Reviewed,
UniProtKB/Swiss-Prot P51779 (CFAD_PIG)
Last modified
June 16, 2009.
Version 58.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Complement factor D EC=3.4.21.46 Alternative name(s): C3 convertase activator Properdin factor D Adipsin | ||||
| Gene names |
| ||||
| Organism | Sus scrofa (Pig) | ||||
| Taxonomic identifier | 9823 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus |
Protein attributes
| Sequence length | 259 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Factor D cleaves factor B when the latter is complexed with factor C3b, activating the C3bbb complex, which then becomes the C3 convertase of the alternate pathway. Its function is homologous to that of C1s in the classical pathway By similarity. |
| Catalytic activity | Selective cleavage of Arg-|-Lys bond in complement factor B when in complex with complement subcomponent C3b or with cobra venom factor. |
| Subcellular location | |
| Sequence similarities | Belongs to the peptidase S1 family. Contains 1 peptidase S1 domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Complement alternate pathway Immune response Innate immunity |
| Cellular component | Secreted |
| Domain | Signal |
| Molecular function | Hydrolase Protease Serine protease |
| PTM | Disulfide bond Zymogen |
| Gene Ontology (GO) | |
| Biological process | complement activation, alternative pathway Inferred from electronic annotation. Source: UniProtKB-KW proteolysisInferred from electronic annotation. Source: InterPro |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 21 | 21 | Potential | ||||||||
| Propeptide | 22 – 26 | 5 | Activation peptide Potential | PRO_0000027564 | |||||||
| Chain | 27 – 259 | 233 | Complement factor D | PRO_0000027565 | |||||||
Regions | |||||||||||
| Domain | 27 – 254 | 228 | Peptidase S1 | ||||||||
Sites | |||||||||||
| Active site | 67 | 1 | Charge relay system | ||||||||
| Active site | 115 | 1 | Charge relay system | ||||||||
| Active site | 209 | 1 | Charge relay system | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 52 ↔ 68 | By similarity | |||||||||
| Disulfide bond | 149 ↔ 215 | By similarity | |||||||||
| Disulfide bond | 180 ↔ 196 | By similarity | |||||||||
| Disulfide bond | 205 ↔ 230 | By similarity | |||||||||
Sequences
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References
| [1] | Miner J.L., Hahn K.J., Staten N.R., Baile C.A. Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Adipose tissue. |
| [2] | Nicolas N. Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 69-259. Tissue: Adipose tissue. |
Cross-references
Sequence databases | |
|---|---|
| U29948 mRNA. Translation: AAA73627.1. Z49058 mRNA. Translation: CAA88844.1. | |
| PIR | S54115. |
| UniGene | Ssc.11074 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1FDP based on UniProtKB P00746. |
| SMR | P51779. Positions 27-254. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | S01.191. |
Phylogenomic databases | |
| HOVERGEN | P51779. |
Enzyme and pathway databases | |
| BRENDA | 3.4.21.46. 249. |
Family and domain databases | |
| InterPro | IPR018114. Peptidase_S1/S6_AS. IPR001254. Peptidase_S1_S6. IPR001314. Peptidase_S1A. [Graphical view] |
| Pfam | PF00089. Trypsin. 1 hit. [Graphical view] |
| PRINTS | PR00722. CHYMOTRYPSIN. |
| SMART | SM00020. Tryp_SPc. 1 hit. [Graphical view] |
| PROSITE | PS50240. TRYPSIN_DOM. 1 hit. PS00134. TRYPSIN_HIS. 1 hit. PS00135. TRYPSIN_SER. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CFAD_PIG | ||||||||
| Accession | Primary (citable) accession number: P51779 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


