PROP_HUMAN
ID PROP_HUMAN Reviewed; 469 AA.
AC P27918; O15134; O15135; O15136; O75826;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Properdin;
DE AltName: Full=Complement factor P;
DE Flags: Precursor;
GN Name=CFP; Synonyms=PFC;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2009915; DOI=10.1002/eji.1830210333;
RA Nolan K.F., Schwaeble W., Kaluz S., Dierich M.P., Reid K.B.M.;
RT "Molecular cloning of the cDNA coding for properdin, a positive regulator
RT of the alternative pathway of human complement.";
RL Eur. J. Immunol. 21:771-776(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1417780; DOI=10.1042/bj2870291;
RA Nolan K.F., Kaluz S., Higgins J.M., Goundis D., Reid K.B.M.;
RT "Characterization of the human properdin gene.";
RL Biochem. J. 287:291-297(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1431505;
RA Weiler J.M., Maves K.K.;
RT "Detection of properdin mRNA in human peripheral blood monocytes and
RT spleen.";
RL J. Lab. Clin. Med. 120:762-766(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PFC TYPE-II DEFICIENCY
RP TRP-100.
RX PubMed=8530058; DOI=10.1006/geno.1995.1208;
RA Westberg J., Fredrikson G.N., Truedsson L., Sjoeholm A.G., Uhlen M.;
RT "Sequence-based analysis of properdin deficiency: identification of point
RT mutations in two phenotypic forms of an X-linked immunodeficiency.";
RL Genomics 29:1-8(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS MET-53; LEU-204 AND
RP SER-250.
RG SeattleSNPs variation discovery resource;
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP GLYCOSYLATION AT TRP-83; TRP-86; TRP-139; TRP-142; TRP-145; TRP-196;
RP TRP-199; TRP-260; TRP-263; TRP-321; TRP-324; TRP-382; TRP-385 AND TRP-388.
RX PubMed=10878002; DOI=10.1074/jbc.m001732200;
RA Hartmann S., Hofsteenge J.;
RT "Properdin, the positive regulator of complement, is highly C-
RT mannosylated.";
RL J. Biol. Chem. 275:28569-28574(2000).
RN [9]
RP GLYCOSYLATION AT THR-92; THR-151; SER-208 AND THR-272.
RX PubMed=12096136; DOI=10.1074/mcp.m100011-mcp200;
RA Gonzalez de Peredo A., Klein D., Macek B., Hess D., Peter-Katalinic J.,
RA Hofsteenge J.;
RT "C-mannosylation and O-fucosylation of thrombospondin type 1 repeats.";
RL Mol. Cell. Proteomics 1:11-18(2002).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-428.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [11]
RP GLYCOSYLATION AT ASN-428.
RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [12]
RP FUNCTION, AND SUBUNIT.
RX PubMed=20382442; DOI=10.1016/j.imbio.2010.02.002;
RA Ferreira V.P., Cortes C., Pangburn M.K.;
RT "Native polymeric forms of properdin selectively bind to targets and
RT promote activation of the alternative pathway of complement.";
RL Immunobiology 215:932-940(2010).
RN [13]
RP X-RAY SCATTERING SOLUTION STRUCTURE OF 28-469 IN DIMERIC AND TRIMERIC
RP FORMS, TSP DOMAINS, AND SUBUNIT.
RX PubMed=15491616; DOI=10.1016/j.jmb.2004.09.001;
RA Sun Z., Reid K.B., Perkins S.J.;
RT "The dimeric and trimeric solution structures of the multidomain complement
RT protein properdin by X-ray scattering, analytical ultracentrifugation and
RT constrained modelling.";
RL J. Mol. Biol. 343:1327-1343(2004).
RN [14] {ECO:0007744|PDB:6RUR}
RP X-RAY CRYSTALLOGRAPHY (6.0 ANGSTROMS) OF 28-191 AND 256-469 IN COMPLEX WITH
RP COMPLEMENT C3 BETA CHAIN; COMPLEMENT FACTOR B BB FRAGMENT AND
RP STAPHYLOCOCCUS AUREUS PROTEIN SCN, FUNCTION, INTERACTION WITH COMPLEMENT C3
RP BETA CHAIN, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, VARIANT PFD LYS-244, AND
RP CHARACTERIZATION OF VARIANT PFD LYS-244.
