Q05315 (LPPL_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 123.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Eosinophil lysophospholipase EC=3.1.1.5 Alternative name(s): Charcot-Leyden crystal protein Short name=CLC Galectin-10 Short name=Gal-10 Lysolecithin acylhydrolase | ||
| Gene names |
| ||
| Organism | Homo sapiens (Human) | ||
| Taxonomic identifier | 9606 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 142 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 | May have both lysophospholipase and carbohydrate-binding activities. |
| Catalytic activity | 2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate. |
| Subcellular location | Cytoplasmic granule. Note: Localized in granules from where it may be secreted or transported to other locations in the cell. |
| Tissue specificity | Expressed exclusively by eosinophils and basophils. Not detected in monocytes and neutrophils. |
| Miscellaneous | Forms hexagonal bipyramidal crystals, known as Charcot-Leyden crystals, in tissues and secretions from sites of eosinophil-associated inflammation and some myeloid leukemias. |
| Sequence similarities | Contains 1 galectin domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Lipid degradation |
| Coding sequence diversity | Polymorphism |
| Ligand | Lectin |
| Molecular function | Hydrolase Serine esterase |
| PTM | Acetylation |
| Technical term | 3D-structure Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological process | lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW multicellular organismal developmentTraceable author statement. Source: ProtInc |
| Molecular function | carboxylesterase activity Inferred from electronic annotation. Source: UniProtKB-KW lysophospholipase activityInferred from electronic annotation. Source: EC sugar bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.6 | ||||||||||||||||||||||||||||||
| Chain | 2 – 142 | 141 | Eosinophil lysophospholipase | PRO_0000076960 | |||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||
| Domain | 6 – 138 | 133 | Galectin | ||||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||
| Site | 136 | 1 | Not glycosylated | ||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||
| Modified residue | 2 | 1 | N-acetylserine Ref.6 | ||||||||||||||||||||||||||||||
Natural variations | |||||||||||||||||||||||||||||||||
| Natural variant | 28 | 1 | A → V. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Corresponds to variant rs17608 [ dbSNP | Ensembl ]. | VAR_014765 | |||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||
| Beta strand | 6 – 11 | 6 | |||||||||||||||||||||||||||||||
| Beta strand | 19 – 28 | 10 | |||||||||||||||||||||||||||||||
| Helix | 30 – 32 | 3 | |||||||||||||||||||||||||||||||
| Beta strand | 35 – 45 | 11 | |||||||||||||||||||||||||||||||
| Beta strand | 50 – 57 | 8 | |||||||||||||||||||||||||||||||
| Turn | 58 – 60 | 3 | |||||||||||||||||||||||||||||||
| Beta strand | 61 – 68 | 8 | |||||||||||||||||||||||||||||||
| Beta strand | 76 – 78 | 3 | |||||||||||||||||||||||||||||||
| Beta strand | 89 – 95 | 7 | |||||||||||||||||||||||||||||||
| Beta strand | 97 – 104 | 8 | |||||||||||||||||||||||||||||||
| Beta strand | 107 – 113 | 7 | |||||||||||||||||||||||||||||||
| Helix | 118 – 120 | 3 | |||||||||||||||||||||||||||||||
| Beta strand | 123 – 137 | 15 | |||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Molecular cloning and characterization of human eosinophil Charcot-Leyden crystal protein (lysophospholipase). Similarities to IgE binding proteins and the S-type animal lectin superfamily." Ackerman S.J., Corrette S.E., Rosenberg H.F., Bennett J.C., Mastrianni D.M., Nicholson-Weller A., Weller P.F., Chin D.T., Tenen D.G. J. Immunol. 150:456-468(1993) [PubMed: 8419478] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 3-18 AND 93-110, VARIANT VAL-28. |
| [2] | "Localization of the human eosinophil Charcot-Leyden crystal protein (lysophospholipase) gene (CLC) to chromosome 19 and the human ribonuclease 2 (eosinophil-derived neurotoxin) and ribonuclease 3 (eosinophil cationic protein) genes (RNS2 and RNS3) to chromosome 14." Mastrianni D.M., Eddy R.L., Rosenberg H.F., Corrette S.E., Shows T.B., Tenen D.G., Ackerman S.J. Genomics 13:240-242(1992) [PubMed: 1577491] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-28. |
| [3] | "The genomic structure of the human Charcot-Leyden crystal protein gene is analogous to those of the galectin genes." Dyer K.D., Handen J.S., Rosenberg H.F. Genomics 40:217-221(1997) [PubMed: 9119387] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-28. |
| [4] | "The DNA sequence and biology of human chromosome 19." Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. Lucas S.M.Nature 428:529-535(2004) [PubMed: 15057824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT VAL-28. |
| [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-28. |
| [6] | "Comparative proteomics of nasal fluid in seasonal allergic rhinitis." Ghafouri B., Irander K., Lindbom J., Tagesson C., Lindahl M. J. Proteome Res. 5:330-338(2006) [PubMed: 16457599] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-23; 92-99 AND 135-141, ACETYLATION AT SER-2, LACK OF GLYCOSYLATION AT ASN-136, MASS SPECTROMETRY. |
| [7] | "Crystal structure of human Charcot-Leyden crystal protein, an eosinophil lysophospholipase, identifies it as a new member of the carbohydrate-binding family of galectins." Leonidas D.D., Elbert B.L., Zhou Z., Leffler H., Ackerman S.J., Acharya K.R. Structure 3:1379-1393(1995) [PubMed: 8747464] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). |
| [8] | "Selective recognition of mannose by the human eosinophil Charcot-Leyden crystal protein (galectin-10): a crystallographic study at 1.8 A resolution." Swaminathan G.J., Leonidas D.D., Savage M.P., Ackerman S.J., Acharya K.R. Biochemistry 38:13837-13843(1999) [PubMed: 10529229] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). |
| + | Additional computationally mapped references. |
Web resources
| Functional Glycomics Gateway - Glycan Binding Galectin-10 |
Cross-references
Sequence databases | |||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | L01664 mRNA. Translation: AAA36190.1. L01665 Genomic DNA. Translation: AAC37530.1. U68398 U68396 Genomic DNA. Translation: AAC51157.1.AC005393 Genomic DNA. Translation: AAC28912.1. AC006133 Genomic DNA. No translation available. BC119711 mRNA. Translation: AAI19712.1. BC119712 mRNA. Translation: AAI19713.1. | ||||||||||||||||||||||||||||||
| IPI | IPI00216071. | ||||||||||||||||||||||||||||||
| PIR | A46523. | ||||||||||||||||||||||||||||||
| RefSeq | NP_001819.2. NM_001828.5. | ||||||||||||||||||||||||||||||
| UniGene | Hs.889. | ||||||||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | Q05315. | ||||||||||||||||||||||||||||||
| SMR | Q05315. Positions 2-142. | ||||||||||||||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||||||||||||||
| STRING | Q05315. | ||||||||||||||||||||||||||||||
Polymorphism databases | |||||||||||||||||||||||||||||||
| DMDM | 547870. | ||||||||||||||||||||||||||||||
Proteomic databases | |||||||||||||||||||||||||||||||
| PRIDE | Q05315. | ||||||||||||||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||||||||
| Ensembl | ENST00000221804; ENSP00000221804; ENSG00000105205. | ||||||||||||||||||||||||||||||
| GeneID | 1178. | ||||||||||||||||||||||||||||||
| KEGG | hsa:1178. | ||||||||||||||||||||||||||||||
| UCSC | uc002omh.1. human. | ||||||||||||||||||||||||||||||
Organism-specific databases | |||||||||||||||||||||||||||||||
| CTD | 1178. | ||||||||||||||||||||||||||||||
| GeneCards | GC19M040221. | ||||||||||||||||||||||||||||||
| H-InvDB | HIX0040154. | ||||||||||||||||||||||||||||||
| HGNC | HGNC:2014. CLC. | ||||||||||||||||||||||||||||||
| HPA | HPA041751. | ||||||||||||||||||||||||||||||
| MIM | 153310. gene. | ||||||||||||||||||||||||||||||
| neXtProt | NX_Q05315. | ||||||||||||||||||||||||||||||
| GenAtlas | Search... | ||||||||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||||||||
| eggNOG | prNOG20158. | ||||||||||||||||||||||||||||||
| GeneTree | ENSGT00530000064497. | ||||||||||||||||||||||||||||||
| HOGENOM | HBG099916. | ||||||||||||||||||||||||||||||
| HOVERGEN | HBG006255. | ||||||||||||||||||||||||||||||
| InParanoid | Q05315. | ||||||||||||||||||||||||||||||
| OMA | QVWRDIS. | ||||||||||||||||||||||||||||||
| OrthoDB | EOG47H5RQ. | ||||||||||||||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||||||||||||||
| BRENDA | 3.1.1.5. 2681. | ||||||||||||||||||||||||||||||
Gene expression databases | |||||||||||||||||||||||||||||||
| ArrayExpress | Q05315. | ||||||||||||||||||||||||||||||
| Bgee | Q05315. | ||||||||||||||||||||||||||||||
| CleanEx | HS_CLC. | ||||||||||||||||||||||||||||||
| Genevestigator | Q05315. | ||||||||||||||||||||||||||||||
| GermOnline | ENSG00000105205. Homo sapiens. | ||||||||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||||||||
| InterPro | IPR008985. ConA-like_lec_gl. IPR013320. ConA-like_subgrp. IPR001079. Galectin_CRD. [Graphical view] | ||||||||||||||||||||||||||||||
| Gene3D | G3DSA:2.60.120.200. ConA_like_subgrp. 1 hit. | ||||||||||||||||||||||||||||||
| KO | K13334. | ||||||||||||||||||||||||||||||
| Pfam | PF00337. Gal-bind_lectin. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||
| SMART | SM00908. Gal-bind_lectin. 1 hit. SM00276. GLECT. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||
| SUPFAM | SSF49899. ConA_like_lec_gl. 1 hit. | ||||||||||||||||||||||||||||||
| PROSITE | PS51304. GALECTIN. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||||||||
Other | |||||||||||||||||||||||||||||||
| NextBio | 4868. | ||||||||||||||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||||||||||||||
Entry information
| Entry name | LPPL_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q05315 Secondary accession number(s): Q0VDE3 | ||||||||
| Entry 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. | ||||||||
Relevant documents
| Human chromosome 19 Human chromosome 19: 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 |

Clusters with