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ProteinQ21116923· pop 7· linked from 361 articles

CD93 molecule

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Also known as C1qR, C1q receptor 1, C1qRp, C1q/MBL/SPA receptor, complement component C1q receptor, complement component 1 q subcomponent receptor 1, matrix-remodelling associated 4, matrix-remodeling-associated protein 4

CD93 (Cluster of Differentiation 93) is a protein that in humans is encoded by the CD93 gene. CD93 is a C-type lectin transmembrane receptor which plays a role not only in cell–cell adhesion processes but also in host defense.

Protein · UniProt

Complement component C1q receptor

Gene
CD93
Organism
Homo sapiens (Human)
Length
652 aa
Molecular mass
68,560 Da
Evidence
1: Evidence at protein level

Cell surface receptor that plays a role in various physiological processes including inflammation, phagocytosis, and cell adhesion. Plays a role in phagocytosis and enhances the uptake of apoptotic cells and immune complexes by acting as a receptor for defense collagens including surfactant protein A/SFTPA1, C1q, and mannose-binding lectin (MBL2) (PubMed:7977768). Plays a role in the regulation of endothelial cell function and adhesion by activating angiogenesis (PubMed:24809468). Mechanistically, exerts its angiogenic function by associating with beta-dystroglycan, leading to SRC-dependent…

3D-structureCell adhesionCell membraneDirect protein sequencingDisulfide bondEGF-like domainGlycoproteinHost-virus interaction
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Swiss-Prot (reviewed) · via UniProt

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Article

7 sections
Contents
  • Family
  • Expression
  • Function
  • See also
  • References
  • Further reading
  • External links

CD93 (Cluster of Differentiation 93) is a protein that in humans is encoded by the CD93 gene. CD93 is a C-type lectin transmembrane receptor which plays a role not only in cell–cell adhesion processes but also in host defense.

== Family == CD93 belongs to the Group XIV C-Type lectin family, a group containing three other members, endosialin (CD248), CLEC14A and thrombomodulin, a well characterized anticoagulant. All of them contain a C-type lectin domain, a series of epidermal growth factor like domains, a highly glycosylated mucin-like domain, a unique transmembrane domain and a short cytoplasmic tail. Due to their strong homology and their close proximity on chromosome 20, CD93 has been suggested to have arisen from the thrombomodulin gene through a duplication event.

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