ID   LIPH_RABIT              Reviewed;         452 AA.
AC   Q9BDJ4;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Lipase member H;
DE            EC=3.1.1.-;
DE   AltName: Full=Lacrimal lipase;
DE   Flags: Precursor;
GN   Name=LIPH;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lacrimal gland;
RX   PubMed=12454027;
RA   Remington S.G., Nelson J.D.;
RT   "mRNA encoding a new lipolytic enzyme expressed in rabbit lacrimal
RT   glands.";
RL   Invest. Ophthalmol. Vis. Sci. 43:3617-3624(2002).
CC   -!- FUNCTION: Hydrolyzes specifically phosphatidic acid (PA) to produce 2-
CC       acyl lysophosphatidic acid (LPA; a potent bioactive lipid mediator) and
CC       fatty acid (By similarity). Does not hydrolyze other phospholipids,
CC       like phosphatidylserine (PS), phosphatidylcholine (PC) and
CC       phosphatidylethanolamine (PE) or triacylglycerol (TG) (By similarity).
CC       {ECO:0000250|UniProtKB:Q8WWY8}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate +
CC         H2O = 2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H(+) +
CC         hexadecanoate; Xref=Rhea:RHEA:40943, ChEBI:CHEBI:7896,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:64839,
CC         ChEBI:CHEBI:77593; Evidence={ECO:0000250|UniProtKB:Q8WWY8};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40944;
CC         Evidence={ECO:0000250|UniProtKB:Q8WWY8};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8WWY8}. Cell
CC       membrane {ECO:0000250|UniProtKB:Q8WWY8}; Peripheral membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed in liver and lacrimal gland.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
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DR   EMBL; AF351188; AAK30250.1; -; mRNA.
DR   RefSeq; NP_001075575.1; NM_001082106.1.
DR   AlphaFoldDB; Q9BDJ4; -.
DR   SMR; Q9BDJ4; -.
DR   STRING; 9986.ENSOCUP00000004368; -.
DR   ESTHER; rabit-LIPH; Phospholipase.
DR   GeneID; 100008812; -.
DR   KEGG; ocu:100008812; -.
DR   CTD; 200879; -.
DR   eggNOG; ENOG502QUQT; Eukaryota.
DR   InParanoid; Q9BDJ4; -.
DR   OrthoDB; 534956at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:InterPro.
DR   GO; GO:0016298; F:lipase activity; IEA:InterPro.
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.
DR   InterPro; IPR016272; Lipase_LIPH.
DR   InterPro; IPR033906; Lipase_N.
DR   InterPro; IPR000734; TAG_lipase.
DR   PANTHER; PTHR11610; PTHR11610; 1.
DR   Pfam; PF00151; Lipase; 1.
DR   PIRSF; PIRSF000865; Lipoprotein_lipase_LIPH; 1.
DR   PRINTS; PR00821; TAGLIPASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Glycoprotein; Hydrolase; Lipid degradation;
KW   Lipid metabolism; Membrane; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..452
FT                   /note="Lipase member H"
FT                   /id="PRO_0000273323"
FT   ACT_SITE        154
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        178
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        249
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        50
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        66
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        122
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        263
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        233..247
FT                   /evidence="ECO:0000250"
FT   DISULFID        271..282
FT                   /evidence="ECO:0000250"
FT   DISULFID        285..293
FT                   /evidence="ECO:0000250"
FT   DISULFID        428..447
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   452 AA;  51164 MW;  54F6639B60D4BA6A CRC64;
     MLRFYLFISL LCLVRSDTDE TCPSFTKLSF HSAVVGTELN VRLLLYTRKN YTCAQIINST
     TFGNLNVTKK TTFVVHGFRP TGSPPVWLQD LVKALLMVED MNLVVVDWNR GATTVIYTQA
     SNKTRKVAII LKEFIDQMLA RGASLDDIYM IGVSLGAHIS GFVGKMYNGQ LGRITGLDPA
     GPLFNGKPPQ DRLDPSDAQF VDVIHSDTDA LGYKEPLGNI DFYPNGGVDQ PGCPKTIFEA
     GMQYFKCDHQ MSVYLYLSSL RKNCTITAYP CDSYRDYRNG KCINCGLPQG KPCPLLGYYA
     DNWKDYLSEK DPPMTKAFFD TAEKEPYCMY HYFVDIITWN KSIRRGSITI KLKDEAGNTT
     ESKINHEPVT FEKYHQVSLL ARFNQDLDKV AEISLVFSTG AVIGPKYKLR ILRMKLRSLA
     HPERPQLCRY DLVLTENVET PFQPIVCQKL QM