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Database: UniProt
Entry: Q5R5A4
LinkDB: Q5R5A4
Original site: Q5R5A4 
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   08-MAY-2019, entry version 82.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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
CC       in 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-
CC       linked. The fully processed and mature protein circulates as a
CC       zymogen, and is allosterically activated by substrate-induced
CC       remodeling of the active site (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC   -!- TISSUE SPECIFICITY: Plasma.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
DR   EMBL; CR860960; CAH93062.1; -; mRNA.
DR   RefSeq; NP_001127624.1; NM_001134152.1.
DR   SMR; Q5R5A4; -.
DR   MEROPS; S01.199; -.
DR   PRIDE; Q5R5A4; -.
DR   GeneID; 100174703; -.
DR   CTD; 3426; -.
DR   InParanoid; Q5R5A4; -.
DR   Proteomes; UP000001595; Unplaced.
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:InterPro.
DR   GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   CDD; cd00112; LDLa; 2.
DR   CDD; cd00190; Tryp_SPc; 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; 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   Complete proteome; Disulfide bond; Glycoprotein; Hydrolase; Immunity;
KW   Innate immunity; Metal-binding; Protease; Reference proteome; Repeat;
KW   Secreted; Serine protease; Signal.
FT   SIGNAL        1     18       {ECO:0000250}.
FT   CHAIN        19    583       Complement factor I.
FT                                /FTId=PRO_0000285861.
FT   CHAIN        19    335       Complement factor I heavy chain.
FT                                /FTId=PRO_0000285862.
FT   CHAIN       340    583       Complement factor I light chain.
FT                                /FTId=PRO_0000285863.
FT   DOMAIN       55    108       Kazal-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00798}.
FT   DOMAIN      114    212       SRCR. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00196}.
FT   DOMAIN      213    257       LDL-receptor class A 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      258    294       LDL-receptor class A 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      340    574       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   CA_BIND     239    253       1. {ECO:0000250}.
FT   CA_BIND     276    290       2. {ECO:0000250}.
FT   ACT_SITE    380    380       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    429    429       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    525    525       Charge relay system. {ECO:0000250}.
FT   CARBOHYD     70     70       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    103    103       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    173    173       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    177    177       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    464    464       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    494    494       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    536    536       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     33    255       {ECO:0000250}.
FT   DISULFID     43     54       {ECO:0000250}.
FT   DISULFID     48     59       {ECO:0000250}.
FT   DISULFID     61     93       {ECO:0000250}.
FT   DISULFID     67     86       {ECO:0000250}.
FT   DISULFID     75    106       {ECO:0000250}.
FT   DISULFID    141    181       {ECO:0000250}.
FT   DISULFID    154    214       {ECO:0000250}.
FT   DISULFID    186    196       {ECO:0000250}.
FT   DISULFID    229    247       {ECO:0000250}.
FT   DISULFID    259    271       {ECO:0000250}.
FT   DISULFID    266    284       {ECO:0000250}.
FT   DISULFID    278    293       {ECO:0000250}.
FT   DISULFID    327    453       Interchain (between heavy and light
FT                                chains). {ECO:0000255|PROSITE-
FT                                ProRule:PRU00124, ECO:0000255|PROSITE-
FT                                ProRule:PRU00196, ECO:0000255|PROSITE-
FT                                ProRule:PRU00274, ECO:0000255|PROSITE-
FT                                ProRule:PRU00798}.
FT   DISULFID    365    381       {ECO:0000250}.
FT   DISULFID    373    444       {ECO:0000250}.
FT   DISULFID    467    531       {ECO:0000250}.
FT   DISULFID    495    510       {ECO:0000250}.
FT   DISULFID    521    550       {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
//
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