NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8083356 [NCBI, ExPASy, EBI, Israel, Japan]
Zhu L., Wigle D., Hinek A., Kobayashi J., Ye C., Zuker M., Dodo H., Keeley F.W., Rabinovitch M.;
"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.";
J. Clin. Invest. 94:1163-1171(1994).

[2]

PROTEIN SEQUENCE OF 26-55.
PubMed=1953671 [NCBI, ExPASy, EBI, Israel, Japan]
Baker B.C., Campbell C.J., Grinham C.J., Turcatti G.;
"Purification and partial characterization of rat factor D.";
Biochem. J. 279:775-779(1991).

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.
PTM: N-glycosylated.
SIMILARITY: Belongs to the peptidase S1 family [view classification].
SIMILARITY: Contains 1 peptidase S1 domain [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

S73894; AAB31922.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

I55608; I55608.

NP_001071110.1; -.

3D structure databases

HSSP

P00746; 1FDP. [HSSP ENTRY / PDB]

SMR

P32038; 26-254.

ModBase

P32038.

Protein family/group databases

MEROPS

S01.191; -.

Organism-specific databases

RGD

2498; Cfd.

Gene expression databases

ArrayExpress

P32038; -.

GermOnline

ENSRNOG00000033564; Rattus norvegicus.

Ontologies

GO:0004252;	Molecular function: serine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0006957;	Biological process: complement activation, alternative pathway (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001254; Peptidase_S1_S6.
IPR001314; Peptidase_S1A.
Graphical view of domain structure.

Pfam

PF00089; Trypsin; 1.
Pfam graphical view of domain structure.

PRINTS

PR00722; CHYMOTRYPSIN.

SMART

SM00020; Tryp_SPc; 1.
SMART graphical view of domain structure.

PROSITE

PS50240; TRYPSIN_DOM; 1.
PS00134; TRYPSIN_HIS; 1.
PS00135; TRYPSIN_SER; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

Ensembl

ENSRNOG00000033564; Rattus norvegicus. [Contig view]

GeneID

54249; -.

KEGG

rno:54249; -.

Phylogenomic databases

HOVERGEN

P32038; -.

Other

NextBio

610740; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complement alternate pathway; Direct protein sequencing; Glycoprotein; Hydrolase; Immune response; Innate immunity; Protease; Secreted; Serine protease; Signal; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 20`	`20`	`Potential.`
`PROPEP`	`21 25`	`5`	`Activation peptide.`	`PRO_0000027566`
`CHAIN`	`26 263`	`238`	`Complement factor D.`	`PRO_0000027567`
`DOMAIN`	`26 254`	`229`	`Peptidase S1.`
`ACT_SITE`	`66 66`		`Charge relay system.`
`ACT_SITE`	`115 115`		`Charge relay system.`
`ACT_SITE`	`209 209`		`Charge relay system.`
`CARBOHYD`	`46 46`		`N-linked (GlcNAc...).`
`DISULFID`	`51 67`		`By similarity.`
`DISULFID`	`149 215`		`By similarity.`
`DISULFID`	`180 196`		`By similarity.`
`DISULFID`	`205 230`		`By similarity.`

Sequence information

Length: 263 AA [This is the length of the unprocessed precursor]

Molecular weight: 28442 Da [This is the MW of the unprocessed precursor]

CRC64: D573133568A31CE0 [This is a checksum on the sequence]

        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

P32038 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools