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Signal-regulatory protein (SIRP) immunoglobulin-like domain. IgC_SIRP: Immunoglobulin-like domain of signal-regulatory proteins (SIRP); the signal-regulatory proteins (SIRP) are Ig-like cell surface receptors detected in hematopoietic and non-hematopoietic cells. While their extracellular domains are similar, SIRP are classified as alpha or beta based on the length of the intracytoplasmic domain. Those having a 110- to 113-amino acid tail are classified as SIRP-alpha, and those having a 5-amino acid tail as SIRP-beta. SIRP-alpha and SIRP-beta molecules are thought to have complementary roles in signal regulation: SIRP-alpha inhibit signalling via their immunoreceptor tyrosine (IT)-based inhibition motifs while SIRP-beta are activating. SIRP-beta lack the cytoplasmic domainof SIRP-alpha, and associate with at least one other transmembrane protein (DAP-12 or KARAP). The IT-based activation motifs within DAP-12's cytoplasmic domain may link SIRP-beta to the activating machinery.
No pairwise interactions are available for this conserved domain.
Tips:  If you've navigated here from a protein, hovering over a position on the weblogo will display the corresponding protein position for that domain position. The histograms below the weblogo indicate mutations found on the domain. Red is for disease (OMIM) and blue is for SNPs. Functional Features are displayed as orange boxes under the histograms. You can choose which features are displayed in the box below. Range on the Protein: Protein ID Protein Position Domain Position: 
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