ID   CFAD_BOVIN              Reviewed;         259 AA.
AC   Q3T0A3;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   16-JUN-2009, entry version 26.
DE   RecName: Full=Complement factor D;
DE            EC=3.4.21.46;
DE   AltName: Full=C3 convertase activator;
DE   AltName: Full=Properdin factor D;
DE   AltName: Full=Adipsin;
DE   Flags: Precursor;
GN   Name=CFD;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Factor D cleaves factor B when the latter is complexed
CC       with factor C3b, activating the C3bbb complex, which then becomes
CC       the C3 convertase of the alternate pathway. Its function is
CC       homologous to that of C1s in the classical pathway (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Selective cleavage of Arg-|-Lys bond in
CC       complement factor B when in complex with complement subcomponent
CC       C3b or with cobra venom factor.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC   -!- SIMILARITY: Contains 1 peptidase S1 domain.
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DR   EMBL; BC102479; AAI02480.1; -; mRNA.
DR   IPI; IPI00686338; -.
DR   RefSeq; NP_001029427.1; -.
DR   UniGene; Bt.41326; -.
DR   SMR; Q3T0A3; 27-254.
DR   GeneID; 505647; -.
DR   KEGG; bta:505647; -.
DR   HOVERGEN; Q3T0A3; -.
DR   BRENDA; 3.4.21.46; 251.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006957; P:complement activation, alternative pathway; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR018114; Peptidase_S1/S6_AS.
DR   InterPro; IPR001254; Peptidase_S1_S6.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   2: Evidence at transcript level;
KW   Complement alternate pathway; Disulfide bond; Hydrolase;
KW   Immune response; Innate immunity; Protease; Secreted; Serine protease;
KW   Signal; Zymogen.
FT   SIGNAL        1     21       Potential.
FT   PROPEP       22     26       Activation peptide (Potential).
FT                                /FTId=PRO_0000285859.
FT   CHAIN        27    259       Complement factor D.
FT                                /FTId=PRO_0000285860.
FT   DOMAIN       27    254       Peptidase S1.
FT   ACT_SITE     67     67       Charge relay system.
FT   ACT_SITE    115    115       Charge relay system.
FT   ACT_SITE    209    209       Charge relay system.
FT   DISULFID     52     68       By similarity.
FT   DISULFID    149    215       By similarity.
FT   DISULFID    180    196       By similarity.
FT   DISULFID    205    230       By similarity.
SQ   SEQUENCE   259 AA;  27878 MW;  0D56DB06FEC4C2A9 CRC64;
     MADRSLHLVV LILLGTALCA AQPRGRILRG QEAPSHSRPY MASVQVNGKH VCGGFLIAEQ
     WVMSAAHCLE DVADGKVQVL LGAHSLSQPE PSKRLYDVLR VVPHPGSRTE TIDHDLLLLQ
     LSEKAVLGPA VQLLPWQRED RDVAAGTLCD VAGWGVVSHT GRKPDRLQHL LLPVLDRATC
     NLRTYHDGTI TERMMCAESN RRDTCKGDSG GPLVCGSVAE GVVTSGSRIC GNHKKPGIYT
     RLASYVAWID GVMAEGAAA
//