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P02748

- CO9_HUMAN

UniProt

P02748 - CO9_HUMAN

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Protein
Complement component C9
Gene
C9
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells. C9 is the pore-forming subunit of the MAC.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei265 – 2662Cleavage; by thrombin

GO - Biological processi

  1. complement activation, alternative pathway Source: UniProtKB-KW
  2. complement activation, classical pathway Source: UniProtKB-KW
  3. hemolysis by symbiont of host erythrocytes Source: ProtInc
  4. innate immune response Source: Reactome
  5. regulation of complement activation Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Complement alternate pathway, Complement pathway, Cytolysis, Immunity, Innate immunity

Enzyme and pathway databases

ReactomeiREACT_118707. Regulation of Complement cascade.
REACT_8028. Terminal pathway of complement.

Names & Taxonomyi

Protein namesi
Recommended name:
Complement component C9
Cleaved into the following 2 chains:
Gene namesi
Name:C9
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:1358. C9.

Subcellular locationi

Secreted. Cell membrane; Multi-pass membrane protein
Note: Secreted as soluble monomer. Oligomerizes at target membranes, forming a pre-pore. A conformation change then leads to the formation of a 100 Angstrom diameter pore.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei314 – 33017Beta stranded; Reviewed prediction
Add
BLAST
Transmembranei335 – 35420Beta stranded; Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. blood microparticle Source: UniProt
  2. cytoplasm Source: HPA
  3. extracellular region Source: Reactome
  4. extracellular vesicular exosome Source: UniProt
  5. integral component of plasma membrane Source: ProtInc
  6. membrane attack complex Source: UniProtKB-KW
  7. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Membrane attack complex, Secreted

Pathology & Biotechi

Involvement in diseasei

Complement component 9 deficiency (C9D) [MIM:613825]: A rare defect of the complement classical pathway associated with susceptibility to severe recurrent infections predominantly by Neisseria gonorrhoeae or Neisseria meningitidis. Some patients may develop dermatomyositis.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti119 – 1191C → G in C9D. 1 Publication
VAR_012648
Macular degeneration, age-related, 15 (ARMD15) [MIM:615591]: A form of age-related macular degeneration, a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti167 – 1671P → S in ARMD15. 1 Publication
VAR_070940

Keywords - Diseasei

Age-related macular degeneration, Disease mutation

Organism-specific databases

MIMi613825. phenotype.
615591. phenotype.
Orphaneti279. Age-related macular degeneration.
169150. Immunodeficiency due to a late component of complements deficiency.
PharmGKBiPA25968.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 21211 Publication
Add
BLAST
Chaini22 – 559538Complement component C9
PRO_0000023602Add
BLAST
Chaini22 – 265244Complement component C9a
PRO_0000023603Add
BLAST
Chaini266 – 559294Complement component C9b
PRO_0000023604Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi43 ↔ 781 Publication
Glycosylationi48 – 481C-linked (Man)1 Publication
Glycosylationi51 – 511C-linked (Man); partial1 Publication
Disulfide bondi54 ↔ 571 Publication
Disulfide bondi88 ↔ 941 Publication
Disulfide bondi101 ↔ 1121 Publication
Disulfide bondi107 ↔ 1251 Publication
Disulfide bondi119 ↔ 1341 Publication
Disulfide bondi142 ↔ 1811 Publication
Disulfide bondi254 ↔ 2551 Publication
Glycosylationi277 – 2771N-linked (GlcNAc...)3 Publications
Disulfide bondi380 ↔ 4051 Publication
Glycosylationi415 – 4151N-linked (GlcNAc...) (complex)6 Publications
Disulfide bondi510 ↔ 5261 Publication
Disulfide bondi513 ↔ 5281 Publication
Disulfide bondi530 ↔ 5391 Publication

Post-translational modificationi

Thrombin cleaves factor C9 to produce C9a and C9b.
Phosphorylation sites are present in the extracellular medium.

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP02748.
PaxDbiP02748.
PeptideAtlasiP02748.
PRIDEiP02748.

PTM databases

PhosphoSiteiP02748.

Expressioni

Tissue specificityi

Plasma.

Gene expression databases

ArrayExpressiP02748.
BgeeiP02748.
CleanExiHS_C9.
GenevestigatoriP02748.

Organism-specific databases

HPAiCAB002151.
HPA029577.

Interactioni

Subunit structurei

Component of the membrane attack complex (MAC). MAC assembly is initiated by protelytic cleavage of C5 into C5a and C5b. C5b binds sequentially C6, C7, C8 and multiple copies of the pore-forming subunit C9.

Protein-protein interaction databases

BioGridi107196. 3 interactions.
DIPiDIP-1124N.
MINTiMINT-2800316.
STRINGi9606.ENSP00000263408.

Structurei

3D structure databases

ProteinModelPortaliP02748.
SMRiP02748. Positions 36-540.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini42 – 9554TSP type-1
Add
BLAST
Domaini99 – 13638LDL-receptor class A
Add
BLAST
Domaini138 – 509372MACPF
Add
BLAST
Domaini510 – 54031EGF-like
Add
BLAST

Sequence similaritiesi

Contains 1 EGF-like domain.
Contains 1 MACPF domain.
Contains 1 TSP type-1 domain.

Keywords - Domaini

EGF-like domain, Signal, Transmembrane, Transmembrane beta strand

Phylogenomic databases

eggNOGiNOG46204.
HOGENOMiHOG000111869.
HOVERGENiHBG106792.
InParanoidiP02748.
KOiK04000.
OMAiPWNVASL.
OrthoDBiEOG7D85W9.
PhylomeDBiP02748.
TreeFamiTF330498.

Family and domain databases

Gene3Di4.10.400.10. 1 hit.
InterProiIPR009030. Growth_fac_rcpt_N_dom.
IPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
IPR001862. MAC_perforin.
IPR020864. MACPF.
IPR020863. MACPF_CS.
IPR000884. Thrombospondin_1_rpt.
[Graphical view]
PfamiPF00057. Ldl_recept_a. 1 hit.
PF01823. MACPF. 1 hit.
PF00090. TSP_1. 1 hit.
[Graphical view]
PRINTSiPR00764. COMPLEMENTC9.
SMARTiSM00192. LDLa. 1 hit.
SM00457. MACPF. 1 hit.
SM00209. TSP1. 1 hit.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 2 hits.
SSF57424. SSF57424. 1 hit.
SSF82895. SSF82895. 1 hit.
PROSITEiPS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS01209. LDLRA_1. 1 hit.
PS50068. LDLRA_2. 1 hit.
PS00279. MACPF_1. 1 hit.
PS51412. MACPF_2. 1 hit.
PS50092. TSP1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P02748-1 [UniParc]FASTAAdd to Basket

« Hide

MSACRSFAVA ICILEISILT AQYTTSYDPE LTESSGSASH IDCRMSPWSE    50
WSQCDPCLRQ MFRSRSIEVF GQFNGKRCTD AVGDRRQCVP TEPCEDAEDD 100
CGNDFQCSTG RCIKMRLRCN GDNDCGDFSD EDDCESEPRP PCRDRVVEES 150
ELARTAGYGI NILGMDPLST PFDNEFYNGL CNRDRDGNTL TYYRRPWNVA 200
SLIYETKGEK NFRTEHYEEQ IEAFKSIIQE KTSNFNAAIS LKFTPTETNK 250
AEQCCEETAS SISLHGKGSF RFSYSKNETY QLFLSYSSKK EKMFLHVKGE 300
IHLGRFVMRN RDVVLTTTFV DDIKALPTTY EKGEYFAFLE TYGTHYSSSG 350
SLGGLYELIY VLDKASMKRK GVELKDIKRC LGYHLDVSLA FSEISVGAEF 400
NKDDCVKRGE GRAVNITSEN LIDDVVSLIR GGTRKYAFEL KEKLLRGTVI 450
DVTDFVNWAS SINDAPVLIS QKLSPIYNLV PVKMKNAHLK KQNLERAIED 500
YINEFSVRKC HTCQNGGTVI LMDGKCLCAC PFKFEGIACE ISKQKISEGL 550
PALEFPNEK 559
Length:559
Mass (Da):63,173
Last modified:February 1, 1996 - v2
Checksum:i7403F6AD77B3ECE1
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti5 – 51R → W.
Corresponds to variant rs700233 [ dbSNP | Ensembl ].
VAR_022024
Natural varianti119 – 1191C → G in C9D. 1 Publication
VAR_012648
Natural varianti127 – 1271D → Y.
Corresponds to variant rs696763 [ dbSNP | Ensembl ].
VAR_050481
Natural varianti167 – 1671P → S in ARMD15. 1 Publication
VAR_070940
Natural varianti203 – 2031I → V.
Corresponds to variant rs13361416 [ dbSNP | Ensembl ].
VAR_027651
Natural varianti279 – 2791T → S.
Corresponds to variant rs34625111 [ dbSNP | Ensembl ].
VAR_033802
Natural varianti427 – 4271S → T.
Corresponds to variant rs34421659 [ dbSNP | Ensembl ].
VAR_061503

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti43 – 431C → R in AAA51889. 1 Publication
Sequence conflicti314 – 3141Missing in AAA51889. 1 Publication
Sequence conflicti417 – 4171T → P in AAA51889. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X02176 mRNA. Translation: CAA26117.1.
BC020721 mRNA. Translation: AAH20721.1.
K02766 mRNA. Translation: AAA51889.1.
J02833 Genomic DNA. Translation: AAA51890.1.
Y08545
, Y08546, Y08547, Y08548, Y08549, Y08550, Y08551, Y08552, Y08553, Y08554 Genomic DNA. Translation: CAA69849.1.
CCDSiCCDS3929.1.
PIRiA59363. C9HU.
RefSeqiNP_001728.1. NM_001737.3.
UniGeneiHs.654443.

Genome annotation databases

EnsembliENST00000263408; ENSP00000263408; ENSG00000113600.
GeneIDi735.
KEGGihsa:735.
UCSCiuc003jlv.4. human.

Polymorphism databases

DMDMi1352108.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

C9base

C9 mutation db

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X02176 mRNA. Translation: CAA26117.1 .
BC020721 mRNA. Translation: AAH20721.1 .
K02766 mRNA. Translation: AAA51889.1 .
J02833 Genomic DNA. Translation: AAA51890.1 .
Y08545
, Y08546 , Y08547 , Y08548 , Y08549 , Y08550 , Y08551 , Y08552 , Y08553 , Y08554 Genomic DNA. Translation: CAA69849.1 .
CCDSi CCDS3929.1.
PIRi A59363. C9HU.
RefSeqi NP_001728.1. NM_001737.3.
UniGenei Hs.654443.

3D structure databases

ProteinModelPortali P02748.
SMRi P02748. Positions 36-540.
ModBasei Search...

Protein-protein interaction databases

BioGridi 107196. 3 interactions.
DIPi DIP-1124N.
MINTi MINT-2800316.
STRINGi 9606.ENSP00000263408.

PTM databases

PhosphoSitei P02748.

Polymorphism databases

DMDMi 1352108.

Proteomic databases

MaxQBi P02748.
PaxDbi P02748.
PeptideAtlasi P02748.
PRIDEi P02748.

Protocols and materials databases

DNASUi 735.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000263408 ; ENSP00000263408 ; ENSG00000113600 .
GeneIDi 735.
KEGGi hsa:735.
UCSCi uc003jlv.4. human.

Organism-specific databases

CTDi 735.
GeneCardsi GC05M039320.
HGNCi HGNC:1358. C9.
HPAi CAB002151.
HPA029577.
MIMi 120940. gene.
613825. phenotype.
615591. phenotype.
neXtProti NX_P02748.
Orphaneti 279. Age-related macular degeneration.
169150. Immunodeficiency due to a late component of complements deficiency.
PharmGKBi PA25968.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG46204.
HOGENOMi HOG000111869.
HOVERGENi HBG106792.
InParanoidi P02748.
KOi K04000.
OMAi PWNVASL.
OrthoDBi EOG7D85W9.
PhylomeDBi P02748.
TreeFami TF330498.

Enzyme and pathway databases

Reactomei REACT_118707. Regulation of Complement cascade.
REACT_8028. Terminal pathway of complement.

Miscellaneous databases

GenomeRNAii 735.
NextBioi 2992.
PROi P02748.
SOURCEi Search...

Gene expression databases

ArrayExpressi P02748.
Bgeei P02748.
CleanExi HS_C9.
Genevestigatori P02748.

Family and domain databases

Gene3Di 4.10.400.10. 1 hit.
InterProi IPR009030. Growth_fac_rcpt_N_dom.
IPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
IPR001862. MAC_perforin.
IPR020864. MACPF.
IPR020863. MACPF_CS.
IPR000884. Thrombospondin_1_rpt.
[Graphical view ]
Pfami PF00057. Ldl_recept_a. 1 hit.
PF01823. MACPF. 1 hit.
PF00090. TSP_1. 1 hit.
[Graphical view ]
PRINTSi PR00764. COMPLEMENTC9.
SMARTi SM00192. LDLa. 1 hit.
SM00457. MACPF. 1 hit.
SM00209. TSP1. 1 hit.
[Graphical view ]
SUPFAMi SSF57184. SSF57184. 2 hits.
SSF57424. SSF57424. 1 hit.
SSF82895. SSF82895. 1 hit.
PROSITEi PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS01209. LDLRA_1. 1 hit.
PS50068. LDLRA_2. 1 hit.
PS00279. MACPF_1. 1 hit.
PS51412. MACPF_2. 1 hit.
PS50092. TSP1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The sequence and topology of human complement component C9."
    Stanley K.K., Kocher H.-P., Luzio J.P., Jackson P., Tschopp J.
    EMBO J. 4:375-382(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Liver.
  3. "Nucleotide sequence of cDNA and derived amino acid sequence of human complement component C9."
    Discipio R.G., Gehring M.R., Podack E.R., Kan C.C., Hugli T.E., Fey G.H.
    Proc. Natl. Acad. Sci. U.S.A. 81:7298-7302(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-559, PROTEIN SEQUENCE OF N-TERMINUS.
  4. "Relationships between the gene and protein structure in human complement component C9."
    Marazziti D., Eggertsen G., Fey G.H., Stanley K.K.
    Biochemistry 27:6529-6534(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 62-159.
  5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 27-559, VARIANT C9D GLY-119.
  6. "The architecture of complement component C9 and poly(C9)."
    DiScipio R.G., Hugli T.E.
    J. Biol. Chem. 260:14802-14809(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, ELECTRON MICROSCOPY, GLYCOSYLATION AT ASN-277 AND ASN-415.
  7. "Identification of disulfide bonds in the ninth component (C9) of human complement."
    Lengweiler S., Schaller J., Rickli E.E.
    FEBS Lett. 380:8-12(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS.
  8. "The four terminal components of the complement system are C-mannosylated on multiple tryptophan residues."
    Hofsteenge J., Blommers M., Hess D., Furmanek A., Miroshnichenko O.
    J. Biol. Chem. 274:32786-32794(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT TRP-48 AND TRP-51.
  9. "Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."
    Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.
    Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-415.
    Tissue: Plasma.
  10. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-277 AND ASN-415.
    Tissue: Plasma.
  11. "Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach."
    Lewandrowski U., Moebius J., Walter U., Sickmann A.
    Mol. Cell. Proteomics 5:226-233(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-415.
    Tissue: Platelet.
  12. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-277 AND ASN-415.
    Tissue: Liver.
  13. Cited for: GLYCOSYLATION AT ASN-415.
  14. "Localization and molecular modelling of the membrane-inserted domain of the ninth component of human complement and perforin."
    Peitsch M.C., Amiguet P., Guy R., Brunner J., Maizel J.V. Jr., Tschopp J.
    Mol. Immunol. 27:589-602(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING OF MEMBRANE-SPANNING DOMAIN (MSB).
  15. Cited for: VARIANT ARMD15 SER-167.

Entry informationi

Entry nameiCO9_HUMAN
AccessioniPrimary (citable) accession number: P02748
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 1, 1996
Last modified: September 3, 2014
This is version 155 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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