Reviewed,
UniProtKB/Swiss-Prot O35348 (COLQ_MOUSE)
Last modified
November 24, 2009.
Version 68.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Acetylcholinesterase collagenic tail peptide Alternative name(s): AChE Q subunit Acetylcholinesterase-associated collagen | ||
| Gene names |
| ||
| Organism | Mus musculus (Mouse) | ||
| Taxonomic identifier | 10090 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus |
Protein attributes
| Sequence length | 457 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Anchors the catalytic subunits of asymmetric AChE to the synaptic basal lamina By similarity. |
| Subunit structure | Homotrimer. Component of the asymmetric form of AChE, a disulfide-bonded oligomer composed of the collagenic subunits (Q) and a variable number of asymmetric catalytic subunits (T). The N-terminal of a collagenic subunit (Q) associates with the C-terminal of a catalytic subunit (T) By similarity. |
| Subcellular location | Cell junction › synapse By similarity. |
| Domain | The proline-rich attachment domain (PRAD) binds the AChE catalytic subunits By similarity. |
| Post-translational modification | The triple-helical tail is stabilized by disulfide bonds at each end By similarity. |
| Sequence similarities | Belongs to the COLQ family. Contains 2 collagen-like domains. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Neurotransmitter degradation |
| Cellular component | Cell junction Synapse |
| Domain | Collagen Repeat Signal |
| PTM | Disulfide bond |
| Gene Ontology (GO) | |
| Biological process | neurotransmitter catabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cell junction Inferred from electronic annotation. Source: UniProtKB-KW synapseInferred from electronic annotation. Source: UniProtKB-SubCell |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 29 | 29 | Potential | ||||||
| Chain | 30 – 457 | 428 | Acetylcholinesterase collagenic tail peptide | PRO_0000059415 | |||||
Regions | |||||||||
| Domain | 95 – 154 | 60 | Collagen-like 1 | ||||||
| Domain | 158 – 271 | 114 | Collagen-like 2 | ||||||
| Region | 51 – 67 | 17 | PRAD By similarity | ||||||
| Region | 129 – 132 | 4 | Heparan sulfate proteoglycan binding Potential | ||||||
| Region | 234 – 237 | 4 | Heparan sulfate proteoglycan binding Potential | ||||||
Amino acid modifications | |||||||||
| Disulfide bond | 51 | Interchain (with T subunit) Potential | |||||||
| Disulfide bond | 52 | Interchain (with T subunit) Potential | |||||||
| Disulfide bond | 92 | Interchain Potential | |||||||
| Disulfide bond | 293 | Interchain Potential | |||||||
| Disulfide bond | 295 | Interchain Potential | |||||||
Experimental info | |||||||||
| Sequence conflict | 105 | 1 | Missing in AAB72195. Ref.2 | ||||||
| Sequence conflict | 250 | 1 | P → H in AAB72195. Ref.2 | ||||||
| Sequence conflict | 267 | 1 | P → A in AAB72195. Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "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]. |
| [2] | "The mammalian gene of acetylcholinesterase-associated collagen." Krejci E., Thomine S., Boschetti N., Legay C., Sketelj J., Massoulie J. J. Biol. Chem. 272:22840-22847(1997) [PubMed: 9278446] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-273. Strain: 129/SvJ. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| BC107386 mRNA. Translation: AAI07387.1. AF021231 AF021230 Genomic DNA. Translation: AAB72195.1. | |
| IPI | IPI00761778. |
| RefSeq | NP_034067.2. |
| UniGene | Mm.239821 |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | O35348. |
Proteomic databases | |
| PRIDE | O35348. |
Genome annotation databases | |
| Ensembl | ENSMUST00000112027; ENSMUSP00000107658; ENSMUSG00000057606; Mus musculus. [Genome view] |
| GeneID | 382864. |
| KEGG | mmu:382864. |
| UCSC | uc007sxv.1. mouse. |
Organism-specific databases | |
| CTD | 382864. |
| MGI | MGI:1338761. Colq. |
Phylogenomic databases | |
| HOGENOM | O35348. |
| HOVERGEN | O35348. |
| OMA | YPVDYTV |
| OrthoDB | EOG9M94B0 |
Gene expression databases | |
| ArrayExpress | O35348. |
| Bgee | O35348. |
| Genevestigator | O35348. |
| GermOnline | ENSMUSG00000057606. Mus musculus. |
Family and domain databases | |
| InterPro | IPR008160. Collagen. IPR011936. Myxo_disulph_rpt. [Graphical view] |
| Pfam | PF01391. Collagen. 3 hits. [Graphical view] |
| TIGRFAMs | TIGR02232. myxo_disulf_rpt. 1 hit. |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 403537. |
| SOURCE | Search... |
Entry information
| Entry name | COLQ_MOUSE | ||||||||
| Accession | Primary (citable) accession number: O35348 Secondary accession number(s): Q08EK8 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with


