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Protein

Pancreatic lipase-related protein 2

Gene

PNLIPRP2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Lipase with broad substrate specificity. Can hydrolyze both phospholipids and galactolipids. Acts preferentially on monoglycerides, phospholipids and galactolipids. Contributes to milk fat hydrolysis.3 Publications

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.1 Publication
1,2-diacyl-3-beta-D-galactosyl-sn-glycerol + 2 H2O = 3-beta-D-galactosyl-sn-glycerol + 2 carboxylates.1 Publication

Enzyme regulationi

CLPS stimulates triacylglycerol lipase activity. Triacylglycerol lipase activity is not inhibited by increasing bile salt concentration.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei171Nucleophile1 Publication1
Active sitei195Charge relay systemPROSITE-ProRule annotation1 Publication1
Metal bindingi206Calcium; via carbonyl oxygen1
Metal bindingi209Calcium; via carbonyl oxygen1
Metal bindingi211Calcium1
Metal bindingi214Calcium1
Active sitei282Charge relay systemPROSITE-ProRule annotation1 Publication1

GO - Molecular functioni

  • acylglycerol lipase activity Source: UniProtKB
  • calcium ion binding Source: UniProtKB
  • galactolipase activity Source: UniProtKB
  • phospholipase activity Source: UniProtKB
  • triglyceride lipase activity Source: UniProtKB

GO - Biological processi

  • galactolipid catabolic process Source: UniProtKB
  • lipid digestion Source: Reactome
  • phospholipid catabolic process Source: UniProtKB
  • triglyceride metabolic process Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:HS09295-MONOMER.
BRENDAi3.1.1.26. 2681.
ReactomeiR-HSA-192456. Digestion of dietary lipid.

Protein family/group databases

ESTHERihuman-PNLIPRP2. Pancreatic_lipase.

Chemistry databases

SwissLipidsiSLP:000001434.

Names & Taxonomyi

Protein namesi
Recommended name:
Pancreatic lipase-related protein 2Imported (EC:3.1.1.26, EC:3.1.1.3)
Short name:
PL-RP21 Publication
Alternative name(s):
Galactolipase
Gene namesi
Name:PNLIPRP2Imported
Synonyms:PLRP21 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:9157. PNLIPRP2.

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi353N → Q: Loss of N-glycosylation. 1 Publication1

Organism-specific databases

DisGeNETi5408.
PharmGKBiPA33480.

Chemistry databases

ChEMBLiCHEMBL2169728.

Polymorphism and mutation databases

BioMutaiPNLIPRP2.
DMDMi1708840.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Sequence analysisAdd BLAST17
ChainiPRO_000001779318 – 469Pancreatic lipase-related protein 2Add BLAST452

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi21 ↔ 27PROSITE-ProRule annotation1 Publication
Disulfide bondi109 ↔ 120PROSITE-ProRule annotation1 Publication
Disulfide bondi256 ↔ 280PROSITE-ProRule annotation1 Publication
Disulfide bondi304 ↔ 315PROSITE-ProRule annotation1 Publication
Disulfide bondi318 ↔ 323PROSITE-ProRule annotation1 Publication
Glycosylationi353N-linked (GlcNAc...)1 Publication1
Glycosylationi428N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi453 ↔ 469PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PeptideAtlasiP54317.
PRIDEiP54317.

Expressioni

Tissue specificityi

Pancreas.

Gene expression databases

CleanExiHS_PNLIPRP2.

Interactioni

Protein-protein interaction databases

BioGridi111409. 3 interactors.

Structurei

Secondary structure

1469
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi19 – 21Combined sources3
Helixi23 – 25Combined sources3
Beta strandi27 – 29Combined sources3
Turni32 – 34Combined sources3
Beta strandi35 – 37Combined sources3
Helixi49 – 52Combined sources4
Beta strandi55 – 59Combined sources5
Beta strandi61 – 66Combined sources6
Beta strandi68 – 70Combined sources3
Beta strandi72 – 74Combined sources3
Helixi76 – 80Combined sources5
Beta strandi87 – 93Combined sources7
Helixi104 – 112Combined sources9
Turni113 – 115Combined sources3
Beta strandi118 – 124Combined sources7
Helixi126 – 129Combined sources4
Helixi133 – 158Combined sources26
Helixi162 – 164Combined sources3
Beta strandi165 – 170Combined sources6
Helixi173 – 183Combined sources11
Turni184 – 186Combined sources3
Beta strandi188 – 195Combined sources8
Turni199 – 203Combined sources5
Turni206 – 208Combined sources3
Helixi212 – 214Combined sources3
Beta strandi215 – 221Combined sources7
Beta strandi223 – 226Combined sources4
Beta strandi228 – 230Combined sources3
Beta strandi234 – 236Combined sources3
Beta strandi241 – 247Combined sources7
Turni248 – 251Combined sources4
Helixi276 – 278Combined sources3
Helixi280 – 294Combined sources15
Beta strandi298 – 300Combined sources3
Helixi307 – 311Combined sources5
Turni312 – 315Combined sources4
Beta strandi325 – 327Combined sources3
Helixi330 – 332Combined sources3
Turni334 – 337Combined sources4
Beta strandi338 – 346Combined sources9
Beta strandi357 – 369Combined sources13
Beta strandi371 – 380Combined sources10
Beta strandi385 – 396Combined sources12
Beta strandi401 – 410Combined sources10
Beta strandi417 – 423Combined sources7
Beta strandi434 – 443Combined sources10
Turni444 – 446Combined sources3
Beta strandi449 – 453Combined sources5
Beta strandi464 – 468Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2OXEX-ray2.80A/B18-469[»]
2PVSX-ray3.00A/B18-469[»]
ProteinModelPortaliP54317.
SMRiP54317.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP54317.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini357 – 469PLATPROSITE-ProRule annotationAdd BLAST113

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG003243.
InParanoidiP54317.
KOiK14075.
PhylomeDBiP54317.