RX PubMed=28264884; DOI=10.15252/embj.201696173;
RA Pedersen D.V., Roumenina L., Jensen R.K., Gadeberg T.A., Marinozzi C.,
RA Picard C., Rybkine T., Thiel S., Soerensen U.B., Stover C.,
RA Fremeaux-Bacchi V., Andersen G.R.;
RT "Functional and structural insight into properdin control of complement
RT alternative pathway amplification.";
RL EMBO J. 36:1084-1099(2017).
RN [15] {ECO:0007744|PDB:6RUS}
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 28-191 AND 256-469 IN COMPLEX WITH
RP COMPLEMENT C3 BETA CHAIN; COMPLEMENT FACTOR B BB FRAGMENT AND
RP STAPHYLOCOCCUS AUREUS PROTEIN SCN, IDENTIFICATION BY MASS SPECTROMETRY,
RP FUNCTION, SUBUNIT, INTERACTION WITH COMPLEMENT C3 BETA CHAIN AND COMPLEMENT
RP FACTOR B BB FRAGMENT, SUBCELLULAR LOCATION, DOMAIN, GLYCOSYLATION AT
RP TRP-83; TRP-86; THR-92; TRP-139; TRP-142; TRP-145; THR-151; TRP-196;
RP TRP-199; TRP-202; SER-208; TRP-260; TRP-263; THR-272; TRP-321; TRP-324;
RP TRP-382; TRP-385 AND TRP-388, DISULFIDE BOND, VARIANT PFD TYR-32,
RP CHARACTERIZATION OF VARIANTS PFD TYR-32; ARG-343 AND ASP-414, AND
RP MUTAGENESIS OF LEU-47; LEU-58; GLU-244; LEU-275; ARG-329; ARG-330; ARG-351;
RP ARG-353; ARG-359; 364-GLN-GLN-365 AND LEU-456.
RX PubMed=31507604; DOI=10.3389/fimmu.2019.02007;
RA Pedersen D.V., Gadeberg T.A.F., Thomas C., Wang Y., Joram N., Jensen R.K.,
RA Mazarakis S.M.M., Revel M., El Sissy C., Petersen S.V., Lindorff-Larsen K.,
RA Thiel S., Laursen N.S., Fremeaux-Bacchi V., Andersen G.R.;
RT "Structural Basis for Properdin Oligomerization and Convertase Stimulation
RT in the Human Complement System.";
RL Front. Immunol. 10:2007-2007(2019).
RN [16]
RP VARIANT PFD ASP-414.
RX PubMed=8871668;
RA Fredrikson G.N., Westberg J., Kuijper E.J., Tijssen C.C., Sjoeholm A.G.,
RA Uhlen M., Truedsson L.;
RT "Molecular characterization of properdin deficiency type III: dysfunction
RT produced by a single point mutation in exon 9 of the structural gene
RT causing a tyrosine to aspartic acid interchange.";
RL J. Immunol. 157:3666-3671(1996).
RN [17]
RP VARIANT PFD ARG-343.
RX PubMed=9710744; DOI=10.1023/a:1027385806871;
RA Fredrikson G.N., Gullstrand B., Westberg J., Sjoeholm A.G., Uhlen M.,
RA Truedsson L.;
RT "Expression of properdin in complete and incomplete deficiency: normal in
RT vitro synthesis by monocytes in two cases with properdin deficiency type II
RT due to distinct mutations.";
RL J. Clin. Immunol. 18:272-282(1998).
RN [18]
RP VARIANT PFD VAL-298.
RX PubMed=10909851; DOI=10.1038/sj.ejhg.5200496;
RA van den Bogaard R., Fijen C.A.P., Schipper M.G.J., de Galan L.,
RA Kuijper E.J., Mannens M.M.A.M.;
RT "Molecular characterisation of 10 Dutch properdin type I deficient
RT families: mutation analysis and X-inactivation studies.";
RL Eur. J. Hum. Genet. 8:513-518(2000).
