LIPR1_MOUSE
ID LIPR1_MOUSE Reviewed; 473 AA.
AC Q5BKQ4; O70478; Q6NV82;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Inactive pancreatic lipase-related protein 1;
DE Short=PL-RP1;
DE Flags: Precursor;
GN Name=Pnliprp1;
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Swiss Webster; TISSUE=Lacrimal gland;
RX PubMed=10235541;
RA Remington S.G., Lima P.H., Nelson J.D.;
RT "Pancreatic lipase-related protein 1 mRNA in female mouse lacrimal gland.";
RL Invest. Ophthalmol. Vis. Sci. 40:1081-1090(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pancreas;
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].
RC TISSUE=Liver;
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).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=21115337; DOI=10.1016/j.jnutbio.2010.06.002;
RA Ren J., Chen Z., Zhang W., Li L., Sun R., Deng C., Fei Z., Sheng Z.,
RA Wang L., Sun X., Wang Z., Fei J.;
RT "Increased fat mass and insulin resistance in mice lacking pancreatic
RT lipase-related protein 1.";
RL J. Nutr. Biochem. 22:691-698(2011).
CC -!- FUNCTION: May function as inhibitor of dietary triglyceride digestion.
CC Lacks detectable lipase activity (in vitro) (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10235541}.
CC Note=Secreted in acinar cells.
CC -!- TISSUE SPECIFICITY: Expressed in female, but not in male, lacrimal
CC gland. Expressed in male and female sublingual gland and pancreas.
CC {ECO:0000269|PubMed:10235541}.
CC -!- DISRUPTION PHENOTYPE: Mice have no visible phenotype during the first
CC 10 weeks after birth and are fertile. Adult mice have normal body
CC weight, but higher than normal body fat and lower than normal lean
CC mass. They display impaired glucose tolerance and decreased insulin
CC sensitivity, and obesity and insulin resistance are exacerbated by
CC high-fat diet. Their pancreatic juice has greater ability to hydrolyze
CC triglycerides than that from wild-type littermates.
CC {ECO:0000269|PubMed:21115337}.
CC -!- MISCELLANEOUS: Expression is gender and species-specific.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; AF061274; AAC15774.1; -; mRNA.
DR EMBL; AK028105; BAC25750.1; -; mRNA.
DR EMBL; BC068266; AAH68266.1; -; mRNA.
DR EMBL; BC090985; AAH90985.1; -; mRNA.
DR CCDS; CCDS29931.1; -.
DR RefSeq; NP_061362.1; NM_018874.2.
DR AlphaFoldDB; Q5BKQ4; -.
DR SMR; Q5BKQ4; -.
DR STRING; 10090.ENSMUSP00000045465; -.
DR ESTHER; mouse-1plrp; Pancreatic_lipase.
DR PhosphoSitePlus; Q5BKQ4; -.
DR CPTAC; non-CPTAC-3721; -.
DR MaxQB; Q5BKQ4; -.
DR PaxDb; Q5BKQ4; -.
DR PeptideAtlas; Q5BKQ4; -.
DR PRIDE; Q5BKQ4; -.
DR ProteomicsDB; 292262; -.
DR Antibodypedia; 35303; 76 antibodies from 15 providers.
DR DNASU; 18946; -.
DR Ensembl; ENSMUST00000048644; ENSMUSP00000045465; ENSMUSG00000042179.
DR GeneID; 18946; -.
DR KEGG; mmu:18946; -.
DR UCSC; uc008iat.1; mouse.
DR CTD; 5407; -.
DR MGI; MGI:97723; Pnliprp1.
DR VEuPathDB; HostDB:ENSMUSG00000042179; -.
DR eggNOG; ENOG502QUK7; Eukaryota.
DR GeneTree; ENSGT00940000162375; -.
DR HOGENOM; CLU_027171_0_2_1; -.
DR InParanoid; Q5BKQ4; -.
