P54317 (LIPR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pancreatic lipase-related protein 2
Short name=PL-RP2
EC=3.1.1.26
EC=3.1.1.3

Alternative name(s):
Galactolipase

Gene names

Name:	PNLIPRP2
Synonyms:	PLRP2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	469 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Lipase with broad substrate specificity. Can hydrolyze both phospholipids and galactolipids. Acts preferentially on monoglycerides, phospholipids and galactolipids. Contributes to milk fat hydrolysis. Ref.6 Ref.7 Ref.8
Catalytic activity	Triacylglycerol + H2O = diacylglycerol + a carboxylate. Ref.8 1,2-diacyl-3-beta-D-galactosyl-sn-glycerol + 2 H2O = 3-beta-D-galactosyl-sn-glycerol + 2 carboxylates. Ref.8
Subcellular location	Secreted Ref.6 Ref.8.
Tissue specificity	Pancreas.
Sequence similarities	Belongs to the AB hydrolase superfamily. Lipase family. Contains 1 PLAT domain.

Ontologies

Keywords
Biological process	Lipid degradation Lipid metabolism
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	galactolipid catabolic process Inferred from direct assay Ref.8. Source: UniProtKB lipid digestion Traceable author statement. Source: Reactome phospholipid catabolic process Inferred from direct assay Ref.8. Source: UniProtKB small molecule metabolic process Traceable author statement. Source: Reactome triglyceride metabolic process Traceable author statement Ref.1. Source: ProtInc
Cellular_component	extracellular space Inferred from direct assay Ref.8. Source: UniProtKB
Molecular_function	acylglycerol lipase activity Inferred from direct assay Ref.8. Source: UniProtKB calcium ion binding Inferred from direct assay Ref.8. Source: UniProtKB galactolipase activity Inferred from direct assay Ref.8. Source: UniProtKB phospholipase activity Inferred from direct assay Ref.8. Source: UniProtKB retinyl-palmitate esterase activity Inferred from electronic annotation. Source: EC triglyceride lipase activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 17

17

Potential

Chain

18 – 469

452

Pancreatic lipase-related protein 2

PRO_0000017793

Regions

Domain

357 – 469

113

PLAT

Sites

Active site

171

1

Nucleophile Ref.8

Active site

195

1

Charge relay system Ref.8

Active site

282

1

Charge relay system Ref.8

Metal binding

206

1

Calcium; via carbonyl oxygen

Metal binding

209

1

Calcium; via carbonyl oxygen

Metal binding

211

1

Calcium

Metal binding

214

1

Calcium

Amino acid modifications

Glycosylation

353

1

N-linked (GlcNAc...) Ref.8

Glycosylation

428

1

N-linked (GlcNAc...) Potential

Disulfide bond

21 ↔ 27

Ref.8

Disulfide bond

109 ↔ 120

Ref.8

Disulfide bond

256 ↔ 280

Ref.8

Disulfide bond

304 ↔ 315

Ref.8

Disulfide bond

318 ↔ 323

Ref.8

Disulfide bond

453 ↔ 469

Ref.8

Experimental info

Mutagenesis

353

1

N → Q: Loss of N-glycosylation. Ref.8

Sequence conflict

239

1

K → R in BAF84181. Ref.2

Sequence conflict

352

1

G → V in BAF84181. Ref.2

Secondary structure

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469

Helix Strand Turn

Details...

