UniProt functional annotation for O35179

UniProt code: O35179.

Organism: Rattus norvegicus (Rat).
Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus.
 
Function: Implicated in synaptic vesicle endocytosis. May recruit other proteins to membranes with high curvature. Required for BDNF-dependent dendrite outgrowth. Cooperates with SH3GL2 to mediate BDNF-NTRK2 early endocytic trafficking and signaling from early endosomes (By similarity). {ECO:0000250|UniProtKB:Q62420, ECO:0000269|PubMed:11604418, ECO:0000269|PubMed:16763559}.
 
Subunit: Monomer; in cytoplasm. Homodimer; when associated with membranes (By similarity). Interacts with OPHN1 (By similarity). Interacts with SYNJ1 (PubMed:9341169, PubMed:9238017, PubMed:11384986). Interacts with DNM1 (PubMed:9238017, PubMed:11384986). Interacts with MAP4K3; the interaction appears to regulate MAP4K3-mediated JNK activation (PubMed:11384986). Interacts with PDCD6IP (By similarity). Interacts with ATXN2 (By similarity). Interacts with ADAM9 and ADAM15 cytoplasmic tails (By similarity). Interacts with BIN2 (By similarity). Interacts with TMEM108 (By similarity). Interacts with ADGRB2 (By similarity). {ECO:0000250|UniProtKB:Q62420, ECO:0000250|UniProtKB:Q99962, ECO:0000269|PubMed:11384986, ECO:0000269|PubMed:9238017, ECO:0000269|PubMed:9341169}.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9238017, ECO:0000269|PubMed:9341169}. Membrane {ECO:0000269|PubMed:9238017}; Peripheral membrane protein {ECO:0000269|PubMed:9238017}. Early endosome {ECO:0000250|UniProtKB:Q62420}. Cell junction, synapse, presynapse {ECO:0000269|PubMed:9341169}.
Tissue specificity: Expressed in the brain (PubMed:9341169). Expressed at low level in the kidney. {ECO:0000269|PubMed:9238017, ECO:0000269|PubMed:9341169}.
Domain: An N-terminal amphipathic helix, the BAR domain and a second amphipathic helix inserted into helix 1 of the BAR domain (N-BAR domain) induce membrane curvature and bind curved membranes. The BAR domain dimer forms a rigid crescent shaped bundle of helices with the pair of second amphipathic helices protruding towards the membrane- binding surface. {ECO:0000269|PubMed:11604418, ECO:0000269|PubMed:16763557, ECO:0000269|PubMed:16763559}.
Miscellaneous: The N-BAR domain binds liposomes and mediates dimerization of BAR domains upon liposome binding. It induces formation of tubules from liposomes as well as fusion of liposome tubules. Cells overexpressing Sh3gl2 show no effect on transferrin uptake.
Similarity: Belongs to the endophilin family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.