P16233 (LIPP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pancreatic triacylglycerol lipase
Short name=PL
Short name=PTL
Short name=Pancreatic lipase
EC=3.1.1.3

Gene names

Name:

PNLIP

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	465 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)

Catalytic activity	Triacylglycerol + H2O = diacylglycerol + a carboxylate. Ref.8
Subcellular location	Secreted.
Induction	By colipase/CLPS in the presence of bile salts.
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	intestinal cholesterol absorption Inferred from electronic annotation. Source: Compara lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW lipid digestion Traceable author statement. Source: Reactome retinoid metabolic process Traceable author statement. Source: Reactome small molecule metabolic process Traceable author statement. Source: Reactome steroid metabolic process Traceable author statement. Source: Reactome
Cellular_component	extracellular region Traceable author statement. Source: Reactome
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW retinyl-palmitate esterase activity Inferred from electronic annotation. Source: EC triglyceride lipase activity Traceable author statement PubMed 1783385. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 16

16

Chain

17 – 465

449

Pancreatic triacylglycerol lipase

PRO_0000017785

Regions

Domain

355 – 465

111

PLAT

Sites

Active site

169

1

Nucleophile

Active site

193

1

Charge relay system

Active site

280

1

Charge relay system

Metal binding

204

1

Calcium; via carbonyl oxygen

Metal binding

207

1

Calcium; via carbonyl oxygen

Metal binding

209

1

Calcium

Metal binding

212

1

Calcium

Amino acid modifications

Glycosylation

183

1

N-linked (GlcNAc...)

Disulfide bond

20 ↔ 26

Disulfide bond

107 ↔ 118

Disulfide bond

254 ↔ 278

Disulfide bond

302 ↔ 313

Disulfide bond

316 ↔ 321

Disulfide bond

449 ↔ 465

Secondary structure

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465

Helix Strand Turn

Details...

