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Reviewed, UniProtKB/Swiss-Prot P51779 (CFAD_PIG)

Last modified June 16, 2009. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Complement factor D
    EC=3.4.21.46
Alternative name(s):
    C3 convertase activator
    Properdin factor D
    Adipsin
Gene names
Name: CFD
Synonyms: DF
OrganismSus scrofa (Pig)
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length259 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Secreted.

Sequence similarities

Belongs to the peptidase S1 family.

Contains 1 peptidase S1 domain.

Ontologies

Keywords
   Biological processComplement alternate pathway
Immune response
Innate immunity
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Zymogen
Gene Ontology (GO)
   Biological processcomplement activation, alternative pathway

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionserine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Propeptide22 – 265Activation peptide Potential
PRO_0000027564
Chain27 – 259233Complement factor D
PRO_0000027565

Regions

Domain27 – 254228Peptidase S1

Sites

Active site671Charge relay system
Active site1151Charge relay system
Active site2091Charge relay system

Amino acid modifications

Disulfide bond52 ↔ 68 By similarity
Disulfide bond149 ↔ 215 By similarity
Disulfide bond180 ↔ 196 By similarity
Disulfide bond205 ↔ 230 By similarity

Sequences

Sequence LengthMass (Da)Tools
P51779-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 0121AAE0E34CA1ED

FASTA25927,764
        10         20         30         40         50         60 
MADRSGHLAA LILLGAAVCV AQPRGRILGG QEAKSHERPY MASVQVNGKH VCGGFLVSEQ 

        70         80         90        100        110        120 
WVLSAAHCLE DVAEGKLQVL LGAHSLSQPE PSKRLYDVLR AVPHPDSQPD TIDHDLLLLK 

       130        140        150        160        170        180 
LSEKAELGPA VQPLAWQRED HEVPAGTLCD VAGWGVVSHT GRRPDRLQHL LLPVLDRTTC 

       190        200        210        220        230        240 
NLRTYHDGTI TERMMCAESN RRDSCKGDSG GPLVCGGVAE GVVTSGSRVC GNRKKPGIYT 

       250 
RLASYVAWID GVMADSAAA 

« Hide

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.
PIRS54115.
UniGeneSsc.11074

3D structure databases

HSSPHSSP built from PDB template 1FDP based on UniProtKB P00746.
SMRP51779. Positions 27-254.
ModBaseSearch...

Protein family/group databases

MEROPSS01.191.

Phylogenomic databases

HOVERGENP51779.

Enzyme and pathway databases

BRENDA3.4.21.46. 249.

Family and domain databases

InterProIPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCFAD_PIG
AccessionPrimary (citable) accession number: P51779
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 16, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents