Q4VA61 · DSCL1_MOUSE
- ProteinCell adhesion molecule DSCAML1
- GeneDscaml1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2053 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Cell adhesion molecule that plays a role in neuronal self-avoidance. Promotes repulsion between specific neuronal processes of either the same cell or the same subtype of cells. Promotes both isoneuronal self-avoidance for creating an orderly neurite arborization in retinal rod bipolar cells and heteroneuronal self-avoidance to maintain mosaic spacing between AII amacrine cells (PubMed:19945391).
Adhesion molecule that promotes lamina-specific synaptic connections in the retina: expressed in specific subsets of interneurons and retinal ganglion cells (RGCs) and promotes synaptic connectivity via homophilic interactions (By similarity).
Adhesion molecule that promotes lamina-specific synaptic connections in the retina: expressed in specific subsets of interneurons and retinal ganglion cells (RGCs) and promotes synaptic connectivity via homophilic interactions (By similarity).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | axon | |
Cellular Component | plasma membrane | |
Cellular Component | synapse | |
Molecular Function | cell-cell adhesion mediator activity | |
Biological Process | axon guidance | |
Biological Process | calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules | |
Biological Process | central nervous system development | |
Biological Process | dendrite self-avoidance | |
Biological Process | homophilic cell adhesion via plasma membrane adhesion molecules | |
Biological Process | negative regulation of cell adhesion |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCell adhesion molecule DSCAML1
- 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 accessionQ4VA61
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 19-1591 | Extracellular | ||||
Sequence: EDVGTSLYFVNDSLQHVTFSSSVGVVVPCPAAGSPSAALRWYLATGDDIYDVPHIRHVHANGTLQLFPFSPSAFNSFIHDNDYFCTAENAAGKIRSPNIRIKAVFREPYTVRVEDQRSMRGNVAVFKCLIPSSVQEYVSVVSWEKDTVSITPENRFFITSHGGLYISDVQKEDALSTYRCITQHKYSGETRQSNGARLSVTDPAESIPTILDGFHSQEVWTGHSVELPCAASGYPIPAIRWLKDGRPLPADSRWAKRITGLTISDLRTEDSGTYICEVTNTFGSAEANGILTVIDPLHVTLTPKKLKTGIGSTVILSCALTGSPEFTIRWYRNTELVLPGEAISIRGLSNETLLISSAQKSHSGAYQCFATRKAQTAQDFAIIVLEDGTPRIVSSFSEKVVNPGEQFSLMCAAKGAPPPTVTWALDDEPVVRDGSHRTNQYTMSDGTTISHMNVTGPQIRDGGVYRCTARNSVGSAEYQARINVRGPPSIRAMRNITAVAGRDTLINCRVIGYPYYSIKWYKDALLLPDNHRQVVFENGTLKLTDVQKGMDEGEYLCSVLIQPQLSISQSVHVAVKVPPLIQPFEFPPASIGQLLYIPCVVSSGDMPIRITWRKDGQVIISGSGVTIESKEFMSSLQISSVSLKHNGNYTCIASNAAATVSRERQLIVRVPPRFVVQPNNQDGIYGKAGVLNCSVDGYPPPKVMWKHAKGSGNPQQYHPVPLTGRIQILPNSSLLIRHVLEEDIGYYLCQASNGVGTDISKAMFLTVKIPAMITSHPNTTIAIKGHPKELNCTARGERPIIIRWEKGDTVIDPDRVMRYAIATKDNGDEVVSTLKLKPADRGDSVFFSCHAINSYGEDRGLIQLTVQEPPDPPELEIREVKARSMNLRWTQRFDGNSIITGFDIEYKNKSDSWDFKQSTRNISPTINQANIVDLHPASVYSIRMYSFNKIGRSEPSKELTISTEEAAPDGPPMDVTLQPVTSQSIQVTWKAPKKELQNGVIRGYQIGYRENSPGSNGQYSIVEMKATGDSEVYTLDNLKKFAQYGVVVQAFNRAGTGPSSSEINATTLEDVPSQPPENVRALSITSDVAVISWSEPPRSTLNGVLKGYRVIFWSLYVDGEWGEMQNVTTTRERVELRGMEKFTNYSVQVLAYTQAGDGVRSSVLYIQTKEDVPGPPAGIKAVPSSASSVVVSWLPPTKPNGVIRKYTIFCSSPGSGQPAPSEYETSPEQLFYRIAHLNRGQQYLLWVAAVTSAGRGNSSEKVTIEPAGKAPAKIISFGGTVTTPWMKDVRLPCNSVGDPAPAVKWTKDSEDSAIPVSLDGHRLIHTNGTLLLRAVKAEDSGYYTCTATNTGGFDTIIVNLLVQVPPDQPRLTVSKTSASSITLTWIPGDNGGSSIRGFVLQYSVDNSEEWKDVFISSSERSFKLDSLKCGTWYKVKLAAKNSVGSGRISEIIEAKTHGREPSFSKDQHLFTHINSTHARLNLQGWNNGGCPITAIVLEYRPKGTWAWQGVRANSSTEVFLTELREATWYELRMRACNSAGCGNETAQFATLDYDGSTIPPIKSAQGEGDDVKK | ||||||
Transmembrane | 1592-1612 | Helical | ||||
Sequence: LFTIGCPVILATLGVALLFVV | ||||||
Topological domain | 1613-2053 | Cytoplasmic | ||||
Sequence: RKKRKEKRLKRLRDAKSLAEMLISKNNRSFDTPVKGPPQGPRLHIDIPRVQLLIEDKEGIKQLGDDKATIPVTDAEFSQAVNPQSFCTGVSLHHPALIQSTGPLIDMSDIRPGTNPVSRKNVKSAHSTRNRYSSQWTLTKCQASTPARTLTSDWRTVGSQHGVTVTESDSYSASLSQDTDKGRNSMVSTESASSTYEELARAYEHAKLEEQLQHAKFEITECFISDSSSDQMTTGTNENADSMTSMSTPSEPGICRFTASPPKPQDADRGKNVAVPIPHRANKSDYCNLPLYTKSEAFFRKADGREPCPVVPPREASMRNLTRAYHTQARHLTLDPASKPLGLPHPGATAATATATLPQRTLAMPAPPAGTAPPAPGPTPSEPSAAPSAAPPAPSTEPPRAGGPHTKMGGSRDSLLEMSTPGVGRSQKQGAGAYSKSYTLV |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
The inner nuclear and inner plexiform layers in the retina are disorganised at postnatal day 20 (P20). AII amacrine cell populations are randomly distributed or pulled into clumps and rod bipolar show fasciculated dendrites.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 82 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MWLVTFLLLLDSLHKARP | ||||||
Chain | PRO_0000392480 | 19-2053 | Cell adhesion molecule DSCAML1 | |||
Sequence: EDVGTSLYFVNDSLQHVTFSSSVGVVVPCPAAGSPSAALRWYLATGDDIYDVPHIRHVHANGTLQLFPFSPSAFNSFIHDNDYFCTAENAAGKIRSPNIRIKAVFREPYTVRVEDQRSMRGNVAVFKCLIPSSVQEYVSVVSWEKDTVSITPENRFFITSHGGLYISDVQKEDALSTYRCITQHKYSGETRQSNGARLSVTDPAESIPTILDGFHSQEVWTGHSVELPCAASGYPIPAIRWLKDGRPLPADSRWAKRITGLTISDLRTEDSGTYICEVTNTFGSAEANGILTVIDPLHVTLTPKKLKTGIGSTVILSCALTGSPEFTIRWYRNTELVLPGEAISIRGLSNETLLISSAQKSHSGAYQCFATRKAQTAQDFAIIVLEDGTPRIVSSFSEKVVNPGEQFSLMCAAKGAPPPTVTWALDDEPVVRDGSHRTNQYTMSDGTTISHMNVTGPQIRDGGVYRCTARNSVGSAEYQARINVRGPPSIRAMRNITAVAGRDTLINCRVIGYPYYSIKWYKDALLLPDNHRQVVFENGTLKLTDVQKGMDEGEYLCSVLIQPQLSISQSVHVAVKVPPLIQPFEFPPASIGQLLYIPCVVSSGDMPIRITWRKDGQVIISGSGVTIESKEFMSSLQISSVSLKHNGNYTCIASNAAATVSRERQLIVRVPPRFVVQPNNQDGIYGKAGVLNCSVDGYPPPKVMWKHAKGSGNPQQYHPVPLTGRIQILPNSSLLIRHVLEEDIGYYLCQASNGVGTDISKAMFLTVKIPAMITSHPNTTIAIKGHPKELNCTARGERPIIIRWEKGDTVIDPDRVMRYAIATKDNGDEVVSTLKLKPADRGDSVFFSCHAINSYGEDRGLIQLTVQEPPDPPELEIREVKARSMNLRWTQRFDGNSIITGFDIEYKNKSDSWDFKQSTRNISPTINQANIVDLHPASVYSIRMYSFNKIGRSEPSKELTISTEEAAPDGPPMDVTLQPVTSQSIQVTWKAPKKELQNGVIRGYQIGYRENSPGSNGQYSIVEMKATGDSEVYTLDNLKKFAQYGVVVQAFNRAGTGPSSSEINATTLEDVPSQPPENVRALSITSDVAVISWSEPPRSTLNGVLKGYRVIFWSLYVDGEWGEMQNVTTTRERVELRGMEKFTNYSVQVLAYTQAGDGVRSSVLYIQTKEDVPGPPAGIKAVPSSASSVVVSWLPPTKPNGVIRKYTIFCSSPGSGQPAPSEYETSPEQLFYRIAHLNRGQQYLLWVAAVTSAGRGNSSEKVTIEPAGKAPAKIISFGGTVTTPWMKDVRLPCNSVGDPAPAVKWTKDSEDSAIPVSLDGHRLIHTNGTLLLRAVKAEDSGYYTCTATNTGGFDTIIVNLLVQVPPDQPRLTVSKTSASSITLTWIPGDNGGSSIRGFVLQYSVDNSEEWKDVFISSSERSFKLDSLKCGTWYKVKLAAKNSVGSGRISEIIEAKTHGREPSFSKDQHLFTHINSTHARLNLQGWNNGGCPITAIVLEYRPKGTWAWQGVRANSSTEVFLTELREATWYELRMRACNSAGCGNETAQFATLDYDGSTIPPIKSAQGEGDDVKKLFTIGCPVILATLGVALLFVVRKKRKEKRLKRLRDAKSLAEMLISKNNRSFDTPVKGPPQGPRLHIDIPRVQLLIEDKEGIKQLGDDKATIPVTDAEFSQAVNPQSFCTGVSLHHPALIQSTGPLIDMSDIRPGTNPVSRKNVKSAHSTRNRYSSQWTLTKCQASTPARTLTSDWRTVGSQHGVTVTESDSYSASLSQDTDKGRNSMVSTESASSTYEELARAYEHAKLEEQLQHAKFEITECFISDSSSDQMTTGTNENADSMTSMSTPSEPGICRFTASPPKPQDADRGKNVAVPIPHRANKSDYCNLPLYTKSEAFFRKADGREPCPVVPPREASMRNLTRAYHTQARHLTLDPASKPLGLPHPGATAATATATLPQRTLAMPAPPAGTAPPAPGPTPSEPSAAPSAAPPAPSTEPPRAGGPHTKMGGSRDSLLEMSTPGVGRSQKQGAGAYSKSYTLV | ||||||
Disulfide bond | 47↔103 | |||||
Sequence: CPAAGSPSAALRWYLATGDDIYDVPHIRHVHANGTLQLFPFSPSAFNSFIHDNDYFC | ||||||
Glycosylation | 79 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 146↔198 | |||||
Sequence: CLIPSSVQEYVSVVSWEKDTVSITPENRFFITSHGGLYISDVQKEDALSTYRC | ||||||
Disulfide bond | 247↔294 | |||||
Sequence: CAASGYPIPAIRWLKDGRPLPADSRWAKRITGLTISDLRTEDSGTYIC | ||||||
Disulfide bond | 336↔386 | |||||
Sequence: CALTGSPEFTIRWYRNTELVLPGEAISIRGLSNETLLISSAQKSHSGAYQC | ||||||
Glycosylation | 368 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 429↔485 | |||||
Sequence: CAAKGAPPPTVTWALDDEPVVRDGSHRTNQYTMSDGTTISHMNVTGPQIRDGGVYRC | ||||||
Glycosylation | 471 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 526↔575 | |||||
Sequence: CRVIGYPYYSIKWYKDALLLPDNHRQVVFENGTLKLTDVQKGMDEGEYLC | ||||||
Disulfide bond | 617↔669 | |||||
Sequence: CVVSSGDMPIRITWRKDGQVIISGSGVTIESKEFMSSLQISSVSLKHNGNYTC | ||||||
Glycosylation | 666 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 710 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 711↔767 | |||||
Sequence: CSVDGYPPPKVMWKHAKGSGNPQQYHPVPLTGRIQILPNSSLLIRHVLEEDIGYYLC | ||||||
Glycosylation | 809 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 810↔867 | |||||
Sequence: CTARGERPIIIRWEKGDTVIDPDRVMRYAIATKDNGDEVVSTLKLKPADRGDSVFFSC | ||||||
Glycosylation | 1144 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1162 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1311↔1363 | |||||
Sequence: CNSVGDPAPAVKWTKDSEDSAIPVSLDGHRLIHTNGTLLLRAVKAEDSGYYTC | ||||||
Glycosylation | 1345 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1561 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
In the retina, expressed in the rod photoreceptors, AII amacrine cells and rod bipolar cells (at protein level).
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 19-119 | Ig-like C2-type 1 | ||||
Sequence: EDVGTSLYFVNDSLQHVTFSSSVGVVVPCPAAGSPSAALRWYLATGDDIYDVPHIRHVHANGTLQLFPFSPSAFNSFIHDNDYFCTAENAAGKIRSPNIRI | ||||||
Domain | 115-217 | Ig-like C2-type 2 | ||||
Sequence: PNIRIKAVFREPYTVRVEDQRSMRGNVAVFKCLIPSSVQEYVSVVSWEKDTVSITPENRFFITSHGGLYISDVQKEDALSTYRCITQHKYSGETRQSNGARLS | ||||||
Domain | 226-310 | Ig-like C2-type 3 | ||||
Sequence: PTILDGFHSQEVWTGHSVELPCAASGYPIPAIRWLKDGRPLPADSRWAKRITGLTISDLRTEDSGTYICEVTNTFGSAEANGILT | ||||||
Domain | 314-396 | Ig-like C2-type 4 | ||||
Sequence: PLHVTLTPKKLKTGIGSTVILSCALTGSPEFTIRWYRNTELVLPGEAISIRGLSNETLLISSAQKSHSGAYQCFATRKAQTAQ | ||||||
Domain | 408-501 | Ig-like C2-type 5 | ||||
Sequence: PRIVSSFSEKVVNPGEQFSLMCAAKGAPPPTVTWALDDEPVVRDGSHRTNQYTMSDGTTISHMNVTGPQIRDGGVYRCTARNSVGSAEYQARIN | ||||||
Domain | 506-586 | Ig-like C2-type 6 | ||||
Sequence: PSIRAMRNITAVAGRDTLINCRVIGYPYYSIKWYKDALLLPDNHRQVVFENGTLKLTDVQKGMDEGEYLCSVLIQPQLSIS | ||||||
Domain | 596-685 | Ig-like C2-type 7 | ||||
Sequence: PPLIQPFEFPPASIGQLLYIPCVVSSGDMPIRITWRKDGQVIISGSGVTIESKEFMSSLQISSVSLKHNGNYTCIASNAAATVSRERQLI | ||||||
Domain | 690-784 | Ig-like C2-type 8 | ||||
Sequence: PRFVVQPNNQDGIYGKAGVLNCSVDGYPPPKVMWKHAKGSGNPQQYHPVPLTGRIQILPNSSLLIRHVLEEDIGYYLCQASNGVGTDISKAMFLT | ||||||
Domain | 788-885 | Ig-like C2-type 9 | ||||
Sequence: PAMITSHPNTTIAIKGHPKELNCTARGERPIIIRWEKGDTVIDPDRVMRYAIATKDNGDEVVSTLKLKPADRGDSVFFSCHAINSYGEDRGLIQLTVQ | ||||||
Domain | 887-984 | Fibronectin type-III 1 | ||||
Sequence: PPDPPELEIREVKARSMNLRWTQRFDGNSIITGFDIEYKNKSDSWDFKQSTRNISPTINQANIVDLHPASVYSIRMYSFNKIGRSEPSKELTISTEEA | ||||||
Domain | 989-1088 | Fibronectin type-III 2 | ||||
Sequence: PPMDVTLQPVTSQSIQVTWKAPKKELQNGVIRGYQIGYRENSPGSNGQYSIVEMKATGDSEVYTLDNLKKFAQYGVVVQAFNRAGTGPSSSEINATTLED | ||||||
Domain | 1093-1189 | Fibronectin type-III 3 | ||||
Sequence: PPENVRALSITSDVAVISWSEPPRSTLNGVLKGYRVIFWSLYVDGEWGEMQNVTTTRERVELRGMEKFTNYSVQVLAYTQAGDGVRSSVLYIQTKED | ||||||
Domain | 1193-1288 | Fibronectin type-III 4 | ||||
Sequence: PPAGIKAVPSSASSVVVSWLPPTKPNGVIRKYTIFCSSPGSGQPAPSEYETSPEQLFYRIAHLNRGQQYLLWVAAVTSAGRGNSSEKVTIEPAGKA | ||||||
Domain | 1278-1377 | Ig-like C2-type 10 | ||||
