CFAD_PIG
ID CFAD_PIG Reviewed; 259 AA.
AC P51779;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 132.
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; Synonyms=DF;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Adipose tissue;
RA Miner J.L., Hahn K.J., Staten N.R., Baile C.A.;
RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 69-259.
RC TISSUE=Adipose tissue;
RA Nicolas N.;
RL Submitted (APR-1995) 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; U29948; AAA73627.1; -; mRNA.
DR EMBL; Z49058; CAA88844.1; -; mRNA.
DR PIR; S54115; S54115.
DR RefSeq; XP_013850255.1; XM_013994801.1.
DR AlphaFoldDB; P51779; -.
DR SMR; P51779; -.
DR STRING; 9823.ENSSSCP00000014267; -.
DR MEROPS; S01.191; -.
DR PaxDb; P51779; -.
DR PeptideAtlas; P51779; -.
DR PRIDE; P51779; -.
DR Ensembl; ENSSSCT00000014662; ENSSSCP00000014267; ENSSSCG00000013418.
DR Ensembl; ENSSSCT00015110733; ENSSSCP00015047364; ENSSSCG00015081206.
DR Ensembl; ENSSSCT00025010178; ENSSSCP00025004071; ENSSSCG00025007659.
DR Ensembl; ENSSSCT00030023893; ENSSSCP00030010712; ENSSSCG00030017276.
DR Ensembl; ENSSSCT00035100272; ENSSSCP00035042561; ENSSSCG00035073930.
DR Ensembl; ENSSSCT00040088052; ENSSSCP00040038691; ENSSSCG00040064392.
DR Ensembl; ENSSSCT00045054307; ENSSSCP00045037812; ENSSSCG00045031770.
DR Ensembl; ENSSSCT00050091537; ENSSSCP00050039408; ENSSSCG00050067127.
DR Ensembl; ENSSSCT00055048922; ENSSSCP00055039056; ENSSSCG00055024762.
DR Ensembl; ENSSSCT00060013955; ENSSSCP00060005354; ENSSSCG00060010731.
DR Ensembl; ENSSSCT00065009398; ENSSSCP00065003919; ENSSSCG00065007012.
DR Ensembl; ENSSSCT00070053755; ENSSSCP00070045575; ENSSSCG00070026800.
DR GeneID; 396877; -.
DR KEGG; ssc:396877; -.
DR CTD; 1675; -.
DR VGNC; VGNC:86609; CFD.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000162255; -.
DR HOGENOM; CLU_006842_1_0_1; -.
DR InParanoid; P51779; -.
DR OMA; ISHYTQW; -.
DR OrthoDB; 1314811at2759; -.
DR TreeFam; TF333630; -.
DR Reactome; R-SSC-114608; Platelet degranulation.
DR Reactome; R-SSC-6798695; Neutrophil degranulation.
DR Proteomes; UP000008227; Chromosome 2.
DR Proteomes; UP000314985; Chromosome 2.
DR Bgee; ENSSSCG00000013418; Expressed in blood and 40 other tissues.
DR ExpressionAtlas; P51779; baseline and differential.
DR Genevisible; P51779; SS.
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_0000027564"
FT CHAIN 27..259
FT /note="Complement factor D"
FT /id="PRO_0000027565"
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; 27764 MW; 0121AAE0E34CA1ED CRC64;
MADRSGHLAA LILLGAAVCV AQPRGRILGG QEAKSHERPY MASVQVNGKH VCGGFLVSEQ
WVLSAAHCLE DVAEGKLQVL LGAHSLSQPE PSKRLYDVLR AVPHPDSQPD TIDHDLLLLK
LSEKAELGPA VQPLAWQRED HEVPAGTLCD VAGWGVVSHT GRRPDRLQHL LLPVLDRTTC
NLRTYHDGTI TERMMCAESN RRDSCKGDSG GPLVCGGVAE GVVTSGSRVC GNRKKPGIYT
RLASYVAWID GVMADSAAA
