Protein detail
COLQ
Acetylcholinesterase collagenic tail peptide (AChE Q subunit) (Acetylcholinesterase-associated collagen)
Entry name COLQ | UniProt ID | EVMP confidence score 0.38 |
Supporting publications (n) 2 | Transmembrane count | Protein classification |
EVMP confidence score
Annotation confidence score; open for threshold definitions.
Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40Basic Information6
Protein Names
Acetylcholinesterase collagenic tail peptide (AChE Q subunit) (Acetylcholinesterase-associated collagen)
Protein Function (4)
- Disease related genes
- Predicted secreted proteins
- Human disease related genes:Nervous system diseases:Other nervous and sensory system diseases
- Predicted intracellular proteins
Ensembl
Entrez Gene Symbol
Supporting publications (n)
2
EVMP confidence score
0.38
Fluorescence & Localization1
Function & Pathway6
Protein Function (4)
- Disease related genes
- Predicted secreted proteins
- Human disease related genes:Nervous system diseases:Other nervous and sensory system diseases
- Predicted intracellular proteins
Cellular Component (8)
Molecular Function (4)
Biological Process (3)
Canonical Pathways
M108 Pid netrin pathway
Mediation Categories
Other mediation
Relations & Evidence12
Ligand-Receptor Signaling (11)
11 records.
| Category | Parent | Database | Transmitter | Receiver | Secreted | Plasma Membrane (Transmembrane) | Plasma Membrane (Peripheral) |
|---|---|---|---|---|---|---|---|
| basement_membrane | ecm | Matrisome | Yes | No | Yes | No | No |
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Isolation & Detection Technology (1)
1 record.
| EV Isolation Method | Detection Method | Number of References | References |
|---|---|---|---|
| FACSMass spectrometry | 0 |
Sequence, Structure & Domains12
Sequences
Length
455
Mass
47,766
Sequence
MVVLNPMTLGIYLQLFFLSIVSQPTFINSVLPISAALPSLDQKKRGGHKACCLLTPPPPPLFPPPFFRGGRSPLLSPDMKNLMLELETSQSPCMQGSLGSPGPPGPQGPPGLPGKTGPKGEKGELGRPGRKGRPGPPGVPGMPGPIGWPGPEGPRGEKGDLGMMGLPGSRGPMGSKGYPGSRGEKGSRGEKGDLGPKGEKGFPGFPGMLGQKGEMGPKGEPGIAGHRGPTGRPGKRGKQGQKGDSGVMGPPGKPGPSGQPGRPGPPGPPPAGQLIMGPKGERGFPGPPGRCLCGPTMNVNNPSYGESVYGPSSPRVPVIFVVNNQEELERLNTQNAIAFRRDQRSLYFKDSLGWLPIQLTPFYPVDYTADQHGTCGDGLLQPGEECDDGNSDVGDDCIRCHRAYCGDGHRHEGVEDCDGSDFGYLTCETYLPGSYGDLQCTQYCYIDSTPCRYFT
Alternative Products
Event=Alternative splicing; Named isoforms=8; Name=I; IsoId=Q9Y215-1; Sequence=Displayed; Name=II; IsoId=Q9Y215-2; Sequence=VSP_001175; Name=III; IsoId=Q9Y215-3; Sequence=VSP_001177; Name=IV; IsoId=Q9Y215-4; Sequence=VSP_001176; Name=V; IsoId=Q9Y215-5; Sequence=VSP_001178; Name=VI; IsoId=Q9Y215-6; Sequence=VSP_001179, VSP_001183; Name=VII; IsoId=Q9Y215-7; Sequence=VSP_001180, VSP_001182; Name=VIII; IsoId=Q9Y215-8; Sequence=VSP_001181, VSP_001184
Alternative Sequence
1..35; MVVLNPMTLGIYLQLFFLSIVSQPTFINSVLPISA -> MTGSSFSLAHLLIISGLLCYSAGCL (in isoform II); 73..76; Missing (in isoform IV); 74..107; Missing (in isoform III); 124..132; Missing (in isoform V); 240..291; GQKGDSGVMGPPGKPGPSGQPGRPGPPGPPPAGQLIMGPKGERGFPGPPGRC -> SSRTPCTLPRRPPVPCGQGSRSPVTVVAGNESQACLLPRFEEDYISSGTERG (in isoform VI); 272..281; GQLIMGPKGE -> DFCGQQPGGA (in isoform VII); 273..329; QLIMGPKGERGFPGPPGRCLCGPTMNVNNPSYGESVYGPSSPRVPVIFVVNNQEELE -> HMETCNAPSTATSTPRPAATSPEGREEKVGCAPQNWQQLLHCHQTGHVLAPSPPTFV (in isoform VIII); 282..455; Missing (in isoform VII); 292..455; Missing (in isoform VI); 330..455; Missing (in isoform VIII)
3D Structural Models
3D Structure
X-ray crystallography (1)
Domain & Motif Annotations
Compositional Bias
101..112; Pro residues; 118..127; Basic and acidic residues; 134..152; Pro residues; 182..200; Basic and acidic residues; 262..271; Pro residues
Domain (CC)
The proline-rich attachment domain (PRAD) binds the AChE catalytic subunits.
Domain (FT)
96..269; Collagen-like 1; 277..291; Collagen-like 2
Region
51..67; PRAD; 90..282; Disordered; 130..133; Heparan sulfate proteoglycan binding; 235..238; Heparan sulfate proteoglycan binding
Protein Families
COLQ family
Sequence Similarities
Belongs to the COLQ family.
Supporting Publications2
| PMID | Title | Abstract |
|---|---|---|
| 31137684 | TNF-α Modulates P-Glycoprotein Expression and Contributes to Cellular Proliferation via Extracellular Vesicles. | Here, we examined the role of cancer cells in self-maintenance and promotion of cellular malignancy through the transport of Pgp and TNF-α molecules by extracellular vesicles (membrane microparticles (MP)). |
| 31141251 | Exosomes containing ErbB2/CRK induce vascular growth in premetastatic niches and promote metastasis of bladder cancer. | Here, we clarified a novel role of exosomes containing ErbB2 and CRK in a formation of premetastatic niches and subsequent metastases. Mass spectrometry analysis identified that ErbB2 was contained in UM-UC-3-derived exosomes in a CRK-dependent manner; the exosomes significantly increased proliferation and invasion properties of low-grade 5637 BC cells and HUVECs through FAK and PI3K/AKT signaling pathways. Taken together, we showed that CRK adaptors elevated the expression of ErbB2/3 in BC cells, and these tyrosine kinase/adaptor units were transferred from host BC cells to metastatic recipient cells by exosomes, leading to vascular leakiness and proliferation and contributing to the formation of distant metastasis. |