Detail Information for IndEnz0009000321
IED ID IndEnz0009000321
Enzyme Type ID chitinase000321
Protein Name VPS10 domain-containing receptor SorCS2
Cleaved into: SorCS2 122 kDa chain; SorCS2 104 kDa chain; SorCS2 18 kDa chain
Gene Name SORCS2 KIAA1329
Organism Homo sapiens (Human)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MAHRGPSRASKGPGPTARAPSPGAPPPPRSPRSRPLLLLLLLLGACGAAGRSPEPGRLGPHAQLTRVPRSPPAGRAEPGGGEDRQARGTEPGAPGPSPGPAPGPGEDGAPAAGYRRWERAAPLAGVASRAQVSLISTSFVLKGDATHNQAMVHWTGENSSVILILTKYYHADMGKVLESSLWRSSDFGTSYTKLTLQPGVTTVIDNFYICPTNKRKVILVSSSLSDRDQSLFLSADEGATFQKQPIPFFVETLIFHPKEEDKVLAYTKESKLYVSSDLGKKWTLLQERVTKDHVFWSVSGVDADPDLVHVEAQDLGGDFRYVTCAIHNCSEKMLTAPFAGPIDHGSLTVQDDYIFFKATSANQTKYYVSYRRNEFVLMKLPKYALPKDLQIISTDESQVFVAVQEWYQMDTYNLYQSDPRGVRYALVLQDVRSSRQAEESVLIDILEVRGVKGVFLANQKIDGKVMTLITYNKGRDWDYLRPPSMDMNGKPTNCKPPDCHLHLHLRWADNPYVSGTVHTKDTAPGLIMGAGNLGSQLVEYKEEMYITSDCGHTWRQVFEEEHHILYLDHGGVIVAIKDTSIPLKILKFSVDEGLTWSTHNFTSTSVFVDGLLSEPGDETLVMTVFGHISFRSDWELVKVDFRPSFSRQCGEEDYSSWELSNLQGDRCIMGQQRSFRKRKSTSWCIKGRSFTSALTSRVCECRDSDFLCDYGFERSSSSESSTNKCSANFWFNPLSPPDDCALGQTYTSSLGYRKVVSNVCEGGVDMQQSQVQLQCPLTPPRGLQVSIQGEAVAVRPGEDVLFVVRQEQGDVLTTKYQVDLGDGFKAMYVNLTLTGEPIRHRYESPGIYRVSVRAENTAGHDEAVLFVQVNSPLQALYLEVVPVIGLNQEVNLTAVLLPLNPNLTVFYWWIGHSLQPLLSLDNSVTTRFSDTGDVRVTVQAACGNSVLQDSRVLRVLDQFQVMPLQFSKELDAYNPNTPEWREDVGLVVTRLLSKETSVPQELLVTVVKPGLPTLADLYVLLPPPRPTRKRSLSSDKRLAAIQQVLNAQKISFLLRGGVRVLVALRDTGTGAEQLGGGGGYWAVVVLFVIGLFAAGAFILYKFKRKRPGRTVYAQMHNEKEQEMTSPVSHSEDVQGAVQGNHSGVVLSINSREMHSYLVS
Enzyme Length 1159
Uniprot Accession Number Q96PQ0
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: The heterodimer formed by NGFR and SORCS2 functions as receptor for the precursor forms of NGF (proNGF) and BDNF (proBDNF) (PubMed:22155786, PubMed:24908487). ProNGF and proBDNF binding both promote axon growth cone collapse (in vitro) (PubMed:22155786, PubMed:24908487). Plays a role in the regulation of dendritic spine density in hippocampus neurons (By similarity). Required for normal neurite branching and extension in response to BDNF (PubMed:27457814). Plays a role in BDNF-dependent hippocampal synaptic plasticity. Together with NGFR and NTRK2, is required both for BDNF-mediated synaptic long-term depression and long-term potentiation (PubMed:27457814). ProNGF binding promotes dissociation of TRIO from the heterodimer, which leads to inactivation of RAC1 and/or RAC2 and subsequent reorganization of the actin cytoskeleton (PubMed:22155786). Together with the retromer complex subunit VPS35, required for normal expression of GRIN2A at synapses and dendritic cell membranes. Required for normal expression of the amino acid transporter SLC1A1 at the cell membrane, and thereby contributes to protect cells against oxidative stress (By similarity). {ECO:0000250|UniProtKB:Q9EPR5, ECO:0000269|PubMed:22155786, ECO:0000269|PubMed:24908487, ECO:0000269|PubMed:27457814}.; FUNCTION: [SorCS2 122 kDa chain]: Does not promote Schwann cell apoptosis in response to proBDNF. {ECO:0000269|PubMed:24908487}.; FUNCTION: SorCS2 104 kDa chain and SorCS2 18 kDa chain together promote Schwann cell apoptosis in response to proBDNF. {ECO:0000269|PubMed:24908487}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (8); Chain (4); Compositional bias (1); Disulfide bond (7); Domain (1); Glycosylation (7); Helix (1); Mutagenesis (4); Natural variant (3); Region (2); Repeat (6); Sequence conflict (1); Signal peptide (1); Site (3); Topological domain (2); Transmembrane (1)
Keywords 3D-structure;Cell junction;Cell membrane;Cell projection;Cytoplasmic vesicle;Disulfide bond;Endosome;Glycoprotein;Membrane;Postsynaptic cell membrane;Reference proteome;Repeat;Signal;Synapse;Synaptosome;Transmembrane;Transmembrane helix
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22155786, ECO:0000269|PubMed:24908487}; Single-pass type I membrane protein {ECO:0000269|PubMed:24908487}. Cell projection {ECO:0000250|UniProtKB:Q9EPR5}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:24908487}; Single-pass type I membrane protein {ECO:0000269|PubMed:24908487}. Early endosome membrane {ECO:0000250|UniProtKB:Q9EPR5}. Recycling endosome membrane {ECO:0000250|UniProtKB:Q9EPR5}. Cell junction, synapse, synaptosome {ECO:0000250|UniProtKB:Q9EPR5}. Perikaryon {ECO:0000269|PubMed:28469074}. Cell projection, dendrite {ECO:0000269|PubMed:28469074}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q9EPR5}. Cell junction, synapse, postsynaptic density membrane {ECO:0000250|UniProtKB:Q9EPR5}.
Modified Residue
Post Translational Modification PTM: Proteolytic cleavage removes a propeptide, giving rise to a 122 kDa chain that includes a cytoplasmic tail. Further cleavage gives rise to a 104 kDa chain that lacks the cytoplasmic tail, and a membrane-bound 18 kDa chain. The 104 kDa chain remains bound to the 18 kDa chain. {ECO:0000269|PubMed:24908487}.; PTM: N-glycosylated. {ECO:0000269|PubMed:24908487}.
Signal Peptide SIGNAL 1..50; /evidence=ECO:0000255
Structure 3D NMR spectroscopy (1)
Cross Reference PDB 1WGO;
Mapped Pubmed ID 19308021; 19328558; 19851296; 20080650; 20198315; 20379614; 26420026; 28827148; 29315502; 30252935; 31562781;
Motif
Gene Encoded By
Mass 128,152
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda