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   03-AUG-2022, entry version 98.
DE   RecName: Full=Complement factor D;
DE            EC=3.4.21.46;
DE   AltName: Full=Adipsin;
DE   AltName: Full=C3 convertase activator;
DE   AltName: Full=Properdin factor D;
DE   Flags: Precursor;
GN   Name=CFD;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   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 with
CC       factor C3b, activating the C3bbb complex, which then becomes the C3
CC       convertase of the alternate pathway. Its function is homologous to that
CC       of C1s in the classical pathway (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Selective cleavage of Arg-|-Lys bond in complement factor B
CC         when in complex with complement subcomponent C3b or with cobra venom
CC         factor.; EC=3.4.21.46;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   EMBL; BC102479; AAI02480.1; -; mRNA.
DR   RefSeq; NP_001029427.1; NM_001034255.2.
DR   RefSeq; XP_005209319.1; XM_005209262.1.
DR   AlphaFoldDB; Q3T0A3; -.
DR   SMR; Q3T0A3; -.
DR   STRING; 9913.ENSBTAP00000055802; -.
DR   MEROPS; S01.191; -.
DR   PaxDb; Q3T0A3; -.
DR   PRIDE; Q3T0A3; -.
DR   Ensembl; ENSBTAT00000063284; ENSBTAP00000055802; ENSBTAG00000048122.
DR   GeneID; 505647; -.
DR   KEGG; bta:505647; -.
DR   CTD; 1675; -.
DR   VEuPathDB; HostDB:ENSBTAG00000048122; -.
DR   VGNC; VGNC:97253; CFD.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT00940000162255; -.
DR   HOGENOM; CLU_006842_7_0_1; -.
DR   InParanoid; Q3T0A3; -.
DR   OMA; ISHYTQW; -.
DR   OrthoDB; 1314811at2759; -.
DR   TreeFam; TF333630; -.
DR   Reactome; R-BTA-114608; Platelet degranulation.
DR   Reactome; R-BTA-6798695; Neutrophil degranulation.
DR   Proteomes; UP000009136; Chromosome 7.
DR   Bgee; ENSBTAG00000048122; Expressed in lung and 103 other tissues.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006957; P:complement activation, alternative pathway; IEA:UniProtKB-KW.
DR   GO; GO:0007219; P:Notch signaling pathway; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; -; 2.
DR   InterPro; IPR037561; Complement_factor_D.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24271:SF54; PTHR24271:SF54; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 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; Immunity;
KW   Innate immunity; Protease; Reference proteome; Secreted; Serine protease;
KW   Signal; Zymogen.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..26
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000285859"
FT   CHAIN           27..259
FT                   /note="Complement factor D"
FT                   /id="PRO_0000285860"
FT   DOMAIN          27..254
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        67
FT                   /note="Charge relay system"
FT   ACT_SITE        115
FT                   /note="Charge relay system"
FT   ACT_SITE        209
FT                   /note="Charge relay system"
FT   DISULFID        52..68
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        149..215
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        180..196
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        205..230
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
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