Clstn3
entrez
232370
canonical
uniprot
Q99JH7
canonical
ensembl
ENSMUSG00000008153
resolver
ensp
ENSMUSP00000008297
resolver
ensp
ENSMUSP00000108142
resolver
enst
ENSMUST00000112523
resolver
genesymbol
Clstn3
resolver
genesymbol_syn
Cs3
resolver
genesymbol_syn
Cstn3
resolver
uniprot
A0A4P8DYG6
resolver
uniprot
D3Z601
resolver
uniprot
Q544R0
resolver
uniprot_entry
CSTN3_MOUSE
resolver
uniprot_entry
D3Z601_MOUSE
resolver
uniprot_sec
A0A4P8DYG6
resolver
uniprot_sec
Q544R0
resolver
amino_acid_sequence
MTLLLVSLLLASLLQISSGNKANKHKPWIEAEYQGIVMENDNTVLLNPPLFALDKDAPLRYAGEICGFRLHGSGVPFEAVILDKATGEGLIRAKEPVDCEAQKEHTFTIQAYDCGEGPDGTNTKKSHKATVHVRVNDVNEFAPVFVERLYRAAVTEGKLYDRILRVEAIDGDCSPQYSQICYYEILTPNTPFLIDNDGNIENTEKLQYSGEKLYKFTVTAYDCGKKRAADDAEVEIQVKPTCKPSWQGWNKRIEYAPGAGSLALFPGIRLETCDEPLWNIQATIELQTSHVAKGCDRDNYSERALRKLCGAATGEVDLLPMPGPNANWTAGLSVHYSQDSSLIYWFNGTQAVQVPLGGPAGLGSGPQDGFSDHFTLSFWMKHSVTPSKGKKEEETIVCNTVQNEDGYSHYSLTVHGCRIAFLYWPLLESARPVKFLWKLEQVCDDEWHHYALNLEFPTVTLYTDGISFDPALIHDNGLIHPPRREPALMIGACWTEEKNKEKKGGENSTDTASGDPLLIHHYFHGYLAGFSVRSGRLESREVIECLYACREGLDYRDFESLGKGMKVHVNPSQSLLTLEGDDVETFNHALQHVAYMNTLRFATPGVRPLRLTTAVKCFSEESCVSIPEVEGYVVVLQPDAPQILLSGTAHFARPAVDFEGPEGVPLFPDLQITCSISHQVEAKADESWQGTVTDTRMSDEIVHNLDGCEISLVGDDLDPERESLLLDMASLQQRGLELTNTSAYLTIAGVETITVYEEILRQARYQLRHGAALYARKFRLSCSEMNGRYSSNEFIVEVNVLHSMNRVAHPSHVLSSQQFLHRGHQPPPEMAGHSLASSHRNSMVPSAATLIIVVCVGFLVLMVILGLVRIHSLHRRVSGTGGPSGASTDPKDPDLFWDDSALTIIVNPMESYQNQQTCVAGVAGGQQEEEDSSDSEAADSPSSDERRIIESPPHRY
uniprot
proteins
function
FUNCTION: Postsynaptic adhesion molecule that binds to presynaptic neurexins to mediate both excitatory and inhibitory synapse formation (PubMed:24094106, PubMed:24613359, PubMed:32434929, PubMed:35420982). Promotes synapse development by acting as a cell adhesion molecule at the postsynaptic membrane, which associates with both neurexin-alpha and neurexin-beta proteins at the presynaptic membrane (PubMed:24094106, PubMed:24613359, PubMed:32434929). Regulates the balance between excitatory and inhibitory synapses by inhibiting formation of excitatory parallel-fiber synapses and promoting formation of inhibitory synapses in the same neuron (PubMed:35420982). May also be involved in ascorbate (vitamin C) uptake via its interaction with SLC23A2/SVCT2 (PubMed:33672967). Complex formation with APBA2 and APP, stabilizes APP metabolism and enhances APBA2-mediated suppression of beta-APP40 secretion, due to the retardation of intracellular APP maturation (By similarity). {ECO:0000250|UniProtKB:Q9BQT9, ECO:0000269|PubMed:24094106, ECO:0000269|PubMed:24613359, ECO:0000269|PubMed:32434929, ECO:0000269|PubMed:33672967, ECO:0000269|PubMed:35420982}.; FUNCTION: [Isoform CLSTN3beta]: Adipose-specific isoform that plays a key role in adaptive thermogenesis (PubMed:31043739, PubMed:36477540). Facilitates the efficient use of stored triglyceride by promoting multilocular morphology of thermogenic adipocytes: acts by inhibiting the activity of CIDEA and CIDEC on lipid droplets, thereby preventing lipid droplet fusion and facilitating lipid utilization (PubMed:36477540). May also participate in adaptive thermogenesis by promoting sympathetic innervation of thermogenic adipose tissue: acts by driving secretion of neurotrophic factor S100B from brown adipocytes, stimulating neurite outgrowth from sympathetic neurons (PubMed:31043739). {ECO:0000269|PubMed:31043739, ECO:0000269|PubMed:36477540}.
