SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P54317

- LIPR2_HUMAN

UniProt

P54317 - LIPR2_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Pancreatic lipase-related protein 2
Gene
PNLIPRP2, PLRP2
Organism
Homo sapiens (Human)
Status
Reviewed - 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei171 – 1711Nucleophile1 Publication
Active sitei195 – 1951Charge relay system1 Publication
Metal bindingi206 – 2061Calcium; via carbonyl oxygen
Metal bindingi209 – 2091Calcium; via carbonyl oxygen
Metal bindingi211 – 2111Calcium
Metal bindingi214 – 2141Calcium
Active sitei282 – 2821Charge relay system1 Publication

GO - Molecular functioni

  1. acylglycerol lipase activity Source: UniProtKB
  2. calcium ion binding Source: UniProtKB
  3. galactolipase activity Source: UniProtKB
  4. phospholipase activity Source: UniProtKB
  5. triglyceride lipase activity Source: ProtInc

GO - Biological processi

  1. galactolipid catabolic process Source: UniProtKB
  2. lipid digestion Source: Reactome
  3. phospholipid catabolic process Source: UniProtKB
  4. small molecule metabolic process Source: Reactome
  5. 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

ReactomeiREACT_9518. Digestion of dietary lipid.

Names & Taxonomyi

Protein namesi
Recommended name:
Pancreatic lipase-related protein 2 (EC:3.1.1.26, EC:3.1.1.3)
Short name:
PL-RP2
Alternative name(s):
Galactolipase
Gene namesi
Synonyms:PLRP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:9157. PNLIPRP2.

Subcellular locationi

Secreted 2 Publications

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. extracellular space Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi353 – 3531N → Q: Loss of N-glycosylation. 1 Publication

Organism-specific databases

PharmGKBiPA33480.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717 Reviewed prediction
Add
BLAST
Chaini18 – 469452Pancreatic lipase-related protein 2
PRO_0000017793Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi21 ↔ 271 Publication
Disulfide bondi109 ↔ 1201 Publication
Disulfide bondi256 ↔ 2801 Publication
Disulfide bondi304 ↔ 3151 Publication
Disulfide bondi318 ↔ 3231 Publication
Glycosylationi353 – 3531N-linked (GlcNAc...)1 Publication
Glycosylationi428 – 4281N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi453 ↔ 4691 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP54317.

Expressioni

Tissue specificityi

Pancreas.

Gene expression databases

CleanExiHS_PNLIPRP2.
GenevestigatoriP54317.

Interactioni

Protein-protein interaction databases

BioGridi111409. 2 interactions.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi19 – 213
Helixi23 – 253
Beta strandi27 – 293
Turni32 – 343
Beta strandi35 – 373
Helixi49 – 524
Beta strandi55 – 595
Beta strandi61 – 666
Beta strandi68 – 703
Beta strandi72 – 743
Helixi76 – 805
Beta strandi87 – 937
Helixi104 – 1129
Turni113 – 1153
Beta strandi118 – 1247
Helixi126 – 1294
Helixi133 – 15826
Helixi162 – 1643
Beta strandi165 – 1706
Helixi173 – 18311
Turni184 – 1863
Beta strandi188 – 1958
Turni199 – 2035
Turni206 – 2083
Helixi212 – 2143
Beta strandi215 – 2217
Beta strandi223 – 2264
Beta strandi228 – 2303
Beta strandi234 – 2363
Beta strandi241 – 2477
Turni248 – 2514
Helixi276 – 2783
Helixi280 – 29415
Beta strandi298 – 3003
Helixi307 – 3115
Turni312 – 3154
Beta strandi325 – 3273
Helixi330 – 3323
Turni334 – 3374
Beta strandi338 – 3469
Beta strandi357 – 36913
Beta strandi371 – 38010
Beta strandi385 – 39612
Beta strandi401 – 41010
Beta strandi417 – 4237
Beta strandi434 – 44310
Turni444 – 4463
Beta strandi449 – 4535
Beta strandi464 – 4685

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OXEX-ray2.80A/B18-469[»]
2PVSX-ray3.00A/B18-469[»]
ProteinModelPortaliP54317.
SMRiP54317. Positions 18-469.

Miscellaneous databases

EvolutionaryTraceiP54317.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini357 – 469113PLAT
Add
BLAST

Sequence similaritiesi

Contains 1 PLAT domain.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG139430.
HOVERGENiHBG003243.
InParanoidiP54317.
KOiK14075.
PhylomeDBiP54317.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000734. Lipase.
IPR008976. Lipase_LipOase.
IPR013818. Lipase_N.
IPR002331. Lipase_panc.
IPR016272. Lipoprotein_lipase_LIPH.
IPR001024. PLAT/LH2_dom.
[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

