P27918 · PROP_HUMAN
- ProteinProperdin
- GeneCFP
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids469 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
A positive regulator of the alternate pathway (AP) of complement (PubMed:20382442, PubMed:28264884).
It binds to and stabilizes the C3- and C5-convertase enzyme complexes (PubMed:20382442, PubMed:28264884).
Inhibits CFI-CFH mediated degradation of Complement C3 beta chain (C3b) (PubMed:31507604).
It binds to and stabilizes the C3- and C5-convertase enzyme complexes (PubMed:20382442, PubMed:28264884).
Inhibits CFI-CFH mediated degradation of Complement C3 beta chain (C3b) (PubMed:31507604).
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasmic side of Golgi membrane | |
Cellular Component | endoplasmic reticulum lumen | |
Cellular Component | extracellular region | |
Cellular Component | extracellular space | |
Cellular Component | specific granule lumen | |
Cellular Component | tertiary granule lumen | |
Biological Process | complement activation | |
Biological Process | complement activation, alternative pathway | |
Biological Process | defense response to bacterium | |
Biological Process | immune response | |
Biological Process | positive regulation of immune response | |
Biological Process | positive regulation of opsonization |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProperdin
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP27918
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Properdin deficiency (PFD)
- Note
- DescriptionResults in higher susceptibility to bacterial infections; especially to meningococcal infections. Three phenotypes have been reported: complete deficiency (type I), incomplete deficiency (type II), and dysfunction of properdin (type III).
- See alsoMIM:312060
Natural variants in PFD
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_083038 | 32 | C>Y | in PFD; type II; inhibits secretion and oligomerization | |
VAR_002002 | 100 | R>W | in PFD; type II; dbSNP:rs132630259 | |
VAR_083039 | 244 | E>K | in PFD; type II; decreases expression, inhibits oligomerization and fails to stimulate bacteriolysis; does not affect binding to Complement C3 beta chain | |
VAR_013139 | 298 | G>V | in PFD; type I; dbSNP:rs28935480 | |
VAR_002003 | 343 | Q>R | in PFD; type II; significantly decreases Complement C3 beta chain binding | |
VAR_002004 | 414 | Y>D | in PFD; type III; significantly decreases Complement C3 beta chain binding; dbSNP:rs132630261 |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_035813 | 3 | in a breast cancer sample; somatic mutation | |||
Sequence: T → I | ||||||
Natural variant | VAR_083038 | 32 | in PFD; type II; inhibits secretion and oligomerization | |||
Sequence: C → Y | ||||||
Mutagenesis | 47 | Inhibits oligomerization; when associated with A-58 and A-275. | ||||
Sequence: L → A | ||||||
Natural variant | VAR_020395 | 53 | in dbSNP:rs8177068 | |||
Sequence: V → M | ||||||
Mutagenesis | 58 | Inhibits oligomerization; when associated with A-47 and A-275. | ||||
Sequence: L → A | ||||||
Natural variant | VAR_002002 | 100 | in PFD; type II; dbSNP:rs132630259 | |||
Sequence: R → W | ||||||
Natural variant | VAR_020396 | 204 | in dbSNP:rs8177076 | |||
Sequence: P → L | ||||||
Natural variant | VAR_083039 | 244 | in PFD; type II; decreases expression, inhibits oligomerization and fails to stimulate bacteriolysis; does not affect binding to Complement C3 beta chain | |||
Sequence: E → K | ||||||
Mutagenesis | 244 | Inhibits oligomerization. | ||||
Sequence: E → R | ||||||
Natural variant | VAR_020397 | 250 | in dbSNP:rs8177077 | |||
Sequence: G → S | ||||||
Mutagenesis | 275 | Inhibits oligomerization; when associated with A-47 and A-58. | ||||
Sequence: L → A | ||||||
Natural variant | VAR_013139 | 298 | in PFD; type I; dbSNP:rs28935480 | |||
Sequence: G → V | ||||||
Mutagenesis | 329 | Significantly decreases Complement C3 beta chain binding. | ||||
Sequence: R → A | ||||||
Mutagenesis | 330 | Slightly decreases Complement C3 beta chain binding. | ||||
Sequence: R → A | ||||||
Natural variant | VAR_002003 | 343 | in PFD; type II; significantly decreases Complement C3 beta chain binding | |||
Sequence: Q → R | ||||||
Mutagenesis | 351 | Decreases Complement C3 beta chain binding. | ||||
Sequence: R → A | ||||||
Mutagenesis | 353 | Significantly decreases Complement C3 beta chain binding. | ||||
Sequence: R → A | ||||||
Mutagenesis | 359 | Significantly decreases Complement C3 beta chain binding. | ||||
Sequence: R → A | ||||||
Mutagenesis | 364-365 | Decreases Complement C3 beta chain binding. | ||||
Sequence: QQ → AA | ||||||
Natural variant | VAR_002004 | 414 | in PFD; type III; significantly decreases Complement C3 beta chain binding; dbSNP:rs132630261 | |||
Sequence: Y → D | ||||||
Mutagenesis | 456 | Inhibits oligomerization; when associated with A-47 and A-58. | ||||
Sequence: L → V |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 467 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-27 | |||||
Sequence: MITEGAQAPRLLLPPLLLLLTLPATGS | ||||||
Chain | PRO_0000035863 | 28-469 | Properdin | |||
Sequence: DPVLCFTQYEESSGKCKGLLGGGVSVEDCCLNTAFAYQKRSGGLCQPCRSPRWSLWSTWAPCSVTCSEGSQLRYRRCVGWNGQCSGKVAPGTLEWQLQACEDQQCCPEMGGWSGWGPWEPCSVTCSKGTRTRRRACNHPAPKCGGHCPGQAQESEACDTQQVCPTHGAWATWGPWTPCSASCHGGPHEPKETRSRKCSAPEPSQKPPGKPCPGLAYEQRRCTGLPPCPVAGGWGPWGPVSPCPVTCGLGQTMEQRTCNHPVPQHGGPFCAGDATRTHICNTAVPCPVDGEWDSWGEWSPCIRRNMKSISCQEIPGQQSRGRTCRGRKFDGHRCAGQQQDIRHCYSIQHCPLKGSWSEWSTWGLCMPPCGPNPTRARQRLCTPLLPKYPPTVSMVEGQGEKNVTFWGRPLPRCEELQGQKLVVEEKRPCLHVPACKDPEEEEL | ||||||
Disulfide bond | 32↔56 | |||||
Sequence: CFTQYEESSGKCKGLLGGGVSVEDC | ||||||
Disulfide bond | 43↔72 | |||||
Sequence: CKGLLGGGVSVEDCCLNTAFAYQKRSGGLC | ||||||
Disulfide bond | 57↔75 | |||||
Sequence: CLNTAFAYQKRSGGLCQPC | ||||||
Glycosylation | 83 | C-linked (Man) tryptophan | ||||
Sequence: W | ||||||
Glycosylation | 86 | C-linked (Man) tryptophan | ||||
Sequence: W | ||||||
Disulfide bond | 89↔127 | |||||
Sequence: CSVTCSEGSQLRYRRCVGWNGQCSGKVAPGTLEWQLQAC | ||||||
Glycosylation | 92 | O-linked (Fuc...) threonine | ||||
Sequence: T | ||||||
Disulfide bond | 93↔133 | |||||
Sequence: CSEGSQLRYRRCVGWNGQCSGKVAPGTLEWQLQACEDQQCC | ||||||
Disulfide bond | 104↔111 | |||||
Sequence: CVGWNGQC | ||||||
Disulfide bond | 132↔170 | |||||
Sequence: CCPEMGGWSGWGPWEPCSVTCSKGTRTRRRACNHPAPKC | ||||||
Glycosylation | 139 | C-linked (Man) tryptophan | ||||
Sequence: W | ||||||
Glycosylation | 142 | C-linked (Man) tryptophan | ||||
Sequence: W | ||||||
Glycosylation | 145 | C-linked (Man) tryptophan | ||||
Sequence: W | ||||||
Disulfide bond | 148↔184 | |||||
Sequence: CSVTCSKGTRTRRRACNHPAPKCGGHCPGQAQESEAC | ||||||
Glycosylation | 151 | O-linked (Fuc...) threonine | ||||
Sequence: T | ||||||
Disulfide bond | 152↔190 | |||||
Sequence: CSKGTRTRRRACNHPAPKCGGHCPGQAQESEACDTQQVC | ||||||
Disulfide bond | 163↔174 | |||||
Sequence: CNHPAPKCGGHC | ||||||
Glycosylation | 196 | C-linked (Man) tryptophan | ||||
Sequence: W | ||||||
Glycosylation | 199 | C-linked (Man) tryptophan | ||||
Sequence: W | ||||||
Glycosylation | 202 | C-linked (Man) tryptophan | ||||
Sequence: W | ||||||
Disulfide bond | 205↔248 | |||||
Sequence: CSASCHGGPHEPKETRSRKCSAPEPSQKPPGKPCPGLAYEQRRC | ||||||
Glycosylation | 208 | O-linked (Fuc...) serine | ||||
Sequence: S | ||||||
Disulfide bond | 209↔254 | |||||
Sequence: CHGGPHEPKETRSRKCSAPEPSQKPPGKPCPGLAYEQRRCTGLPPC | ||||||
Disulfide bond | 224↔238 | |||||
Sequence: CSAPEPSQKPPGKPC | ||||||
Glycosylation | 260 | C-linked (Man) tryptophan | ||||
Sequence: W | ||||||
Glycosylation | 263 | C-linked (Man) tryptophan | ||||
Sequence: W | ||||||
Disulfide bond | 269↔306 | |||||
Sequence: CPVTCGLGQTMEQRTCNHPVPQHGGPFCAGDATRTHIC | ||||||
Glycosylation | 272 | O-linked (Fuc...) threonine | ||||
Sequence: T | ||||||
Disulfide bond | 273↔312 | |||||
Sequence: CGLGQTMEQRTCNHPVPQHGGPFCAGDATRTHICNTAVPC | ||||||
Disulfide bond | 284↔296 | |||||
Sequence: CNHPVPQHGGPFC | ||||||
Glycosylation | 321 | C-linked (Man) tryptophan | ||||
Sequence: W | ||||||
Glycosylation | 324 | C-linked (Man) tryptophan | ||||
Sequence: W | ||||||
Disulfide bond | 327↔370 | |||||
Sequence: CIRRNMKSISCQEIPGQQSRGRTCRGRKFDGHRCAGQQQDIRHC | ||||||
Disulfide bond | 337↔376 | |||||
Sequence: CQEIPGQQSRGRTCRGRKFDGHRCAGQQQDIRHCYSIQHC | ||||||
Disulfide bond | 350↔360 | |||||
Sequence: CRGRKFDGHRC | ||||||
Glycosylation | 382 | C-linked (Man) tryptophan | ||||
Sequence: W | ||||||
Glycosylation | 385 | C-linked (Man) tryptophan | ||||
Sequence: W | ||||||
Glycosylation | 388 | C-linked (Man) tryptophan | ||||
Sequence: W | ||||||
Disulfide bond | 391↔455 | |||||
Sequence: CMPPCGPNPTRARQRLCTPLLPKYPPTVSMVEGQGEKNVTFWGRPLPRCEELQGQKLVVEEKRPC | ||||||
Disulfide bond | 395↔461 | |||||
Sequence: CGPNPTRARQRLCTPLLPKYPPTVSMVEGQGEKNVTFWGRPLPRCEELQGQKLVVEEKRPCLHVPAC | ||||||
Disulfide bond | 407↔439 | |||||
Sequence: CTPLLPKYPPTVSMVEGQGEKNVTFWGRPLPRC | ||||||
Glycosylation | 428 | N-linked (GlcNAc...) (complex) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
In plasma, properdin exists as dimers, trimers or tetramers in the relative proportions of 26:54:20 (PubMed:15491616, PubMed:20382442, PubMed:28264884, PubMed:31507604).
Interacts with the pro-C3-convertase enzyme complex (C3b-Bb) comprised of Complement C3 beta chain (C3b) and the Complement factor B Bb fragment (Bb), where it binds (via its TSP type-1 5 domain) with C3b and Bb (PubMed:28264884, PubMed:31507604).
This interaction stabilizes the complex and allows it to become the active C3-convertase enzyme complex (C3b-Bb-FP) (PubMed:28264884, PubMed:31507604).
Interacts with C3b (PubMed:28264884, PubMed:31507604).
Interacts with CFB (PubMed:31507604).
Interacts with the pro-C3-convertase enzyme complex (C3b-Bb) comprised of Complement C3 beta chain (C3b) and the Complement factor B Bb fragment (Bb), where it binds (via its TSP type-1 5 domain) with C3b and Bb (PubMed:28264884, PubMed:31507604).
This interaction stabilizes the complex and allows it to become the active C3-convertase enzyme complex (C3b-Bb-FP) (PubMed:28264884, PubMed:31507604).
Interacts with C3b (PubMed:28264884, PubMed:31507604).
Interacts with CFB (PubMed:31507604).
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 28-76 | TSP type-1 0 | ||||
Sequence: DPVLCFTQYEESSGKCKGLLGGGVSVEDCCLNTAFAYQKRSGGLCQPCR | ||||||
Domain | 77-134 | TSP type-1 1 | ||||
Sequence: SPRWSLWSTWAPCSVTCSEGSQLRYRRCVGWNGQCSGKVAPGTLEWQLQACEDQQCCP | ||||||
Domain | 136-191 | TSP type-1 2 | ||||
Sequence: MGGWSGWGPWEPCSVTCSKGTRTRRRACNHPAPKCGGHCPGQAQESEACDTQQVCP | ||||||
Domain | 193-255 | TSP type-1 3 | ||||
Sequence: HGAWATWGPWTPCSASCHGGPHEPKETRSRKCSAPEPSQKPPGKPCPGLAYEQRRCTGLPPCP | ||||||
Region | 219-238 | Disordered | ||||
Sequence: TRSRKCSAPEPSQKPPGKPC | ||||||
Domain | 257-313 | TSP type-1 4 | ||||
Sequence: AGGWGPWGPVSPCPVTCGLGQTMEQRTCNHPVPQHGGPFCAGDATRTHICNTAVPCP | ||||||
Domain | 315-377 | TSP type-1 5 | ||||
Sequence: DGEWDSWGEWSPCIRRNMKSISCQEIPGQQSRGRTCRGRKFDGHRCAGQQQDIRHCYSIQHCP | ||||||
Region | 351-359 | Interaction with Complement C3 beta chain | ||||
Sequence: RGRKFDGHR | ||||||
Domain | 379-462 | TSP type-1 6 | ||||
Sequence: KGSWSEWSTWGLCMPPCGPNPTRARQRLCTPLLPKYPPTVSMVEGQGEKNVTFWGRPLPRCEELQGQKLVVEEKRPCLHVPACK |
Domain
TSP type-1 domain 0 binds to TSP type-1 domain 4, and TSP type-1 domain 1 binds to TSP type-1 domain 6 (PubMed:15491616, PubMed:28264884, PubMed:31507604).
These interactions mediate multimerization (PubMed:15491616, PubMed:28264884, PubMed:31507604).
These interactions mediate multimerization (PubMed:15491616, PubMed:28264884, PubMed:31507604).
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length469
- Mass (Da)51,276
- Last updated1994-02-01 v2
- Checksum5EB42B63F0283917
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X57748 EMBL· GenBank· DDBJ | CAA40914.1 EMBL· GenBank· DDBJ | mRNA | ||
X70872 EMBL· GenBank· DDBJ | CAA50220.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M83652 EMBL· GenBank· DDBJ | AAA36489.1 EMBL· GenBank· DDBJ | mRNA | ||
AF005664 EMBL· GenBank· DDBJ | AAB63279.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF005665 EMBL· GenBank· DDBJ | AAB63280.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF005666 EMBL· GenBank· DDBJ | AAC51626.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF005668 EMBL· GenBank· DDBJ | AAB62886.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF005667 EMBL· GenBank· DDBJ | AAB62886.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY297813 EMBL· GenBank· DDBJ | AAP43692.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL009172 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC015756 EMBL· GenBank· DDBJ | AAH15756.1 EMBL· GenBank· DDBJ | mRNA |