CFAD_RAT
ID CFAD_RAT Reviewed; 263 AA.
AC P32038;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 136.
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=Endogenous vascular elastase;
DE AltName: Full=Properdin factor D;
DE Flags: Precursor;
GN Name=Cfd; Synonyms=Adn, Df;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8083356; DOI=10.1172/jci117432;
RA Zhu L., Wigle D., Hinek A., Kobayashi J., Ye C., Zuker M., Dodo H.,
RA Keeley F.W., Rabinovitch M.;
RT "The endogenous vascular elastase that governs development and progression
RT of monocrotaline-induced pulmonary hypertension in rats is a novel enzyme
RT related to the serine proteinase adipsin.";
RL J. Clin. Invest. 94:1163-1171(1994).
RN [2]
RP PROTEIN SEQUENCE OF 26-55.
RX PubMed=1953671; DOI=10.1042/bj2790775;
RA Baker B.C., Campbell C.J., Grinham C.J., Turcatti G.;
RT "Purification and partial characterization of rat factor D.";
RL Biochem. J. 279:775-779(1991).
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.
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 -!- PTM: N-glycosylated.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; S73894; AAB31922.1; -; mRNA.
DR PIR; I55608; I55608.
DR RefSeq; NP_001071110.1; NM_001077642.1.
DR AlphaFoldDB; P32038; -.
DR SMR; P32038; -.
DR STRING; 10116.ENSRNOP00000015029; -.
DR BindingDB; P32038; -.
DR ChEMBL; CHEMBL4295743; -.
DR MEROPS; S01.191; -.
DR GlyGen; P32038; 1 site.
DR PaxDb; P32038; -.
DR GeneID; 54249; -.
DR KEGG; rno:54249; -.
DR UCSC; RGD:2498; rat.
DR CTD; 1675; -.
DR RGD; 2498; Cfd.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; P32038; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; P32038; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:P32038; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0004175; F:endopeptidase activity; IDA:RGD.
DR GO; GO:0004252; F:serine-type endopeptidase activity; TAS:RGD.
DR GO; GO:0006957; P:complement activation, alternative pathway; ISO:RGD.
DR GO; GO:0007219; P:Notch signaling pathway; IMP:RGD.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR GO; GO:0060041; P:retina development in camera-type eye; ISO:RGD.
DR GO; GO:0035886; P:vascular associated smooth muscle cell differentiation; ISO:RGD.
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 1: Evidence at protein level;
KW Complement alternate pathway; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Hydrolase; Immunity; Innate immunity; Protease;
KW Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..25
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:1953671"
FT /id="PRO_0000027566"
FT CHAIN 26..263
FT /note="Complement factor D"
FT /id="PRO_0000027567"
FT DOMAIN 26..254
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 66
FT /note="Charge relay system"
FT ACT_SITE 115
FT /note="Charge relay system"
FT ACT_SITE 209
FT /note="Charge relay system"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 51..67
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 263 AA; 28442 MW; D573133568A31CE0 CRC64;
MHSSVYLVAL VVLEAAVCVA QPRGRILGGQ EAMAHARPYM ASVQVNGTHV CGGTLVDEQW
VLSAAHCMDG VTKDEVVQVL LGAHSLSSPE PYKHLYDVQS VVLHPGSRPD SVEDDLMLFK
LSHNASLGPH VRPLPLQRED REVKPGTLCD VAGWGVVTHA GRRPDVLQQL TVSIMDRNTC
NLRTYHDGAI TKNMMCAESN RRDTCRGDSG GPLVCGDAVE AVVTWGSRVC GNRRKPGVFT
RVATYVPWIE NVLSGNVSVN VTA
