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P29183 (LIPP_HORSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Pancreatic triacylglycerol lipase
Short name=PL
Short name=PTL
Short name=Pancreatic lipase
EC=3.1.1.3
Gene names
Name:PNLIP
OrganismEquus caballus (Horse) [Reference proteome]
Taxonomic identifier9796 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Perissodactyla › Equidae › Equus ›

Protein attributes

Sequence length461 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide‹1 – 12›12
Chain13 – 461449Pancreatic triacylglycerol lipase
PRO_0000017784

Regions

Domain351 – 461111PLAT

Sites

Active site1651Nucleophile
Active site1891Charge relay system
Active site2761Charge relay system
Metal binding2001Calcium; via carbonyl oxygen
Metal binding2031Calcium; via carbonyl oxygen
Metal binding2051Calcium
Metal binding2081Calcium

Amino acid modifications

Disulfide bond16 ↔ 22
Disulfide bond103 ↔ 114
Disulfide bond250 ↔ 274
Disulfide bond298 ↔ 309
Disulfide bond312 ↔ 317
Disulfide bond445 ↔ 461

Experimental info

Mutagenesis1651S → X: 80% loss of P-nitrophenyl acetate hydrolysis activity.
Non-terminal residue11

Secondary structure

1 .......................................................................... 461
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P29183 [UniParc].

Last modified April 1, 1993. Version 2.
Checksum: 382F33F3CE446738

FASTA46150,921
        10         20         30         40         50         60 
WTLSLLLGAV VGNEVCYERL GCFSDDSPWA GIVERPLKIL PWSPEKVNTR FLLYTNENPD 

        70         80         90        100        110        120 
NFQEIVADPS TIQSSNFNTG RKTRFIIHGF IDKGEESWLS TMCQNMFKVE SVNCICVDWK 

       130        140        150        160        170        180 
SGSRTAYSQA SQNVRIVGAE VAYLVGVLQS SFDYSPSNVH IIGHSLGSHA AGEAGRRTNG 

       190        200        210        220        230        240 
AVGRITGLDP AEPCFQGTPE LVRLDPSDAQ FVDVIHTDIA PFIPNLGFGM SQTAGHLDFF 

       250        260        270        280        290        300 
PNGGKEMPGC QKNVLSQIVD IDGIWQGTRD FAACNHLRSY KYYTDSILNP DGFAGFSCAS 

       310        320        330        340        350        360 
YSDFTANKCF PCSSEGCPQM GHYADRFPGR TKGVGQLFYL NTGDASNFAR WRYRVDVTLS 

       370        380        390        400        410        420 
GKKVTGHVLV SLFGNKGNSR QYEIFQGTLK PDNTYSNEFD SDVEVGDLEK VKFIWYNNVI 

       430        440        450        460 
NLTLPKVGAS KITVERNDGS VFNFCSEETV REDVLLTLTA C

« Hide

References

[1]"Sequence of horse pancreatic lipase as determined by protein and cDNA sequencing. Implications for p-nitrophenyl acetate hydrolysis by pancreatic lipases."
Kerfelec B., Foglizzo E., Bonicel J., Bougis P.E., Chapus C.
Eur. J. Biochem. 206:279-287(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"Horse pancreatic lipase. The crystal structure refined at 2.3-A resolution."
Bourne Y., Martinez C., Kerfelec B., Lombardo D., Chapus C., Cambillau C.
J. Mol. Biol. 238:709-732(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X66218 mRNA. Translation: CAA46961.1.
PIRS21223.
RefSeqNP_001157421.1. NM_001163949.1.
UniGeneEca.12462.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HPLX-ray2.30A/B13-461[»]
ProteinModelPortalP29183.
SMRP29183. Positions 13-461.
ModBaseSearch...

Protein-protein interaction databases

STRING9796.ENSECAP00000007877.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100034202.
KEGGecb:100034202.

Organism-specific databases

CTD5406.

Phylogenomic databases

eggNOGNOG40923.
HOGENOMHOG000038552.
HOVERGENHBG003243.
InParanoidP29183.
KOK14073.
OrthoDBEOG4WH8KM.

Family and domain databases

Gene3D2.60.60.20. 1 hit.
InterProIPR000734. Lipase.
IPR008976. Lipase_LipOase.
IPR013818. Lipase_N.
IPR002331. Lipase_panc.
IPR001024. LipOase_LH2.
IPR016272. Lipoprotein_lipase_LIPH.
[Graphical view]
PANTHERPTHR11610. PTHR11610. 1 hit.
PTHR11610:SF8. PTHR11610:SF8. 1 hit.
PfamPF00151. Lipase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PIRSFPIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTSPR00823. PANCLIPASE.
PR00821. TAGLIPASE.
SMARTSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMSSF49723. Lipase_LipOase. 1 hit.
PROSITEPS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP29183.

Entry information

Entry nameLIPP_HORSE
AccessionPrimary (citable) accession number: P29183
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: April 1, 1993
Last modified: April 3, 2013
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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