Q99JH7 · CSTN3_MOUSE
- ProteinCalsyntenin-3
- GeneClstn3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids956 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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).
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).
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).
GO annotations
Keywords
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameCalsyntenin-3
- Short namesCst-3
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ99JH7
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Postsynaptic cell membrane ; Single-pass type I membrane protein
Endoplasmic reticulum membrane ; Single-pass type I membrane protein
Golgi apparatus membrane ; Single-pass type I membrane protein
Note: Most prominent in the postsynaptic specializations of asymmetric (type I) synapses with both axodendritic and axospinous localization.
Isoform CLSTN3beta
Endoplasmic reticulum membrane ; Single-pass membrane protein
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.
Features
Showing features for topological domain, intramembrane, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-21 | In isoform Q99JH7-2; Cytoplasmic | ||||
Sequence: MTLLLVSLLLASLLQISSGNK | ||||||
Topological domain | 20-847 | Extracellular | ||||
Sequence: NKANKHKPWIEAEYQGIVMENDNTVLLNPPLFALDKDAPLRYAGEICGFRLHGSGVPFEAVILDKATGEGLIRAKEPVDCEAQKEHTFTIQAYDCGEGPDGTNTKKSHKATVHVRVNDVNEFAPVFVERLYRAAVTEGKLYDRILRVEAIDGDCSPQYSQICYYEILTPNTPFLIDNDGNIENTEKLQYSGEKLYKFTVTAYDCGKKRAADDAEVEIQVKPTCKPSWQGWNKRIEYAPGAGSLALFPGIRLETCDEPLWNIQATIELQTSHVAKGCDRDNYSERALRKLCGAATGEVDLLPMPGPNANWTAGLSVHYSQDSSLIYWFNGTQAVQVPLGGPAGLGSGPQDGFSDHFTLSFWMKHSVTPSKGKKEEETIVCNTVQNEDGYSHYSLTVHGCRIAFLYWPLLESARPVKFLWKLEQVCDDEWHHYALNLEFPTVTLYTDGISFDPALIHDNGLIHPPRREPALMIGACWTEEKNKEKKGGENSTDTASGDPLLIHHYFHGYLAGFSVRSGRLESREVIECLYACREGLDYRDFESLGKGMKVHVNPSQSLLTLEGDDVETFNHALQHVAYMNTLRFATPGVRPLRLTTAVKCFSEESCVSIPEVEGYVVVLQPDAPQILLSGTAHFARPAVDFEGPEGVPLFPDLQITCSISHQVEAKADESWQGTVTDTRMSDEIVHNLDGCEISLVGDDLDPERESLLLDMASLQQRGLELTNTSAYLTIAGVETITVYEEILRQARYQLRHGAALYARKFRLSCSEMNGRYSSNEFIVEVNVLHSMNRVAHPSHVLSSQQFLHRGHQPPPEMAGHSLASSHRNSMVPSA | ||||||
Intramembrane | 22-42 | In isoform Q99JH7-2; Helical | ||||
Sequence: ANKHKPWIEAEYQGIVMENDN | ||||||
Topological domain | 43-73 | In isoform Q99JH7-2; Cytoplasmic | ||||
Sequence: TVLLNPPLFALDKDAPLRYAGEICGFRLHGS | ||||||
Intramembrane | 74-94 | In isoform Q99JH7-2; Helical | ||||
Sequence: GVPFEAVILDKATGEGLIRAK | ||||||
Topological domain | 95-139 | In isoform Q99JH7-2; Cytoplasmic | ||||
Sequence: EPVDCEAQKEHTFTIQAYDCGEGPDGTNTKKSHKATVHVRVNDVN | ||||||
Intramembrane | 140-160 | In isoform Q99JH7-2; Helical | ||||
Sequence: EFAPVFVERLYRAAVTEGKLY | ||||||
Topological domain | 161-248 | In isoform Q99JH7-2; Cytoplasmic | ||||
Sequence: DRILRVEAIDGDCSPQYSQICYYEILTPNTPFLIDNDGNIENTEKLQYSGEKLYKFTVTAYDCGKKRAADDAEVEIQVKPTCKPSWQG | ||||||
Transmembrane | 249-269 | In isoform Q99JH7-2; Helical | ||||
Sequence: WNKRIEYAPGAGSLALFPGIR | ||||||
Topological domain | 270-357 | In isoform Q99JH7-2; Lumenal | ||||
Sequence: LETCDEPLWNIQATIELQTSHVAKGCDRDNYSERALRKLCGAATGEVDLLPMPGPNANWTAGLSVHYSQDSSLIYWFNGTQAVQVPLG | ||||||
Transmembrane | 848-868 | Helical | ||||
Sequence: ATLIIVVCVGFLVLMVILGLV | ||||||
Topological domain | 869-956 | Cytoplasmic | ||||
Sequence: RIHSLHRRVSGTGGPSGASTDPKDPDLFWDDSALTIIVNPMESYQNQQTCVAGVAGGQQEEEDSSDSEAADSPSSDERRIIESPPHRY |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Mice are defective in both excitatory and inhibitory synapse development (PubMed:24094106).
Mice also show reduced body mass and increased energy expenditure (PubMed:32382066).
Mice also display reduced marrow volume and cortical bone mass without alteration of trabecular bone microarchitecture (PubMed:32382066).
Conditional deletion in neurons leads to a significant reduction in number of excitatory synaptic inputs (PubMed:32434929).
Conditional deletion in the cerebellum causes major impairments in motor learning due to a large decrease in inhibitory synapse, associated with a robust increase in excitatory parallel-fiber synapses in Purkinje cells (PubMed:35420982).
As a result, inhibitory synaptic transmission is suppressed, whereas parallel-fiber synaptic transmission is enhanced in Purkinje cells (PubMed:35420982).
No changes in the dendritic architecture of Purkinje cells or in climbing-fiber synapses is observed (PubMed:35420982).
Mice lacking Clstn1, Clstn2 and Clstn3 display behavior disorders, characterized by hyperactivity in normal environment, hypersensitivity to stress, and show tendency to freeze in novel environments (PubMed:35279170).
Mice also show reduced body mass and increased energy expenditure (PubMed:32382066).
Mice also display reduced marrow volume and cortical bone mass without alteration of trabecular bone microarchitecture (PubMed:32382066).
Conditional deletion in neurons leads to a significant reduction in number of excitatory synaptic inputs (PubMed:32434929).
Conditional deletion in the cerebellum causes major impairments in motor learning due to a large decrease in inhibitory synapse, associated with a robust increase in excitatory parallel-fiber synapses in Purkinje cells (PubMed:35420982).
As a result, inhibitory synaptic transmission is suppressed, whereas parallel-fiber synaptic transmission is enhanced in Purkinje cells (PubMed:35420982).
No changes in the dendritic architecture of Purkinje cells or in climbing-fiber synapses is observed (PubMed:35420982).
Mice lacking Clstn1, Clstn2 and Clstn3 display behavior disorders, characterized by hyperactivity in normal environment, hypersensitivity to stress, and show tendency to freeze in novel environments (PubMed:35279170).
Isoform CLSTN3beta
Mice are defective in energy expenditure and adaptive thermogenesis: mutant mice are hypothermic at a faster rate than controls during acute cold challenge (PubMed:31043739, PubMed:36477540).
Mice show larger and paler brown adipose tissue and display abnormal lipid droplet forms (PubMed:36477540).
Mice show larger and paler brown adipose tissue and display abnormal lipid droplet forms (PubMed:36477540).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 896 | Increased KLC1-binding. | ||||
Sequence: F → D |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 42 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-19 | |||||
Sequence: MTLLLVSLLLASLLQISSG | ||||||
Chain | PRO_0000004027 | 20-956 | Calsyntenin-3 | |||
Sequence: NKANKHKPWIEAEYQGIVMENDNTVLLNPPLFALDKDAPLRYAGEICGFRLHGSGVPFEAVILDKATGEGLIRAKEPVDCEAQKEHTFTIQAYDCGEGPDGTNTKKSHKATVHVRVNDVNEFAPVFVERLYRAAVTEGKLYDRILRVEAIDGDCSPQYSQICYYEILTPNTPFLIDNDGNIENTEKLQYSGEKLYKFTVTAYDCGKKRAADDAEVEIQVKPTCKPSWQGWNKRIEYAPGAGSLALFPGIRLETCDEPLWNIQATIELQTSHVAKGCDRDNYSERALRKLCGAATGEVDLLPMPGPNANWTAGLSVHYSQDSSLIYWFNGTQAVQVPLGGPAGLGSGPQDGFSDHFTLSFWMKHSVTPSKGKKEEETIVCNTVQNEDGYSHYSLTVHGCRIAFLYWPLLESARPVKFLWKLEQVCDDEWHHYALNLEFPTVTLYTDGISFDPALIHDNGLIHPPRREPALMIGACWTEEKNKEKKGGENSTDTASGDPLLIHHYFHGYLAGFSVRSGRLESREVIECLYACREGLDYRDFESLGKGMKVHVNPSQSLLTLEGDDVETFNHALQHVAYMNTLRFATPGVRPLRLTTAVKCFSEESCVSIPEVEGYVVVLQPDAPQILLSGTAHFARPAVDFEGPEGVPLFPDLQITCSISHQVEAKADESWQGTVTDTRMSDEIVHNLDGCEISLVGDDLDPERESLLLDMASLQQRGLELTNTSAYLTIAGVETITVYEEILRQARYQLRHGAALYARKFRLSCSEMNGRYSSNEFIVEVNVLHSMNRVAHPSHVLSSQQFLHRGHQPPPEMAGHSLASSHRNSMVPSAATLIIVVCVGFLVLMVILGLVRIHSLHRRVSGTGGPSGASTDPKDPDLFWDDSALTIIVNPMESYQNQQTCVAGVAGGQQEEEDSSDSEAADSPSSDERRIIESPPHRY | ||||||
Glycosylation | 299 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 327 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 347 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 507 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 740 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
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.
Isoform CLSTN3beta
Ubiquitinated: endoplasmic reticulum-localized protein is ubiquitinated and degraded by the endoplasmic reticulum-associated degradation (ERAD) pathway.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Restricted to the brain (at protein level) (PubMed:12498782, PubMed:24094106).
In the cerebral cortex, found in the somas and neuropil of all layers (PubMed:12498782).
Expressed at highest levels in neurons of cortical layer 5 and, at lower levels, in neurons of the upper layers (PubMed:12498782).
Highly expressed in Purkinje cells (PubMed:12498782).
Also found in a few scattered interneurons throughout the granule cell layer and occasionally in neurons in the molecular layer (at protein level) (PubMed:12498782).
In all layers, high levels in a subpopulation of presumptive GABAergic neurons (based on morphology) (PubMed:12498782).
In the cerebral cortex, found in the somas and neuropil of all layers (PubMed:12498782).
Expressed at highest levels in neurons of cortical layer 5 and, at lower levels, in neurons of the upper layers (PubMed:12498782).
Highly expressed in Purkinje cells (PubMed:12498782).
Also found in a few scattered interneurons throughout the granule cell layer and occasionally in neurons in the molecular layer (at protein level) (PubMed:12498782).
In all layers, high levels in a subpopulation of presumptive GABAergic neurons (based on morphology) (PubMed:12498782).
Isoform CLSTN3beta
Expression is restricted to adipose tissue, with high expression in thermogenic adipocytes (brown adipose tissue).
Induction
Isoform CLSTN3beta
Expression is induced by cold and PPAR-gamma (PPARG).
Gene expression databases
Interaction
Subunit
Interacts (via cadherin domains) with both alpha and beta isoforms of neurexins (NRXN1, NRXN2 and NRXN3) (PubMed:24094106, PubMed:24613359, PubMed:32434929).
Directly interacts with APBA2 (By similarity).
Forms a tripartite complex with APBA2 and APP (By similarity).
Interacts with low affinity with KLC1 (PubMed:16760430).
Interacts with SLC23A2/SVCT2 (By similarity).
Directly interacts with APBA2 (By similarity).
Forms a tripartite complex with APBA2 and APP (By similarity).
Interacts with low affinity with KLC1 (PubMed:16760430).
Interacts with SLC23A2/SVCT2 (By similarity).
Isoform CLSTN3beta
Interacts with CIDEA; inhibiting the lipid transferase activity of CIDEA (PubMed:36477540).
Interacts with CIDEC; inhibiting the lipid transferase activity of CIDEC (PubMed:36477540).
Interacts with CIDEC; inhibiting the lipid transferase activity of CIDEC (PubMed:36477540).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 29-145 | Cadherin 1 | ||||
Sequence: IEAEYQGIVMENDNTVLLNPPLFALDKDAPLRYAGEICGFRLHGSGVPFEAVILDKATGEGLIRAKEPVDCEAQKEHTFTIQAYDCGEGPDGTNTKKSHKATVHVRVNDVNEFAPVF | ||||||
Domain | 146-246 | Cadherin 2 | ||||
Sequence: VERLYRAAVTEGKLYDRILRVEAIDGDCSPQYSQICYYEILTPNTPFLIDNDGNIENTEKLQYSGEKLYKFTVTAYDCGKKRAADDAEVEIQVKPTCKPSW | ||||||
Region | 916-956 | Disordered | ||||
Sequence: QTCVAGVAGGQQEEEDSSDSEAADSPSSDERRIIESPPHRY | ||||||
Compositional bias | 939-956 | Basic and acidic residues | ||||
Sequence: DSPSSDERRIIESPPHRY |
Domain
The cytoplasmic domain binds synaptic Ca2+.
Sequence similarities
Belongs to the calsyntenin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
Q99JH7-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length956
- Mass (Da)105,872
- Last updated2001-06-01 v1
- ChecksumBF9CB267B1D0B578
Q99JH7-2
- NameCLSTN3beta
- SynonymsCalsyntenin-3beta
- Differences from canonical
- 1-843: MTLLLVSLLLASLLQISSGNKANKHKPWIEAEYQGIVMENDNTVLLNPPLFALDKDAPLRYAGEICGFRLHGSGVPFEAVILDKATGEGLIRAKEPVDCEAQKEHTFTIQAYDCGEGPDGTNTKKSHKATVHVRVNDVNEFAPVFVERLYRAAVTEGKLYDRILRVEAIDGDCSPQYSQICYYEILTPNTPFLIDNDGNIENTEKLQYSGEKLYKFTVTAYDCGKKRAADDAEVEIQVKPTCKPSWQGWNKRIEYAPGAGSLALFPGIRLETCDEPLWNIQATIELQTSHVAKGCDRDNYSERALRKLCGAATGEVDLLPMPGPNANWTAGLSVHYSQDSSLIYWFNGTQAVQVPLGGPAGLGSGPQDGFSDHFTLSFWMKHSVTPSKGKKEEETIVCNTVQNEDGYSHYSLTVHGCRIAFLYWPLLESARPVKFLWKLEQVCDDEWHHYALNLEFPTVTLYTDGISFDPALIHDNGLIHPPRREPALMIGACWTEEKNKEKKGGENSTDTASGDPLLIHHYFHGYLAGFSVRSGRLESREVIECLYACREGLDYRDFESLGKGMKVHVNPSQSLLTLEGDDVETFNHALQHVAYMNTLRFATPGVRPLRLTTAVKCFSEESCVSIPEVEGYVVVLQPDAPQILLSGTAHFARPAVDFEGPEGVPLFPDLQITCSISHQVEAKADESWQGTVTDTRMSDEIVHNLDGCEISLVGDDLDPERESLLLDMASLQQRGLELTNTSAYLTIAGVETITVYEEILRQARYQLRHGAALYARKFRLSCSEMNGRYSSNEFIVEVNVLHSMNRVAHPSHVLSSQQFLHRGHQPPPEMAGHSLASSHRNSM → MWQVAIQLPRRVLGLGLYLWGLFLHLLFLGFGAPLLCFLVLLRVLSLAAQNGAQVVFMAARSVALRVQVCSVYVFLQGGAWFAQLVGSWVTLLIRLFGGMLETLTHIPLILLCEQAARWLVQAVVWVTRGLARVWGMATFVQLCAHSFFIGMCLCLHICFSTISSKVHVRVHMPFCLSLPVRVHVPLNLGIRMRLQGGRPRSAAVEVGRPQGETPQEQQPCRTRNLRPTRRREVSRNRSEPRRV
