PNLIPRP1

Functionⁱ

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

Sites

Feature key	Position(s)	Length	Description
Active siteⁱ	171 – 171	1	Nucleophile
Active siteⁱ	194 – 194	1	Charge relay system
Metal bindingⁱ	205 – 205	1	Calcium; via carbonyl oxygen
Metal bindingⁱ	208 – 208	1	Calcium; via carbonyl oxygen
Metal bindingⁱ	210 – 210	1	Calcium
Metal bindingⁱ	213 – 213	1	Calcium
Active siteⁱ	281 – 281	1	Charge relay system

GO - Molecular functionⁱ

calcium ion binding Source: UniProtKB
triglyceride lipase activity
Source: ProtInc
Traceable author statementⁱ
- 1379598

GO - Biological processⁱ

lipid metabolic process Source: InterPro

Complete GO annotation...

Keywords - Ligandⁱ

Calcium, Metal-binding

Enzyme and pathway databases

Reactomeⁱ	REACT_9518. Digestion of dietary lipid.

Reactomeⁱ

REACT_9518. Digestion of dietary lipid.

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Inactive pancreatic lipase-related protein 1 Short name: PL-RP1
Gene namesⁱ	Name:PNLIPRP1 Synonyms:PLRP1
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640: Chromosome 10

Organism-specific databases

HGNCⁱ	HGNC:9156. PNLIPRP1.

HGNCⁱ

HGNC:9156. PNLIPRP1.

Subcellular locationⁱ

Secreted 2 Publications

GO - Cellular componentⁱ

extracellular region
Source: ProtInc
Traceable author statementⁱ
- 1379598

Complete GO annotation...

Keywords - Cellular componentⁱ

Secreted

Pathology & Biotechⁱ

Organism-specific databases

PharmGKBⁱ	PA33479.

PharmGKBⁱ

PA33479.

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Signal peptideⁱ	1 – 17	17	Sequence Analysis			Add BLAST
Chainⁱ	18 – 467	450	Inactive pancreatic lipase-related protein 1		PRO_0000017790	Add BLAST

Amino acid modifications

Feature key	Position(s)	Description
Disulfide bondⁱ	21 ↔ 27	1 Publication Manual assertion based on experiment inⁱ Ref.5 "Structure of the human pancreatic lipase-related protein 1." Structural genomics consortium (SGC) Submitted (FEB-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 18-467 IN COMPLEX WITH CALCIUM IONS, DISULFIDE BONDS. PROSITE-ProRule annotation Manual assertion according to rulesⁱ PROSITE-ProRule:PRU00152
Disulfide bondⁱ	109 ↔ 120	1 Publication Manual assertion based on experiment inⁱ Ref.5 "Structure of the human pancreatic lipase-related protein 1." Structural genomics consortium (SGC) Submitted (FEB-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 18-467 IN COMPLEX WITH CALCIUM IONS, DISULFIDE BONDS. PROSITE-ProRule annotation Manual assertion according to rulesⁱ PROSITE-ProRule:PRU00152
Disulfide bondⁱ	255 ↔ 279	1 Publication Manual assertion based on experiment inⁱ Ref.5 "Structure of the human pancreatic lipase-related protein 1." Structural genomics consortium (SGC) Submitted (FEB-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 18-467 IN COMPLEX WITH CALCIUM IONS, DISULFIDE BONDS. PROSITE-ProRule annotation Manual assertion according to rulesⁱ PROSITE-ProRule:PRU00152
Disulfide bondⁱ	303 ↔ 314	1 Publication Manual assertion based on experiment inⁱ Ref.5 "Structure of the human pancreatic lipase-related protein 1." Structural genomics consortium (SGC) Submitted (FEB-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 18-467 IN COMPLEX WITH CALCIUM IONS, DISULFIDE BONDS. PROSITE-ProRule annotation Manual assertion according to rulesⁱ PROSITE-ProRule:PRU00152
Disulfide bondⁱ	317 ↔ 322	1 Publication Manual assertion based on experiment inⁱ Ref.5 "Structure of the human pancreatic lipase-related protein 1." Structural genomics consortium (SGC) Submitted (FEB-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 18-467 IN COMPLEX WITH CALCIUM IONS, DISULFIDE BONDS. PROSITE-ProRule annotation Manual assertion according to rulesⁱ PROSITE-ProRule:PRU00152
Disulfide bondⁱ	451 ↔ 467	1 Publication Manual assertion based on experiment inⁱ Ref.5 "Structure of the human pancreatic lipase-related protein 1." Structural genomics consortium (SGC) Submitted (FEB-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 18-467 IN COMPLEX WITH CALCIUM IONS, DISULFIDE BONDS. PROSITE-ProRule annotation Manual assertion according to rulesⁱ PROSITE-ProRule:PRU00152

Keywords - PTMⁱ

Disulfide bond

Proteomic databases

PaxDbⁱ	P54315.
PRIDEⁱ	P54315.