RN [19]
RP VARIANT [LARGE SCALE ANALYSIS] ILE-3.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: A positive regulator of the alternate pathway (AP) of
CC complement (PubMed:20382442, PubMed:28264884). It binds to and
CC stabilizes the C3- and C5-convertase enzyme complexes (PubMed:20382442,
CC PubMed:28264884). Inhibits CFI-CFH mediated degradation of Complement
CC C3 beta chain (C3b) (PubMed:31507604). {ECO:0000269|PubMed:20382442,
CC ECO:0000269|PubMed:28264884, ECO:0000269|PubMed:31507604}.
CC -!- SUBUNIT: In plasma, properdin exists as dimers, trimers or tetramers in
CC the relative proportions of 26:54:20 (PubMed:20382442, PubMed:15491616,
CC PubMed:28264884, PubMed:31507604). Interacts with the pro-C3-convertase
CC enzyme complex (C3b-Bb) comprised of Complement C3 beta chain (C3b) and
CC the Complement factor B Bb fragment (Bb), where it binds (via its TSP
CC type-1 5 domain) with C3b and Bb (PubMed:28264884, PubMed:31507604).
CC This interaction stabilizes the complex and allows it to become the
CC active C3-convertase enzyme complex (C3b-Bb-FP) (PubMed:28264884,
CC PubMed:31507604). Interacts with C3b (PubMed:28264884,
CC PubMed:31507604). Interacts with CFB (PubMed:31507604).
CC {ECO:0000269|PubMed:15491616, ECO:0000269|PubMed:20382442,
CC ECO:0000269|PubMed:28264884, ECO:0000269|PubMed:31507604}.
CC -!- INTERACTION:
CC P27918; P0C7Q2: ARMS2; NbExp=8; IntAct=EBI-9038570, EBI-21986906;
CC P27918; Q9H503-2: BANF2; NbExp=3; IntAct=EBI-9038570, EBI-11977289;
CC P27918; Q8IYR0: CFAP206; NbExp=3; IntAct=EBI-9038570, EBI-749051;
CC P27918; Q92496-1: CFHR4; NbExp=2; IntAct=EBI-9038570, EBI-22033617;
CC P27918; Q92496-3: CFHR4; NbExp=2; IntAct=EBI-9038570, EBI-22033638;
CC P27918; PRO_0000023526 [P02741]: CRP; NbExp=2; IntAct=EBI-9038570, EBI-22033103;
CC P27918; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-9038570, EBI-3867333;
CC P27918; Q5TD97: FHL5; NbExp=3; IntAct=EBI-9038570, EBI-750641;
CC P27918; O75344: FKBP6; NbExp=4; IntAct=EBI-9038570, EBI-744771;
CC P27918; P57678: GEMIN4; NbExp=3; IntAct=EBI-9038570, EBI-356700;
CC P27918; Q9Y223-2: GNE; NbExp=3; IntAct=EBI-9038570, EBI-11975289;
CC P27918; Q96MH2: HEXIM2; NbExp=3; IntAct=EBI-9038570, EBI-5460660;
CC P27918; P49639: HOXA1; NbExp=3; IntAct=EBI-9038570, EBI-740785;
CC P27918; Q7L273: KCTD9; NbExp=3; IntAct=EBI-9038570, EBI-4397613;
CC P27918; Q2WGJ6: KLHL38; NbExp=3; IntAct=EBI-9038570, EBI-6426443;
CC P27918; Q8IUC1: KRTAP11-1; NbExp=3; IntAct=EBI-9038570, EBI-1052037;
CC P27918; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-9038570, EBI-10176379;
CC P27918; Q9BYR8: KRTAP3-1; NbExp=3; IntAct=EBI-9038570, EBI-9996449;
CC P27918; Q3LI66: KRTAP6-2; NbExp=5; IntAct=EBI-9038570, EBI-11962084;
CC P27918; Q5T7P2: LCE1A; NbExp=3; IntAct=EBI-9038570, EBI-11962058;
CC P27918; Q17RB8: LONRF1; NbExp=3; IntAct=EBI-9038570, EBI-2341787;
CC P27918; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-9038570, EBI-10172526;
CC P27918; P05164: MPO; NbExp=4; IntAct=EBI-9038570, EBI-2556173;
CC P27918; Q9HC98-4: NEK6; NbExp=3; IntAct=EBI-9038570, EBI-11750983;
