ID G1QJT7_NOMLE Unreviewed; 207 AA.
AC G1QJT7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Complement factor D {ECO:0000256|ARBA:ARBA00018673};
DE EC=3.4.21.46 {ECO:0000256|ARBA:ARBA00011933};
DE AltName: Full=Adipsin {ECO:0000256|ARBA:ARBA00030720};
DE AltName: Full=C3 convertase activator {ECO:0000256|ARBA:ARBA00030992};
DE AltName: Full=Properdin factor D {ECO:0000256|ARBA:ARBA00029950};
GN Name=CFD {ECO:0000313|Ensembl:ENSNLEP00000001182.2};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000001182.2, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000001182.2, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000001182.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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. {ECO:0000256|ARBA:ARBA00024765}.
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; Evidence={ECO:0000256|ARBA:ARBA00000303};
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DR EMBL; ADFV01098457; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01098458; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1QJT7; -.
DR STRING; 61853.ENSNLEP00000001182; -.
DR Ensembl; ENSNLET00000001249.2; ENSNLEP00000001182.2; ENSNLEG00000001013.2.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000162255; -.
DR HOGENOM; CLU_006842_13_2_1; -.
DR InParanoid; G1QJT7; -.
DR OMA; WACCAPL; -.
DR Proteomes; UP000001073; Chromosome 17.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
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; IPR001254; Trypsin_dom.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24271:SF54; COMPLEMENT FACTOR D; 1.
DR PANTHER; PTHR24271; KALLIKREIN-RELATED; 1.
DR Pfam; PF00089; Trypsin; 2.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001073};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..207
FT /note="Complement factor D"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014147951"
FT DOMAIN 33..207
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 207 AA; 22159 MW; E4B0F1FBABF03EF3 CRC64;
MHSWERLAVL VLLGAAACGE GARAWAAQPR GRILGGREAE AHARPYMASV QVNGAHLCGG
VLVADFFFFS PPPTLSEKGR WACCAPLPWQ RVDRDVAPGT LCDVAGWGTV NHAGSRPDRL
QHVLLPVLDR ATCNRRMHHD GAITERMMCA ESNRRDSCKG DSGGPLVCGG VLEGVVTSGS
RVCGNRKKPG IYTRVASYAA WIDSVLA
//