Beta strand

19 – 21

3

Helix

23 – 25

3

Beta strand

27 – 29

3

Turn

32 – 34

3

Beta strand

35 – 37

3

Helix

49 – 52

4

Beta strand

55 – 59

5

Beta strand

61 – 66

6

Beta strand

68 – 70

3

Beta strand

72 – 74

3

Helix

76 – 80

5

Beta strand

87 – 93

7

Helix

104 – 112

9

Turn

113 – 115

3

Beta strand

118 – 124

7

Helix

126 – 129

4

Helix

133 – 158

26

Helix

162 – 164

3

Beta strand

165 – 170

6

Helix

173 – 183

11

Turn

184 – 186

3

Beta strand

188 – 195

8

Turn

199 – 203

5

Turn

206 – 208

3

Helix

212 – 214

3

Beta strand

215 – 221

7

Beta strand

223 – 226

4

Beta strand

228 – 230

3

Beta strand

234 – 236

3

Beta strand

241 – 247

7

Turn

248 – 251

4

Helix

276 – 278

3

Helix

280 – 294

15

Beta strand

298 – 300

3

Helix

307 – 311

5

Turn

312 – 315

4

Beta strand

325 – 327

3

Helix

330 – 332

3

Turn

334 – 337

4

Beta strand

338 – 346

9

Beta strand

357 – 369

13

Beta strand

371 – 380

10

Beta strand

385 – 396

12

Beta strand

401 – 410

10

Beta strand

417 – 423

7

Beta strand

434 – 443

10

Turn

444 – 446

3

Beta strand

449 – 453

5

Beta strand

464 – 468

5

Sequences

	Sequence		Length	Mass (Da)
	P54317 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: D0E130295A94A725	FASTA	469	51,947
	10 20 30 40 50 60 MLPPWTLGLL LLATVRGKEV CYGQLGCFSD EKPWAGTLQR PVKLLPWSPE DIDTRFLLYT 70 80 90 100 110 120 NENPNNFQLI TGTEPDTIEA SNFQLDRKTR FIIHGFLDKA EDSWPSDMCK KMFEVEKVNC 130 140 150 160 170 180 ICVDWRHGSR AMYTQAVQNI RVVGAETAFL IQALSTQLGY SLEDVHVIGH SLGAHTAAEA 190 200 210 220 230 240 GRRLGGRVGR ITGLDPAGPC FQDEPEEVRL DPSDAVFVDV IHTDSSPIVP SLGFGMSQKV 250 260 270 280 290 300 GHLDFFPNGG KEMPGCKKNV LSTITDIDGI WEGIGGFVSC NHLRSFEYYS SSVLNPDGFL 310 320 330 340 350 360 GYPCASYDEF QESKCFPCPA EGCPKMGHYA DQFKGKTSAV EQTFFLNTGE SGNFTSWRYK 370 380 390 400 410 420 VSVTLSGKEK VNGYIRIALY GSNENSKQYE IFKGSLKPDA SHTCAIDVDF NVGKIQKVKF 430 440 450 460 LWNKRGINLS EPKLGASQIT VQSGEDGTEY NFCSSDTVEE NVLQSLYPC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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, MASS SPECTROMETRY, ACTIVE SITE, DISULFIDE BONDS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00005924.

PIR

B43357.

RefSeq

NP_005387.2. NM_005396.4.

UniGene

Hs.423598.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P54317.

ModBase

Search...

Polymorphism databases

DMDM

1708840.

Proteomic databases

PRIDE

P54317.

Protocols and materials databases

DNASU

5408.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

5408.

KEGG

hsa:5408.

UCSC

uc001lcq.3. human.

Organism-specific databases

CTD

5408.

GeneCards

GC10P118370.

H-InvDB

HIX0009237.

HGNC

HGNC:9157. PNLIPRP2.

MIM

604423. gene.

neXtProt

NX_P54317.

PharmGKB

PA33480.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG139430.

HOVERGEN

HBG003243.

InParanoid

P54317.

KO

K14075.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

Gene expression databases

CleanEx

HS_PNLIPRP2.

Genevestigator

P54317.

GermOnline

ENSG00000165862. Homo sapiens.

Family and domain databases

Gene3D

2.60.60.20. 1 hit.

InterPro

IPR000734. Lipase.
IPR008976. Lipase_LipOase.
IPR013818. Lipase_N.
IPR002331. Lipase_panc.
IPR001024. LipOase_LH2.
IPR016272. Lipoprotein_lipase_LIPH.
[Graphical view]

PANTHER

PTHR11610. PTHR11610. 1 hit.
PTHR11610:SF8. PTHR11610:SF8. 1 hit.

Pfam

PF00151. Lipase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]

PIRSF

PIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.

PRINTS

PR00823. PANCLIPASE.
PR00821. TAGLIPASE.

SMART

SM00308. LH2. 1 hit.
[Graphical view]

SUPFAM

SSF49723. Lipase_LipOase. 1 hit.

PROSITE

PS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P54317.

GenomeRNAi

5408.

NextBio

20939.

SOURCE

Search...

Entry information

Entry name

LIPR2_HUMAN

Accession

Primary (citable) accession number: P54317
Secondary accession number(s): A8K627, Q6IB55

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.