PTM databases

PhosphoSiteⁱ	P54315.

PhosphoSiteⁱ

P54315.

Expressionⁱ

Tissue specificityⁱ

Pancreas.1 Publication

Gene expression databases

Bgeeⁱ	P54315.
CleanExⁱ	HS_PNLIPRP1.
ExpressionAtlasⁱ	P54315. baseline and differential.
Genevestigatorⁱ	P54315.

Interactionⁱ

Protein-protein interaction databases

IntActⁱ	P54315. 1 interaction.
STRINGⁱ	9606.ENSP00000351695.

Structureⁱ

Secondary structure

1

467

Legend: HelixTurnBeta strand

Show more details

Feature key	Position(s)	Length	Description
Beta strandⁱ	19 – 22	4	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2PPL
Turnⁱ	23 – 25	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2PPL
Beta strandⁱ	26 – 30	5	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2PPL
Turnⁱ	32 – 34	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2PPL
Beta strandⁱ	35 – 40	6	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2PPL
Helixⁱ	49 – 52	4	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2PPL
Beta strandⁱ	55 – 63	9	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2PPL
Beta strandⁱ	68 – 71	4	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2PPL
Helixⁱ	76 – 80	5	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2PPL
Beta strandⁱ	87 – 93	7	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2PPL
Helixⁱ	104 – 115	12	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2PPL
Beta strandⁱ	118 – 124	7	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2PPL
Helixⁱ	126 – 129	4	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2PPL
Helixⁱ	133 – 158	26	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2PPL
Helixⁱ	162 – 164	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2PPL
Beta strandⁱ	165 – 170	6	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2PPL
Helixⁱ	173 – 182	10	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2PPL
Beta strandⁱ	189 – 194	6	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2PPL
Turnⁱ	198 – 202	5	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2PPL
Turnⁱ	205 – 207	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2PPL
Helixⁱ	211 – 213	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2PPL
Beta strandⁱ	214 – 220	7	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2PPL
Helixⁱ	227 – 230	4	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2PPL
Beta strandⁱ	240 – 246	7	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2PPL
Beta strandⁱ	249 – 251	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2PPL
Helixⁱ	266 – 270	5	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2PPL
Helixⁱ	279 – 293	15	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2PPL
Turnⁱ	295 – 298	4	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2PPL
Helixⁱ	306 – 310	5	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2PPL
Beta strandⁱ	324 – 326	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2PPL
Helixⁱ	327 – 331	5	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2PPL
Beta strandⁱ	341 – 345	5	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2PPL
Beta strandⁱ	349 – 352	4	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2PPL
Beta strandⁱ	356 – 367	12	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2PPL
Beta strandⁱ	369 – 379	11	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2PPL
Beta strandⁱ	387 – 394	8	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2PPL
Beta strandⁱ	399 – 408	10	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2PPL
Beta strandⁱ	412 – 421	10	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2PPL
Beta strandⁱ	432 – 441	10	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2PPL
Beta strandⁱ	447 – 451	5	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2PPL
Beta strandⁱ	462 – 466	5	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2PPL

3D structure databases

Select the link destinations:
PDBeⁱ
RCSB PDBⁱ
PDBjⁱ

Links Updated

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2PPL	X-ray	2.20	A	18-467	[»]

ProteinModelPortalⁱ

P54315.

SMRⁱ

P54315. Positions 18-467.

ModBaseⁱ

Search...

MobiDBⁱ

Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P54315.

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Domainⁱ	356 – 467	112	PLATPROSITE-ProRule annotation Manual assertion according to rulesⁱ PROSITE-ProRule:PRU00152			Add BLAST

Sequence similaritiesⁱ

Belongs to the AB hydrolase superfamily. Lipase family.Curated

Contains 1 PLAT domain.PROSITE-ProRule annotation

Keywords - Domainⁱ

Signal

Phylogenomic databases

eggNOGⁱ	NOG40923.
GeneTreeⁱ	ENSGT00760000119069.
HOGENOMⁱ	HOG000038552.
HOVERGENⁱ	HBG003243.
InParanoidⁱ	P54315.
KOⁱ	K14074.
OMAⁱ	KGDESWV.
PhylomeDBⁱ	P54315.
TreeFamⁱ	TF324997.

