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Protein

Inactive pancreatic lipase-related protein 1

Gene

Pnliprp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

May function as inhibitor of dietary triglyceride digestion. Lacks detectable lipase activity (in vitro) (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei171 – 1711NucleophileBy similarity
Active sitei194 – 1941Charge relay systemPROSITE-ProRule annotation
Metal bindingi205 – 2051Calcium; via carbonyl oxygenBy similarity
Metal bindingi208 – 2081Calcium; via carbonyl oxygenBy similarity
Metal bindingi210 – 2101CalciumBy similarity
Metal bindingi213 – 2131CalciumBy similarity
Active sitei281 – 2811Charge relay systemPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Protein family/group databases

ESTHERimouse-1plrp. Pancreatic_lipase.

Names & Taxonomyi

Protein namesi
Recommended name:
Inactive pancreatic lipase-related protein 1
Short name:
PL-RP1
Gene namesi
Name:Pnliprp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:97723. Pnliprp1.

Subcellular locationi

  • Secreted 1 Publication

  • Note: Secreted in acinar cells.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Disruption phenotypei

Mice have no visible phenotype during the first 10 weeks after birth and are fertile. Adult mice have normal body weight, but higher than normal body fat and lower than normal lean mass. They display impaired glucose tolerance and decreased insulin sensitivity, and obesity and insulin resistance are exacerbated by high-fat diet. Their pancreatic juice has greater ability to hydrolyze triglycerides than that from wild-type littermates.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence analysisAdd
BLAST
Chaini18 – 473456Inactive pancreatic lipase-related protein 1PRO_0000017791Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi21 ↔ 27PROSITE-ProRule annotation
Disulfide bondi109 ↔ 120PROSITE-ProRule annotation
Disulfide bondi255 ↔ 279PROSITE-ProRule annotation
Disulfide bondi303 ↔ 314PROSITE-ProRule annotation
Disulfide bondi317 ↔ 322PROSITE-ProRule annotation
Disulfide bondi451 ↔ 467PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiQ5BKQ4.
PaxDbiQ5BKQ4.
PRIDEiQ5BKQ4.

PTM databases

PhosphoSiteiQ5BKQ4.

Expressioni

Tissue specificityi

Expressed in female, but not in male, lacrimal gland. Expressed in male and female sublingual gland and pancreas.1 Publication

Gene expression databases

BgeeiQ5BKQ4.
CleanExiMM_PNLIPRP1.
GenevisibleiQ5BKQ4. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000045465.

Structurei

3D structure databases

ProteinModelPortaliQ5BKQ4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini356 – 467112PLATPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the AB hydrolase superfamily. Lipase family.Curated
Contains 1 PLAT domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IHRX. Eukaryota.
ENOG410Y92X. LUCA.
GeneTreeiENSGT00760000119069.
HOGENOMiHOG000038552.
HOVERGENiHBG003243.
InParanoidiQ5BKQ4.
KOiK14074.
OMAiLGFGTNQ.
OrthoDBiEOG7KSX8B.
PhylomeDBiQ5BKQ4.
TreeFamiTF324997.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR016272. Lipase_LIPH.
IPR013818. Lipase_N.
IPR002331. Lipase_panc.
IPR001024. PLAT/LH2_dom.
IPR000734. TAG_lipase.
[Graphical view]
PANTHERiPTHR11610. PTHR11610. 1 hit.
PfamiPF00151. Lipase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PIRSFiPIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTSiPR00823. PANCLIPASE.
PR00821. TAGLIPASE.
SMARTiSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMiSSF49723. SSF49723. 1 hit.
SSF53474. SSF53474. 1 hit.
PROSITEiPS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5BKQ4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLILWTIPLF LLGAAQGKEV CYDNLGCFSD AEPWAGTAIR PLKLLPWSPE
60 70 80 90 100
KINTRFLLYT NENPTAFQTL QLSDPSTIEA SNFQVARKTR FIIHGFIDKG
110 120 130 140 150
EENWVVDMCK NMFQVEEVNC ICVDWKRGSQ TTYTQAANNV RVVGAQVAQM
160 170 180 190 200
IDILVRNFNY SASKVHLIGH SLGAHVAGEA GSRTPGLGRI TGLDPVEANF
210 220 230 240 250
EGTPEEVRLD PSDADFVDVI HTDAAPLIPF LGFGTNQMVG HFDFFPNGGQ
260 270 280 290 300
YMPGCKKNAL SQIVDIDGIW SGTRDFVACN HLRSYKYYLE SILNPDGFAA
310 320 330 340 350
YPCASYRDFE SNKCFPCPDQ GCPQMGHYAD KFANNTSVEP QKFFLNTGEA
360 370 380 390 400
KNFARWRYRV SLTFSGRTVT GQVKVSLFGS NGNTRQCDIF RGIIKPGATH
410 420 430 440 450
SNEFDAKLDV GTIEKVKFLW NNHVVNPSFP KVGAAKITVQ KGEERTEHNF
460 470
CSEETVREDI LLTLLPCKTS DTM
Length:473
Mass (Da):52,696
Last modified:June 21, 2005 - v2
Checksum:iFB11C08E6BBC2763
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti59 – 591Y → H in AAH90985 (PubMed:15489334).Curated
Sequence conflicti97 – 11519IDKGE…NMFQV → RPTSWPPGPSSGNNAEYAG in AAH68266 (PubMed:16141072).CuratedAdd
BLAST
Sequence conflicti159 – 1613NYS → KYY in AAH68266 (PubMed:16141072).Curated
Sequence conflicti159 – 1591N → D in AAH90985 (PubMed:15489334).Curated
Sequence conflicti282 – 2821L → P in AAH68266 (PubMed:16141072).Curated
Sequence conflicti351 – 3511K → R in AAH68266 (PubMed:16141072).Curated
Sequence conflicti407 – 4071K → E in AAH68266 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF061274 mRNA. Translation: AAC15774.1.
AK028105 mRNA. Translation: BAC25750.1.
BC068266 mRNA. Translation: AAH68266.1.
BC090985 mRNA. Translation: AAH90985.1.
CCDSiCCDS29931.1.
RefSeqiNP_061362.1. NM_018874.2.
UniGeneiMm.10753.

