Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Complement factor D

Gene

CFD

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

Selective cleavage of Arg-|-Lys bond in complement factor B when in complex with complement subcomponent C3b or with cobra venom factor.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei67Charge relay system1
Active sitei115Charge relay system1
Active sitei209Charge relay system1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Complement alternate pathway, Immunity, Innate immunity

Enzyme and pathway databases

ReactomeiR-BTA-114608. Platelet degranulation.
R-BTA-173736. Alternative complement activation.
R-BTA-6798695. Neutrophil degranulation.

Protein family/group databases

MEROPSiS01.191.

Names & Taxonomyi

Protein namesi
Recommended name:
Complement factor D (EC:3.4.21.46)
Alternative name(s):
Adipsin
C3 convertase activator
Properdin factor D
Gene namesi
Name:CFD
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 7

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
PropeptideiPRO_000028585922 – 26Activation peptideSequence analysis5
ChainiPRO_000028586027 – 259Complement factor DAdd BLAST233

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi52 ↔ 68PROSITE-ProRule annotation
Disulfide bondi149 ↔ 215PROSITE-ProRule annotation
Disulfide bondi180 ↔ 196PROSITE-ProRule annotation
Disulfide bondi205 ↔ 230PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Zymogen

Proteomic databases

PaxDbiQ3T0A3.
PRIDEiQ3T0A3.

Expressioni

Gene expression databases

BgeeiENSBTAG00000048122.

Interactioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000055802.

Structurei

3D structure databases

ProteinModelPortaliQ3T0A3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini27 – 254Peptidase S1PROSITE-ProRule annotationAdd BLAST228

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118895.
HOVERGENiHBG013304.
InParanoidiQ3T0A3.
KOiK01334.
OMAiESHARPY.
OrthoDBiEOG091G0DF7.
TreeFamiTF333630.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
InterProiIPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q3T0A3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADRSLHLVV LILLGTALCA AQPRGRILRG QEAPSHSRPY MASVQVNGKH
60 70 80 90 100
VCGGFLIAEQ WVMSAAHCLE DVADGKVQVL LGAHSLSQPE PSKRLYDVLR
110 120 130 140 150
VVPHPGSRTE TIDHDLLLLQ LSEKAVLGPA VQLLPWQRED RDVAAGTLCD
160 170 180 190 200
VAGWGVVSHT GRKPDRLQHL LLPVLDRATC NLRTYHDGTI TERMMCAESN
210 220 230 240 250
RRDTCKGDSG GPLVCGSVAE GVVTSGSRIC GNHKKPGIYT RLASYVAWID

GVMAEGAAA
Length:259
Mass (Da):27,878
Last modified:October 11, 2005 - v1
Checksum:i0D56DB06FEC4C2A9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC102479 mRNA. Translation: AAI02480.1.
RefSeqiNP_001029427.1. NM_001034255.2.
XP_005209319.1. XM_005209262.1.
UniGeneiBt.41326.

Genome annotation databases

EnsembliENSBTAT00000063284; ENSBTAP00000055802; ENSBTAG00000048122.
GeneIDi505647.
KEGGibta:505647.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC102479 mRNA. Translation: AAI02480.1.
RefSeqiNP_001029427.1. NM_001034255.2.
XP_005209319.1. XM_005209262.1.
UniGeneiBt.41326.

3D structure databases

ProteinModelPortaliQ3T0A3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000055802.

Protein family/group databases

MEROPSiS01.191.

Proteomic databases

PaxDbiQ3T0A3.
PRIDEiQ3T0A3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000063284; ENSBTAP00000055802; ENSBTAG00000048122.
GeneIDi505647.
KEGGibta:505647.

Organism-specific databases

CTDi1675.

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118895.
HOVERGENiHBG013304.
InParanoidiQ3T0A3.
KOiK01334.
OMAiESHARPY.
OrthoDBiEOG091G0DF7.
TreeFamiTF333630.

Enzyme and pathway databases

ReactomeiR-BTA-114608. Platelet degranulation.
R-BTA-173736. Alternative complement activation.
R-BTA-6798695. Neutrophil degranulation.

Gene expression databases

BgeeiENSBTAG00000048122.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
InterProiIPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCFAD_BOVIN
AccessioniPrimary (citable) accession number: Q3T0A3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: October 11, 2005
Last modified: November 30, 2016
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.