Protein detail
COLQ
Acetylcholinesterase collagenic tail peptide (AChE Q subunit) (Acetylcholinesterase-associated collagen)
Entry name COLQ | UniProt ID | EVMP score 0.38 |
Frequency 2 | Transmembrane count | Protein classification |
EVMP score: annotation confidence score.
Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
Basic Information
Protein Names
Acetylcholinesterase collagenic tail peptide (AChE Q subunit) (Acetylcholinesterase-associated collagen)
Protein Function
- 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
Frequency
2
EVMP Score
0.38
Fluorescence & Localization
Function & Pathway
Protein Function
- Disease related genes
- Predicted secreted proteins
- Human disease related genes:Nervous system diseases:Other nervous and sensory system diseases
- Predicted intracellular proteins
Cellular Component
Molecular Function
Biological Process
Canonical Pathways
M108 Pid netrin pathway
Mediation Categories
Other mediation
Relations & Evidence
Enzyme-Mediated Modification
0 records.
Ligand-Receptor Signaling
11 records.
| Category | Parent | Database | Transmitter | Receiver | Secreted | Plasma Membrane (Transmembrane) | Plasma Membrane (Peripheral) |
|---|---|---|---|---|---|---|---|
| ecm | ecm | GO_Intercell | Yes | No | Yes | No | No |
| ecm | ecm | OmniPath | Yes | No | Yes | No | No |
| extracellular | extracellular | LOCATE | No | No | Yes | No | No |
| extracellular | extracellular | OmniPath | No | No | Yes | No | No |
| transmembrane | transmembrane | LOCATE | No | No | Yes | No | No |
| transmembrane | transmembrane | OmniPath | No | No | Yes | No | No |
| secreted | secreted | HPA_secretome | No | No | Yes | No | No |
| secreted | secreted | connectomeDB2020 | No | No | Yes | No | No |
| secreted | secreted | OmniPath | No | No | Yes | No | No |
| ecm | ecm | Cellinker | Yes | No | Yes | No | No |
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Regulatory Interaction Network
0 records.
Protein Complex Composition
0 records.
Isolation & Detection Technology
1 record.
| EV Isolation Method | Detection Method | Number of References | References |
|---|---|---|---|
| FACSMass spectrometry | 0 |
Sequence, Structure & Domains
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.