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 24-JAN-2024, entry version 99.
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 -!- SUBUNIT: Interacts with TTMP/C3orf52. {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.ENSOCUP00000030384; -.
DR ESTHER; rabit-LIPH; Phospholipase.
DR GlyCosmos; Q9BDJ4; 4 sites, No reported glycans.
DR PaxDb; 9986-ENSOCUP00000004368; -.
DR GeneID; 100008812; -.
DR KEGG; ocu:100008812; -.
DR CTD; 200879; -.
DR eggNOG; ENOG502QUQT; Eukaryota.
DR InParanoid; Q9BDJ4; -.
DR OrthoDB; 3428256at2759; -.
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; alpha/beta hydrolase; 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; LIPASE; 1.
DR PANTHER; PTHR11610:SF12; LIPASE MEMBER H; 1.
DR Pfam; PF00151; Lipase; 1.
DR PIRSF; PIRSF000865; Lipoprotein_lipase_LIPH; 1.
DR PRINTS; PR00821; TAGLIPASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 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
//
