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Protein

Inactive pancreatic lipase-related protein 1

Gene

PNLIPRP1

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May function as inhibitor of dietary triglyceride digestion. Lacks detectable lipase activity towards triglycerides, diglycerides, phosphatidylcholine, galactolipids or cholesterol esters (in vitro).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei171 – 1711Nucleophile
Active sitei194 – 1941Charge relay system
Metal bindingi205 – 2051Calcium; via carbonyl oxygen
Metal bindingi208 – 2081Calcium; via carbonyl oxygen
Metal bindingi210 – 2101Calcium
Metal bindingi213 – 2131Calcium
Active sitei281 – 2811Charge relay system

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB
  • carboxylic ester hydrolase activity Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.1.1.26. 1153.

Protein family/group databases

ESTHERicanfa-1plip. Pancreatic_lipase.

Names & Taxonomyi

Protein namesi
Recommended name:
Inactive pancreatic lipase-related protein 1
Short name:
PL-RP1
Gene namesi
Name:PNLIPRP1
Synonyms:PLRP1
OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
Proteomesi
  • UP000002254 Componenti: Chromosome 28

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi196 – 1961V → A: Removes steric hindrance and restores lipase activity; when associated with P-198. 1 Publication
Mutagenesisi198 – 1981A → P: Removes steric hindrance and restores lipase activity; when associated with A-196. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 17171 PublicationAdd
BLAST
Chaini18 – 467450Inactive pancreatic lipase-related protein 1PRO_0000017789Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi21 ↔ 27PROSITE-ProRule annotation1 Publication
Disulfide bondi109 ↔ 120PROSITE-ProRule annotation1 Publication
Glycosylationi157 – 1571N-linked (GlcNAc...)1 Publication
Disulfide bondi255 ↔ 279PROSITE-ProRule annotation1 Publication
Disulfide bondi303 ↔ 314PROSITE-ProRule annotation1 Publication
Disulfide bondi317 ↔ 322PROSITE-ProRule annotation1 Publication
Disulfide bondi451 ↔ 467PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP06857.

Expressioni

Tissue specificityi

Detected in pancreas (at protein level).1 Publication

Interactioni

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000017453.

Structurei

Secondary structure

1
467
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi19 – 224Combined sources
Turni23 – 253Combined sources
Beta strandi26 – 294Combined sources
Turni32 – 343Combined sources
Beta strandi35 – 406Combined sources
Helixi49 – 524Combined sources
Beta strandi55 – 595Combined sources
Beta strandi61 – 666Combined sources
Beta strandi68 – 703Combined sources
Helixi76 – 794Combined sources
Beta strandi87 – 937Combined sources
Helixi104 – 1129Combined sources
Turni113 – 1153Combined sources
Beta strandi118 – 1247Combined sources
Helixi126 – 1294Combined sources
Helixi133 – 15826Combined sources
Helixi162 – 1643Combined sources
Beta strandi165 – 1706Combined sources
Helixi173 – 18210Combined sources
Beta strandi189 – 1946Combined sources
Turni198 – 2025Combined sources
Turni205 – 2073Combined sources
Helixi211 – 2133Combined sources
Beta strandi214 – 2207Combined sources
Helixi227 – 2304Combined sources
Beta strandi240 – 2467Combined sources
Turni247 – 2504Combined sources
Helixi266 – 2705Combined sources
Helixi279 – 29315Combined sources
Turni295 – 2984Combined sources
Helixi306 – 3105Combined sources
Beta strandi324 – 3263Combined sources
Helixi327 – 3315Combined sources
Beta strandi342 – 3454Combined sources
Beta strandi349 – 3513Combined sources
Beta strandi356 – 36712Combined sources
Beta strandi369 – 37911Combined sources
Beta strandi387 – 3948Combined sources
Beta strandi399 – 40810Combined sources
Beta strandi411 – 42212Combined sources
Beta strandi432 – 44110Combined sources
Beta strandi448 – 4514Combined sources
Beta strandi462 – 4665Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RP1X-ray2.10A18-467[»]
ProteinModelPortaliP06857.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06857.

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.
InParanoidiP06857.
KOiK14074.
OMAiKAKEVCY.
OrthoDBiEOG7KSX8B.
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.

P06857-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVSIWTIALF LLGAAKAKEV CYEQIGCFSD AEPWAGTAIR PLKVLPWSPE
60 70 80 90 100
RIGTRFLLYT NKNPNNFQTL LPSDPSTIEA SNFQTDKKTR FIIHGFIDKG
110 120 130 140 150
EENWLLDMCK NMFKVEEVNC ICVDWKKGSQ TSYTQAANNV RVVGAQVAQM
160 170 180 190 200
LSMLSANYSY SPSQVQLIGH SLGAHVAGEA GSRTPGLGRI TGLDPVEASF
210 220 230 240 250
QGTPEEVRLD PTDADFVDVI HTDAAPLIPF LGFGTSQQMG HLDFFPNGGE
260 270 280 290 300
EMPGCKKNAL SQIVDLDGIW EGTRDFVACN HLRSYKYYSE SILNPDGFAS
310 320 330 340 350
YPCASYRAFE SNKCFPCPDQ GCPQMGHYAD KFAVKTSDET QKYFLNTGDS
360 370 380 390 400
SNFARWRYGV SITLSGKRAT GQAKVALFGS KGNTHQFNIF KGILKPGSTH
410 420 430 440 450
SNEFDAKLDV GTIEKVKFLW NNNVVNPTFP KVGAAKITVQ KGEEKTVHSF
460
CSESTVREDV LLTLTPC
Length:467
Mass (Da):51,482
Last modified:November 1, 1990 - v2
Checksum:i5B186845404E5B5C
GO

Sequence cautioni

The sequence AAA30840.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti92 – 921I → T in AAA30885 (PubMed:3562437).Curated
Sequence conflicti98 – 981D → N in AAA30885 (PubMed:3562437).Curated
Sequence conflicti265 – 2651D → N in AAA30885 (PubMed:3562437).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M35302 mRNA. Translation: AAA30885.1.
M28151
, M28141, M28142, M28143, M28145, M28148, M28147, M28146, M28144, M28149, M28150 Genomic DNA. Translation: AAA30840.1. Sequence problems.
PIRiB24392. LIDG.
RefSeqiNP_001003319.2. NM_001003319.2.
UniGeneiCfa.3881.

Genome annotation databases

EnsembliENSCAFT00000018834; ENSCAFP00000017453; ENSCAFG00000011852.
GeneIDi404010.
KEGGicfa:404010.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M35302 mRNA. Translation: AAA30885.1.
M28151
, M28141, M28142, M28143, M28145, M28148, M28147, M28146, M28144, M28149, M28150 Genomic DNA. Translation: AAA30840.1. Sequence problems.
PIRiB24392. LIDG.
RefSeqiNP_001003319.2. NM_001003319.2.
UniGeneiCfa.3881.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RP1X-ray2.10A18-467[»]
ProteinModelPortaliP06857.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000017453.

Protein family/group databases

ESTHERicanfa-1plip. Pancreatic_lipase.

Proteomic databases

PaxDbiP06857.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSCAFT00000018834; ENSCAFP00000017453; ENSCAFG00000011852.
GeneIDi404010.
KEGGicfa:404010.

Organism-specific databases

CTDi5407.

Phylogenomic databases

eggNOGiENOG410IHRX. Eukaryota.
ENOG410Y92X. LUCA.
GeneTreeiENSGT00760000119069.
HOGENOMiHOG000038552.
HOVERGENiHBG003243.
InParanoidiP06857.
KOiK14074.
OMAiKAKEVCY.
OrthoDBiEOG7KSX8B.
TreeFamiTF324997.

Enzyme and pathway databases

BRENDAi3.1.1.26. 1153.

Miscellaneous databases

EvolutionaryTraceiP06857.
NextBioi20817497.

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

  1. "Primary structures of canine pancreatic lipase and phospholipase A2 messenger RNAs."
    Kerfelec B., Laforge K.S., Puigserver A., Scheele G.A.
    Pancreas 1:430-437(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Structure of the canine pancreatic lipase gene."
    Mickel F.S., Weidenbach F., Swarovsky B., Laforge K.S., Scheele G.A.
    J. Biol. Chem. 264:12895-12901(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Reactivation of the totally inactive pancreatic lipase RP1 by structure-predicted point mutations."
    Roussel A., de Caro J., Bezzine S., Gastinel L., de Caro A., Carriere F., Leydier S., Verger R., Cambillau C.
    Proteins 32:523-531(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH CALCIUM IONS, GLYCOSYLATION AT ASN-157, PROTEIN SEQUENCE OF 18-33, ABSENCE OF LIPASE ACTIVITY, DISULFIDE BONDS, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF VAL-196 AND ALA-198, TISSUE SPECIFICITY.
    Tissue: Pancreas.

Entry informationi

Entry nameiLIPR1_CANLF
AccessioniPrimary (citable) accession number: P06857
Secondary accession number(s): Q28287
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: November 1, 1990
Last modified: December 9, 2015
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Was originally (PubMed:3562437 and PubMed:2502543) thought to be the pancreatic lipase, but has been shown to lack lipase activity.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.