ID G7P631_MACFA Unreviewed; 591 AA.
AC G7P631;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Complement factor I {ECO:0008006|Google:ProtNLM};
GN ORFNames=EGM_14609 {ECO:0000313|EMBL:EHH53899.1};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1] {ECO:0000313|EMBL:EHH53899.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CE-4 {ECO:0000313|EMBL:EHH53899.1};
RX PubMed=22002653; DOI=10.1038/nbt.1992;
RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT "Genome sequencing and comparison of two nonhuman primate animal models,
RT the cynomolgus and Chinese rhesus macaques.";
RL Nat. Biotechnol. 29:1019-1023(2011).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00196}.
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DR EMBL; CM001280; EHH53899.1; -; Genomic_DNA.
DR AlphaFoldDB; G7P631; -.
DR MEROPS; S01.199; -.
DR eggNOG; KOG3627; Eukaryota.
DR Proteomes; UP000009130; Chromosome 5.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
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; 3.30.60.30; -; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 2.
DR Gene3D; 3.10.250.10; SRCR-like domain; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR048722; CFAI_FIMAC_N.
DR InterPro; IPR048719; CFAI_KAZAL.
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 PANTHER; PTHR24264:SF40; HYALURONAN-BINDING PROTEIN 2; 1.
DR PANTHER; PTHR24264; TRYPSIN-RELATED; 1.
DR Pfam; PF21286; CFAI_FIMAC_N; 1.
DR Pfam; PF21287; CFAI_KAZAL; 1.
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; Kazal-type serine protease inhibitors; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 2.
DR SUPFAM; SSF56487; SRCR-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
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 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00196}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU363034};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..591
FT /note="Complement factor I"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003501906"
FT DOMAIN 60..108
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 114..215
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 348..582
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 186..196
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 229..247
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 241..256
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 259..271
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 266..284
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 278..293
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 591 AA; 66329 MW; FAAD560E806CC6AE CRC64;
MKLLHVFLLF LCFHLSFCKV TSTFQEDRVE KKCLAKKYTH LSCNKVFCQP WQRCIEGTCV
CKLPYQCPKN GTVVCATNGR SFPTYCQQKS LECLRPGTKF LNNGTCIAGG KFSVSLKHGN
TDSEGIVEVK LVDQDKAMFV CKSSWSMREA NVACLDLGFQ QGADSERRFK LSDLSINSTE
CLHVHCRGLE TSLAECTFTK RRTMDYQDLA DVVCYTQKAD SPTNDSFQCV NGKYISQTKA
CDGINDCGDQ SDELCCKACH GRSFHCKSDV CIPSQYRCNG EVDCITGDDE VGCEAARHPT
IQGKSILTEE ETEILTADMD AERRRIKSLL PKLSCGVKNR MHVRRKRIVG GKLAKLGDFP
WQVGIKDAKG ITCGGIYIGG CWVLTAAHCL SASKTHRYQI WTTVVDWIHP SIKDIVVEYA
DRIIFHENYN AGTYQNDIAL IKMKKEGNKK DCELPRSIPA CVPWSPYLFQ PDDTCIISGW
GREKDNEKVF SLRWGEVKLI SNCSKFYGNR FYEKEMECAG TYDGSIDACK GDSGGPLVCM
DANNVTYVWG VVSWGENCGK PEFPGVYTKV ANYFDWISYH VGRPLISQHN V
//
