P22648 · FAS2_SCHAM
- ProteinFasciclin-2
- GeneFAS2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids898 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Neuronal recognition molecule. Involved in a pathway recognition for axons during the development of nerve fascicles.
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 | membrane | |
Biological Process | anatomical structure morphogenesis | |
Biological Process | cell adhesion | |
Biological Process | cell differentiation | |
Biological Process | nervous system development |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameFasciclin-2
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Polyneoptera > Orthoptera > Caelifera > Acrididea > Acridomorpha > Acridoidea > Acrididae > Cyrtacanthacridinae > Schistocerca
Accessions
- Primary accessionP22648
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Single-pass type I membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 23-764 | Extracellular | ||||
Sequence: QSAGLEILPNSENQTKPIGRSMLLTCKPNVTNKNLISQLRWTDPSGREVPFKNPTLLKPHIFVDWLPPPGEKVLTLMIPELREADTGTYTCSALYSNTKQLSKSVHVRTIMPITWDDAPEEQYPTVNETFKIRCRVSANPPAIVNWMRDGHIVETGDRYVVEQDGLTILNVTEMDDGTYTCRAIVIATGEMALRPIRVEVHTPPQMSGALPPKLEAVEGTDFTAKCAASGKPVPRYTWIRVDTARDLTKDGDRVSADVLLGELRIREVRPEDAANYSCTAKNAAGTATATVEVTVVVRPRIGRFDNISVASGKDSEAVLECHATGSPLPAVTFRKLSNPNRYINGIQPTEDRITVDGVDSPDGRTRIGKLIISNVLRSDDGLYECIATNKGGEVKKNGHLMVEFKPSFADTPQKEVWGWEQHAVNLTCLAHSIPNATISWHFNGADLFRGREGQELQQTGYTLFGSGPRSTLQVIPFNRKMYGNYKCTATNKHGTAVHEIMLREARVPSAVLQVKMDVMTATTVTFKFFGPGNDGGLPTKNYAVQYKQDSQGWEDALNRTWPVDSPYILENLKPQTRYNFRFAAQNEVGFGPWSSQQTHTTPRISAPEEPRLLGLPLSATSGTENEVVVSPYPNRYELRWQVPADNGEPITHYSVKSCPVEKYDTEWRLLPYPCQEHKLEGQATTFQLESLQPDTHYKVEVRATNAIGNSVPGQIIVRTVKDPSQMPGVANVEDGSEGQMSS | ||||||
Transmembrane | 765-782 | Helical | ||||
Sequence: AAIVVLVVAALLLALLVV | ||||||
Topological domain | 783-898 | Cytoplasmic | ||||
Sequence: DLVCCLVWRGGLIAALCHRCCSAAKTDDSDAKIASLYSWRFPLPYCSNKEDPAMLAPAKMQQATVKIPVIEEKEPLRDGKEPVPIIKERVKRETAVDFDVKKSVSRTSFVGKDSAV |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-22 | |||||
Sequence: MRTVACAVLLACFMGCLAGAWA | ||||||
Chain | PRO_0000014759 | 23-898 | Fasciclin-2 | |||
Sequence: QSAGLEILPNSENQTKPIGRSMLLTCKPNVTNKNLISQLRWTDPSGREVPFKNPTLLKPHIFVDWLPPPGEKVLTLMIPELREADTGTYTCSALYSNTKQLSKSVHVRTIMPITWDDAPEEQYPTVNETFKIRCRVSANPPAIVNWMRDGHIVETGDRYVVEQDGLTILNVTEMDDGTYTCRAIVIATGEMALRPIRVEVHTPPQMSGALPPKLEAVEGTDFTAKCAASGKPVPRYTWIRVDTARDLTKDGDRVSADVLLGELRIREVRPEDAANYSCTAKNAAGTATATVEVTVVVRPRIGRFDNISVASGKDSEAVLECHATGSPLPAVTFRKLSNPNRYINGIQPTEDRITVDGVDSPDGRTRIGKLIISNVLRSDDGLYECIATNKGGEVKKNGHLMVEFKPSFADTPQKEVWGWEQHAVNLTCLAHSIPNATISWHFNGADLFRGREGQELQQTGYTLFGSGPRSTLQVIPFNRKMYGNYKCTATNKHGTAVHEIMLREARVPSAVLQVKMDVMTATTVTFKFFGPGNDGGLPTKNYAVQYKQDSQGWEDALNRTWPVDSPYILENLKPQTRYNFRFAAQNEVGFGPWSSQQTHTTPRISAPEEPRLLGLPLSATSGTENEVVVSPYPNRYELRWQVPADNGEPITHYSVKSCPVEKYDTEWRLLPYPCQEHKLEGQATTFQLESLQPDTHYKVEVRATNAIGNSVPGQIIVRTVKDPSQMPGVANVEDGSEGQMSSAAIVVLVVAALLLALLVVDLVCCLVWRGGLIAALCHRCCSAAKTDDSDAKIASLYSWRFPLPYCSNKEDPAMLAPAKMQQATVKIPVIEEKEPLRDGKEPVPIIKERVKRETAVDFDVKKSVSRTSFVGKDSAV | ||||||
Glycosylation | 35 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 48↔113 | |||||
Sequence: CKPNVTNKNLISQLRWTDPSGREVPFKNPTLLKPHIFVDWLPPPGEKVLTLMIPELREADTGTYTC | ||||||
Glycosylation | 51 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 149 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 156↔203 | |||||
Sequence: CRVSANPPAIVNWMRDGHIVETGDRYVVEQDGLTILNVTEMDDGTYTC | ||||||
Glycosylation | 192 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 248↔300 | |||||
Sequence: CAASGKPVPRYTWIRVDTARDLTKDGDRVSADVLLGELRIREVRPEDAANYSC | ||||||
Glycosylation | 297 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 328 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 343↔407 | |||||
Sequence: CHATGSPLPAVTFRKLSNPNRYINGIQPTEDRITVDGVDSPDGRTRIGKLIISNVLRSDDGLYEC | ||||||
Glycosylation | 447 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 450↔509 | |||||
Sequence: CLAHSIPNATISWHFNGADLFRGREGQELQQTGYTLFGSGPRSTLQVIPFNRKMYGNYKC | ||||||
Glycosylation | 457 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 580 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
PTM databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 31-124 | Ig-like C2-type 1 | ||||
Sequence: PNSENQTKPIGRSMLLTCKPNVTNKNLISQLRWTDPSGREVPFKNPTLLKPHIFVDWLPPPGEKVLTLMIPELREADTGTYTCSALYSNTKQLS | ||||||
Domain | 134-219 | Ig-like C2-type 2 | ||||
Sequence: PITWDDAPEEQYPTVNETFKIRCRVSANPPAIVNWMRDGHIVETGDRYVVEQDGLTILNVTEMDDGTYTCRAIVIATGEMALRPIR | ||||||
Domain | 226-316 | Ig-like C2-type 3 | ||||
Sequence: PQMSGALPPKLEAVEGTDFTAKCAASGKPVPRYTWIRVDTARDLTKDGDRVSADVLLGELRIREVRPEDAANYSCTAKNAAGTATATVEVT | ||||||
Domain | 321-423 | Ig-like C2-type 4 | ||||
Sequence: PRIGRFDNISVASGKDSEAVLECHATGSPLPAVTFRKLSNPNRYINGIQPTEDRITVDGVDSPDGRTRIGKLIISNVLRSDDGLYECIATNKGGEVKKNGHLM | ||||||
Domain | 428-525 | Ig-like C2-type 5 | ||||
Sequence: PSFADTPQKEVWGWEQHAVNLTCLAHSIPNATISWHFNGADLFRGREGQELQQTGYTLFGSGPRSTLQVIPFNRKMYGNYKCTATNKHGTAVHEIMLR | ||||||
Domain | 532-626 | Fibronectin type-III 1 | ||||
Sequence: AVLQVKMDVMTATTVTFKFFGPGNDGGLPTKNYAVQYKQDSQGWEDALNRTWPVDSPYILENLKPQTRYNFRFAAQNEVGFGPWSSQQTHTTPRI | ||||||
Domain | 644-745 | Fibronectin type-III 2 | ||||
Sequence: GTENEVVVSPYPNRYELRWQVPADNGEPITHYSVKSCPVEKYDTEWRLLPYPCQEHKLEGQATTFQLESLQPDTHYKVEVRATNAIGNSVPGQIIVRTVKDP |
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length898
- Mass (Da)99,065
- Last updated1994-02-01 v2
- Checksum07989EA4F39604AC
Keywords
- Technical term