ID   Q6FHW3_HUMAN            Unreviewed;       228 AA.
AC   Q6FHW3;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 93.
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=DF {ECO:0000313|EMBL:CAG38812.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:CAG38812.1};
RN   [1] {ECO:0000313|EMBL:CAG38812.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA   Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA   LaBaer J.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) 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. {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; CR536575; CAG38812.1; -; mRNA.
DR   AlphaFoldDB; Q6FHW3; -.
DR   SMR; Q6FHW3; -.
DR   MEROPS; S01.191; -.
DR   PeptideAtlas; Q6FHW3; -.
DR   ChiTaRS; CFD; human.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000256|RuleBase:RU363034};
KW   Protease {ECO:0000256|RuleBase:RU363034};
KW   Serine protease {ECO:0000256|RuleBase:RU363034}.
FT   DOMAIN          1..228
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
SQ   SEQUENCE   228 AA;  24423 MW;  B1B9EA3B73E802C5 CRC64;
     MLGGREAEAH ARPYMASVQL NGAHLCGGVL VAEQWVLSAA HCLEDAADGK VQVLLGAHSL
     SQPEPSKRLY DVLRAVPHPD SQPDTIDHDL LLLQLSEKAT LGPAVRPLPW QRVDRDVAPG
     TLCDVAGWGI VNHAGRRPDS LQHVLLPVLD RATCNRRTHH DGAITERLMC AESNRRDSCK
     GDSGGPLVCG GVLEGVVTSG SRVCGNRKKP GIYTRVASYA AWIDSVLA
//