ID K7ERG9_HUMAN Unreviewed; 260 AA. AC K7ERG9; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 16-JAN-2019, entry version 53. DE SubName: Full=Complement factor D {ECO:0000313|Ensembl:ENSP00000468253}; GN Name=CFD {ECO:0000313|Ensembl:ENSP00000468253}; 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:ENSP00000468253, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000468253, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M., RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [2] {ECO:0000213|PubMed:22905912} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22905912; DOI=10.1021/pr300539b; RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., RA Fischer-Posovszky P., Mariman E.C., Renes J.; RT "Resveratrol-induced changes of the human adipocyte secretion RT profile."; RL J. Proteome Res. 11:4733-4743(2012). RN [3] {ECO:0000313|Ensembl:ENSP00000468253} RP IDENTIFICATION. RG Ensembl; RL Submitted (NOV-2012) to UniProtKB. RN [4] {ECO:0000313|Ensembl:ENSP00000488580} RP IDENTIFICATION. RG Ensembl; RL Submitted (AUG-2015) to UniProtKB. CC -!- SIMILARITY: Belongs to the peptidase S1 family. CC {ECO:0000256|SAAS:SAAS00559343}. 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; AC112706; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC212840; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_001304264.1; NM_001317335.1. DR UniGene; Hs.155597; -. DR jPOST; K7ERG9; -. DR PRIDE; K7ERG9; -. DR Ensembl; ENST00000592860; ENSP00000468253; ENSG00000197766. DR Ensembl; ENST00000632706; ENSP00000488580; ENSG00000274619. DR GeneID; 1675; -. DR UCSC; uc060qro.1; human. DR CTD; 1675; -. DR EuPathDB; HostDB:ENSG00000197766.7; -. DR HGNC; HGNC:2771; CFD. DR OpenTargets; ENSG00000197766; -. DR eggNOG; KOG3627; Eukaryota. DR eggNOG; COG5640; LUCA. DR GeneTree; ENSGT00940000162255; -. DR OMA; NGGKKCG; -. DR OrthoDB; 1314811at2759; -. DR ChiTaRS; CFD; human. DR GenomeRNAi; 1675; -. DR Proteomes; UP000005640; Chromosome 19. DR Bgee; ENSG00000197766; Expressed in 194 organ(s), highest expression level in adipose tissue of abdominal region. DR ExpressionAtlas; K7ERG9; baseline and differential. DR GO; GO:0005615; C:extracellular space; IEA:Ensembl. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0006957; P:complement activation, alternative pathway; IEA:InterPro. DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl. DR CDD; cd00190; Tryp_SPc; 1. DR InterPro; IPR037561; Complement_factor_D. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR001314; Peptidase_S1A. DR InterPro; IPR001254; Trypsin_dom. DR InterPro; IPR018114; TRYPSIN_HIS. DR InterPro; IPR033116; TRYPSIN_SER. DR PANTHER; PTHR43890:SF17; PTHR43890:SF17; 1. DR Pfam; PF00089; Trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00020; Tryp_SPc; 1. DR SUPFAM; SSF50494; SSF50494; 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|SAAS:SAAS00037407}; KW Hydrolase {ECO:0000256|RuleBase:RU363034}; KW Protease {ECO:0000256|RuleBase:RU363034}; KW Proteomics identification {ECO:0000213|MaxQB:K7ERG9, KW ECO:0000213|PeptideAtlas:K7ERG9}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Serine protease {ECO:0000256|RuleBase:RU363034}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 260 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014099472. FT DOMAIN 33 260 Peptidase S1. FT {ECO:0000259|PROSITE:PS50240}. SQ SEQUENCE 260 AA; 27863 MW; 271B5A14D64E0990 CRC64; MHSWERLAVL VLLGAAACGE EAWAWAAPPR GRILGGREAE AHARPYMASV QLNGAHLCGG VLVAEQWVLS AAHCLEDAAD GKVQVLLGAH SLSQPEPSKR LYDVLRAVPH PDSQPDTIDH DLLLLQLSEK ATLGPAVRPL PWQRVDRDVA PGTLCDVAGW GIVNHAGRRP DSLQHVLLPV LDRATCNRRT HHDGAITERL MCAESNRRDS CKGDSGGPLV CGGVLEGVVT SGSRVCGNRK KPGIYTRVAS YAAWIDSVLA //