Q91XX6 · Q91XX6_MOUSE
- ProteinProtocadherin gamma B4
- GenePcdhgb4
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids912 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score2/5
Function
function
Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 39 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 40 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 91 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 93 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 125 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 126 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 127 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 128 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 129 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 144 | Ca2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 159 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 161 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 165 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 201 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 203 | Ca2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 216 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 234 | Ca2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 235 | Ca2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 236 | Ca2+ 6 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 237 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 238 | Ca2+ 6 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 253 | Ca2+ 7 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 268 | Ca2+ 6 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 270 | Ca2+ 6 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 274 | Ca2+ 6 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 306 | Ca2+ 7 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 308 | Ca2+ 8 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 321 | Ca2+ 6 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 337 | Ca2+ 8 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 339 | Ca2+ 9 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 340 | Ca2+ 7 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 341 | Ca2+ 9 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 356 | Ca2+ 10 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 371 | Ca2+ 9 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 373 | Ca2+ 9 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 377 | Ca2+ 9 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 409 | Ca2+ 10 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 411 | Ca2+ 11 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 424 | Ca2+ 9 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 442 | Ca2+ 11 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 444 | Ca2+ 12 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 445 | Ca2+ 10 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 446 | Ca2+ 13 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 461 | Ca2+ 14 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 476 | Ca2+ 13 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 478 | Ca2+ 13 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 482 | Ca2+ 13 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 519 | Ca2+ 14 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 521 | Ca2+ 14 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 534 | Ca2+ 13 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 552 | Ca2+ 15 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 553 | Ca2+ 15 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 554 | Ca2+ 16 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 555 | Ca2+ 15 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 556 | Ca2+ 16 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 593 | Ca2+ 16 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 595 | Ca2+ 16 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 599 | Ca2+ 16 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 646 | Ca2+ 16 (UniProtKB | ChEBI) | ||||
Sequence: D |
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 | |
Cellular Component | plasma membrane | |
Molecular Function | calcium ion binding | |
Biological Process | homophilic cell adhesion via plasma membrane adhesion molecules |
Keywords
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Submitted 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 accessionQ91XX6
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 688-711 | Helical | ||||
Sequence: FYLVVALALISVLFLLAVILAIAL |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-30 | |||||
Sequence: MREGTAERGRGQRRPMLLPFLLPLFCPTLS | ||||||
Chain | PRO_5015099494 | 31-912 | ||||
Sequence: EQIRYKIPEEMPTGSVVGNLAKDLGFSVQELPTRKLRISSEKPYFSVSSESGELLVSSRLDREQICGKKLMCALEFEAVAENPLNFYHLSVELEDINDHTPKFAHTSFELQISESSKPGTRFILGSAHDADIGTNSLQNYQLSPNDHFSLVNKEKSDGSKYPEMILKTALDREKQKLYHLTLTALDFGHPPLNSTAQIQVLVTDANDNPPVFSQDIYRVSLPENVYPGTTVLRVVATDQDEGVNSEITFSFSEAGQVTQFNLDSNTGEITTLHTLDFEEVKEYSLVLEAKDGGGMIAQCTVEIEVLDENDNVPEVLFQSLPDLIMEDAEPGTYIALLKTRDKDSGRNGEVICKLEGGAPFKILTSSGNTYKLVTDGVLDREQNPEYNITIRATDKGDPPLSSSSSVTLHIGDVNDNAPVFTKVSYLVHVAENNPPGASIAQVSASDPDLGANGQVTYYIIASDLEPESLWSYVTINAQSGVLFAQRAFDHEQLRSFQLTLQARDHGSPTLSANVSMRLLVGDRNDNAPRVLYPTLEPDGSALFDMVPRSAEPGYLVTKVVAVDADSGHNAWLSYHVLQASDPGLFSLGLRTGEVRTARALGDRDSARQRLLVAVRDGGQPPLSATATLHLIFADSLQEVLPDLSDDPLPPDPQSELQFYLVVALALISVLFLLAVILAIALRLRHSSSRKAWGCFQSEVVVPPNYSEGTLPYSYNLCAAEFNSLTCNDQLKSGQDLQFADSAGALFPLCNSNESTSHQQAPPNTDWRFSQAQRPGTSGSQNGDETGTWPNNQFDTEMLQAMILASASEAADGSSTLGGGAGTMGLSARYGPQFTLQHVPDYRQNVYIPGSNATLTNAAGKRDGKAPAGGNGNKKKSGKKEKK | ||||||
Disulfide bond | 96↔102 | |||||
Sequence: CGKKLMC | ||||||
Glycosylation | 223 | N-acetyl-D-glucosamine 1 | ||||
Sequence: N | ||||||
Glycosylation | 223 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 417 | N-acetyl-D-glucosamine 2 | ||||
Sequence: N | ||||||
Glycosylation | 417 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 468 | Mannose 1 | ||||
Sequence: S | ||||||
Glycosylation | 468 | O-linked (Man...) serine | ||||
Sequence: S | ||||||
Glycosylation | 645 | Mannose 2 | ||||
Sequence: R | ||||||
Glycosylation | 653 | Mannose 2 | ||||
Sequence: S | ||||||
Glycosylation | 653 | O-linked (Man...) serine | ||||
Sequence: S |
Expression
Gene expression databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 29-133 | Cadherin | ||||
Sequence: LSEQIRYKIPEEMPTGSVVGNLAKDLGFSVQELPTRKLRISSEKPYFSVSSESGELLVSSRLDREQICGKKLMCALEFEAVAENPLNFYHLSVELEDINDHTPKF | ||||||
Domain | 134-242 | Cadherin | ||||
Sequence: AHTSFELQISESSKPGTRFILGSAHDADIGTNSLQNYQLSPNDHFSLVNKEKSDGSKYPEMILKTALDREKQKLYHLTLTALDFGHPPLNSTAQIQVLVTDANDNPPVF | ||||||
Domain | 243-345 | Cadherin | ||||
Sequence: SQDIYRVSLPENVYPGTTVLRVVATDQDEGVNSEITFSFSEAGQVTQFNLDSNTGEITTLHTLDFEEVKEYSLVLEAKDGGGMIAQCTVEIEVLDENDNVPEV | ||||||
Domain | 354-450 | Cadherin | ||||
Sequence: IMEDAEPGTYIALLKTRDKDSGRNGEVICKLEGGAPFKILTSSGNTYKLVTDGVLDREQNPEYNITIRATDKGDPPLSSSSSVTLHIGDVNDNAPVF | ||||||
Domain | 451-560 | Cadherin | ||||
Sequence: TKVSYLVHVAENNPPGASIAQVSASDPDLGANGQVTYYIIASDLEPESLWSYVTINAQSGVLFAQRAFDHEQLRSFQLTLQARDHGSPTLSANVSMRLLVGDRNDNAPRV | ||||||
Domain | 576-673 | Cadherin | ||||
Sequence: VPRSAEPGYLVTKVVAVDADSGHNAWLSYHVLQASDPGLFSLGLRTGEVRTARALGDRDSARQRLLVAVRDGGQPPLSATATLHLIFADSLQEVLPDL | ||||||
Region | 782-821 | Disordered | ||||
Sequence: NESTSHQQAPPNTDWRFSQAQRPGTSGSQNGDETGTWPNN | ||||||
Region | 882-912 | Disordered | ||||
Sequence: ATLTNAAGKRDGKAPAGGNGNKKKSGKKEKK |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length912
- Mass (Da)99,243
- Last updated2001-12-01 v1
- ChecksumBFD952F754578C68
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BC138701 EMBL· GenBank· DDBJ | AAI38702.1 EMBL· GenBank· DDBJ | mRNA | ||
AY013806 EMBL· GenBank· DDBJ | AAK26095.1 EMBL· GenBank· DDBJ | mRNA |