P51779 (CFAD_PIG) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 72.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Complement factor D EC=3.4.21.46 Alternative name(s): Adipsin C3 convertase activator Properdin factor D | ||||
| Gene names |
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| Organism | Sus scrofa (Pig) [Complete proteome] | ||||
| 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 Immunity Innate immunity |
| Cellular component | Secreted |
| Domain | Signal |
| Molecular function | Hydrolase Protease Serine protease |
| PTM | Disulfide bond Zymogen |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | complement activation, alternative pathway Inferred from electronic annotation. Source: UniProtKB-KW proteolysisInferred from electronic annotation. Source: UniProtKB-KW |
| 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. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U29948 mRNA. Translation: AAA73627.1. Z49058 mRNA. Translation: CAA88844.1. |
| PIR | S54115. |
| RefSeq | XP_003123033.1. XM_003122985.1. |
| UniGene | Ssc.11074. |
3D structure databases | |
| ProteinModelPortal | P51779. |
| SMR | P51779. Positions 27-254. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P51779. |
Protein family/group databases | |
| MEROPS | S01.191. |
Proteomic databases | |
| PRIDE | P51779. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSSSCT00000014662; ENSSSCP00000014267; ENSSSCG00000013418. |
| GeneID | 396877. |
| KEGG | ssc:396877. |
Phylogenomic databases | |
| HOVERGEN | HBG013304. |
| OMA | EAHARPY. |
| OrthoDB | EOG4FXR89. |
Family and domain databases | |
| InterPro | IPR009003. Pept_cys/ser_Trypsin-like. IPR018114. Peptidase_S1/S6_AS. IPR001254. Peptidase_S1_S6. IPR001314. Peptidase_S1A. [Graphical view] |
| KO | K01334. |
| Pfam | PF00089. Trypsin. 1 hit. [Graphical view] |
| PRINTS | PR00722. CHYMOTRYPSIN. |
| SMART | SM00020. Tryp_SPc. 1 hit. [Graphical view] |
| SUPFAM | SSF50494. Pept_Ser_Cys. 1 hit. |
| 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 |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

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