V9KDA3 · V9KDA3_CALMI
- ProteinAmyloid-beta A4 protein
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids753 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
function
Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis.
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 | cell surface | |
Cellular Component | early endosome | |
Cellular Component | Golgi apparatus | |
Cellular Component | Golgi-associated vesicle | |
Cellular Component | membrane raft | |
Cellular Component | plasma membrane | |
Molecular Function | heparin binding | |
Molecular Function | serine-type endopeptidase inhibitor activity | |
Molecular Function | signaling receptor activator activity | |
Molecular Function | signaling receptor binding | |
Molecular Function | transition metal ion binding | |
Biological Process | axonogenesis | |
Biological Process | central nervous system development | |
Biological Process | negative regulation of peptidase activity |
Keywords
- Molecular function
- Ligand
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameAmyloid-beta A4 protein
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Chondrichthyes > Holocephali > Chimaeriformes > Callorhinchidae > Callorhinchus
Accessions
- Primary accessionV9KDA3
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
Membrane ; Single-pass type I membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 684-706 | Helical | ||||
Sequence: AIIGLMVGGVVIATVIVITLVML |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MFLQPAARLLLLSAIGTVTV | ||||||
Chain | PRO_5004778687 | 21-753 | Amyloid-beta A4 protein | |||
Sequence: SPSALTALEVPTDGGTGLLAAEPQIAMFCDKLNMHMNVQTGKWISDPSGTNSCFGTKEGILQYCQEVYPDLQITNVVEANQPVTIQNWCKKGRKQCKGHPHIVIPYRCLVGEFVSDALLVPDKCKFLHREKMDTCENHLYWHTVAKEACGDKTMNLKDYGMLLPCGIDQFRGVEFVCCPISEENEKVDSVDVDEEDSYIWWGGADAEYSDGGDKVIEEEPMDEEEEVDIEDDDDEEEDEDDEDDDQYEDPTEHTTSSTTTTTEAIEEVVREVCSEQAETGPCRAMIPRWYFDIGEGKCAQFIYGGCGGNRNNFDSEEYCLSVCSSVIPATAASTPDAIDQYLETPGDENEHAYFQKAKERQEARHRERMSQIMREWEEAERQARNLHKADKKAVIQRFQEMVESLEQEAASERQQLVETHMARVEAMLNDRRRIALENYLAALQADPPRPRHVLNALKKYIRAEQKDRQHTLKHFEHVRMVDPKKAAQIKSQVMTHLRVIDERMNQSLSLLYKVPAVAEEIQDEVDELLQKEQSYIDDMVANSVSDTRVSYGNDALVPSLSETKTTIELLPDQGEFTLDDLQPLHPFVVDSIPVNTENEVEPVDARPAADRGLTTRPGSGLTGIKTQEIAEVKMETKFRQDSGYEVHHQKLVFFPEDVGSNKGAIIGLMVGGVVIATVIVITLVMLKKKQYTSIHHGVIEVDAAVTPEERHLSKMQQNGYENPTYKFFEQMQN | ||||||
Disulfide bond | 84↔128 | |||||
Sequence: CQEVYPDLQITNVVEANQPVTIQNWCKKGRKQCKGHPHIVIPYRC | ||||||
Disulfide bond | 109↔116 | |||||
Sequence: CKKGRKQC | ||||||
Disulfide bond | 144↔198 | |||||
Sequence: CKFLHREKMDTCENHLYWHTVAKEACGDKTMNLKDYGMLLPCGIDQFRGVEFVCC | ||||||
Disulfide bond | 155↔185 | |||||
Sequence: CENHLYWHTVAKEACGDKTMNLKDYGMLLPC | ||||||
Disulfide bond | 169↔197 | |||||
Sequence: CGDKTMNLKDYGMLLPCGIDQFRGVEFVC |
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 39-134 | GFLD subdomain | ||||
Sequence: LAAEPQIAMFCDKLNMHMNVQTGKWISDPSGTNSCFGTKEGILQYCQEVYPDLQITNVVEANQPVTIQNWCKKGRKQCKGHPHIVIPYRCLVGEFV | ||||||
Domain | 39-200 | E1 | ||||
Sequence: LAAEPQIAMFCDKLNMHMNVQTGKWISDPSGTNSCFGTKEGILQYCQEVYPDLQITNVVEANQPVTIQNWCKKGRKQCKGHPHIVIPYRCLVGEFVSDALLVPDKCKFLHREKMDTCENHLYWHTVAKEACGDKTMNLKDYGMLLPCGIDQFRGVEFVCCPI | ||||||
Region | 142-200 | CuBD subdomain | ||||
Sequence: DKCKFLHREKMDTCENHLYWHTVAKEACGDKTMNLKDYGMLLPCGIDQFRGVEFVCCPI | ||||||
Compositional bias | 237-269 | Acidic residues | ||||
Sequence: EEEPMDEEEEVDIEDDDDEEEDEDDEDDDQYED | ||||||
Region | 237-283 | Disordered | ||||
Sequence: EEEPMDEEEEVDIEDDDDEEEDEDDEDDDQYEDPTEHTTSSTTTTTE | ||||||
Domain | 293-343 | BPTI/Kunitz inhibitor | ||||
Sequence: CSEQAETGPCRAMIPRWYFDIGEGKCAQFIYGGCGGNRNNFDSEEYCLSVC | ||||||
Domain | 357-548 | E2 | ||||
Sequence: AIDQYLETPGDENEHAYFQKAKERQEARHRERMSQIMREWEEAERQARNLHKADKKAVIQRFQEMVESLEQEAASERQQLVETHMARVEAMLNDRRRIALENYLAALQADPPRPRHVLNALKKYIRAEQKDRQHTLKHFEHVRMVDPKKAAQIKSQVMTHLRVIDERMNQSLSLLYKVPAVAEEIQDEVDEL | ||||||
Coiled coil | 382-442 | |||||
Sequence: EARHRERMSQIMREWEEAERQARNLHKADKKAVIQRFQEMVESLEQEAASERQQLVETHMA |
Sequence similarities
Belongs to the APP family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length753
- Mass (Da)85,057
- Last updated2014-03-19 v1
- ChecksumA31797CD026019F0
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 237-269 | Acidic residues | ||||
Sequence: EEEPMDEEEEVDIEDDDDEEEDEDDEDDDQYED |