Family and domain databases

CDDicd00707. Pancreat_lipase_like. 1 hit.
Gene3Di2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR013818. Lipase/vitellogenin.
IPR016272. Lipase_LIPH.
IPR033906. 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.

P54317-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPPWTLGLL LLATVRGKEV CYGQLGCFSD EKPWAGTLQR PVKLLPWSPE
60 70 80 90 100
DIDTRFLLYT NENPNNFQLI TGTEPDTIEA SNFQLDRKTR FIIHGFLDKA
110 120 130 140 150
EDSWPSDMCK KMFEVEKVNC ICVDWRHGSR AMYTQAVQNI RVVGAETAFL
160 170 180 190 200
IQALSTQLGY SLEDVHVIGH SLGAHTAAEA GRRLGGRVGR ITGLDPAGPC
210 220 230 240 250
FQDEPEEVRL DPSDAVFVDV IHTDSSPIVP SLGFGMSQKV GHLDFFPNGG
260 270 280 290 300
KEMPGCKKNV LSTITDIDGI WEGIGGFVSC NHLRSFEYYS SSVLNPDGFL
310 320 330 340 350
GYPCASYDEF QESKCFPCPA EGCPKMGHYA DQFKGKTSAV EQTFFLNTGE
360 370 380 390 400
SGNFTSWRYK VSVTLSGKEK VNGYIRIALY GSNENSKQYE IFKGSLKPDA
410 420 430 440 450
SHTCAIDVDF NVGKIQKVKF LWNKRGINLS EPKLGASQIT VQSGEDGTEY
460
NFCSSDTVEE NVLQSLYPC
Length:469
Mass (Da):51,947
Last modified:October 1, 1996 - v1
Checksum:iD0E130295A94A725
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti239K → R in BAF84181 (PubMed:14702039).Curated1
Sequence conflicti352G → V in BAF84181 (PubMed:14702039).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M93284 mRNA. Translation: AAA59533.1.
AK291492 mRNA. Translation: BAF84181.1.
CR456949 mRNA. Translation: CAG33230.1.
CH471066 Genomic DNA. Translation: EAW49448.1.
BC005989 mRNA. Translation: AAH05989.1.
PIRiB43357.
RefSeqiNP_005387.2. NM_005396.4.
UniGeneiHs.423598.

Genome annotation databases

GeneIDi5408.
KEGGihsa:5408.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M93284 mRNA. Translation: AAA59533.1.
AK291492 mRNA. Translation: BAF84181.1.
CR456949 mRNA. Translation: CAG33230.1.
CH471066 Genomic DNA. Translation: EAW49448.1.
BC005989 mRNA. Translation: AAH05989.1.
PIRiB43357.
RefSeqiNP_005387.2. NM_005396.4.
UniGeneiHs.423598.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2OXEX-ray2.80A/B18-469[»]
2PVSX-ray3.00A/B18-469[»]
ProteinModelPortaliP54317.
SMRiP54317.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111409. 3 interactors.

Chemistry databases

ChEMBLiCHEMBL2169728.
SwissLipidsiSLP:000001434.

Protein family/group databases

ESTHERihuman-PNLIPRP2. Pancreatic_lipase.

Polymorphism and mutation databases

BioMutaiPNLIPRP2.
DMDMi1708840.

Proteomic databases

PeptideAtlasiP54317.
PRIDEiP54317.

Protocols and materials databases

DNASUi5408.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi5408.
KEGGihsa:5408.

Organism-specific databases

CTDi5408.
DisGeNETi5408.
GeneCardsiPNLIPRP2.
H-InvDBHIX0009237.
HGNCiHGNC:9157. PNLIPRP2.
MIMi604423. gene.
neXtProtiNX_P54317.
PharmGKBiPA33480.
GenAtlasiSearch...

Phylogenomic databases

HOVERGENiHBG003243.
InParanoidiP54317.
KOiK14075.
PhylomeDBiP54317.

Enzyme and pathway databases

BioCyciZFISH:HS09295-MONOMER.
BRENDAi3.1.1.26. 2681.
ReactomeiR-HSA-192456. Digestion of dietary lipid.

Miscellaneous databases

EvolutionaryTraceiP54317.
GenomeRNAii5408.
PROiP54317.
SOURCEiSearch...

Gene expression databases

CleanExiHS_PNLIPRP2.

Family and domain databases

CDDicd00707. Pancreat_lipase_like. 1 hit.
Gene3Di2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR013818. Lipase/vitellogenin.
IPR016272. Lipase_LIPH.
IPR033906. 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...

Entry informationi

Entry nameiLIPR2_HUMAN
AccessioniPrimary (citable) accession number: P54317
Secondary accession number(s): A8K627, Q6IB55
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 30, 2016
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.