ID   E7ETH0_HUMAN            Unreviewed;       591 AA.
AC   E7ETH0;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   16-JAN-2019, entry version 75.
DE   SubName: Full=Complement factor I {ECO:0000313|Ensembl:ENSP00000378131};
GN   Name=CFI {ECO:0000313|Ensembl:ENSP00000378131};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000378131, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000378131, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 4.";
RL   Nature 434:724-731(2005).
RN   [2] {ECO:0000313|Ensembl:ENSP00000378131}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2011) to UniProtKB.
RN   [3] {ECO:0000213|PubMed:24275569}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000256|SAAS:SAAS00559343}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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DR   EMBL; AC126283; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   ProteinModelPortal; E7ETH0; -.
DR   EPD; E7ETH0; -.
DR   jPOST; E7ETH0; -.
DR   MaxQB; E7ETH0; -.
DR   PeptideAtlas; E7ETH0; -.
DR   PRIDE; E7ETH0; -.
DR   Ensembl; ENST00000394635; ENSP00000378131; ENSG00000205403.
DR   UCSC; uc011cft.3; human.
DR   EuPathDB; HostDB:ENSG00000205403.12; -.
DR   HGNC; HGNC:5394; CFI.
DR   OpenTargets; ENSG00000205403; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   eggNOG; COG5640; LUCA.
DR   GeneTree; ENSGT00930000151042; -.
DR   OMA; GREKDNQ; -.
DR   OrthoDB; 1314811at2759; -.
DR   PhylomeDB; E7ETH0; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   Bgee; ENSG00000205403; Expressed in 177 organ(s), highest expression level in visceral pleura.
DR   ExpressionAtlas; E7ETH0; baseline and differential.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   CDD; cd00112; LDLa; 2.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 3.10.250.10; -; 1.
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   1: Evidence at protein level;
KW   Complete proteome {ECO:0000313|Proteomes:UP000005640};
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00124,
KW   ECO:0000256|SAAS:SAAS00037407};
KW   Hydrolase {ECO:0000256|RuleBase:RU363034};
KW   Protease {ECO:0000256|RuleBase:RU363034};
KW   Proteomics identification {ECO:0000213|MaxQB:E7ETH0,
KW   ECO:0000213|PeptideAtlas:E7ETH0};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Serine protease {ECO:0000256|RuleBase:RU363034};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     18       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        19    591       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003219005.
FT   DOMAIN       60    108       Kazal-like.
FT                                {ECO:0000259|PROSITE:PS51465}.
FT   DOMAIN      114    215       SRCR. {ECO:0000259|PROSITE:PS50287}.
FT   DOMAIN      348    582       Peptidase S1.
FT                                {ECO:0000259|PROSITE:PS50240}.
FT   DISULFID    186    196       {ECO:0000256|PROSITE-ProRule:PRU00196}.
FT   DISULFID    229    247       {ECO:0000256|PROSITE-ProRule:PRU00124}.
FT   DISULFID    241    256       {ECO:0000256|PROSITE-ProRule:PRU00124}.
FT   DISULFID    259    271       {ECO:0000256|PROSITE-ProRule:PRU00124}.
FT   DISULFID    266    284       {ECO:0000256|PROSITE-ProRule:PRU00124}.
FT   DISULFID    278    293       {ECO:0000256|PROSITE-ProRule:PRU00124}.
SQ   SEQUENCE   591 AA;  66625 MW;  1ADD28D0BFCC4A09 CRC64;
     MKLLHVFLLF LCFHLRFCKV TYTSQEDLVE KKCLAKKYTH LSCDKVFCQP WQRCIEGTCV
     CKLPYQCPKN GTAVCATNRR SFPTYCQQKS LECLHPGTKF LNNGTCTAEG KFSVSLKHGN
     TDSEGIVEVK LVDQDKTMFI CKSSWSMREA NVACLDLGFQ QGADTQRRFK LSDLSINSTE
     CLHVHCRGLE TSLAECTFTK RRTMGYQDFA DVVCYTQKAD SPMDDFFQCV NGKYISQMKA
     CDGINDCGDQ SDELCCKACQ GKGFHCKSGV CIPSQYQCNG EVDCITGEDE VGCAAARHPT
     IQGFASVTQE ETEILTADMD AERRRIKSLL PKLSCGVKNR MHIRRKRIVG GKRAQLGDLP
     WQVAIKDASG ITCGGIYIGG CWILTAAHCL RASKTHRYQI WTTVVDWIHP DLKRIVIEYV
     DRIIFHENYN AGTYQNDIAL IEMKKDGNKK DCELPRSIPA CVPWSPYLFQ PNDTCIVSGW
     GREKDNERVF SLQWGEVKLI SNCSKFYGNR FYEKEMECAG TYDGSIDACK GDSGGPLVCM
     DANNVTYVWG VVSWGENCGK PEFPGVYTKV ANYFDWISYH VGRPFISQYN V
//