CLSTN3
entrez
9746
canonical
uniprot
Q9BQT9
canonical
ensembl
ENSG00000139182
resolver
ensembl
ENSG00000288427
resolver
ensp
ENSP00000266546
resolver
ensp
ENSP00000560418
resolver
ensp
ENSP00000560419
resolver
genesymbol
CLSTN3
resolver
genesymbol_syn
CS3
resolver
genesymbol_syn
KIAA0726
resolver
hgnc
HGNC:18371
resolver
uniprot
A0A3B3IRF8
resolver
uniprot
D3DUT6
resolver
uniprot
O94831
resolver
uniprot
Q2T9J5
resolver
uniprot
Q5UE57
resolver
uniprot_entry
CSTN3_HUMAN
resolver
uniprot_sec
A0A3B3IRF8
resolver
uniprot_sec
D3DUT6
resolver
uniprot_sec
O94831
resolver
uniprot_sec
Q2T9J5
resolver
uniprot_sec
Q5UE57
resolver
amino_acid_sequence
MTLLLLPLLLASLLASCSCNKANKHKPWIEAEYQGIVMENDNTVLLNPPLFALDKDAPLRYAGEICGFRLHGSGVPFEAVILDKATGEGLIRAKEPVDCEAQKEHTFTIQAYDCGEGPDGANTKKSHKATVHVRVNDVNEFAPVFVERLYRAAVTEGKLYDRILRVEAIDGDCSPQYSQICYYEILTPNTPFLIDNDGNIENTEKLQYSGERLYKFTVTAYDCGKKRAADDAEVEIQVKPTCKPSWQGWNKRIEYAPGAGSLALFPGIRLETCDEPLWNIQATIELQTSHVAKGCDRDNYSERALRKLCGAATGEVDLLPMPGPNANWTAGLSVHYSQDSSLIYWFNGTQAVQVPLGGPSGLGSGPQDSLSDHFTLSFWMKHGVTPNKGKKEEETIVCNTVQNEDGFSHYSLTVHGCRIAFLYWPLLESARPVKFLWKLEQVCDDEWHHYALNLEFPTVTLYTDGISFDPALIHDNGLIHPPRREPALMIGACWTEEKNKEKEKGDNSTDTTQGDPLSIHHYFHGYLAGFSVRSGRLESREVIECLYACREGLDYRDFESLGKGMKVHVNPSQSLLTLEGDDVETFNHALQHVAYMNTLRFATPGVRPLRLTTAVKCFSEESCVSIPEVEGYVVVLQPDAPQILLSGTAHFARPAVDFEGTNGVPLFPDLQITCSISHQVEAKKDESWQGTVTDTRMSDEIVHNLDGCEISLVGDDLDPERESLLLDTTSLQQRGLELTNTSAYLTIAGVESITVYEEILRQARYRLRHGAALYTRKFRLSCSEMNGRYSSNEFIVEVNVLHSMNRVAHPSHVLSSQQFLHRGHQPPPEMAGHSLASSHRNSMIPSAATLIIVVCVGFLVLMVVLGLVRIHSLHRRVSGAGGPPGASSDPKDPDLFWDDSALTIIVNPMESYQNRQSCVTGAVGGQQEDEDSSDSEVADSPSSDERRIIETPPHRY
uniprot
proteins
function
FUNCTION: Postsynaptic adhesion molecule that binds to presynaptic neurexins to mediate both excitatory and inhibitory synapse formation (PubMed:25352602). 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:25352602). 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 (By similarity). May also be involved in ascorbate (vitamin C) uptake via its interaction with SLC23A2/SVCT2 (PubMed:34673103). 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 (Probable) (PubMed:12972431). {ECO:0000250|UniProtKB:Q99JH7, ECO:0000269|PubMed:25352602, ECO:0000269|PubMed:34673103, ECO:0000305|PubMed:12972431}.; FUNCTION: [Isoform CLSTN3beta]: Adipose-specific isoform that plays a key role in adaptive thermogenesis. 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. 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. {ECO:0000250|UniProtKB:Q99JH7}.
uniprot
proteins
mass_dalton
106098
uniprot
proteins
post_translational_modification
PTM: Proteolytically processed under normal cellular conditions (PubMed:15037614). A primary zeta-cleavage generates a large extracellular (soluble) N-terminal domain (sAlc) and a short C-terminal transmembrane fragment (CTF1) (PubMed:15037614). 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) (PubMed:15037614). This processing is strongly suppressed in the tripartite complex formed with APBA2 and APP, which seems to prevent the association with gamma-secretase (PubMed:15037614). {ECO:0000269|PubMed:15037614}.; PTM: [Isoform CLSTN3beta]: Ubiquitinated: endoplasmic reticulum-localized protein is ubiquitinated and degraded by the endoplasmic reticulum-associated degradation (ERAD) pathway. {ECO:0000250|UniProtKB:Q99JH7}.
uniprot
proteins
protein_family
Calsyntenin family
uniprot
proteins
pubmed
12498782
uniprot
proteins
pubmed
12972431
uniprot
proteins
pubmed
15037614
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
25352602
uniprot
proteins
pubmed
33101212
uniprot
proteins
pubmed
34673103
uniprot
proteins
pubmed
35753632
uniprot
proteins
pubmed
9872452
uniprot
proteins
sequence_length
956
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q99JH7}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q99JH7}; Single-pass type I membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q99JH7}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q99JH7}. Note=Most prominent in the postsynaptic specializations of asymmetric (type I) synapses with both axodendritic and axospinous localization. {ECO:0000250|UniProtKB:Q99JH7}.; SUBCELLULAR LOCATION: [Isoform CLSTN3beta]: Lipid droplet {ECO:0000250|UniProtKB:Q99JH7}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q99JH7}; 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:0000250|UniProtKB:Q99JH7}.
uniprot
proteins
transmembrane_region
TRANSMEM 848..868; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM Q9BQT9-3:256..276; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins