CFD
entrez
1675
canonical
uniprot
P00746
canonical
ensembl
ENSG00000197766
resolver
ensembl
ENSG00000274619
resolver
ensp
ENSP00000332139
resolver
ensp
ENSP00000468253
resolver
ensp
ENSP00000478745
resolver
ensp
ENSP00000488580
resolver
ensp
ENSP00000536246
resolver
enst
ENST00000327726
resolver
enst
ENST00000592860
resolver
enst
ENST00000617994
resolver
enst
ENST00000632706
resolver
enst
ENST00000866187
resolver
genesymbol
CFD
resolver
genesymbol_syn
DF
resolver
genesymbol_syn
PFD
resolver
hgnc
HGNC:2771
resolver
uniprot
A6XNE2
resolver
uniprot
B4DV76
resolver
uniprot
K7ERG9
resolver
uniprot
Q5U5S1
resolver
uniprot
Q86VJ5
resolver
uniprot
Q8N4E0
resolver
uniprot
Q8WZB4
resolver
uniprot_entry
A6XNE2_HUMAN
resolver
uniprot_entry
CFAD_HUMAN
resolver
uniprot_entry
K7ERG9_HUMAN
resolver
uniprot_sec
B4DV76
resolver
uniprot_sec
Q5U5S1
resolver
uniprot_sec
Q86VJ5
resolver
uniprot_sec
Q8N4E0
resolver
uniprot_sec
Q8WZB4
resolver
activity_regulation
ACTIVITY REGULATION: Circulates in plasma in a mature but self-inhibited form (PubMed:10022823, PubMed:21205667). Activated by factor B (CFB), which displaces the self-inhibition loop (PubMed:21205667). Associates with CFB complexed with complement C3b (PubMed:21205667). Specifically inhibited by anti-factor D Fab fragment (AFD) antibody (PubMed:22362762). {ECO:0000269|PubMed:10022823, ECO:0000269|PubMed:21205667, ECO:0000269|PubMed:22362762}.
uniprot
proteins
amino_acid_sequence
MHSWERLAVLVLLGAAACAAPPRGRILGGREAEAHARPYMASVQLNGAHLCGGVLVAEQWVLSAAHCLEDAADGKVQVLLGAHSLSQPEPSKRLYDVLRAVPHPDSQPDTIDHDLLLLQLSEKATLGPAVRPLPWQRVDRDVAPGTLCDVAGWGIVNHAGRRPDSLQHVLLPVLDRATCNRRTHHDGAITERLMCAESNRRDSCKGDSGGPLVCGGVLEGVVTSGSRVCGNRKKPGIYTRVASYAAWIDSVLA
uniprot
proteins
disease_involvement
DISEASE: Complement factor D deficiency (CFDD) [MIM:613912]: An immunologic disorder characterized by increased susceptibility to bacterial infections, particularly Neisseria infections, due to a defect in the alternative complement pathway. {ECO:0000269|PubMed:16527897}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.4.21.46
uniprot
proteins
function
FUNCTION: Serine protease that initiates the alternative pathway of the complement system, a cascade of proteins that leads to phagocytosis and breakdown of pathogens and signaling that strengthens the adaptive immune system (PubMed:21205667, PubMed:22362762, PubMed:6769474, PubMed:874324, PubMed:9748277). In contrast to other complement pathways (classical, lectin and GZMK) that are directly activated by pathogens or antigen-antibody complexes, the alternative complement pathway is initiated by the spontaneous hydrolysis of complement C3 (PubMed:21205667, PubMed:22362762, PubMed:6769474, PubMed:874324). The alternative complement pathway acts as an amplification loop that enhances complement activation by mediating the formation of C3 and C5 convertases (PubMed:21205667, PubMed:22362762, PubMed:6769474, PubMed:874324). Activated CFD cleaves factor B (CFB) when the latter is complexed with complement C3b, activating the C3 convertase of the alternative pathway (PubMed:21205667, PubMed:6769474, PubMed:874324, PubMed:9748277). {ECO:0000269|PubMed:21205667, ECO:0000269|PubMed:22362762, ECO:0000269|PubMed:6769474, ECO:0000269|PubMed:874324, ECO:0000269|PubMed:9748277}.
uniprot
proteins
mass_dalton
27033
uniprot
proteins
mutagenesis
MUTAGEN 158; /note="H->A: Abolished ability to cleave CFB."; /evidence="ECO:0000269|PubMed:21205667"; MUTAGEN 182; /note="R->A: Abolished ability to cleave CFB."; /evidence="ECO:0000269|PubMed:21205667"; MUTAGEN 208; /note="S->A: Abolished serine endopeptidase activity."; /evidence="ECO:0000269|PubMed:21205667, ECO:0000269|PubMed:22362762"; MUTAGEN 227; /note="R->A: Increased serine endopeptidase activity in absence of CFB, while decreased ability to cleave CFB."; /evidence="ECO:0000269|PubMed:21205667"; MUTAGEN 227; /note="R->G: Abolished ability to cleave CFB."; /evidence="ECO:0000269|PubMed:21205667"; MUTAGEN 228; /note="V->A: Abolished ability to cleave CFB."; /evidence="ECO:0000269|PubMed:21205667
uniprot
proteins
post_translational_modification
PTM: CFD is activated by the removal of 5 residues at the N-terminus, named activation peptide, by the MASP-3 isoform of MASP1. {ECO:0000269|PubMed:20038603, ECO:0000269|PubMed:27535802}.
uniprot
proteins
protein_family
Peptidase S1 family
uniprot
proteins
pubmed
10022823
uniprot
proteins
pubmed
1374388
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16527897
uniprot
proteins
pubmed
20038603
uniprot
proteins
pubmed
21205667
uniprot
proteins
pubmed
22362762
uniprot
proteins
pubmed
22905912
uniprot
proteins
pubmed
27535802
uniprot
proteins
pubmed
497171
uniprot
proteins
pubmed
6363133
uniprot
proteins
pubmed
6383466
uniprot
proteins
pubmed
6769474
uniprot
proteins
pubmed
6776531
uniprot
proteins
pubmed
6821372
uniprot
proteins
pubmed
6987665
uniprot
proteins
pubmed
7592653
uniprot
proteins
pubmed
8289289
uniprot
proteins
pubmed
874324
uniprot
proteins
pubmed
9748277
uniprot
proteins
pubmed
9753554
uniprot
proteins
sequence_length
253
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:497171, ECO:0000269|PubMed:874324}.
uniprot
proteins