Family and domain databases

Gene3Dⁱ	2.60.60.20. 1 hit. 3.40.50.1820. 1 hit.
InterProⁱ	IPR029058. AB_hydrolase. IPR016272. Lipase_LIPH. IPR008976. Lipase_LipOase. IPR013818. Lipase_N. IPR002331. Lipase_panc. IPR001024. PLAT/LH2_dom. IPR000734. TAG_lipase. [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]

Sequences (3)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsⁱ produced by alternative splicing. Align

Isoform 1 (identifier: P54315-1) [UniParc]FASTA Add to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLIFWTITLF LLGAAKGKEV CYEDLGCFSD TEPWGGTAIR PLKILPWSPE 
        60         70         80         90        100
KIGTRFLLYT NENPNNFQIL LLSDPSTIEA SNFQMDRKTR FIIHGFIDKG 
       110        120        130        140        150
DESWVTDMCK KLFEVEEVNC ICVDWKKGSQ ATYTQAANNV RVVGAQVAQM 
       160        170        180        190        200
LDILLTEYSY PPSKVHLIGH SLGAHVAGEA GSKTPGLSRI TGLDPVEASF 
       210        220        230        240        250
ESTPEEVRLD PSDADFVDVI HTDAAPLIPF LGFGTNQQMG HLDFFPNGGE 
       260        270        280        290        300
SMPGCKKNAL SQIVDLDGIW AGTRDFVACN HLRSYKYYLE SILNPDGFAA 
       310        320        330        340        350
YPCTSYKSFE SDKCFPCPDQ GCPQMGHYAD KFAGRTSEEQ QKFFLNTGEA 
       360        370        380        390        400
SNFARWRYGV SITLSGRTAT GQIKVALFGN KGNTHQYSIF RGILKPGSTH 
       410        420        430        440        450
SYEFDAKLDV GTIEKVKFLW NNNVINPTLP KVGATKITVQ KGEEKTVYNF 
       460 
CSEDTVREDT LLTLTPC

Length:467

Mass (Da):51,848

Last modified:October 1, 1996 - v1

Checksum:ⁱ2781EA1E22E39E78

GO

Isoform 2 (identifier: P54315-2) [UniParc]FASTA Add to Basket

The sequence of this isoform differs from the canonical sequence as follows:
111-186: KLFEVEEVNC...AGEAGSKTPG → VGASSDPCGQ...EKYSYYLISG
187-467: Missing.

« Hide

        10         20         30         40         50
MLIFWTITLF LLGAAKGKEV CYEDLGCFSD TEPWGGTAIR PLKILPWSPE 
        60         70         80         90        100
KIGTRFLLYT NENPNNFQIL LLSDPSTIEA SNFQMDRKTR FIIHGFIDKG 
       110        120        130        140        150
DESWVTDMCK VGASSDPCGQ LRPTLLLTSL HHFMHSRNLY ILGNFMQLKC 
       160        170        180 
FSSQKLKCLS MFPHYICTLK QPHLLLEKYS YYLISG

Show »

Length:186

Mass (Da):21,354

Checksum:ⁱ00AA562CC980CDF0

GO

Isoform 3 (identifier: P54315-3) [UniParc]FASTA Add to Basket

The sequence of this isoform differs from the canonical sequence as follows:
111-117: KLFEVEE → PGASPRA
118-467: Missing.

« Hide

        10         20         30         40         50
MLIFWTITLF LLGAAKGKEV CYEDLGCFSD TEPWGGTAIR PLKILPWSPE 
        60         70         80         90        100
KIGTRFLLYT NENPNNFQIL LLSDPSTIEA SNFQMDRKTR FIIHGFIDKG 
       110 
DESWVTDMCK PGASPRA

Show »

Length:117

Mass (Da):13,245

Checksum:ⁱ24E13DBDF751B557

GO

Natural variant

Feature key	Position(s)	Length	Description	Feature identifier
Natural variantⁱ	61 – 61	1	N → D. Corresponds to variant rs11197744 [ dbSNP \| Ensembl ].	VAR_049820
Natural variantⁱ	129 – 129	1	S → C in a breast cancer sample; somatic mutation. 1 Publication Manual assertion based on experiment inⁱ Ref.6 "The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-129.	VAR_036379
Natural variantⁱ	271 – 271	1	A → V. Corresponds to variant rs2305205 [ dbSNP \| Ensembl ].	VAR_022082
Natural variantⁱ	414 – 414	1	E → D.1 Publication Manual assertion based on experiment inⁱ Ref.3 "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] (ISOFORMS 1 AND 2), VARIANT ASP-414. Corresponds to variant rs2305204 [ dbSNP \| Ensembl ].	VAR_022659
Natural variantⁱ	461 – 461	1	L → P. Corresponds to variant rs1049125 [ dbSNP \| Ensembl ].	VAR_014915

Alternative sequence

Feature key	Position(s)	Length	Description	Feature identifier	Actions
Alternative sequenceⁱ	111 – 186	76	KLFEV…SKTPG → VGASSDPCGQLRPTLLLTSL HHFMHSRNLYILGNFMQLKC FSSQKLKCLSMFPHYICTLK QPHLLLEKYSYYLISG in isoform 2. 1 Publication Manual assertion based on opinion inⁱ Ref.3 "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] (ISOFORMS 1 AND 2), VARIANT ASP-414.	VSP_014097	Add BLAST
Alternative sequenceⁱ	111 – 117	7	KLFEVEE → PGASPRA in isoform 3. 1 Publication Manual assertion based on opinion inⁱ Ref.2 "The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).	VSP_014098
Alternative sequenceⁱ	118 – 467	350	Missing in isoform 3. 1 Publication Manual assertion based on opinion inⁱ Ref.2 "The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).	VSP_014099	Add BLAST
Alternative sequenceⁱ	187 – 467	281	Missing in isoform 2. 1 Publication Manual assertion based on opinion inⁱ Ref.3 "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] (ISOFORMS 1 AND 2), VARIANT ASP-414.	VSP_014100	Add BLAST

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M93283 mRNA. Translation: AAA59532.1. CR749299 mRNA. Translation: CAH18154.1. CR749524 mRNA. Translation: CAH18337.1. BC005233 mRNA. Translation: AAH05233.1. BC025784 mRNA. Translation: AAH25784.1.
CCDSⁱ	CCDS7595.1. [P54315-1]
PIRⁱ	A43357.
RefSeqⁱ	NP_006220.1. NM_006229.2. [P54315-1] XP_005269960.1. XM_005269903.2. [P54315-1]
UniGeneⁱ	Hs.73923.

Genome annotation databases

Ensemblⁱ	ENST00000358834; ENSP00000351695; ENSG00000187021. [P54315-1] ENST00000528052; ENSP00000433933; ENSG00000187021. [P54315-1]
GeneIDⁱ	5407.
KEGGⁱ	hsa:5407.
UCSCⁱ	uc001lcn.3. human. [P54315-2] uc001lco.1. human. [P54315-1]

Polymorphism databases

DMDMⁱ	1708837.

DMDMⁱ

1708837.

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M93283 mRNA. Translation: AAA59532.1. CR749299 mRNA. Translation: CAH18154.1. CR749524 mRNA. Translation: CAH18337.1. BC005233 mRNA. Translation: AAH05233.1. BC025784 mRNA. Translation: AAH25784.1.
CCDSⁱ	CCDS7595.1. [P54315-1]
PIRⁱ	A43357.
RefSeqⁱ	NP_006220.1. NM_006229.2. [P54315-1] XP_005269960.1. XM_005269903.2. [P54315-1]
UniGeneⁱ	Hs.73923.

3D structure databases

Select the link destinations:
PDBeⁱ
RCSB PDBⁱ
PDBjⁱ

Links Updated

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2PPL	X-ray	2.20	A	18-467	[»]

ProteinModelPortalⁱ

P54315.

SMRⁱ

P54315. Positions 18-467.

ModBaseⁱ

Search...

MobiDBⁱ

Search...

Protein-protein interaction databases

IntActⁱ	P54315. 1 interaction.
STRINGⁱ	9606.ENSP00000351695.

PTM databases

PhosphoSiteⁱ	P54315.

PhosphoSiteⁱ

P54315.

Polymorphism databases

DMDMⁱ	1708837.

DMDMⁱ

1708837.

Proteomic databases

PaxDbⁱ	P54315.
PRIDEⁱ	P54315.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENST00000358834; ENSP00000351695; ENSG00000187021. [P54315-1] ENST00000528052; ENSP00000433933; ENSG00000187021. [P54315-1]
GeneIDⁱ	5407.
KEGGⁱ	hsa:5407.
UCSCⁱ	uc001lcn.3. human. [P54315-2] uc001lco.1. human. [P54315-1]

Organism-specific databases

CTDⁱ	5407.
GeneCardsⁱ	GC10P118340.
HGNCⁱ	HGNC:9156. PNLIPRP1.
MIMⁱ	604422. gene.
neXtProtⁱ	NX_P54315.
PharmGKBⁱ	PA33479.
GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	NOG40923.
GeneTreeⁱ	ENSGT00760000119069.
HOGENOMⁱ	HOG000038552.
HOVERGENⁱ	HBG003243.
InParanoidⁱ	P54315.
KOⁱ	K14074.
OMAⁱ	KGDESWV.
PhylomeDBⁱ	P54315.
TreeFamⁱ	TF324997.

Enzyme and pathway databases

Reactomeⁱ	REACT_9518. Digestion of dietary lipid.

Reactomeⁱ

REACT_9518. Digestion of dietary lipid.

Miscellaneous databases

EvolutionaryTraceⁱ	P54315.
GenomeRNAiⁱ	5407.
NextBioⁱ	20935.
PROⁱ	P54315.
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	P54315.
CleanExⁱ	HS_PNLIPRP1.
ExpressionAtlasⁱ	P54315. baseline and differential.
Genevestigatorⁱ	P54315.

Family and domain databases

Gene3Dⁱ	2.60.60.20. 1 hit. 3.40.50.1820. 1 hit.
InterProⁱ	IPR029058. AB_hydrolase. IPR016272. Lipase_LIPH. IPR008976. Lipase_LipOase. IPR013818. Lipase_N. IPR002331. Lipase_panc. IPR001024. PLAT/LH2_dom. IPR000734. TAG_lipase. [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

"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] (ISOFORM 1), ABSENCE OF LIPASE ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Pancreas.
"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Liver.
"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] (ISOFORMS 1 AND 2), VARIANT ASP-414.
Tissue: Pancreas.
"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, ABSENCE OF CATALYTIC ACTIVITY.
"Structure of the human pancreatic lipase-related protein 1."
Structural genomics consortium (SGC)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 18-467 IN COMPLEX WITH CALCIUM IONS, DISULFIDE BONDS.
"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.
Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-129.

+Additional computationally mapped references.

Entry informationⁱ

Entry nameⁱ

LIPR1_HUMAN

Accessionⁱ

Primary (citable) accession number: P54315
Secondary accession number(s): Q68D83

Q9BS82

Entry historyⁱ

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	January 7, 2015
This is version 134 of the entry and version 1 of the sequence. [Complete history]

Entry statusⁱ

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.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

Human chromosome 10
Human chromosome 10: entries, gene names and cross-references to MIM
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families

External Data

Dasty 3

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 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.

UniProtKB

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UniRef

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P54315 - LIPR1_HUMAN

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P54315 - LIPR1_HUMAN

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Inactive pancreatic lipase-related protein 1

Select a section on the left to see content.

<p>Provides any useful information about the protein, mostly biological knowledge.</p><p><a href='../manual/function_section' target='_top'>More...</a></p>Functioni

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>Provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.</p><p><a href='../manual/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>Provides information on the location and the topology of the mature protein in the cell.</p><p><a href='../manual/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>Provides information on the disease(s) and phenotype(s) associated with the deficiency of a protein.</p><p><a href='../manual/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Organism-specific databases

<p>Describes post-translational modifications (PTMs) and/or processing events.</p><p><a href='../manual/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Proteomic databases

PTM databases

<p>Provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.</p><p><a href='../manual/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

<p>Provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.</p><p><a href='../manual/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>Provides information on the tertiary structure of a protein.</p><p><a href='../manual/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>Provides information on sequence similarities with other proteins and the domain(s) present in a protein.</p><p><a href='../manual/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

<p>Provides information about the sequence similarity with other proteins.</p><p><a href='../manual/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>Displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.</p><p><a href='../manual/sequences_section' target='_top'>More...</a></p>Sequences (3)i

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Polymorphism databases

<p>Is used to point to information related to entries and found in data collections other than UniProtKB.</p><p><a href='../manual/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>Contains the literature citations that are the sources of data used to annotate the entry. Each reference is numbered and contains several subsections allowing a precise description of a given citation.</p><p><a href='../manual/publications_section' target='_top'>More...</a></p>Publicationsi

<p>Provides general information on the entry.</p><p><a href='../manual/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>Contains any relevant information that doesn’t fit in any other defined sections</p><p><a href='../manual/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

External Data

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequences (3)ⁱ

Cross-referencesⁱ

Publicationsⁱ

Entry informationⁱ

Miscellaneousⁱ