MLPPWTLGLL LLATVRGKEV CYGQLGCFSD EKPWAGTLQR PVKLLPWSPE    50
DIDTRFLLYT NENPNNFQLI TGTEPDTIEA SNFQLDRKTR FIIHGFLDKA 100
EDSWPSDMCK KMFEVEKVNC ICVDWRHGSR AMYTQAVQNI RVVGAETAFL 150
IQALSTQLGY SLEDVHVIGH SLGAHTAAEA GRRLGGRVGR ITGLDPAGPC 200
FQDEPEEVRL DPSDAVFVDV IHTDSSPIVP SLGFGMSQKV GHLDFFPNGG 250
KEMPGCKKNV LSTITDIDGI WEGIGGFVSC NHLRSFEYYS SSVLNPDGFL 300
GYPCASYDEF QESKCFPCPA EGCPKMGHYA DQFKGKTSAV EQTFFLNTGE 350
SGNFTSWRYK VSVTLSGKEK VNGYIRIALY GSNENSKQYE IFKGSLKPDA 400
SHTCAIDVDF NVGKIQKVKF LWNKRGINLS EPKLGASQIT VQSGEDGTEY 450
NFCSSDTVEE NVLQSLYPC 469
Length:469
Mass (Da):51,947
Last modified:October 1, 1996 - v1
Checksum:iD0E130295A94A725
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti239 – 2391K → R in BAF84181. 1 Publication
Sequence conflicti352 – 3521G → V in BAF84181. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
UCSCiuc001lcq.3. human.

Polymorphism databases

DMDMi1708840.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi B43357.
RefSeqi NP_005387.2. NM_005396.4.
UniGenei Hs.423598.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2OXE X-ray 2.80 A/B 18-469 [» ]
2PVS X-ray 3.00 A/B 18-469 [» ]
ProteinModelPortali P54317.
SMRi P54317. Positions 18-469.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111409. 2 interactions.

Chemistry

ChEMBLi CHEMBL2169728.

Polymorphism databases

DMDMi 1708840.

Proteomic databases

PRIDEi P54317.

Protocols and materials databases

DNASUi 5408.
Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 5408.
KEGGi hsa:5408.
UCSCi uc001lcq.3. human.

Organism-specific databases

CTDi 5408.
GeneCardsi GC10P118370.
H-InvDB HIX0009237.
HGNCi HGNC:9157. PNLIPRP2.
MIMi 604423. gene.
neXtProti NX_P54317.
PharmGKBi PA33480.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG139430.
HOVERGENi HBG003243.
InParanoidi P54317.
KOi K14075.
PhylomeDBi P54317.

Enzyme and pathway databases

Reactomei REACT_9518. Digestion of dietary lipid.

Miscellaneous databases

EvolutionaryTracei P54317.
GenomeRNAii 5408.
NextBioi 20939.
PROi P54317.
SOURCEi Search...

Gene expression databases

CleanExi HS_PNLIPRP2.
Genevestigatori P54317.

Family and domain databases

Gene3Di 2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR000734. Lipase.
IPR008976. Lipase_LipOase.
IPR013818. Lipase_N.
IPR002331. Lipase_panc.
IPR016272. Lipoprotein_lipase_LIPH.
IPR001024. PLAT/LH2_dom.
[Graphical view ]
PANTHERi PTHR11610. PTHR11610. 1 hit.
Pfami PF00151. Lipase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view ]
PIRSFi PIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTSi PR00823. PANCLIPASE.
PR00821. TAGLIPASE.
SMARTi SM00308. LH2. 1 hit.
[Graphical view ]
SUPFAMi SSF49723. SSF49723. 1 hit.
SSF53474. SSF53474. 1 hit.
PROSITEi PS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Two novel human pancreatic lipase related proteins, hPLRP1 and hPLRP2. Differences in colipase dependence and in lipase activity."
    Giller T., Buchwald P., Blum-Kaelin D., Hunziker W.
    J. Biol. Chem. 267:16509-16516(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Pancreas.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pancreas.
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: Pancreas.
  6. "Individual and combined action of pancreatic lipase and pancreatic lipase-related proteins 1 and 2 on native versus homogenized milk fat globules."
    Berton A., Sebban-Kreuzer C., Rouvellac S., Lopez C., Crenon I.
    Mol. Nutr. Food Res. 53:1592-1602(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  7. "Lipolysis of natural long chain and synthetic medium chain galactolipids by pancreatic lipase-related protein 2."
    Amara S., Barouh N., Lecomte J., Lafont D., Robert S., Villeneuve P., De Caro A., Carriere F.
    Biochim. Biophys. Acta 1801:508-516(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation."
    Eydoux C., Spinelli S., Davis T.L., Walker J.R., Seitova A., Dhe-Paganon S., De Caro A., Cambillau C., Carriere F.
    Biochemistry 47:9553-9564(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-469 IN COMPLEX WITH CALCIUM IONS, CATALYTIC ACTIVITY, FUNCTION, GLYCOSYLATION AT ASN-353, MUTAGENESIS OF ASN-353, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE, DISULFIDE BONDS.

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: September 3, 2014
This is version 119 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

External Data

Dasty 3

Similar proteinsi