CFAD_MOUSE
ID CFAD_MOUSE Reviewed; 259 AA.
AC P03953; Q61280;
DT 23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-1986, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Complement factor D;
DE EC=3.4.21.46;
DE AltName: Full=28 kDa adipocyte protein;
DE AltName: Full=Adipsin;
DE AltName: Full=C3 convertase activator;
DE AltName: Full=Properdin factor D;
DE Flags: Precursor;
GN Name=Cfd; Synonyms=Adn, Df;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3015943; DOI=10.1016/s0021-9258(18)67461-7;
RA Phillips M., Djian P., Green H.;
RT "The nucleotide sequence of three genes participating in the adipose
RT differentiation of 3T3 cells.";
RL J. Biol. Chem. 261:10821-10827(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
RX PubMed=3024123; DOI=10.1093/nar/14.22.8879;
RA Min H.Y., Spiegelman B.M.;
RT "Adipsin, the adipocyte serine protease: gene structure and control of
RT expression by tumor necrosis factor.";
RL Nucleic Acids Res. 14:8879-8892(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Swiss white;
RX PubMed=3901003; DOI=10.1073/pnas.82.19.6480;
RA Cook K.S., Groves D.L., Min H.Y., Spiegelman B.M.;
RT "A developmentally regulated mRNA from 3T3 adipocytes encodes a novel
RT serine protease homologue.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:6480-6484(1985).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-124.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=16944957; DOI=10.1021/pr060186m;
RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT "Proteome-wide characterization of N-glycosylation events by diagonal
RT chromatography.";
RL J. Proteome Res. 5:2438-2447(2006).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-176.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=17330941; DOI=10.1021/pr0604559;
RA Bernhard O.K., Kapp E.A., Simpson R.J.;
RT "Enhanced analysis of the mouse plasma proteome using cysteine-containing
RT tryptic glycopeptides.";
RL J. Proteome Res. 6:987-995(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P03953-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P03953-2; Sequence=VSP_005382;
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:16944957,
CC ECO:0000269|PubMed:17330941}.
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; M11768; AAA40486.1; -; mRNA.
DR EMBL; X04673; CAA28378.1; -; Genomic_DNA.
DR EMBL; X04673; CAA28379.1; -; Genomic_DNA.
DR EMBL; M13386; AAA37262.1; -; Genomic_DNA.
DR CCDS; CCDS23995.1; -. [P03953-1]
DR CCDS; CCDS88051.1; -. [P03953-2]
DR PIR; C25952; WMMS28.
DR RefSeq; NP_001278844.1; NM_001291915.2. [P03953-2]
DR RefSeq; NP_038487.1; NM_013459.4. [P03953-1]
DR PDB; 5FCR; X-ray; 1.25 A; A/B/C/D=26-259.
DR PDBsum; 5FCR; -.
DR AlphaFoldDB; P03953; -.
DR SMR; P03953; -.
DR BioGRID; 197991; 1440.
DR STRING; 10090.ENSMUSP00000056836; -.
DR MEROPS; S01.191; -.
DR GlyGen; P03953; 5 sites.
DR iPTMnet; P03953; -.
DR PhosphoSitePlus; P03953; -.
DR CPTAC; non-CPTAC-3697; -.
DR MaxQB; P03953; -.
DR PaxDb; P03953; -.
DR PRIDE; P03953; -.
DR ProteomicsDB; 281545; -. [P03953-1]
DR ProteomicsDB; 281546; -. [P03953-2]
DR Antibodypedia; 4290; 566 antibodies from 33 providers.
DR DNASU; 11537; -.
DR Ensembl; ENSMUST00000061653; ENSMUSP00000056836; ENSMUSG00000061780. [P03953-1]
DR Ensembl; ENSMUST00000217837; ENSMUSP00000151894; ENSMUSG00000061780. [P03953-2]
DR GeneID; 11537; -.
DR KEGG; mmu:11537; -.
DR UCSC; uc007gaj.3; mouse. [P03953-1]
DR CTD; 1675; -.
DR MGI; MGI:87931; Cfd.
DR VEuPathDB; HostDB:ENSMUSG00000061780; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000162255; -.
DR HOGENOM; CLU_006842_1_0_1; -.
DR InParanoid; P03953; -.
DR OMA; ISHYTQW; -.
DR PhylomeDB; P03953; -.
DR TreeFam; TF333630; -.
DR BRENDA; 3.4.21.46; 3474.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR Reactome; R-MMU-173736; Alternative complement activation.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 11537; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Cfd; mouse.
DR PRO; PR:P03953; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P03953; protein.
DR Bgee; ENSMUSG00000061780; Expressed in white adipose tissue and 92 other tissues.
DR ExpressionAtlas; P03953; baseline and differential.
DR Genevisible; P03953; MM.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0004175; F:endopeptidase activity; ISO:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006957; P:complement activation, alternative pathway; IMP:MGI.
DR GO; GO:0007219; P:Notch signaling pathway; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
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 3D-structure; Alternative splicing; Complement alternate pathway;
KW Disulfide bond; Glycoprotein; Hydrolase; Immunity; Innate immunity;
KW Protease; 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:0000255"
FT /id="PRO_0000027562"
FT CHAIN 26..259
FT /note="Complement factor D"
FT /id="PRO_0000027563"
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 /evidence="ECO:0000255"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17330941"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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"
FT VAR_SEQ 20
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_005382"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:5FCR"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:5FCR"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:5FCR"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:5FCR"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:5FCR"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:5FCR"
FT STRAND 94..103
FT /evidence="ECO:0007829|PDB:5FCR"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:5FCR"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:5FCR"
FT STRAND 168..175
FT /evidence="ECO:0007829|PDB:5FCR"
FT HELIX 177..180
FT /evidence="ECO:0007829|PDB:5FCR"
FT TURN 183..188
FT /evidence="ECO:0007829|PDB:5FCR"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:5FCR"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:5FCR"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:5FCR"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:5FCR"
FT STRAND 237..242
FT /evidence="ECO:0007829|PDB:5FCR"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:5FCR"
FT HELIX 246..253
FT /evidence="ECO:0007829|PDB:5FCR"
SQ SEQUENCE 259 AA; 28057 MW; 8C3A952561247DF9 CRC64;
MHSSVYFVAL VILGAAVCAA QPRGRILGGQ EAAAHARPYM ASVQVNGTHV CGGTLLDEQW
VLSAAHCMDG VTDDDSVQVL LGAHSLSAPE PYKRWYDVQS VVPHPGSRPD SLEDDLILFK
LSQNASLGPH VRPLPLQYED KEVEPGTLCD VAGWGVVTHA GRRPDVLHQL RVSIMNRTTC
NLRTYHDGVV TINMMCAESN RRDTCRGDSG SPLVCGDAVE GVVTWGSRVC GNGKKPGVYT
RVSSYRMWIE NITNGNMTS
