P91268 (PAL_CAEEL) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 73.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Probable peptidyl-alpha-hydroxyglycine alpha-amidating lyase F21F3.1 EC=4.3.2.5 Alternative name(s): Probable peptidylamidoglycolate lyase Short name=PAL | ||
| Gene names |
| ||
| Organism | Caenorhabditis elegans | ||
| Taxonomic identifier | 6239 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis |
Protein attributes
| Sequence length | 350 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 | Probable lyase that catalyzes an essential reaction in C-terminal alpha-amidation of peptides. Mediates the dismutation of the unstable peptidyl(2-hydroxyglycine) intermediate to glyoxylate and the corresponding desglycine peptide amide. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity By similarity. |
| Catalytic activity | Peptidylamidoglycolate = peptidyl amide + glyoxylate. |
| Cofactor | Zinc By similarity. |
| Subcellular location | Secreted Potential. |
| Sequence similarities | Belongs to the peptidyl-alpha-hydroxyglycine alpha-amidating lyase family. Contains 4 NHL repeats. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Secreted |
| Domain | Repeat Signal |
| Ligand | Metal-binding Zinc |
| Molecular function | Lyase |
| PTM | Disulfide bond Glycoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | peptide metabolic process Inferred from electronic annotation. Source: InterPro |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell membraneInferred from electronic annotation. Source: InterPro |
| Molecular function | copper ion binding Inferred from electronic annotation. Source: InterPro peptidylamidoglycolate lyase activityInferred from electronic annotation. Source: EC peptidylglycine monooxygenase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 19 | 19 | Potential | ||||||||
| Chain | 20 – 350 | 331 | Probable peptidyl-alpha-hydroxyglycine alpha-amidating lyase F21F3.1 | PRO_0000248572 | |||||||
Regions | |||||||||||
| Repeat | 46 – 90 | 45 | NHL 1 | ||||||||
| Repeat | 113 – 154 | 42 | NHL 2 | ||||||||
| Repeat | 162 – 206 | 45 | NHL 3 | ||||||||
| Repeat | 212 – 256 | 45 | NHL 4 | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 103 | 1 | N-linked (GlcNAc...) Ref.2 | ||||||||
| Disulfide bond | 176 ↔ 196 | By similarity | |||||||||
| Disulfide bond | 241 ↔ 252 | By similarity | |||||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2. |
| [2] | "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis elegans and suggests an atypical translocation mechanism for integral membrane proteins." Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T., Taoka M., Takahashi N., Isobe T. Mol. Cell. Proteomics 6:2100-2109(2007) [PubMed: 17761667] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-103, MASS SPECTROMETRY. Strain: Bristol N2. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | FO081197 Genomic DNA. Translation: CCD69816.1. |
| PIR | T25723. |
| RefSeq | NP_491475.2. NM_059074.5. |
| UniGene | Cel.36441. |
3D structure databases | |
| ProteinModelPortal | P91268. |
| SMR | P91268. Positions 54-349. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P91268. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblMetazoa | F21F3.1.1; F21F3.1.1; F21F3.1. F21F3.1.2; F21F3.1.2; F21F3.1. |
| GeneID | 172108. |
| KEGG | cel:F21F3.1. |
| NMPDR | fig|6239.3.peg.1034. |
| UCSC | F21F3.1.1. c. elegans. |
Organism-specific databases | |
| CTD | 172108. |
| WormBase | F21F3.1; CE32870; WBGene00017671. |
Phylogenomic databases | |
| eggNOG | meNOG07371. |
| GeneTree | EMGT00050000007482. |
| HOGENOM | HBG046476. |
| InParanoid | P91268. |
| OMA | VRGFTID. |
| PhylomeDB | P91268. |
Gene expression databases | |
| ArrayExpress | P91268. |
Family and domain databases | |
| InterPro | IPR011042. 6-blade_b-propeller_TolB-like. IPR001258. NHL_repeat. IPR013017. NHL_repeat_subgr. IPR000720. Pep_amidat_mOase. [Graphical view] |
| Gene3D | G3DSA:2.120.10.30. 6-blade_b-propeller_TolB-like. 1 hit. |
| Pfam | PF01436. NHL. 3 hits. [Graphical view] |
| PRINTS | PR00790. PAMONOXGNASE. |
| PROSITE | PS51125. NHL. 4 hits. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 874043. |
Entry information
| Entry name | PAL_CAEEL | ||||||||
| Accession | Primary (citable) accession number: P91268 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Caenorhabditis annotation project | ||||||||
Relevant documents
| Caenorhabditis elegans Caenorhabditis elegans: entries, gene names and cross-references to WormPep |
| SIMILARITY comments Index of protein domains and families |

Clusters with