ID F6Y8L7_CALJA Unreviewed; 578 AA.
AC F6Y8L7;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 2.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Complement factor I {ECO:0000313|Ensembl:ENSCJAP00000007709.3};
GN Name=CFI {ECO:0000313|Ensembl:ENSCJAP00000007709.3};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000007709.3, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000007709.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000007709.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00196}.
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DR AlphaFoldDB; F6Y8L7; -.
DR Ensembl; ENSCJAT00000008151.4; ENSCJAP00000007709.3; ENSCJAG00000004249.6.
DR GeneTree; ENSGT00930000151042; -.
DR Proteomes; UP000008225; Chromosome 3.
DR Bgee; ENSCJAG00000004249; Expressed in liver and 6 other cell types or tissues.
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; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000008225};
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..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..578
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015329887"
FT DOMAIN 62..110
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 116..217
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 335..569
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 188..198
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 231..249
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 243..258
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 261..273
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 268..286
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 280..295
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 578 AA; 64839 MW; 2D29FE1C80D6E3E5 CRC64;
MLLHVFLLFL CFHLSFCQVS LRLHTAQEEL VEKKCLAKKY THLSCNKVFC QPWQKCIEGT
CICKLPYQCP KNGTSACATN GRNFLTYCQL KSLECLRPGT KFLNNGTCTA EGKFSVSLKY
GSTDSEGIVE VKLVDQDKTM FICKSSWTMR EANVACLDLG FQQGADTQRS FQSSNLSINA
TECLHVHCRG LETSLTECTF TKRRTVGYQD LADVVCYTQK ADSPTDDSFQ CVNGKYISQA
EACNGINDCG DQSDELCCKA CRGKSFHCKS GVCIPSQYRC NGEVDCITGE DEVGCEEETE
ILTADMDAER RRIKSLLPTI SCGIKNRMHI RRKRVVGGKP AQLGDLPWQV GIKDANGITC
GGVYIGGCWI LTAAHCLRAS KTHRYQIWTT VVDWVKPDRK RIVVELVNRI IFHENYDGHT
YQNDIALIEM KKEGNKKDCE LPHSVPACVP WSPYLFQPND TCIVSGWGRE KENKKVFSLQ
WGEVKLISNC SKFYGNRFYE KEMECAGTYD GSIDACKGDS GGPLVCMDAN NVTYIWGVVS
WGENCGKPEF PGVYTKVANY FDWISYHVGR PLISQHNT
//
