LIPH_MOUSE
ID LIPH_MOUSE Reviewed; 451 AA.
AC Q8CIV3; Q3TRT3; Q3TTZ0; Q3UWA2; Q8BXB5; Q8CI45;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Lipase member H;
DE EC=3.1.1.-;
DE Flags: Precursor;
GN Name=Liph;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=CD-1;
RX PubMed=12213196; DOI=10.1006/geno.2002.6837;
RA Jin W., Broedl U., Monajemi H., Glick J., Rader D.;
RT "Lipase h, a new member of the triglyceride lipase family synthesized by
RT the intestine.";
RL Genomics 80:268-273(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Cecum, Head, Testis, and Urinary bladder;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8CIV3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CIV3-2; Sequence=VSP_022506;
CC Name=3;
CC IsoId=Q8CIV3-3; Sequence=VSP_022505;
CC -!- TISSUE SPECIFICITY: Expressed in placenta and colon. Weakly expressed
CC in small intestine. {ECO:0000269|PubMed:12213196}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; AY093499; AAM18804.1; -; mRNA.
DR EMBL; AK048150; BAC33259.1; -; mRNA.
DR EMBL; AK134352; BAE22108.1; -; mRNA.
DR EMBL; AK136503; BAE23014.1; -; mRNA.
DR EMBL; AK161067; BAE36182.1; -; mRNA.
DR EMBL; AK162492; BAE36944.1; -; mRNA.
DR EMBL; BC037489; AAH37489.1; -; mRNA.
DR CCDS; CCDS37295.1; -. [Q8CIV3-3]
DR CCDS; CCDS37296.1; -. [Q8CIV3-1]
DR CCDS; CCDS88903.1; -. [Q8CIV3-2]
DR RefSeq; NP_001077363.1; NM_001083894.1. [Q8CIV3-1]
DR RefSeq; NP_001276511.1; NM_001289582.1. [Q8CIV3-2]
DR RefSeq; NP_700453.1; NM_153404.3. [Q8CIV3-3]
DR AlphaFoldDB; Q8CIV3; -.
DR SMR; Q8CIV3; -.
DR STRING; 10090.ENSMUSP00000062310; -.
DR ESTHER; mouse-LIPH; Phospholipase.
DR GlyGen; Q8CIV3; 1 site.
DR PhosphoSitePlus; Q8CIV3; -.
DR PaxDb; Q8CIV3; -.
DR PRIDE; Q8CIV3; -.
DR ProteomicsDB; 290031; -. [Q8CIV3-1]
DR ProteomicsDB; 290032; -. [Q8CIV3-2]
DR ProteomicsDB; 290033; -. [Q8CIV3-3]
DR Antibodypedia; 33838; 93 antibodies from 23 providers.
DR Ensembl; ENSMUST00000060673; ENSMUSP00000062310; ENSMUSG00000044626. [Q8CIV3-1]
DR Ensembl; ENSMUST00000074230; ENSMUSP00000073853; ENSMUSG00000044626. [Q8CIV3-3]
DR Ensembl; ENSMUST00000231766; ENSMUSP00000156378; ENSMUSG00000044626. [Q8CIV3-2]
DR GeneID; 239759; -.
DR KEGG; mmu:239759; -.
DR UCSC; uc007yru.1; mouse. [Q8CIV3-1]
DR UCSC; uc007yrv.1; mouse. [Q8CIV3-3]
DR UCSC; uc012adk.1; mouse. [Q8CIV3-2]
DR CTD; 200879; -.
DR MGI; MGI:2388029; Liph.
DR VEuPathDB; HostDB:ENSMUSG00000044626; -.
DR eggNOG; ENOG502QUQT; Eukaryota.
DR GeneTree; ENSGT00940000156285; -.
DR HOGENOM; CLU_027171_3_0_1; -.
DR InParanoid; Q8CIV3; -.
DR OMA; YPCSSYK; -.
DR OrthoDB; 534956at2759; -.
DR PhylomeDB; Q8CIV3; -.
DR TreeFam; TF324997; -.
DR Reactome; R-MMU-1483166; Synthesis of PA.
DR BioGRID-ORCS; 239759; 3 hits in 76 CRISPR screens.
DR ChiTaRS; Liph; mouse.
DR PRO; PR:Q8CIV3; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q8CIV3; protein.
DR Bgee; ENSMUSG00000044626; Expressed in epithelium of stomach and 97 other tissues.
DR ExpressionAtlas; Q8CIV3; baseline and differential.
DR Genevisible; Q8CIV3; MM.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0008201; F:heparin binding; ISO:MGI.
DR GO; GO:0016298; F:lipase activity; IBA:GO_Central.
DR GO; GO:0004465; F:lipoprotein lipase activity; IBA:GO_Central.
DR GO; GO:0004620; F:phospholipase activity; ISO:MGI.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0016042; P:lipid catabolic process; ISO:MGI.
DR GO; GO:0019433; P:triglyceride catabolic process; IBA:GO_Central.
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 Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Hydrolase; Lipid degradation; Lipid metabolism; Membrane;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..451
FT /note="Lipase member H"
FT /id="PRO_0000273322"
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 248
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 233..246
FT /evidence="ECO:0000250"
FT DISULFID 270..281
FT /evidence="ECO:0000250"
FT DISULFID 284..292
FT /evidence="ECO:0000250"
FT DISULFID 427..446
FT /evidence="ECO:0000250"
FT VAR_SEQ 210..239
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022505"
FT VAR_SEQ 210..211
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022506"
FT CONFLICT 29
FT /note="S -> N (in Ref. 2; BAE36182)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="D -> N (in Ref. 2; BAE23014)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="S -> Y (in Ref. 2; BAE36182)"
FT /evidence="ECO:0000305"
FT CONFLICT 395
FT /note="L -> M (in Ref. 1; AAM18804)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 451 AA; 50675 MW; DBB7F5311A08D70A CRC64;
MLRLCFFISF MCLVKSDTDE TCPSFTRLSF HSAVVGTGLS VRLMLYTQRD QTCAQIINST
ALGSLNVTKK TTFIIHGFRP TGSPPVWIEE LVQSLISVQE MNVVVVDWNR GATTVIYPHA
SSKTRQVASI LKEFIDQMLV KGASLDNIYM IGVSLGAHIA GFVGESYEGK LGRVTGLDPA
GPLFNGRPPE ERLDPSDALF VDVIHSDTDA LGYKEALGHI DFYPNGGLDQ PGCPKTIFGG
IKYFKCDHQM SVYLYLASLQ NNCSITAYPC DSYRDYRNGK CVSCGAGQIV PCPRVGYYAD
SWKEYLWDRD PPMTKAFFDT AETKPYCMYH YFVDIVSWNK SVRRGFITIK LRGEDGNITE
SKIDHEPSAF EKYHQVSLLA RFNRDLDKVA EISLLFSTGS VVGPKYKLRV LQMKLRSLAH
PDRPHLCRYD LVLMENVETS FQPILCSQQQ M