DR OMA; NMFKVEE; -.
DR OrthoDB; 534956at2759; -.
DR PhylomeDB; Q5BKQ4; -.
DR TreeFam; TF324997; -.
DR Reactome; R-MMU-192456; Digestion of dietary lipid.
DR BioGRID-ORCS; 18946; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Pnliprp1; mouse.
DR PRO; PR:Q5BKQ4; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q5BKQ4; protein.
DR Bgee; ENSMUSG00000042179; Expressed in lacrimal gland and 64 other tissues.
DR ExpressionAtlas; Q5BKQ4; baseline and differential.
DR Genevisible; Q5BKQ4; MM.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0016298; F:lipase activity; ISO:MGI.
DR GO; GO:0004806; F:triglyceride lipase activity; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
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; IPR002331; Lipase_panc.
DR InterPro; IPR001024; PLAT/LH2_dom.
DR InterPro; IPR036392; PLAT/LH2_dom_sf.
DR InterPro; IPR000734; TAG_lipase.
DR PANTHER; PTHR11610; PTHR11610; 1.
DR Pfam; PF00151; Lipase; 1.
DR Pfam; PF01477; PLAT; 1.
DR PIRSF; PIRSF000865; Lipoprotein_lipase_LIPH; 1.
DR PRINTS; PR00823; PANCLIPASE.
DR PRINTS; PR00821; TAGLIPASE.
DR SMART; SM00308; LH2; 1.
DR SUPFAM; SSF49723; SSF49723; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
DR PROSITE; PS50095; PLAT; 1.
PE 1: Evidence at protein level;
KW Calcium; Disulfide bond; Metal-binding; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..473
FT /note="Inactive pancreatic lipase-related protein 1"
FT /id="PRO_0000017791"
FT DOMAIN 356..467
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT ACT_SITE 171
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 194
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 281
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT BINDING 205
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 21..27
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 109..120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 255..279
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 303..314
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 317..322
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 451..467
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT CONFLICT 59
FT /note="Y -> H (in Ref. 3; AAH90985)"
FT /evidence="ECO:0000305"
FT CONFLICT 97..115
FT /note="IDKGEENWVVDMCKNMFQV -> RPTSWPPGPSSGNNAEYAG (in Ref.
FT 2; AAH68266)"
FT /evidence="ECO:0000305"
FT CONFLICT 159..161
FT /note="NYS -> KYY (in Ref. 2; AAH68266)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="N -> D (in Ref. 3; AAH90985)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="L -> P (in Ref. 2; AAH68266)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="K -> R (in Ref. 2; AAH68266)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="K -> E (in Ref. 2; AAH68266)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 473 AA; 52696 MW; FB11C08E6BBC2763 CRC64;
MLILWTIPLF LLGAAQGKEV CYDNLGCFSD AEPWAGTAIR PLKLLPWSPE KINTRFLLYT
NENPTAFQTL QLSDPSTIEA SNFQVARKTR FIIHGFIDKG EENWVVDMCK NMFQVEEVNC
ICVDWKRGSQ TTYTQAANNV RVVGAQVAQM IDILVRNFNY SASKVHLIGH SLGAHVAGEA
GSRTPGLGRI TGLDPVEANF EGTPEEVRLD PSDADFVDVI HTDAAPLIPF LGFGTNQMVG
HFDFFPNGGQ YMPGCKKNAL SQIVDIDGIW SGTRDFVACN HLRSYKYYLE SILNPDGFAA
YPCASYRDFE SNKCFPCPDQ GCPQMGHYAD KFANNTSVEP QKFFLNTGEA KNFARWRYRV
SLTFSGRTVT GQVKVSLFGS NGNTRQCDIF RGIIKPGATH SNEFDAKLDV GTIEKVKFLW
NNHVVNPSFP KVGAAKITVQ KGEERTEHNF CSEETVREDI LLTLLPCKTS DTM
