Protein detail

C1QR1

Complement component C1q receptor (C1q/MBL/SPA receptor) (C1qR) (C1qR(p)) (C1qRp) (CDw93) (Complement component 1 q subcomponent receptor 1) (Matrix-remodeling-associated protein 4) (CD antigen CD93)

Protein symbol
C1QR1
UniProt ID
EVMP score
0.50
Frequency
1
Transmembrane count
1
Protein classification
CD markersPlasma proteinsPredicted membrane proteins
Basic Information
Protein Names
Complement component C1q receptor (C1q/MBL/SPA receptor) (C1qR) (C1qR(p)) (C1qRp) (CDw93) (Complement component 1 q subcomponent receptor 1) (Matrix-remodeling-associated protein 4) (CD antigen CD93)
Protein Class
CD markersPlasma proteinsPredicted membrane proteins
Protein Function
CD markers
Transmembrane
581..601; Helical
Transmembrane Count
1
Entrez Gene Symbol
Gene Synonym
C1qR(P)C1QR1C1qRPCDw93dJ737E23.1ECSM3MXRA4
Gene Description
CD93 molecule
Chromosome
20
Position
23079360-23086324
Frequency
1
EVMP Score
0.50
Fluorescence & Localization
Cell SpecificConjunctival goblet cellsSingle-Nuclei Brain Specificoligodendrocyte
Function & Pathway
Relations & Evidence

Enzyme-Mediated Modification

2 records.

Substrate Gene SymbolEnzyme Gene SymbolEnzyme UniProt IDResidue TypeResidue OffsetModificationDatabaseReferences
CD93SRCP12931Y644phosphorylationPhosphoSitePhosphoSite_ProtMapperProtMapper
CD93SRCP12931Y628phosphorylationPhosphoSitePhosphoSite_ProtMapperProtMapper

Ligand-Receptor Signaling

57 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
transmembranetransmembraneTopDBNoNoNoYesNo
transmembranetransmembraneLOCATENoNoNoYesNo
transmembranetransmembraneRamilowski_locationNoNoNoYesNo
transmembranetransmembraneOmniPathNoNoNoYesNo
plasma_membraneplasma_membraneUniProt_locationNoNoNoYesNo
plasma_membraneplasma_membraneCellinkerNoNoNoYesNo
plasma_membraneplasma_membraneOmniPathNoNoNoYesNo
plasma_membrane_transmembraneplasma_membrane_transmembraneMembranomeNoNoNoYesNo
plasma_membrane_transmembraneplasma_membrane_transmembraneHPMRNoNoNoYesNo
plasma_membrane_transmembraneplasma_membrane_transmembraneOmniPathNoNoNoYesNo
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Regulatory Interaction Network

0 records.

Protein Complex Composition

0 records.

Isolation & Detection Technology

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationMass spectrometryMass spectrometry [LTQ-FT Ultra]140089067
Sequence, Structure & Domains

Sequences

Length
652
Mass
68,560
Sequence
MATSMGLLLLLLLLLTQPGAGTGADTEAVVCVGTACYTAHSGKLSAAEAQNHCNQNGGNLATVKSKEEAQHVQRVLAQLLRREAALTARMSKFWIGLQREKGKCLDPSLPLKGFSWVGGGEDTPYSNWHKELRNSCISKRCVSLLLDLSQPLLPSRLPKWSEGPCGSPGSPGSNIEGFVCKFSFKGMCRPLALGGPGQVTYTTPFQTTSSSLEAVPFASAANVACGEGDKDETQSHYFLCKEKAPDVFDWGSSGPLCVSPKYGCNFNNGGCHQDCFEGGDGSFLCGCRPGFRLLDDLVTCASRNPCSSSPCRGGATCVLGPHGKNYTCRCPQGYQLDSSQLDCVDVDECQDSPCAQECVNTPGGFRCECWVGYEPGGPGEGACQDVDECALGRSPCAQGCTNTDGSFHCSCEEGYVLAGEDGTQCQDVDECVGPGGPLCDSLCFNTQGSFHCGCLPGWVLAPNGVSCTMGPVSLGPPSGPPDEEDKGEKEGSTVPRAATASPTRGPEGTPKATPTTSRPSLSSDAPITSAPLKMLAPSGSPGVWREPSIHHATAASGPQEPAGGDSSVATQNNDGTDGQKLLLFYILGTVVAILLLLALALGLLVYRKRRAKREEKKEKKPQNAADSYSWVPERAESRAMENQYSPTPGTDC

3D Structural Models

Turn
110..113; 260..266
Helix
46..55; 66..82; 267..270
Beta Strand
29..32; 35..41; 89..99; 101..103; 136..138; 140..147; 154..156; 159..163; 175..183; 198..202; 204..206; 208..210; 213..216; 220..224; 237..239; 241..244; 247..249; 272..277; 279..281; 283..286; 291..293; 300..302
3D Structure
X-ray crystallography (2)

Domain & Motif Annotations

Compositional Bias
512..526; Polar residues; 612..621; Basic and acidic residues; 640..652; Polar residues
Domain (FT)
32..174; C-type lectin; 260..301; EGF-like 1; 302..344; EGF-like 2; 345..384; EGF-like 3; calcium-binding; 385..426; EGF-like 4; calcium-binding; 427..468; EGF-like 5; calcium-binding
Region
472..546; Disordered; 553..572; Disordered; 611..652; Disordered
Clinical Relevance