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P32038 (CFAD_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Complement factor D

EC=3.4.21.46
Alternative name(s):
Adipsin
C3 convertase activator
Endogenous vascular elastase
Properdin factor D
Gene names
Name:Cfd
Synonyms:Adn, Df
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length263 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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.

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.

Post-translational modification

N-glycosylated.

Sequence similarities

Belongs to the peptidase S1 family.

Contains 1 peptidase S1 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Propeptide21 – 255Activation peptide
PRO_0000027566
Chain26 – 263238Complement factor D
PRO_0000027567

Regions

Domain26 – 254229Peptidase S1

Sites

Active site661Charge relay system
Active site1151Charge relay system
Active site2091Charge relay system

Amino acid modifications

Glycosylation461N-linked (GlcNAc...)
Disulfide bond51 ↔ 67 By similarity
Disulfide bond149 ↔ 215 By similarity
Disulfide bond180 ↔ 196 By similarity
Disulfide bond205 ↔ 230 By similarity

Sequences

Sequence LengthMass (Da)Tools
P32038 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: D573133568A31CE0

FASTA26328,442
        10         20         30         40         50         60 
MHSSVYLVAL VVLEAAVCVA QPRGRILGGQ EAMAHARPYM ASVQVNGTHV CGGTLVDEQW 

        70         80         90        100        110        120 
VLSAAHCMDG VTKDEVVQVL LGAHSLSSPE PYKHLYDVQS VVLHPGSRPD SVEDDLMLFK 

       130        140        150        160        170        180 
LSHNASLGPH VRPLPLQRED REVKPGTLCD VAGWGVVTHA GRRPDVLQQL TVSIMDRNTC 

       190        200        210        220        230        240 
NLRTYHDGAI TKNMMCAESN RRDTCRGDSG GPLVCGDAVE AVVTWGSRVC GNRRKPGVFT 

       250        260 
RVATYVPWIE NVLSGNVSVN VTA 

« Hide

References

[1]"The endogenous vascular elastase that governs development and progression of monocrotaline-induced pulmonary hypertension in rats is a novel enzyme related to the serine proteinase adipsin."
Zhu L., Wigle D., Hinek A., Kobayashi J., Ye C., Zuker M., Dodo H., Keeley F.W., Rabinovitch M.
J. Clin. Invest. 94:1163-1171(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Purification and partial characterization of rat factor D."
Baker B.C., Campbell C.J., Grinham C.J., Turcatti G.
Biochem. J. 279:775-779(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 26-55.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S73894 mRNA. Translation: AAB31922.1.
PIRI55608.
RefSeqNP_001071110.1. NM_001077642.1.
UniGeneRn.16172.

3D structure databases

ProteinModelPortalP32038.
SMRP32038. Positions 26-254.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000015029.

Protein family/group databases

MEROPSS01.191.

Proteomic databases

PaxDbP32038.
PRIDEP32038.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID54249.
KEGGrno:54249.
UCSCRGD:2498. rat.

Organism-specific databases

CTD1675.
RGD2498. Cfd.

Phylogenomic databases

eggNOGCOG5640.
HOGENOMHOG000251820.
HOVERGENHBG013304.
InParanoidP32038.
KOK01334.
PhylomeDBP32038.

Gene expression databases

GenevestigatorP32038.

Family and domain databases

InterProIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio610740.
PROP32038.

Entry information

Entry nameCFAD_RAT
AccessionPrimary (citable) accession number: P32038
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries