CFAI_PONAB
ID CFAI_PONAB Reviewed; 583 AA.
AC Q5R5A4;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Complement factor I;
DE EC=3.4.21.45;
DE AltName: Full=C3B/C4B inactivator;
DE Contains:
DE RecName: Full=Complement factor I heavy chain;
DE Contains:
DE RecName: Full=Complement factor I light chain;
DE Flags: Precursor;
GN Name=CFI;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Responsible for cleaving the alpha-chains of C4b and C3b in
CC the presence of the cofactors C4-binding protein and factor H
CC respectively. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Inactivates complement subcomponents C3b, iC3b and C4b by
CC proteolytic cleavage.; EC=3.4.21.45;
CC -!- SUBUNIT: Heterodimer of a light and heavy chains; disulfide-linked. The
CC fully processed and mature protein circulates as a zymogen, and is
CC allosterically activated by substrate-induced remodeling of the active
CC site (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- TISSUE SPECIFICITY: Plasma.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; CR860960; CAH93062.1; -; mRNA.
DR RefSeq; NP_001127624.1; NM_001134152.1.
DR AlphaFoldDB; Q5R5A4; -.
DR SMR; Q5R5A4; -.
DR MEROPS; S01.199; -.
DR Ensembl; ENSPPYT00000017426; ENSPPYP00000016746; ENSPPYG00000014995.
DR GeneID; 100174703; -.
DR CTD; 3426; -.
DR GeneTree; ENSGT00930000151042; -.
DR InParanoid; Q5R5A4; -.
DR OrthoDB; 1314811at2759; -.
DR Proteomes; UP000001595; Chromosome 4.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00112; LDLa; 2.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 1.
DR Gene3D; 3.10.250.10; -; 1.
DR Gene3D; 4.10.400.10; -; 2.
DR InterPro; IPR003884; FacI_MAC.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF00057; Ldl_recept_a; 2.
DR Pfam; PF00530; SRCR; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00057; FIMAC; 1.
DR SMART; SM00192; LDLa; 2.
DR SMART; SM00202; SR; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF100895; SSF100895; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF56487; SSF56487; 1.
DR SUPFAM; SSF57424; SSF57424; 2.
DR PROSITE; PS51465; KAZAL_2; 1.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 2.
DR PROSITE; PS50287; SRCR_2; 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 Calcium; Cleavage on pair of basic residues; Complement pathway;
KW Disulfide bond; Glycoprotein; Hydrolase; Immunity; Innate immunity;
KW Metal-binding; Protease; Reference proteome; Repeat; Secreted;
KW Serine protease; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..583
FT /note="Complement factor I"
FT /id="PRO_0000285861"
FT CHAIN 19..335
FT /note="Complement factor I heavy chain"
FT /id="PRO_0000285862"
FT CHAIN 340..583
FT /note="Complement factor I light chain"
FT /id="PRO_0000285863"
FT DOMAIN 55..108
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 114..212
FT /note="SRCR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 213..257
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 258..294
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 340..574
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 380
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 429
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 525
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P05156"
FT BINDING 242
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P05156"
FT BINDING 244
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P05156"
FT BINDING 246
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P05156"
FT BINDING 252
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P05156"
FT BINDING 253
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P05156"
FT BINDING 276
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P05156"
FT BINDING 279
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P05156"
FT BINDING 281
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P05156"
FT BINDING 283
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P05156"
FT BINDING 289
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P05156"
FT BINDING 290
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P05156"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 494
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 536
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 33..255
FT /evidence="ECO:0000250"
FT DISULFID 43..54
FT /evidence="ECO:0000250"
FT DISULFID 48..59
FT /evidence="ECO:0000250"
FT DISULFID 61..93
FT /evidence="ECO:0000250"
FT DISULFID 67..86
FT /evidence="ECO:0000250"
FT DISULFID 75..106
FT /evidence="ECO:0000250"
FT DISULFID 141..181
FT /evidence="ECO:0000250"
FT DISULFID 154..214
FT /evidence="ECO:0000250"
FT DISULFID 186..196
FT /evidence="ECO:0000250"
FT DISULFID 229..247
FT /evidence="ECO:0000250"
FT DISULFID 259..271
FT /evidence="ECO:0000250"
FT DISULFID 266..284
FT /evidence="ECO:0000250"
FT DISULFID 278..293
FT /evidence="ECO:0000250"
FT DISULFID 327..453
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124,
FT ECO:0000255|PROSITE-ProRule:PRU00196, ECO:0000255|PROSITE-
FT ProRule:PRU00274, ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 365..381
FT /evidence="ECO:0000250"
FT DISULFID 373..444
FT /evidence="ECO:0000250"
FT DISULFID 467..531
FT /evidence="ECO:0000250"
FT DISULFID 495..510
FT /evidence="ECO:0000250"
FT DISULFID 521..550
FT /evidence="ECO:0000250"
SQ SEQUENCE 583 AA; 65620 MW; 8A390600223498AA CRC64;
MKLLHVFLLF LCFHLSFCKV TYTSQEDLVE KKCLAKKHTH LSCNKVFCQP WQICIEGTCI
CKLPYQCPKN GTTVCATNGR SFPTYCQQKS LECLRPGTKF LNNGTCTAEG KFSVSLKHGN
TDSEGIVEVK LVDQDKTMFI CKSSWSMREA NVACLDLGFQ QGADTQRRFK LSNLSINSTE
CLHVHCRGLE TSLAECTFTK RRTMGYQDLA DVVCYTQKAD SPTNDFFQCV NGKYISQMKA
CDGINDCGDQ SDELCCKACQ GKSFHCKSGV CIPSQYRCNG EVDCITGEDE VGCEGFASVA
QEETEILTAD MDAERRRIKS LLPKLSCGVK NRRHIRRKRI VGGKRAQLGD LPWQVGIKDA
SGITCGGIYI GGCWILTAAH CLRASKTHHY QIWTTVVDWI HPDRKRIVIE YVDRIIFHEN
YNAGTYQNDI ALMEMKKDGN KKDCELPRSI PACVPWSPYL FQPNDTCIVS GWGREKDNEK
VFSLQWGEVK LISNCSKFYG NRFYEKEMEC AGTYDGSIDA CKGDSGGPLV CMDANNVTYV
WGVVSWGENC GKPEFPGVYT KVANYFDWIS YHVGRPFISQ YNV
