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 24-JAN-2024, entry version 140. 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 GlyCosmos; P32038; 1 site, No reported glycans. DR GlyGen; P32038; 1 site. DR PhosphoSitePlus; P32038; -. DR PaxDb; 10116-ENSRNOP00000015029; -. DR Ensembl; ENSRNOT00055056642; ENSRNOP00055046748; ENSRNOG00055032763. DR Ensembl; ENSRNOT00060040866; ENSRNOP00060033804; ENSRNOG00060023586. DR Ensembl; ENSRNOT00065034025; ENSRNOP00065027243; ENSRNOG00065020165. DR GeneID; 54249; -. DR KEGG; rno:54249; -. DR UCSC; RGD:2498; rat. DR AGR; RGD:2498; -. DR CTD; 1675; -. DR RGD; 2498; Cfd. DR eggNOG; KOG3627; Eukaryota. DR InParanoid; P32038; -. DR OrthoDB; 4629979at2759; -. 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; Trypsin-like serine proteases; 2. 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; COMPLEMENT FACTOR D; 1. DR PANTHER; PTHR24271; KALLIKREIN-RELATED; 1. DR Pfam; PF00089; Trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00020; Tryp_SPc; 1. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 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 //