CC P27918; Q86UR1-2: NOXA1; NbExp=3; IntAct=EBI-9038570, EBI-12025760;
CC P27918; O43741: PRKAB2; NbExp=3; IntAct=EBI-9038570, EBI-1053424;
CC P27918; Q6P9E2: RECK; NbExp=3; IntAct=EBI-9038570, EBI-10253121;
CC P27918; Q92922: SMARCC1; NbExp=3; IntAct=EBI-9038570, EBI-355653;
CC P27918; Q99932-2: SPAG8; NbExp=4; IntAct=EBI-9038570, EBI-11959123;
CC P27918; O75716: STK16; NbExp=3; IntAct=EBI-9038570, EBI-749295;
CC P27918; O95231: VENTX; NbExp=5; IntAct=EBI-9038570, EBI-10191303;
CC P27918; Q9Y3S2: ZNF330; NbExp=3; IntAct=EBI-9038570, EBI-373456;
CC P27918; Q96IQ9: ZNF414; NbExp=3; IntAct=EBI-9038570, EBI-744257;
CC P27918; Q8C567: Ncr1; Xeno; NbExp=2; IntAct=EBI-9038570, EBI-11707971;
CC PRO_0000035863; O76036: NCR1; NbExp=5; IntAct=EBI-15183949, EBI-13915737;
CC PRO_0000035863; Q8C567: Ncr1; Xeno; NbExp=3; IntAct=EBI-15183949, EBI-11707971;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28264884,
CC ECO:0000269|PubMed:31507604}.
CC -!- DOMAIN: TSP type-1 domain 0 binds to TSP type-1 domain 4, and TSP type-
CC 1 domain 1 binds to TSP type-1 domain 6 (PubMed:15491616,
CC PubMed:28264884, PubMed:31507604). These interactions mediate
CC multimerization (PubMed:15491616, PubMed:28264884, PubMed:31507604).
CC {ECO:0000269|PubMed:15491616, ECO:0000269|PubMed:28264884,
CC ECO:0000269|PubMed:31507604}.
CC -!- DISEASE: Properdin deficiency (PFD) [MIM:312060]: Results in higher
CC susceptibility to bacterial infections; especially to meningococcal
CC infections. Three phenotypes have been reported: complete deficiency
CC (type I), incomplete deficiency (type II), and dysfunction of properdin
CC (type III). {ECO:0000269|PubMed:10909851, ECO:0000269|PubMed:28264884,
CC ECO:0000269|PubMed:31507604, ECO:0000269|PubMed:8871668,
CC ECO:0000269|PubMed:9710744}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- WEB RESOURCE: Name=CFPbase; Note=CFP mutation db;
CC URL="http://structure.bmc.lu.se/idbase/CFPbase/";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/pfc/";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Properdin entry;
CC URL="https://en.wikipedia.org/wiki/Properdin";
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DR EMBL; X57748; CAA40914.1; -; mRNA.
DR EMBL; X70872; CAA50220.1; -; Genomic_DNA.
DR EMBL; M83652; AAA36489.1; -; mRNA.
DR EMBL; AF005664; AAB63279.1; -; Genomic_DNA.
DR EMBL; AF005665; AAB63280.1; -; Genomic_DNA.
DR EMBL; AF005666; AAC51626.1; -; Genomic_DNA.
DR EMBL; AF005668; AAB62886.1; -; Genomic_DNA.
DR EMBL; AF005667; AAB62886.1; JOINED; Genomic_DNA.
DR EMBL; AY297813; AAP43692.1; -; Genomic_DNA.
DR EMBL; AL009172; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015756; AAH15756.1; -; mRNA.
DR CCDS; CCDS14282.1; -.
DR PIR; S29126; S29126.
DR RefSeq; NP_001138724.1; NM_001145252.1.
DR RefSeq; NP_002612.1; NM_002621.2.
DR PDB; 1W0R; X-ray; -; A/B=28-469.
DR PDB; 1W0S; X-ray; -; A/B/C=28-469.
DR PDB; 6RUR; X-ray; 6.00 A; A=28-255, B=256-469.
DR PDB; 6RUS; X-ray; 2.80 A; A=28-255, B=256-469.
DR PDB; 6RUV; X-ray; 6.15 A; U/X=28-191, V/Y=256-469.
DR PDB; 6RV6; X-ray; 3.51 A; A=28-191, B=256-469.
DR PDB; 6S08; X-ray; 2.03 A; A=256-469, B=26-132.
DR PDB; 6S0A; X-ray; 2.52 A; A=256-469, B=26-191.
DR PDB; 6S0B; X-ray; 2.31 A; A=256-469, B=26-132.
DR PDB; 6SEJ; X-ray; 3.50 A; A=28-191, B=256-469.
DR PDB; 7B26; X-ray; 3.40 A; A=1-134, B=256-469.
DR PDBsum; 1W0R; -.
DR PDBsum; 1W0S; -.
DR PDBsum; 6RUR; -.
DR PDBsum; 6RUS; -.
DR PDBsum; 6RUV; -.
DR PDBsum; 6RV6; -.
DR PDBsum; 6S08; -.
DR PDBsum; 6S0A; -.
DR PDBsum; 6S0B; -.
DR PDBsum; 6SEJ; -.
DR PDBsum; 7B26; -.
DR AlphaFoldDB; P27918; -.
DR SASBDB; P27918; -.
DR SMR; P27918; -.
DR BioGRID; 111222; 46.
DR ComplexPortal; CPX-5602; Alternative pathway pathogen cell-bound C3 convertase complex C3bBbP.
DR ComplexPortal; CPX-5605; Alternative pathway pathogen cell-bound C5 convertase complex C3bBbC3bP.
DR IntAct; P27918; 49.
DR STRING; 9606.ENSP00000247153; -.
DR GlyGen; P27918; 20 sites, 1 N-linked glycan (1 site).
DR iPTMnet; P27918; -.
DR PhosphoSitePlus; P27918; -.
DR BioMuta; CFP; -.
DR DMDM; 464473; -.
DR jPOST; P27918; -.
DR MassIVE; P27918; -.
DR PaxDb; P27918; -.
DR PeptideAtlas; P27918; -.
DR PRIDE; P27918; -.
DR ProteomicsDB; 54426; -.
DR ABCD; P27918; 21 sequenced antibodies.
DR Antibodypedia; 11427; 530 antibodies from 31 providers.
DR DNASU; 5199; -.
DR Ensembl; ENST00000247153.7; ENSP00000247153.3; ENSG00000126759.14.
DR Ensembl; ENST00000396992.8; ENSP00000380189.3; ENSG00000126759.14.
DR GeneID; 5199; -.
DR KEGG; hsa:5199; -.
DR MANE-Select; ENST00000396992.8; ENSP00000380189.3; NM_001145252.3; NP_001138724.1.
DR UCSC; uc004dig.5; human.
DR CTD; 5199; -.
DR DisGeNET; 5199; -.
DR GeneCards; CFP; -.
DR HGNC; HGNC:8864; CFP.
DR HPA; ENSG00000126759; Group enriched (bone marrow, lymphoid tissue).
DR MalaCards; CFP; -.
DR MIM; 300383; gene.
DR MIM; 312060; phenotype.
DR neXtProt; NX_P27918; -.
DR OpenTargets; ENSG00000126759; -.
DR Orphanet; 2966; Properdin deficiency.
DR PharmGKB; PA33206; -.
DR VEuPathDB; HostDB:ENSG00000126759; -.
DR eggNOG; KOG4475; Eukaryota.
DR GeneTree; ENSGT00940000161209; -.
DR InParanoid; P27918; -.
DR OMA; RWRTCKG; -.
DR OrthoDB; 304371at2759; -.
DR PhylomeDB; P27918; -.
DR TreeFam; TF315491; -.
DR PathwayCommons; P27918; -.
DR Reactome; R-HSA-173736; Alternative complement activation.
DR Reactome; R-HSA-174577; Activation of C3 and C5.
DR Reactome; R-HSA-5083635; Defective B3GALTL causes PpS.
DR Reactome; R-HSA-5173214; O-glycosylation of TSR domain-containing proteins.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-977606; Regulation of Complement cascade.
DR SignaLink; P27918; -.
DR BioGRID-ORCS; 5199; 10 hits in 697 CRISPR screens.
DR ChiTaRS; CFP; human.
DR EvolutionaryTrace; P27918; -.
DR GenomeRNAi; 5199; -.
DR Pharos; P27918; Tbio.
DR PRO; PR:P27918; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P27918; protein.
DR Bgee; ENSG00000126759; Expressed in granulocyte and 97 other tissues.
DR ExpressionAtlas; P27918; baseline and differential.
DR Genevisible; P27918; HS.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IPI:ComplexPortal.
DR GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
DR GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
DR GO; GO:0006956; P:complement activation; IC:ComplexPortal.
DR GO; GO:0006957; P:complement activation, alternative pathway; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; TAS:ProtInc.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0050778; P:positive regulation of immune response; IC:ComplexPortal.
DR GO; GO:1903028; P:positive regulation of opsonization; IC:ComplexPortal.
DR Gene3D; 2.20.100.10; -; 6.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR Pfam; PF00090; TSP_1; 6.
DR SMART; SM00209; TSP1; 6.
DR SUPFAM; SSF82895; SSF82895; 6.
DR PROSITE; PS50092; TSP1; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Complement alternate pathway; Disease variant;
KW Disulfide bond; Glycoprotein; Immunity; Innate immunity;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..27
FT CHAIN 28..469
FT /note="Properdin"
FT /id="PRO_0000035863"
FT DOMAIN 28..76
FT /note="TSP type-1 0"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 77..134
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 136..191
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 193..255
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 257..313
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 315..377
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 379..462
FT /note="TSP type-1 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT REGION 219..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..359
FT /note="Interaction with Compliment C3 beta chain"
FT /evidence="ECO:0000269|PubMed:28264884,
FT ECO:0000269|PubMed:31507604"
FT CARBOHYD 83
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:10878002,
FT ECO:0000269|PubMed:31507604"
FT CARBOHYD 86
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:10878002,
FT ECO:0000269|PubMed:31507604"
FT CARBOHYD 92
FT /note="O-linked (Fuc...) threonine"
FT /evidence="ECO:0000269|PubMed:12096136,
FT ECO:0000269|PubMed:31507604"
FT CARBOHYD 139
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:10878002,
FT ECO:0000269|PubMed:31507604"
FT CARBOHYD 142
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:10878002,
FT ECO:0000269|PubMed:31507604"
FT CARBOHYD 145
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:10878002,
FT ECO:0000269|PubMed:31507604"
FT CARBOHYD 151
FT /note="O-linked (Fuc...) threonine"
FT /evidence="ECO:0000269|PubMed:12096136,
FT ECO:0000269|PubMed:31507604"
FT CARBOHYD 196
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:10878002,
FT ECO:0000269|PubMed:31507604"
FT CARBOHYD 199
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:10878002,
FT ECO:0000269|PubMed:31507604"
FT CARBOHYD 202
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:31507604"
FT CARBOHYD 208
FT /note="O-linked (Fuc...) serine"
FT /evidence="ECO:0000269|PubMed:12096136,
FT ECO:0000269|PubMed:31507604"
FT CARBOHYD 260
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:10878002,
FT ECO:0000269|PubMed:31507604"
FT CARBOHYD 263
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:10878002,
FT ECO:0000269|PubMed:31507604"
FT CARBOHYD 272
FT /note="O-linked (Fuc...) threonine"
FT /evidence="ECO:0000269|PubMed:12096136,
FT ECO:0000269|PubMed:31507604"
FT CARBOHYD 321
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:10878002,
FT ECO:0000269|PubMed:31507604"
FT CARBOHYD 324
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:10878002,
FT ECO:0000269|PubMed:31507604"
FT CARBOHYD 382
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:10878002,
FT ECO:0000269|PubMed:31507604"
FT CARBOHYD 385
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:10878002,
FT ECO:0000269|PubMed:31507604"
FT CARBOHYD 388
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:10878002,
FT ECO:0000269|PubMed:31507604"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19139490"
FT DISULFID 32..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210,
FT ECO:0000269|PubMed:31507604"
FT DISULFID 43..72
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210,
FT ECO:0000269|PubMed:31507604"
FT DISULFID 57..75
FT /evidence="ECO:0000269|PubMed:31507604"
FT DISULFID 89..127
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210,
FT ECO:0000269|PubMed:31507604"
FT DISULFID 93..133
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210,
FT ECO:0000269|PubMed:31507604"
FT DISULFID 104..111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210,
FT ECO:0000269|PubMed:31507604"
FT DISULFID 132..170
FT /evidence="ECO:0000269|PubMed:31507604"
FT DISULFID 148..184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210,
FT ECO:0000269|PubMed:31507604"
FT DISULFID 152..190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210,
FT ECO:0000269|PubMed:31507604"
FT DISULFID 163..174
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210,
FT ECO:0000269|PubMed:31507604"
FT DISULFID 205..248
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210,
FT ECO:0000269|PubMed:31507604"
FT DISULFID 209..254
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210,
FT ECO:0000269|PubMed:31507604"
FT DISULFID 224..238
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210,
FT ECO:0000269|PubMed:31507604"
FT DISULFID 269..306
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210,
FT ECO:0000269|PubMed:31507604"
FT DISULFID 273..312
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210,
FT ECO:0000269|PubMed:31507604"
FT DISULFID 284..296
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210,
FT ECO:0000269|PubMed:31507604"
FT DISULFID 327..370
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210,
FT ECO:0000269|PubMed:31507604"
FT DISULFID 337..376
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210,
FT ECO:0000269|PubMed:31507604"
FT DISULFID 350..360
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210,
FT ECO:0000269|PubMed:31507604"
FT DISULFID 391..455
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210,
FT ECO:0000269|PubMed:31507604"
FT DISULFID 395..461
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210,
FT ECO:0000269|PubMed:31507604"
FT DISULFID 407..439
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210,
FT ECO:0000269|PubMed:31507604"
FT VARIANT 3
FT /note="T -> I (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035813"
FT VARIANT 32
FT /note="C -> Y (in PFD; type II; inhibits secretion and
FT oligomerization)"
FT /evidence="ECO:0000269|PubMed:31507604"
FT /id="VAR_083038"
FT VARIANT 53
FT /note="V -> M (in dbSNP:rs8177068)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_020395"
FT VARIANT 100
FT /note="R -> W (in PFD; type II; dbSNP:rs132630259)"
FT /evidence="ECO:0000269|PubMed:8530058"
FT /id="VAR_002002"
FT VARIANT 204
FT /note="P -> L (in dbSNP:rs8177076)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_020396"
FT VARIANT 244
FT /note="E -> K (in PFD; type II; decreases expression,
FT inhibits oligomerization and fails to stimulate
FT bacteriolysis; does not affect binding to Complement C3
FT beta chain)"
FT /evidence="ECO:0000269|PubMed:28264884"
FT /id="VAR_083039"
FT VARIANT 250
FT /note="G -> S (in dbSNP:rs8177077)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_020397"
FT VARIANT 298
FT /note="G -> V (in PFD; type I; dbSNP:rs28935480)"
FT /evidence="ECO:0000269|PubMed:10909851"
FT /id="VAR_013139"
FT VARIANT 343
FT /note="Q -> R (in PFD; type II; significantly decreases
FT Complement C3 beta chain binding)"
FT /evidence="ECO:0000269|PubMed:31507604,
FT ECO:0000269|PubMed:9710744"
FT /id="VAR_002003"
FT VARIANT 414
FT /note="Y -> D (in PFD; type III; significantly decreases
FT Complement C3 beta chain binding; dbSNP:rs132630261)"
FT /evidence="ECO:0000269|PubMed:31507604,
FT ECO:0000269|PubMed:8871668"
FT /id="VAR_002004"
FT MUTAGEN 47
FT /note="L->A: Inhibits oligomerization; when associated with
FT A-58 and A-275."
FT /evidence="ECO:0000269|PubMed:31507604"
FT MUTAGEN 58
FT /note="L->A: Inhibits oligomerization; when associated with
FT A-47 and A-275."
FT /evidence="ECO:0000269|PubMed:31507604"
FT MUTAGEN 244
FT /note="E->R: Inhibits oligomerization."
FT /evidence="ECO:0000269|PubMed:31507604"
FT MUTAGEN 275
FT /note="L->A: Inhibits oligomerization; when associated with
FT A-47 and A-58."
FT /evidence="ECO:0000269|PubMed:31507604"
FT MUTAGEN 329
FT /note="R->A: Significantly decreases Complement C3 beta
FT chain binding."
FT /evidence="ECO:0000269|PubMed:31507604"
FT MUTAGEN 330
FT /note="R->A: Slightly decreases Complement C3 beta chain
FT binding."
FT /evidence="ECO:0000269|PubMed:31507604"
FT MUTAGEN 351
FT /note="R->A: Decreases Complement C3 beta chain binding."
FT /evidence="ECO:0000269|PubMed:31507604"
FT MUTAGEN 353
FT /note="R->A: Significantly decreases Complement C3 beta
FT chain binding."
FT /evidence="ECO:0000269|PubMed:31507604"
FT MUTAGEN 359
FT /note="R->A: Significantly decreases Complement C3 beta
FT chain binding."
FT /evidence="ECO:0000269|PubMed:31507604"
FT MUTAGEN 364..365
FT /note="QQ->AA: Decreases Complement C3 beta chain binding."
FT /evidence="ECO:0000269|PubMed:31507604"
FT MUTAGEN 456
FT /note="L->V: Inhibits oligomerization; when associated with
FT A-47 and A-58."
FT /evidence="ECO:0000269|PubMed:31507604"
FT STRAND 30..37
FT /evidence="ECO:0007829|PDB:6S08"
FT TURN 38..41
FT /evidence="ECO:0007829|PDB:6S08"
FT STRAND 42..51
FT /evidence="ECO:0007829|PDB:6S08"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:6S08"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:6S08"
FT STRAND 69..76
FT /evidence="ECO:0007829|PDB:6S08"
FT STRAND 90..109
FT /evidence="ECO:0007829|PDB:6S08"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:6S08"
FT STRAND 120..128
FT /evidence="ECO:0007829|PDB:6S08"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:6RUS"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:6S0A"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:6S0A"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:6S0A"
FT STRAND 208..214
FT /evidence="ECO:0007829|PDB:6RUS"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:6RUS"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:6RUS"
FT STRAND 242..247
FT /evidence="ECO:0007829|PDB:6RUS"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:6S0A"
FT STRAND 272..281
FT /evidence="ECO:0007829|PDB:6S08"
FT STRAND 300..307
FT /evidence="ECO:0007829|PDB:6S08"
FT STRAND 342..347
FT /evidence="ECO:0007829|PDB:6S08"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:6RUS"
FT STRAND 364..372
FT /evidence="ECO:0007829|PDB:6S08"
FT STRAND 377..382
FT /evidence="ECO:0007829|PDB:6S08"
FT STRAND 391..397
FT /evidence="ECO:0007829|PDB:6S08"
FT STRAND 400..409
FT /evidence="ECO:0007829|PDB:6S08"
FT STRAND 416..418
FT /evidence="ECO:0007829|PDB:6S08"
FT STRAND 421..424
FT /evidence="ECO:0007829|PDB:6S0B"
FT STRAND 427..433
FT /evidence="ECO:0007829|PDB:6S08"
FT STRAND 436..438
FT /evidence="ECO:0007829|PDB:6S08"
FT STRAND 442..444
FT /evidence="ECO:0007829|PDB:6RUS"
FT STRAND 445..454
FT /evidence="ECO:0007829|PDB:6S08"
FT TURN 464..466
FT /evidence="ECO:0007829|PDB:6S0B"
SQ SEQUENCE 469 AA; 51276 MW; 5EB42B63F0283917 CRC64;
MITEGAQAPR LLLPPLLLLL TLPATGSDPV LCFTQYEESS GKCKGLLGGG VSVEDCCLNT
AFAYQKRSGG LCQPCRSPRW SLWSTWAPCS VTCSEGSQLR YRRCVGWNGQ CSGKVAPGTL
EWQLQACEDQ QCCPEMGGWS GWGPWEPCSV TCSKGTRTRR RACNHPAPKC GGHCPGQAQE
SEACDTQQVC PTHGAWATWG PWTPCSASCH GGPHEPKETR SRKCSAPEPS QKPPGKPCPG
LAYEQRRCTG LPPCPVAGGW GPWGPVSPCP VTCGLGQTME QRTCNHPVPQ HGGPFCAGDA
TRTHICNTAV PCPVDGEWDS WGEWSPCIRR NMKSISCQEI PGQQSRGRTC RGRKFDGHRC
AGQQQDIRHC YSIQHCPLKG SWSEWSTWGL CMPPCGPNPT RARQRLCTPL LPKYPPTVSM
VEGQGEKNVT FWGRPLPRCE ELQGQKLVVE EKRPCLHVPA CKDPEEEEL