Sequence: EKVTIEPAGKAPAKIISFGGTVTTPWMKDVRLPCNSVGDPAPAVKWTKDSEDSAIPVSLDGHRLIHTNGTLLLRAVKAEDSGYYTCTATNTGGFDTIIVN | ||||||
Domain | 1383-1477 | Fibronectin type-III 5 | ||||
Sequence: PPDQPRLTVSKTSASSITLTWIPGDNGGSSIRGFVLQYSVDNSEEWKDVFISSSERSFKLDSLKCGTWYKVKLAAKNSVGSGRISEIIEAKTHGR | ||||||
Domain | 1478-1578 | Fibronectin type-III 6 | ||||
Sequence: EPSFSKDQHLFTHINSTHARLNLQGWNNGGCPITAIVLEYRPKGTWAWQGVRANSSTEVFLTELREATWYELRMRACNSAGCGNETAQFATLDYDGSTIPP | ||||||
Region | 1716-1741 | Disordered | ||||
Sequence: LIDMSDIRPGTNPVSRKNVKSAHSTR | ||||||
Compositional bias | 1726-1741 | Polar residues | ||||
Sequence: TNPVSRKNVKSAHSTR | ||||||
Region | 1773-1803 | Disordered | ||||
Sequence: HGVTVTESDSYSASLSQDTDKGRNSMVSTES | ||||||
Region | 1840-1862 | Disordered | ||||
Sequence: SSDQMTTGTNENADSMTSMSTPS | ||||||
Region | 1974-2053 | Disordered | ||||
Sequence: LAMPAPPAGTAPPAPGPTPSEPSAAPSAAPPAPSTEPPRAGGPHTKMGGSRDSLLEMSTPGVGRSQKQGAGAYSKSYTLV | ||||||
Compositional bias | 1979-2011 | Pro residues | ||||
Sequence: PPAGTAPPAPGPTPSEPSAAPSAAPPAPSTEPP | ||||||
Compositional bias | 2032-2053 | Polar residues | ||||
Sequence: TPGVGRSQKQGAGAYSKSYTLV |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length2,053
- Mass (Da)224,240
- Last updated2010-03-23 v2
- Checksum0C0806C47D7ADCD6
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A1L1SQZ7 | A0A1L1SQZ7_MOUSE | Dscaml1 | 286 | ||
A0A1L1SQ53 | A0A1L1SQ53_MOUSE | Dscaml1 | 34 | ||
E9QPR7 | E9QPR7_MOUSE | Dscaml1 | 2111 |
Sequence caution
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1726-1741 | Polar residues | ||||
Sequence: TNPVSRKNVKSAHSTR | ||||||
Compositional bias | 1979-2011 | Pro residues | ||||
Sequence: PPAGTAPPAPGPTPSEPSAAPSAAPPAPSTEPP | ||||||
Compositional bias | 2032-2053 | Polar residues | ||||
Sequence: TPGVGRSQKQGAGAYSKSYTLV |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC119237 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC159893 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC174644 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC126804 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC096527 EMBL· GenBank· DDBJ | AAH96527.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |