ENSORLT00000002321.2; ENSORLP00000002320.2; ENSORLG00000001863.2.
DR   GeneID; 101173311; -.
DR   KEGG; ola:101173311; -.
DR   CTD; 9388; -.
DR   GeneTree; ENSGT00940000159394; -.
DR   InParanoid; H2L8Y7; -.
DR   OrthoDB; 3428256at2759; -.
DR   Proteomes; UP000001038; Chromosome 9.
DR   Bgee; ENSORLG00000001863; Expressed in animal zygote and 14 other cell types or tissues.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
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   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:UP000001038};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           35..507
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017486026"
FT   DOMAIN          355..492
FT                   /note="PLAT"
FT                   /evidence="ECO:0000259|PROSITE:PS50095"
FT   ACT_SITE        178
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT   ACT_SITE        202
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT   ACT_SITE        282
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT   BINDING         213
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000865-2"
FT   BINDING         216
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000865-2"
FT   BINDING         221
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000865-2"
SQ   SEQUENCE   507 AA;  57100 MW;  B94627ACBB63669F CRC64;
     MSCSFVCGWT MDRKAILSWT FLLCLCVMIS SAAGANTVLK DEEELEDWSN RKAPTGRIKY
     NMRKSLNLDQ DGCYLQRGKN ASLEECGFNA TAKTIFIIHG WTMSGMFETW MRKLVSAVMQ
     RENEANVVVV DWLSLAQQLY PDAVNHTHTV GSDIAAMLNW LQDERALPLE NVHLIGYSLG
     AHVAGYAGTY VKGSIGRITG LDPAGPMFEG VEEQKRLSPD DADFVDVLHT YTREALGVSI
     GIQQAIGDID IYPNGGEVQP GCGLADVLSL AGNFMEVMKC EHERAVHLFV DSLMNKEHVS
     YAFQCTDPQR FRKGICLSCR KNRCNGIGYN ARKMRKRRNS KMYLKTRAVT PFGGYHYQMK
     MHVFDRKHSE NADPTFFVKL YGSHNDTGNM PVEIADSIGL NHTNTFLVFT EEDIGDLLKI
     KLTWEGASES WTSLWSNVRK SLMTWNTKPA KAVLEVRRIR VKAGETQKKY TFCAQDSSQT
     EISPGDSITY VKCRDGWEVK PKKRLPM
//
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