Hyaluronan binding protein 1 (HABP1), also known as C1qBP/C1qR and p32, is a ubiquitous acidic glycoprotein that functions in spermatogenesis and as a receptor for proinflammatory molecules. HABP1 is synthesized with a 71 amino acid (aa) N-terminal preproprotein and a 208aa mature region. The 3kD mature mouse HABP1, which contains a MAM33-like sequence, shares 90% and 99% aa sequence identity with human and rat HABP1, respectively. HABP1 assembles into a doughnut shaped trimer, with negatively charged residues asymmetrically distributed on one face lining the channel of the complex. HABP1 can be cleaved by cell surface MMP-14/MT1-MMP, a protease important in angiogenesis and tumor metastasis. Cell surface HABP1 binds a wide range of extracellular molecules, including hyaluronan, vitronectin, complement component C1q, HMW kininogen, and bacterial and viral proteins. Within the cell, HABP1 binds to molecules containing the C1q globular domain, multiple isoforms of PKC, mitochondrial Hrk, the cytoplasmic tails of adrenergic and GABA-A receptors, the mRNA splicing factor ASF/SF2, and the CBF transcription factor. Apoptosis and direct phosphorylation by Erk1/2 induces HABP1 translocation to the nucleus.
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