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Database: UniProt
Entry: A0A3B4H3S4_9CICH
LinkDB: A0A3B4H3S4_9CICH
Original site: A0A3B4H3S4_9CICH 
ID   A0A3B4H3S4_9CICH        Unreviewed;       511 AA.
AC   A0A3B4H3S4;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Lipoprotein lipase-like {ECO:0000313|Ensembl:ENSPNYP00000029119.1, ECO:0000313|RefSeq:XP_013766585.1};
GN   Name=LOC102201047 {ECO:0000313|RefSeq:XP_013766585.1};
OS   Pundamilia nyererei.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX   NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000029119.1, ECO:0000313|Proteomes:UP000261460};
RN   [1] {ECO:0000313|Ensembl:ENSPNYP00000029119.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_013766585.1}
RP   IDENTIFICATION.
RG   RefSeq;
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_013766585.1; XM_013911131.1.
DR   AlphaFoldDB; A0A3B4H3S4; -.
DR   STRING; 303518.ENSPNYP00000029119; -.
DR   Ensembl; ENSPNYT00000029831.1; ENSPNYP00000029119.1; ENSPNYG00000021941.1.
DR   GeneID; 102201047; -.
DR   GeneTree; ENSGT00940000166556; -.
DR   OrthoDB; 3428256at2759; -.
DR   Proteomes; UP000261460; Unplaced.
DR   Proteomes; UP000695023; 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   Lipoprotein {ECO:0000313|RefSeq:XP_013766585.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000865-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000695023};
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_5041073935"
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;  57345 MW;  BDC62EF2AA2C5176 CRC64;
     MRAWKVRFLC FVVLNAAVQN VTSLEEELAG SIFGNFFDPV KGFFDHKAES NATVAKFSLR
     KPSHPDDDLC YIIPGKPDSL ATCTFNGTSK TFLIIHGWTL SGMFESWIPK LVSALYEREQ
     TANVIVVDWL NSAQNHYVVA AQKTKAVGQE IAQFIDWIEE TTNMPLENIH LIGYSLGAHV
     AGFAGSHATN KVGRITGLDP AGPDFEGEHA HRRLSPDDAH FVDVLHTFTR GSLGLSIGIQ
     QPVGHVDIYP NGGSYQPGCN LRGALEKIAN FGIFAVSDAV KCEHERSVHL FIDSLLNEQE
     AAMAYRCGSN DMFDRGMCLS CRKSRCNTVG YDISKVRKPR SVQMYTKTRS SMPFRVYHYQ
     LKIHFSSKVN SSDMEPSLTV SLYGTKGEAE NLQLKLKEKI VTNKTHSFLL VTEKDIGDLL
     MLKFKWEETN VWSASSMLKM VSSWWSGSSD GANVAVHKIR IRAGETQQKM VFCIKDPDAQ
     KLTQELTFVK CKDPWRTNRK RTLRRVTLEN Q
//
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