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A5F8MPB2 | A0A5F8MPB2_MOUSE | Clstn3 | 191 | ||
A0A5F8MQ21 | A0A5F8MQ21_MOUSE | Clstn3 | 78 | ||
A0A0N4SW90 | A0A0N4SW90_MOUSE | Clstn3 | 64 | ||
D3Z601 | D3Z601_MOUSE | Clstn3 | 919 |
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_061881 | 1-843 | in isoform CLSTN3beta | |||
Sequence: MTLLLVSLLLASLLQISSGNKANKHKPWIEAEYQGIVMENDNTVLLNPPLFALDKDAPLRYAGEICGFRLHGSGVPFEAVILDKATGEGLIRAKEPVDCEAQKEHTFTIQAYDCGEGPDGTNTKKSHKATVHVRVNDVNEFAPVFVERLYRAAVTEGKLYDRILRVEAIDGDCSPQYSQICYYEILTPNTPFLIDNDGNIENTEKLQYSGEKLYKFTVTAYDCGKKRAADDAEVEIQVKPTCKPSWQGWNKRIEYAPGAGSLALFPGIRLETCDEPLWNIQATIELQTSHVAKGCDRDNYSERALRKLCGAATGEVDLLPMPGPNANWTAGLSVHYSQDSSLIYWFNGTQAVQVPLGGPAGLGSGPQDGFSDHFTLSFWMKHSVTPSKGKKEEETIVCNTVQNEDGYSHYSLTVHGCRIAFLYWPLLESARPVKFLWKLEQVCDDEWHHYALNLEFPTVTLYTDGISFDPALIHDNGLIHPPRREPALMIGACWTEEKNKEKKGGENSTDTASGDPLLIHHYFHGYLAGFSVRSGRLESREVIECLYACREGLDYRDFESLGKGMKVHVNPSQSLLTLEGDDVETFNHALQHVAYMNTLRFATPGVRPLRLTTAVKCFSEESCVSIPEVEGYVVVLQPDAPQILLSGTAHFARPAVDFEGPEGVPLFPDLQITCSISHQVEAKADESWQGTVTDTRMSDEIVHNLDGCEISLVGDDLDPERESLLLDMASLQQRGLELTNTSAYLTIAGVETITVYEEILRQARYQLRHGAALYARKFRLSCSEMNGRYSSNEFIVEVNVLHSMNRVAHPSHVLSSQQFLHRGHQPPPEMAGHSLASSHRNSM → MWQVAIQLPRRVLGLGLYLWGLFLHLLFLGFGAPLLCFLVLLRVLSLAAQNGAQVVFMAARSVALRVQVCSVYVFLQGGAWFAQLVGSWVTLLIRLFGGMLETLTHIPLILLCEQAARWLVQAVVWVTRGLARVWGMATFVQLCAHSFFIGMCLCLHICFSTISSKVHVRVHMPFCLSLPVRVHVPLNLGIRMRLQGGRPRSAAVEVGRPQGETPQEQQPCRTRNLRPTRRREVSRNRSEPRRV | ||||||
Compositional bias | 939-956 | Basic and acidic residues | ||||
Sequence: DSPSSDERRIIESPPHRY |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ278486 EMBL· GenBank· DDBJ | CAC33088.1 EMBL· GenBank· DDBJ | mRNA | ||
AK032336 EMBL· GenBank· DDBJ | BAC27821.1 EMBL· GenBank· DDBJ | mRNA | ||
MK758090 EMBL· GenBank· DDBJ | QCO31665.1 EMBL· GenBank· DDBJ | mRNA | ||
BC055054 EMBL· GenBank· DDBJ | AAH55054.1 EMBL· GenBank· DDBJ | mRNA |