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Database: UniProt
Entry: A0A3B4U6K8_SERDU
LinkDB: A0A3B4U6K8_SERDU
Original site: A0A3B4U6K8_SERDU 
ID   A0A3B4U6K8_SERDU        Unreviewed;       511 AA.
AC   A0A3B4U6K8;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Lipoprotein lipase-like {ECO:0000313|Ensembl:ENSSDUP00000013470.1};
OS   Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000013470.1, ECO:0000313|Proteomes:UP000261420};
RN   [1] {ECO:0000313|Ensembl:ENSSDUP00000013470.1}
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   AlphaFoldDB; A0A3B4U6K8; -.
DR   STRING; 41447.ENSSDUP00000013470; -.
DR   Ensembl; ENSSDUT00000013715.1; ENSSDUP00000013470.1; ENSSDUG00000009789.1.
DR   GeneTree; ENSGT00940000166556; -.
DR   OMA; TSAQNHY; -.
DR   OrthoDB; 3428256at2759; -.
DR   Proteomes; UP000261420; Unplaced.
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   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; LIPASE; 1.
DR   PANTHER; PTHR11610:SF146; LIPOPROTEIN LIPASE-LIKE ISOFORM X1; 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   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..511
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017406478"
FT   DOMAIN          357..492
FT                   /note="PLAT"
FT                   /evidence="ECO:0000259|PROSITE:PS50095"
FT   ACT_SITE        175
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT   ACT_SITE        199
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT   ACT_SITE        284
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         218
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000865-2"
SQ   SEQUENCE   511 AA;  57662 MW;  AF7E90B65F62B9B9 CRC64;
     MKAWRVRFLY FLVLNAAVQY VTSLEEELAD SIFGNFLEPL SDLFDHKDDG NQTVAKFSLR
     KPSHPDDDLC YIIPGKPDSL AACTFNSTSK TFLVIHGWTL SGMFESWVAK LVSALYEREQ
     TANVIVVDWL TSAQNHYVVA AQNTKAVGQE IARFIDWIEE TTNMPLENIH LIGYSLGAHV
     AGFAGSHATN KVGRITGLDP AGPDFEGEHA HRRLSPDDAY FVDVLHTFTR GSLGLSIGIQ
     QPVGHVDIYP NGGSFQPGCN LRGALEKIAN FGIFAITDAI KCEHERSVHL FIDSLLNEQD
     AAKAYRCGSN DMFNRGMCLS CRKGRCNTVG YDISKVRKAR NVQMYTNTRA SMPFRVYHYQ
     LKMHFSSKVN RSEMEPSITV SLYGTKGEAE NLELKLKEKI ATNRTHSFLL VTEEDIGDLM
     MLTFKWEETN GWSASNMLKM VSSWWSGDSD SANMEVHKIR IRAGETQQKM VFCVKDPETH
     SLKQEVTFVK CKDAWRTDRK QTQKRVTLEN H
//
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