P23805 · CONG_BOVIN
- ProteinConglutinin
- GeneCGN1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids371 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Calcium-dependent lectin-like protein which binds to a yeast cell wall extract and immune complexes through the complement component (C3bi). It is capable of binding non-reducing terminal N-acetylglucosamine, mannose, and fucose residues.
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 | collagen trimer | |
Cellular Component | collagen-containing extracellular matrix | |
Cellular Component | extracellular space | |
Molecular Function | D-mannose binding | |
Molecular Function | extracellular matrix structural constituent conferring tensile strength | |
Biological Process | extracellular matrix organization |
Keywords
- Ligand
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameConglutinin
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos
Accessions
- Primary accessionP23805
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for signal, chain, modified residue, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MLLLPLSVLLLLTQPWRSLG | ||||||
Chain | PRO_0000017370 | 21-371 | Conglutinin | |||
Sequence: AEMTTFSQKILANACTLVMCSPLESGLPGHDGQDGRECPHGEKGDPGSPGPAGRAGRPGWVGPIGPKGDNGFVGEPGPKGDTGPRGPPGMPGPAGREGPSGKQGSMGPPGTPGPKGETGPKGGVGAPGIQGFPGPSGLKGEKGAPGETGAPGRAGVTGPSGAIGPQGPSGARGPPGLKGDRGDPGETGAKGESGLAEVNALKQRVTILDGHLRRFQNAFSQYKKAVLFPDGQAVGEKIFKTAGAVKSYSDAEQLCREAKGQLASPRSSAENEAVTQMVRAQEKNAYLSMNDISTEGRFTYPTGEILVYSNWADGEPNNSDEGQPENCVEIFPDGKWNDVPCSKQLLVICEF | ||||||
Modified residue | 63 | 5-hydroxylysine | ||||
Sequence: K | ||||||
Modified residue | 78 | 4-hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 87 | 5-hydroxylysine | ||||
Sequence: K | ||||||
Modified residue | 96 | 4-hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 99 | 5-hydroxylysine | ||||
Sequence: K | ||||||
Modified residue | 108 | 4-hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 111 | 4-hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 129 | 4-hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 132 | 4-hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 135 | 5-hydroxylysine | ||||
Sequence: K | ||||||
Modified residue | 141 | 5-hydroxylysine | ||||
Sequence: K | ||||||
Modified residue | 147 | 4-hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 153 | 4-hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 159 | 5-hydroxylysine | ||||
Sequence: K | ||||||
Modified residue | 162 | 5-hydroxylysine | ||||
Sequence: K | ||||||
Modified residue | 171 | 4-hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 195 | 4-hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 198 | 5-hydroxylysine | ||||
Sequence: K | ||||||
Disulfide bond | 275↔369 | |||||
Sequence: CREAKGQLASPRSSAENEAVTQMVRAQEKNAYLSMNDISTEGRFTYPTGEILVYSNWADGEPNNSDEGQPENCVEIFPDGKWNDVPCSKQLLVIC | ||||||
Glycosylation | 337 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 347↔361 | |||||
Sequence: CVEIFPDGKWNDVPC |
Post-translational modification
The hydroxylysines may be O-glycosylated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Structure
Family & Domains
Features
Showing features for domain, region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 46-216 | Collagen-like | ||||
Sequence: GLPGHDGQDGRECPHGEKGDPGSPGPAGRAGRPGWVGPIGPKGDNGFVGEPGPKGDTGPRGPPGMPGPAGREGPSGKQGSMGPPGTPGPKGETGPKGGVGAPGIQGFPGPSGLKGEKGAPGETGAPGRAGVTGPSGAIGPQGPSGARGPPGLKGDRGDPGETGAKGESGLA | ||||||
Region | 47-215 | Disordered | ||||
Sequence: LPGHDGQDGRECPHGEKGDPGSPGPAGRAGRPGWVGPIGPKGDNGFVGEPGPKGDTGPRGPPGMPGPAGREGPSGKQGSMGPPGTPGPKGETGPKGGVGAPGIQGFPGPSGLKGEKGAPGETGAPGRAGVTGPSGAIGPQGPSGARGPPGLKGDRGDPGETGAKGESGL | ||||||
Motif | 201-203 | Cell attachment site | ||||
Sequence: RGD | ||||||
Domain | 273-371 | C-type lectin | ||||
Sequence: QLCREAKGQLASPRSSAENEAVTQMVRAQEKNAYLSMNDISTEGRFTYPTGEILVYSNWADGEPNNSDEGQPENCVEIFPDGKWNDVPCSKQLLVICEF |
Sequence similarities
Belongs to the SFTPD family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length371
- Mass (Da)37,995
- Last updated1994-02-01 v2
- Checksum867BB41992544B1F
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 173 | in Ref. 2 and 3 | ||||
Sequence: R → H | ||||||
Sequence conflict | 210 | in Ref. 7; AA sequence | ||||
Sequence: K → S | ||||||
Sequence conflict | 218 | in Ref. 2; CAA50665 | ||||
Sequence: V → A | ||||||
Sequence conflict | 272 | in Ref. 2; CAA50665 | ||||
Sequence: E → V |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D14085 EMBL· GenBank· DDBJ | BAA03170.1 EMBL· GenBank· DDBJ | mRNA | ||
X71774 EMBL· GenBank· DDBJ | CAA50665.1 EMBL· GenBank· DDBJ | mRNA | ||
L18871 EMBL· GenBank· DDBJ | AAA20126.1 EMBL· GenBank· DDBJ | mRNA | ||
U06860 EMBL· GenBank· DDBJ | AAB60624.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U06854 EMBL· GenBank· DDBJ | AAB60624.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U06855 EMBL· GenBank· DDBJ | AAB60624.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U06856 EMBL· GenBank· DDBJ | AAB60624.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U06857 EMBL· GenBank· DDBJ | AAB60624.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U06858 EMBL· GenBank· DDBJ | AAB60624.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U06859 EMBL· GenBank· DDBJ | AAB60624.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
D25302 EMBL· GenBank· DDBJ | BAA04983.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT021850 EMBL· GenBank· DDBJ | AAX46697.1 EMBL· GenBank· DDBJ | mRNA |