uniprot
proteins
mass_dalton
105872
uniprot
proteins
mutagenesis
MUTAGEN 896; /note="F->D: Increased KLC1-binding."; /evidence="ECO:0000269|PubMed:16760430
uniprot
proteins
post_translational_modification
PTM: Proteolytically processed under normal cellular conditions. A primary zeta-cleavage generates a large extracellular (soluble) N-terminal domain (sAlc) and a short C-terminal transmembrane fragment (CTF1). A secondary cleavage catalyzed by gamma-secretase within the transmembrane domain releases the beta-Alc-beta chain in the extracellular milieu and produces an intracellular fragment (AlcICD). This processing is strongly suppressed in the tripartite complex formed with APBA2 and APP, which seems to prevent the association with gamma-secretase. {ECO:0000250|UniProtKB:Q9BQT9}.; PTM: [Isoform CLSTN3beta]: Ubiquitinated: endoplasmic reticulum-localized protein is ubiquitinated and degraded by the endoplasmic reticulum-associated degradation (ERAD) pathway. {ECO:0000269|PubMed:36477540}.
uniprot
proteins
protein_family
Calsyntenin family
uniprot
proteins
pubmed
12498782
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16760430
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
24094106
uniprot
proteins
pubmed
24613359
uniprot
proteins
pubmed
31043739
uniprot
proteins
pubmed
32382066
uniprot
proteins
pubmed
32434929
uniprot
proteins
pubmed
33101212
uniprot
proteins
pubmed
33672967
uniprot
proteins
pubmed
35279170
uniprot
proteins
pubmed
35420982
uniprot
proteins
pubmed
36477540
uniprot
proteins
sequence_length
956
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000269|PubMed:12498782, ECO:0000269|PubMed:24613359}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:12498782}; Single-pass type I membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:12498782}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, dendrite {ECO:0000269|PubMed:12498782}. Note=Most prominent in the postsynaptic specializations of asymmetric (type I) synapses with both axodendritic and axospinous localization. {ECO:0000269|PubMed:12498782}.; SUBCELLULAR LOCATION: [Isoform CLSTN3beta]: Lipid droplet {ECO:0000269|PubMed:36477540}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:31043739, ECO:0000269|PubMed:36477540}; Single-pass membrane protein {ECO:0000255}. Note=Localizes to endoplasmic reticulum-lipid droplet contact sites through the partitioning of its N-terminal hydrophobic hairpins onto lipid droplets while its C-terminal transmembrane domain remains anchored in the endoplasmic reticulum. {ECO:0000269|PubMed:36477540}.
uniprot
proteins
transmembrane_region
TRANSMEM 848..868; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM Q99JH7-2:249..269; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins