Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Properdin

Gene

CFP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

A positive regulator of the alternate pathway of complement. It binds to and stabilizes the C3- and C5-convertase enzyme complexes.1 Publication

GO - Biological processi

  • complement activation Source: Reactome
  • complement activation, alternative pathway Source: Reactome
  • defense response to bacterium Source: ProtInc
  • immune response Source: ProtInc
  • protein O-linked fucosylation Source: Reactome
  • regulation of complement activation Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Complement alternate pathway, Immunity, Innate immunity

Enzyme and pathway databases

BioCyciZFISH:ENSG00000126759-MONOMER.
ReactomeiR-HSA-173736. Alternative complement activation.
R-HSA-174577. Activation of C3 and C5.
R-HSA-5083635. Defective B3GALTL causes Peters-plus syndrome (PpS).
R-HSA-5173214. O-glycosylation of TSR domain-containing proteins.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-977606. Regulation of Complement cascade.

Names & Taxonomyi

Protein namesi
Recommended name:
Properdin
Alternative name(s):
Complement factor P
Gene namesi
Name:CFP
Synonyms:PFC
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:8864. CFP.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum lumen Source: Reactome
  • extracellular region Source: Reactome
  • extracellular space Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Properdin deficiency (PFD)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease 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 also OMIM:312060
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_002002100R → W in PFD; type II. 1 PublicationCorresponds to variant rs132630259dbSNPEnsembl.1
Natural variantiVAR_013139298G → V in PFD; type I. 1 PublicationCorresponds to variant rs28935480dbSNPEnsembl.1
Natural variantiVAR_002003343Q → R in PFD; type II. 1 Publication1
Natural variantiVAR_002004414Y → D in PFD; type III. 1 PublicationCorresponds to variant rs132630261dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi5199.
MalaCardsiCFP.
MIMi312060. phenotype.
OpenTargetsiENSG00000126759.
Orphaneti2966. Properdin deficiency.
PharmGKBiPA33206.

Polymorphism and mutation databases

BioMutaiCFP.
DMDMi464473.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27Add BLAST27
ChainiPRO_000003586328 – 469ProperdinAdd BLAST442

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi32 ↔ 72PROSITE-ProRule annotation
Disulfide bondi43 ↔ 75PROSITE-ProRule annotation
Glycosylationi83C-linked (Man)1 Publication1
Glycosylationi86C-linked (Man)1 Publication1
Disulfide bondi89 ↔ 127PROSITE-ProRule annotation
Glycosylationi92O-linked (Fuc...)1 Publication1
Disulfide bondi93 ↔ 133PROSITE-ProRule annotation
Disulfide bondi104 ↔ 111PROSITE-ProRule annotation
Glycosylationi139C-linked (Man)1 Publication1
Glycosylationi142C-linked (Man)1 Publication1
Glycosylationi145C-linked (Man)1 Publication1
Disulfide bondi148 ↔ 184PROSITE-ProRule annotation
Glycosylationi151O-linked (Fuc...)1 Publication1
Disulfide bondi152 ↔ 190PROSITE-ProRule annotation
Disulfide bondi163 ↔ 174PROSITE-ProRule annotation
Glycosylationi196C-linked (Man)1 Publication1
Glycosylationi199C-linked (Man)1 Publication1
Disulfide bondi205 ↔ 248PROSITE-ProRule annotation
Glycosylationi208O-linked (Fuc...)1 Publication1
Disulfide bondi209 ↔ 254PROSITE-ProRule annotation
Disulfide bondi224 ↔ 238PROSITE-ProRule annotation
Glycosylationi260C-linked (Man)1 Publication1
Glycosylationi263C-linked (Man)1 Publication1
Disulfide bondi269 ↔ 306PROSITE-ProRule annotation
Glycosylationi272O-linked (Fuc...)1 Publication1
Disulfide bondi273 ↔ 312PROSITE-ProRule annotation
Disulfide bondi284 ↔ 296PROSITE-ProRule annotation
Glycosylationi321C-linked (Man)1 Publication1
Glycosylationi324C-linked (Man)1 Publication1
Disulfide bondi327 ↔ 370PROSITE-ProRule annotation
Disulfide bondi337 ↔ 376PROSITE-ProRule annotation
Disulfide bondi350 ↔ 360PROSITE-ProRule annotation
Glycosylationi382C-linked (Man)1 Publication1
Glycosylationi385C-linked (Man)1 Publication1
Glycosylationi388C-linked (Man)1 Publication1
Disulfide bondi391 ↔ 455PROSITE-ProRule annotation
Disulfide bondi395 ↔ 461PROSITE-ProRule annotation
Disulfide bondi407 ↔ 439PROSITE-ProRule annotation
Glycosylationi428N-linked (GlcNAc...) (complex)2 Publications1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP27918.
PeptideAtlasiP27918.
PRIDEiP27918.

PTM databases

iPTMnetiP27918.
PhosphoSitePlusiP27918.

Expressioni

Gene expression databases

BgeeiENSG00000126759.
CleanExiHS_CFP.
ExpressionAtlasiP27918. baseline and differential.
GenevisibleiP27918. HS.

Interactioni

Subunit structurei

In plasma, properdin exists as dimers, trimers or tetramers in the relative proportions of 26:54:20.2 Publications

Protein-protein interaction databases

BioGridi111222. 8 interactors.
IntActiP27918. 5 interactors.
MINTiMINT-6630429.
STRINGi9606.ENSP00000247153.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1W0RX-ray-A/B28-469[»]
1W0SX-ray-A/B/C28-469[»]
ProteinModelPortaliP27918.
SMRiP27918.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27918.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini28 – 76TSP type-1 0PROSITE-ProRule annotationAdd BLAST49
Domaini77 – 134TSP type-1 1PROSITE-ProRule annotationAdd BLAST58
Domaini136 – 191TSP type-1 2PROSITE-ProRule annotationAdd BLAST56
Domaini193 – 255TSP type-1 3PROSITE-ProRule annotationAdd BLAST63
Domaini257 – 313TSP type-1 4PROSITE-ProRule annotationAdd BLAST57
Domaini315 – 377TSP type-1 5PROSITE-ProRule annotationAdd BLAST63
Domaini379 – 462TSP type-1 6PROSITE-ProRule annotationAdd BLAST84

Domaini

TSP type-1 domains 0 and 6 bind to each other and mediate multimerization.

Sequence similaritiesi

Contains 7 TSP type-1 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IUGK. Eukaryota.
ENOG410ZHSM. LUCA.
GeneTreeiENSGT00850000132260.
HOGENOMiHOG000231326.
HOVERGENiHBG008263.
InParanoidiP27918.
KOiK15412.
OMAiQVCPTHG.
OrthoDBiEOG091G07MO.
PhylomeDBiP27918.
TreeFamiTF315491.

Family and domain databases

InterProiIPR000884. TSP1_rpt.
[Graphical view]
PfamiPF00090. TSP_1. 6 hits.
[Graphical view]
SMARTiSM00209. TSP1. 6 hits.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 6 hits.
PROSITEiPS50092. TSP1. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P27918-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MITEGAQAPR LLLPPLLLLL TLPATGSDPV LCFTQYEESS GKCKGLLGGG
60 70 80 90 100
VSVEDCCLNT AFAYQKRSGG LCQPCRSPRW SLWSTWAPCS VTCSEGSQLR
110 120 130 140 150
YRRCVGWNGQ CSGKVAPGTL EWQLQACEDQ QCCPEMGGWS GWGPWEPCSV
160 170 180 190 200
TCSKGTRTRR RACNHPAPKC GGHCPGQAQE SEACDTQQVC PTHGAWATWG
210 220 230 240 250
PWTPCSASCH GGPHEPKETR SRKCSAPEPS QKPPGKPCPG LAYEQRRCTG
260 270 280 290 300
LPPCPVAGGW GPWGPVSPCP VTCGLGQTME QRTCNHPVPQ HGGPFCAGDA
310 320 330 340 350
TRTHICNTAV PCPVDGEWDS WGEWSPCIRR NMKSISCQEI PGQQSRGRTC
360 370 380 390 400
RGRKFDGHRC AGQQQDIRHC YSIQHCPLKG SWSEWSTWGL CMPPCGPNPT
410 420 430 440 450
RARQRLCTPL LPKYPPTVSM VEGQGEKNVT FWGRPLPRCE ELQGQKLVVE
460
EKRPCLHVPA CKDPEEEEL
Length:469
Mass (Da):51,276
Last modified:February 1, 1994 - v2
Checksum:i5EB42B63F0283917
GO

Sequence cautioni

The sequence CAA15658 differs from that shown. Reason: Erroneous gene model prediction.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0358133T → I in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_02039553V → M.1 PublicationCorresponds to variant rs8177068dbSNPEnsembl.1
Natural variantiVAR_002002100R → W in PFD; type II. 1 PublicationCorresponds to variant rs132630259dbSNPEnsembl.1
Natural variantiVAR_020396204P → L.1 PublicationCorresponds to variant rs8177076dbSNPEnsembl.1
Natural variantiVAR_020397250G → S.1 PublicationCorresponds to variant rs8177077dbSNPEnsembl.1
Natural variantiVAR_013139298G → V in PFD; type I. 1 PublicationCorresponds to variant rs28935480dbSNPEnsembl.1
Natural variantiVAR_002003343Q → R in PFD; type II. 1 Publication1
Natural variantiVAR_002004414Y → D in PFD; type III. 1 PublicationCorresponds to variant rs132630261dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57748 mRNA. Translation: CAA40914.1.
X70872 Genomic DNA. Translation: CAA50220.1.
M83652 mRNA. Translation: AAA36489.1.
AF005664 Genomic DNA. Translation: AAB63279.1.
AF005665 Genomic DNA. Translation: AAB63280.1.
AF005666 Genomic DNA. Translation: AAC51626.1.
AF005668, AF005667 Genomic DNA. Translation: AAB62886.1.
AY297813 Genomic DNA. Translation: AAP43692.1.
AL009172 Genomic DNA. Translation: CAA15658.1. Sequence problems.
BC015756 mRNA. Translation: AAH15756.1.
CCDSiCCDS14282.1.
PIRiS29126.
RefSeqiNP_001138724.1. NM_001145252.1.
NP_002612.1. NM_002621.2.
UniGeneiHs.53155.

Genome annotation databases

EnsembliENST00000247153; ENSP00000247153; ENSG00000126759.
ENST00000396992; ENSP00000380189; ENSG00000126759.
GeneIDi5199.
KEGGihsa:5199.
UCSCiuc004dig.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

CFPbase

CFP mutation db

SeattleSNPs
Wikipedia

Properdin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57748 mRNA. Translation: CAA40914.1.
X70872 Genomic DNA. Translation: CAA50220.1.
M83652 mRNA. Translation: AAA36489.1.
AF005664 Genomic DNA. Translation: AAB63279.1.
AF005665 Genomic DNA. Translation: AAB63280.1.
AF005666 Genomic DNA. Translation: AAC51626.1.
AF005668, AF005667 Genomic DNA. Translation: AAB62886.1.
AY297813 Genomic DNA. Translation: AAP43692.1.
AL009172 Genomic DNA. Translation: CAA15658.1. Sequence problems.
BC015756 mRNA. Translation: AAH15756.1.
CCDSiCCDS14282.1.
PIRiS29126.
RefSeqiNP_001138724.1. NM_001145252.1.
NP_002612.1. NM_002621.2.
UniGeneiHs.53155.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1W0RX-ray-A/B28-469[»]
1W0SX-ray-A/B/C28-469[»]
ProteinModelPortaliP27918.
SMRiP27918.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111222. 8 interactors.
IntActiP27918. 5 interactors.
MINTiMINT-6630429.
STRINGi9606.ENSP00000247153.

PTM databases

iPTMnetiP27918.
PhosphoSitePlusiP27918.

Polymorphism and mutation databases

BioMutaiCFP.
DMDMi464473.

Proteomic databases

PaxDbiP27918.
PeptideAtlasiP27918.
PRIDEiP27918.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000247153; ENSP00000247153; ENSG00000126759.
ENST00000396992; ENSP00000380189; ENSG00000126759.
GeneIDi5199.
KEGGihsa:5199.
UCSCiuc004dig.5. human.

Organism-specific databases

CTDi5199.
DisGeNETi5199.
GeneCardsiCFP.
HGNCiHGNC:8864. CFP.
MalaCardsiCFP.
MIMi300383. gene.
312060. phenotype.
neXtProtiNX_P27918.
OpenTargetsiENSG00000126759.
Orphaneti2966. Properdin deficiency.
PharmGKBiPA33206.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IUGK. Eukaryota.
ENOG410ZHSM. LUCA.
GeneTreeiENSGT00850000132260.
HOGENOMiHOG000231326.
HOVERGENiHBG008263.
InParanoidiP27918.
KOiK15412.
OMAiQVCPTHG.
OrthoDBiEOG091G07MO.
PhylomeDBiP27918.
TreeFamiTF315491.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000126759-MONOMER.
ReactomeiR-HSA-173736. Alternative complement activation.
R-HSA-174577. Activation of C3 and C5.
R-HSA-5083635. Defective B3GALTL causes Peters-plus syndrome (PpS).
R-HSA-5173214. O-glycosylation of TSR domain-containing proteins.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-977606. Regulation of Complement cascade.

Miscellaneous databases

ChiTaRSiCFP. human.
EvolutionaryTraceiP27918.
GenomeRNAii5199.
PROiP27918.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000126759.
CleanExiHS_CFP.
ExpressionAtlasiP27918. baseline and differential.
GenevisibleiP27918. HS.

Family and domain databases

InterProiIPR000884. TSP1_rpt.
[Graphical view]
PfamiPF00090. TSP_1. 6 hits.
[Graphical view]
SMARTiSM00209. TSP1. 6 hits.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 6 hits.
PROSITEiPS50092. TSP1. 6 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPROP_HUMAN
AccessioniPrimary (citable) accession number: P27918
Secondary accession number(s): O15134
, O15135, O15136, O75826
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: February 1, 1994
Last modified: November 30, 2016
This is version 165 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.