SNAREs, soluble N-ethylmaleimide-sensitive factor-attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion. SNAP29 is a SNARE involved in autophagy through the direct control of autophagosome membrane fusion with the lysososome membrane. Also plays a role in ciliogenesis by regulating membrane fusions. Forms a SNARE complex, composed of VAMP8, SNAP29 and STX17, involved in fusion of autophagosome with lysosome (PubMed:23217709, PubMed:25686604). Interacts with multiple syntaxins including STX6 (By similarity). Interacts with EIPR1 (PubMed:27440922). Interacts with STX17; this interaction is increased in the absence of TMEM39A (PubMed:31806350, PubMed:33422265). (Microbial infection) Interacts with Hantaan hantavirus nucleoprotein; this interaction prevents the breakdown of the viral glycoprotein N by virus-triggered autophagy. (Microbial infection) The interaction with STX17 is decreased in presence of SARS coronavirus-2/SARS-CoV-2 ORF3A protein. Appears to be mostly membrane-bound, probably via interaction with syntaxins, but a significant portion is cytoplasmic. Localizes to the ciliary pocket from where the cilium protrudes. Found in brain, heart, kidney, liver, lung, placenta, skeletal muscle, spleen and pancreas. The disease is caused by variants affecting the gene represented in this entry. Belongs to the SNAP-25 family.