Genome annotation databases

EnsembliENSMUST00000048644; ENSMUSP00000045465; ENSMUSG00000042179.
GeneIDi18946.
KEGGimmu:18946.
UCSCiuc008iat.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF061274 mRNA. Translation: AAC15774.1.
AK028105 mRNA. Translation: BAC25750.1.
BC068266 mRNA. Translation: AAH68266.1.
BC090985 mRNA. Translation: AAH90985.1.
CCDSiCCDS29931.1.
RefSeqiNP_061362.1. NM_018874.2.
UniGeneiMm.10753.

3D structure databases

ProteinModelPortaliQ5BKQ4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000045465.

Protein family/group databases

ESTHERimouse-1plrp. Pancreatic_lipase.

PTM databases

PhosphoSiteiQ5BKQ4.

Proteomic databases

MaxQBiQ5BKQ4.
PaxDbiQ5BKQ4.
PRIDEiQ5BKQ4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000048644; ENSMUSP00000045465; ENSMUSG00000042179.
GeneIDi18946.
KEGGimmu:18946.
UCSCiuc008iat.1. mouse.

Organism-specific databases

CTDi5407.
MGIiMGI:97723. Pnliprp1.

Phylogenomic databases

eggNOGiENOG410IHRX. Eukaryota.
ENOG410Y92X. LUCA.
GeneTreeiENSGT00760000119069.
HOGENOMiHOG000038552.
HOVERGENiHBG003243.
InParanoidiQ5BKQ4.
KOiK14074.
OMAiLGFGTNQ.
OrthoDBiEOG7KSX8B.
PhylomeDBiQ5BKQ4.
TreeFamiTF324997.

Miscellaneous databases

ChiTaRSiPnliprp1. mouse.
NextBioi295280.
PROiQ5BKQ4.
SOURCEiSearch...

Gene expression databases

BgeeiQ5BKQ4.
CleanExiMM_PNLIPRP1.
GenevisibleiQ5BKQ4. MM.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR016272. Lipase_LIPH.
IPR013818. Lipase_N.
IPR002331. Lipase_panc.
IPR001024. PLAT/LH2_dom.
IPR000734. TAG_lipase.
[Graphical view]
PANTHERiPTHR11610. PTHR11610. 1 hit.
PfamiPF00151. Lipase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PIRSFiPIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTSiPR00823. PANCLIPASE.
PR00821. TAGLIPASE.
SMARTiSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMiSSF49723. SSF49723. 1 hit.
SSF53474. SSF53474. 1 hit.
PROSITEiPS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Pancreatic lipase-related protein 1 mRNA in female mouse lacrimal gland."
    Remington S.G., Lima P.H., Nelson J.D.
    Invest. Ophthalmol. Vis. Sci. 40:1081-1090(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: Swiss Webster.
    Tissue: Lacrimal gland.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Pancreas.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Liver.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver, Lung, Pancreas and Spleen.
  5. "Increased fat mass and insulin resistance in mice lacking pancreatic lipase-related protein 1."
    Ren J., Chen Z., Zhang W., Li L., Sun R., Deng C., Fei Z., Sheng Z., Wang L., Sun X., Wang Z., Fei J.
    J. Nutr. Biochem. 22:691-698(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiLIPR1_MOUSE
AccessioniPrimary (citable) accession number: Q5BKQ4
Secondary accession number(s): O70478, Q6NV82
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: June 21, 2005
Last modified: November 11, 2015
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Expression is gender and species-specific.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.