ID G3XAM2_HUMAN Unreviewed; 576 AA. AC G3XAM2; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 13-FEB-2019, entry version 78. DE SubName: Full=Complement factor I {ECO:0000313|Ensembl:ENSP00000427438}; DE SubName: Full=Complement factor I, isoform CRA_b {ECO:0000313|EMBL:EAX06251.1}; GN Name=CFI {ECO:0000313|EMBL:EAX06251.1, GN ECO:0000313|Ensembl:ENSP00000427438}; GN ORFNames=hCG_21044 {ECO:0000313|EMBL:EAX06251.1}; 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:ENSP00000427438, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|EMBL:EAX06251.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=11181995; DOI=10.1126/science.1058040; RA Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G., RA Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., RA Amanatides P., Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., RA Kodira C.D., Zheng X.H., Chen L., Skupski M., Subramanian G., RA Thomas P.D., Zhang J., Gabor Miklos G.L., Nelson C., Broder S., RA Clark A.G., Nadeau J., McKusick V.A., Zinder N., Levine A.J., RA Roberts R.J., Simon M., Slayman C., Hunkapiller M., Bolanos R., RA Delcher A., Dew I., Fasulo D., Flanigan M., Florea L., Halpern A., RA Hannenhalli S., Kravitz S., Levy S., Mobarry C., Reinert K., RA Remington K., Abu-Threideh J., Beasley E., Biddick K., Bonazzi V., RA Brandon R., Cargill M., Chandramouliswaran I., Charlab R., RA Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K., RA Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., RA Guan P., Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., RA Lai Z., Lei Y., Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., RA Milshina N., Moore H.M., Naik A.K., Narayan V.A., Neelam B., RA Nusskern D., Rusch D.B., Salzberg S., Shao W., Shue B., Sun J., RA Wang Z., Wang A., Wang X., Wang J., Wei M., Wides R., Xiao C., Yan C., RA Yao A., Ye J., Zhan M., Zhang W., Zhang H., Zhao Q., Zheng L., RA Zhong F., Zhong W., Zhu S., Zhao S., Gilbert D., Baumhueter S., RA Spier G., Carter C., Cravchik A., Woodage T., Ali F., An H., Awe A., RA Baldwin D., Baden H., Barnstead M., Barrow I., Beeson K., Busam D., RA Carver A., Center A., Cheng M.L., Curry L., Danaher S., Davenport L., RA Desilets R., Dietz S., Dodson K., Doup L., Ferriera S., Garg N., RA Gluecksmann A., Hart B., Haynes J., Haynes C., Heiner C., Hladun S., RA Hostin D., Houck J., Howland T., Ibegwam C., Johnson J., Kalush F., RA Kline L., Koduru S., Love A., Mann F., May D., McCawley S., RA McIntosh T., McMullen I., Moy M., Moy L., Murphy B., Nelson K., RA Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M., RA Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C., RA Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., RA Tse S., Vech C., Wang G., Wetter J., Williams S., Williams M., RA Windsor S., Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., RA Guigo R., Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., RA Mi H., Lazareva B., Hatton T., Narechania A., Diemer K., RA Muruganujan A., Guo N., Sato S., Bafna V., Istrail S., Lippert R., RA Schwartz R., Walenz B., Yooseph S., Allen D., Basu A., Baxendale J., RA Blick L., Caminha M., Carnes-Stine J., Caulk P., Chiang Y.H., RA Coyne M., Dahlke C., Mays A., Dombroski M., Donnelly M., Ely D., RA Esparham S., Fosler C., Gire H., Glanowski S., Glasser K., Glodek A., RA Gorokhov M., Graham K., Gropman B., Harris M., Heil J., Henderson S., RA Hoover J., Jennings D., Jordan C., Jordan J., Kasha J., Kagan L., RA Kraft C., Levitsky A., Lewis M., Liu X., Lopez J., Ma D., Majoros W., RA McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N., Nodell M., RA Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J., RA Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E., RA Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.; RT "The sequence of the human genome."; RL Science 291:1304-1351(2001). RN [2] {ECO:0000313|Ensembl:ENSP00000427438, 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 [3] {ECO:0000313|EMBL:EAX06251.1} RP NUCLEOTIDE SEQUENCE. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|Ensembl:ENSP00000427438} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. RN [5] {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}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AC126283; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471057; EAX06251.1; -; Genomic_DNA. DR RefSeq; NP_001317964.1; NM_001331035.1. DR UniGene; Hs.312485; -. DR jPOST; G3XAM2; -. DR MaxQB; G3XAM2; -. DR Ensembl; ENST00000512148; ENSP00000427438; ENSG00000205403. DR GeneID; 3426; -. DR UCSC; uc062yzd.1; human. DR CTD; 3426; -. 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 OrthoDB; 1314811at2759; -. DR GenomeRNAi; 3426; -. DR Proteomes; UP000005640; Chromosome 4. DR Bgee; ENSG00000205403; Expressed in 177 organ(s), highest expression level in visceral pleura. DR ExpressionAtlas; G3XAM2; 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:G3XAM2, KW ECO:0000213|PeptideAtlas:G3XAM2}; 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 19 576 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015091879. FT DOMAIN 60 108 Kazal-like. FT {ECO:0000259|PROSITE:PS51465}. FT DOMAIN 114 215 SRCR. {ECO:0000259|PROSITE:PS50287}. FT DOMAIN 333 567 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 576 AA; 65060 MW; AB001AED6C1BF94A 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 VGCAEETEIL TADMDAERRR IKSLLPKLSC GVKNRMHIRR KRIVGGKRAQ LGDLPWQVAI KDASGITCGG IYIGGCWILT AAHCLRASKT HRYQIWTTVV DWIHPDLKRI VIEYVDRIIF HENYNAGTYQ NDIALIEMKK DGNKKDCELP RSIPACVPWS PYLFQPNDTC IVSGWGREKD NERVFSLQWG EVKLISNCSK FYGNRFYEKE MECAGTYDGS IDACKGDSGG PLVCMDANNV TYVWGVVSWG ENCGKPEFPG VYTKVANYFD WISYHVGRPF ISQYNV //