Beta strand

18 – 21

4

Helix

22 – 24

3

Beta strand

25 – 28

4

Beta strand

33 – 39

7

Helix

48 – 51

4

Beta strand

54 – 59

6

Beta strand

60 – 65

6

Beta strand

67 – 69

3

Helix

73 – 78

6

Beta strand

85 – 91

7

Helix

101 – 113

13

Beta strand

116 – 122

7

Helix

124 – 127

4

Helix

131 – 156

26

Helix

160 – 162

3

Beta strand

163 – 168

6

Helix

170 – 180

11

Turn

181 – 184

4

Beta strand

186 – 193

8

Turn

197 – 201

5

Turn

204 – 206

3

Helix

210 – 212

3

Beta strand

213 – 219

7

Helix

226 – 229

4

Beta strand

239 – 245

7

Helix

246 – 248

3

Helix

258 – 262

5

Helix

265 – 269

5

Helix

278 – 292

15

Helix

294 – 297

4

Helix

305 – 309

5

Beta strand

323 – 325

3

Helix

328 – 330

3

Turn

332 – 335

4

Beta strand

336 – 344

9

Beta strand

348 – 351

4

Beta strand

355 – 365

11

Beta strand

368 – 380

13

Beta strand

382 – 393

12

Beta strand

398 – 407

10

Beta strand

411 – 423

13

Beta strand

430 – 439

10

Beta strand

445 – 449

5

Beta strand

460 – 464

5

Sequences

	Sequence		Length	Mass (Da)
	P16233 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: 2BC49CC7F0E2DF52	FASTA	465	51,157
	10 20 30 40 50 60 MLPLWTLSLL LGAVAGKEVC YERLGCFSDD SPWSGITERP LHILPWSPKD VNTRFLLYTN 70 80 90 100 110 120 ENPNNFQEVA ADSSSISGSN FKTNRKTRFI IHGFIDKGEE NWLANVCKNL FKVESVNCIC 130 140 150 160 170 180 VDWKGGSRTG YTQASQNIRI VGAEVAYFVE FLQSAFGYSP SNVHVIGHSL GAHAAGEAGR 190 200 210 220 230 240 RTNGTIGRIT GLDPAEPCFQ GTPELVRLDP SDAKFVDVIH TDGAPIVPNL GFGMSQVVGH 250 260 270 280 290 300 LDFFPNGGVE MPGCKKNILS QIVDIDGIWE GTRDFAACNH LRSYKYYTDS IVNPDGFAGF 310 320 330 340 350 360 PCASYNVFTA NKCFPCPSGG CPQMGHYADR YPGKTNDVGQ KFYLDTGDAS NFARWRYKVS 370 380 390 400 410 420 VTLSGKKVTG HILVSLFGNK GNSKQYEIFK GTLKPDSTHS NEFDSDVDVG DLQMVKFIWY 430 440 450 460 NNVINPTLPR VGASKIIVET NVGKQFNFCS PETVREEVLL TLTPC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of human pancreatic lipase cDNA." Lowe M.E., Rosenblum J.L., Strauss A.W. J. Biol. Chem. 264:20042-20048(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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.
[3]	"The human pancreatic lipase-encoding gene: structure and conservation of an Alu sequence in the lipase gene family." Sims H.F., Jennens M.L., Lowe M.E. Gene 131:281-285(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"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].
[5]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	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].
[7]	"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: Lung.
[8]	"Hydrolysis of retinyl esters by pancreatic triglyceride lipase." van Bennekum A.M., Fisher E.A., Blaner W.S., Harrison E.H. Biochemistry 39:4900-4906(2000) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY.
[9]	"Structure of human pancreatic lipase." Winkler F.K., D'Arcy A., Hunziker W. Nature 343:771-774(1990) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[10]	"Structure of the pancreatic lipase-procolipase complex." van Tilbeurgh H., Sarda L., Verger R., Cambillau C. Nature 359:159-162(1992) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH CLPS.
[11]	"Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography." van Tilbeurgh H., Egloff M.-P., Martinez C., Rugani N., Verger R., Cambillau C. Nature 362:814-820(1993) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH CLPS.
[12]	"Structure-function relationships in naturally occurring mutants of pancreatic lipase." Carriere F., Thirstrup K., Boel E., Verger R., Thim L. Protein Eng. 7:563-569(1994) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 354-465.
+	Additional computationally mapped references.

Web resources

Wikipedia

Pancreatic lipase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J05125 mRNA. Translation: AAA36740.1.
M93285 mRNA. Translation: AAA60129.1.
L24529 , L11242, L24502, L24522, L24523, L24525, L24526, L24527, L24528 Genomic DNA. Translation: AAA99053.1.
AK313941 mRNA. Translation: BAG36659.1.
AL731653 Genomic DNA. Translation: CAH72667.1.
CH471066 Genomic DNA. Translation: EAW49451.1.
BC014309 mRNA. Translation: AAH14309.1.

IPI

IPI00027720.

PIR

C43357.

RefSeq

NP_000927.1. NM_000936.2.

UniGene

Hs.501135.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GPL	X-ray	2.01	A	18-465	[»]
1LPA	X-ray	3.04	B	17-465	[»]
1LPB	X-ray	2.46	B	17-465	[»]
1N8S	X-ray	3.04	A	17-465	[»]

ProteinModelPortal

P16233.

ModBase

Search...

Protein-protein interaction databases

IntAct

P16233. 1 interaction.

MINT

MINT-1179407.

STRING

9606.ENSP00000358223.

PTM databases

PhosphoSite

P16233.

Polymorphism databases

DMDM

126318.

Proteomic databases

PaxDb

P16233.

PRIDE

P16233.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000369221; ENSP00000358223; ENSG00000175535.

GeneID

5406.

KEGG

hsa:5406.

UCSC

uc001lcm.3. human.

Organism-specific databases

CTD

5406.

GeneCards

GC10P118305.

HGNC

HGNC:9155. PNLIP.

MIM

246600. gene+phenotype.

neXtProt

NX_P16233.

PharmGKB

PA33478.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG40923.

HOGENOM

HOG000038552.

HOVERGEN

HBG003243.

InParanoid

P16233.

KO

K14073.

OMA

KFIWYNN.

OrthoDB

EOG4WH8KM.

PhylomeDB

P16233.

Enzyme and pathway databases

BioCyc

MetaCyc:HS10947-MONOMER.

Reactome

REACT_111217. Metabolism.

Gene expression databases

Bgee

P16233.

CleanEx

HS_PNLIP.

Genevestigator

P16233.

GermOnline

ENSG00000175535. 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

BindingDB

P16233.

ChEMBL

CHEMBL1812.

ChiTaRS

PNLIP. human.

DrugBank

DB00522. Bentiromide.
DB01083. Orlistat.

EvolutionaryTrace

P16233.

GenomeRNAi

5406.

NextBio

20931.

SOURCE

Search...

Entry information

Entry name

LIPP_HUMAN

Accession

Primary (citable) accession number: P16233
Secondary accession number(s): Q5VSQ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	May 1, 2013
This is version 144 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.