Q9GL25 · ESPB1_CANLF
- ProteinEpididymal sperm-binding protein 1
- GeneELSPBP1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids245 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Binds to spermatozoa upon ejaculation and may play a role in sperm capacitation. Has phosphorylcholine-binding activity (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 | cell surface | |
Cellular Component | extracellular region | |
Molecular Function | heparin binding | |
Biological Process | single fertilization | |
Biological Process | sperm capacitation |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended nameEpididymal sperm-binding protein 1
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Carnivora > Caniformia > Canidae > Canis
Accessions
- Primary accessionQ9GL25
- Secondary accessions
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-23 | |||||
Sequence: MNPWSSYLLGWTTFLLYFYETSG | ||||||
Chain | PRO_0000308248 | 24-245 | Epididymal sperm-binding protein 1 | |||
Sequence: KIPNLSSLGKHEFTKPWISIKEDQKDSCVFPFVYKGSSYFSCIKTNSFSPWCATRAVYNGQWKFCMADDYPRCIFPFIFRGKSHNSCITEGSFLRRLWCSVTSSFDENQQWKYCETNEYGGNSFSKPCIFPSIFRNSTIFECMEDENNKLWCPTTENMDEDGKWSLCADTRISSLVPGFPCHFPFSYKNKNYYNCIGKGTKENLTWCATSYNYDRDHTWVYC | ||||||
Disulfide bond | 51↔75 | |||||
Sequence: CVFPFVYKGSSYFSCIKTNSFSPWC | ||||||
Disulfide bond | 65↔88 | |||||
Sequence: CIKTNSFSPWCATRAVYNGQWKFC | ||||||
Disulfide bond | 96↔122 | |||||
Sequence: CIFPFIFRGKSHNSCITEGSFLRRLWC | ||||||
Disulfide bond | 110↔137 | |||||
Sequence: CITEGSFLRRLWCSVTSSFDENQQWKYC | ||||||
Disulfide bond | 151↔175 | |||||
Sequence: CIFPSIFRNSTIFECMEDENNKLWC | ||||||
Disulfide bond | 165↔190 | |||||
Sequence: CMEDENNKLWCPTTENMDEDGKWSLC | ||||||
Disulfide bond | 204↔230 | |||||
Sequence: CHFPFSYKNKNYYNCIGKGTKENLTWC | ||||||
Disulfide bond | 218↔245 | |||||
Sequence: CIGKGTKENLTWCATSYNYDRDHTWVYC |
Keywords
- PTM
Proteomic databases
Expression
Tissue specificity
Detected in epididymal duct epithelium, cauda epididymidal fluid and on sperm membrane (at protein level).
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 46-90 | Fibronectin type-II 1 | ||||
Sequence: DQKDSCVFPFVYKGSSYFSCIKTNSFSPWCATRAVYNGQWKFCMA | ||||||
Domain | 91-139 | Fibronectin type-II 2 | ||||
Sequence: DDYPRCIFPFIFRGKSHNSCITEGSFLRRLWCSVTSSFDENQQWKYCET | ||||||
Domain | 146-192 | Fibronectin type-II 3 | ||||
Sequence: SFSKPCIFPSIFRNSTIFECMEDENNKLWCPTTENMDEDGKWSLCAD | ||||||
Domain | 199-245 | Fibronectin type-II 4 | ||||
Sequence: VPGFPCHFPFSYKNKNYYNCIGKGTKENLTWCATSYNYDRDHTWVYC |
Sequence similarities
Belongs to the seminal plasma protein family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length245
- Mass (Da)28,746
- Last updated2001-03-01 v1
- ChecksumDBDF6A6B540D5010
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ278477 EMBL· GenBank· DDBJ | CAC14266.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ278477 EMBL· GenBank· DDBJ | CAC14265.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |