Complement component C9 precursor - Homo sapiens (Human)

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P02748 (CO9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 142. History...

Clusters with 100%, 90%, 50% identity |

Documents (5) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Complement component C9

Gene names

Name:

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	559 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	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.
Subcellular location	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.
Tissue specificity	Plasma.
Post-translational modification	Thrombin cleaves factor C9 to produce C9a and C9b. Phosphorylation sites are present in the extracellular medium.
Involvement in disease	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. Ref.5
Sequence similarities	Belongs to the complement C6/C7/C8/C9 family. Contains 1 EGF-like domain. Contains 1 LDL-receptor class A domain. Contains 1 MACPF domain. Contains 1 TSP type-1 domain.

Ontologies

Keywords
Biological process	Complement alternate pathway Complement pathway Cytolysis Immunity Innate immunity
Cellular component	Cell membrane Membrane Membrane attack complex Secreted
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	EGF-like domain Signal Transmembrane Transmembrane beta strand
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	complement activation, alternative pathway Inferred from electronic annotation. Source: UniProtKB-KW complement activation, classical pathway Inferred from electronic annotation. Source: UniProtKB-KW cytolysis Inferred from electronic annotation. Source: UniProtKB-KW hemolysis by symbiont of host erythrocytes Traceable author statement PubMed 2426252. Source: ProtInc innate immune response Traceable author statement. Source: Reactome
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA extracellular region Traceable author statement. Source: Reactome integral to plasma membrane Traceable author statement PubMed 2426252. Source: ProtInc membrane attack complex Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

Ref.3

Chain

22 – 559

538

Complement component C9

PRO_0000023602

Chain

22 – 265

244

Complement component C9a

PRO_0000023603

Chain

266 – 559

294

Complement component C9b

PRO_0000023604

Regions

Transmembrane

314 – 330

Beta stranded; Potential

Transmembrane

335 – 354

Beta stranded; Potential

Domain

42 – 95

TSP type-1

Domain

99 – 136

LDL-receptor class A

Domain

138 – 509

372

MACPF

Domain

510 – 540

EGF-like

Sites

Site

265 – 266

Cleavage; by thrombin

Amino acid modifications

Glycosylation

C-linked (Man) Ref.8

Glycosylation

C-linked (Man); partial Ref.8

Glycosylation

277

N-linked (GlcNAc...) Ref.6 Ref.10 Ref.12

Glycosylation

415

N-linked (GlcNAc...) Ref.6 Ref.9 Ref.10 Ref.11 Ref.12

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Natural variations

Natural variant

R → W.
Corresponds to variant rs700233 [ dbSNP | Ensembl ].

VAR_022024

Natural variant

119

C → G in C9D. Ref.5

VAR_012648

Natural variant

127

D → Y.
Corresponds to variant rs696763 [ dbSNP | Ensembl ].

VAR_050481

Natural variant

203

I → V.
Corresponds to variant rs13361416 [ dbSNP | Ensembl ].

VAR_027651

Natural variant

279

T → S.
Corresponds to variant rs34625111 [ dbSNP | Ensembl ].

VAR_033802

Natural variant

427

S → T.
Corresponds to variant rs34421659 [ dbSNP | Ensembl ].

VAR_061503

Experimental info

Sequence conflict

C → R in AAA51889. Ref.3

Sequence conflict

314

Missing in AAA51889. Ref.3

Sequence conflict

417

T → P in AAA51889. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

P02748 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: 7403F6AD77B3ECE1
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FASTA

559

63,173

        10         20         30         40         50         60 
MSACRSFAVA ICILEISILT AQYTTSYDPE LTESSGSASH IDCRMSPWSE WSQCDPCLRQ 

        70         80         90        100        110        120 
MFRSRSIEVF GQFNGKRCTD AVGDRRQCVP TEPCEDAEDD CGNDFQCSTG RCIKMRLRCN 

       130        140        150        160        170        180 
GDNDCGDFSD EDDCESEPRP PCRDRVVEES ELARTAGYGI NILGMDPLST PFDNEFYNGL 

       190        200        210        220        230        240 
CNRDRDGNTL TYYRRPWNVA SLIYETKGEK NFRTEHYEEQ IEAFKSIIQE KTSNFNAAIS 

       250        260        270        280        290        300 
LKFTPTETNK AEQCCEETAS SISLHGKGSF RFSYSKNETY QLFLSYSSKK EKMFLHVKGE 

       310        320        330        340        350        360 
IHLGRFVMRN RDVVLTTTFV DDIKALPTTY EKGEYFAFLE TYGTHYSSSG SLGGLYELIY 

       370        380        390        400        410        420 
VLDKASMKRK GVELKDIKRC LGYHLDVSLA FSEISVGAEF NKDDCVKRGE GRAVNITSEN 

       430        440        450        460        470        480 
LIDDVVSLIR GGTRKYAFEL KEKLLRGTVI DVTDFVNWAS SINDAPVLIS QKLSPIYNLV 

       490        500        510        520        530        540 
PVKMKNAHLK KQNLERAIED YINEFSVRKC HTCQNGGTVI LMDGKCLCAC PFKFEGIACE 

       550 
ISKQKISEGL PALEFPNEK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Heterogeneity in the genetic basis of human complement C9 deficiency." Witzel-Schloemp K., Hobart M.J., Fernie B.A., Orren A., Wuerzner R., Rittner C., Kaufmann T., Schneider P.M. Immunogenetics 48:144-147(1998) [PubMed] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Liver.
[13]	"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).
+	Additional computationally mapped references.

Web resources

C9base

C9 mutation db

Cross-references

Sequence databases
EMBL GenBank DDBJ	X02176 mRNA. Translation: CAA26117.1. BC020721 mRNA. Translation: AAH20721.1. K02766 mRNA. Translation: AAA51889.1. J02833 Genomic DNA. Translation: AAA51890.1. Y08545 Y08554 Genomic DNA. Translation: CAA69849.1.
IPI	IPI00022395.
PIR	C9HU. A59363.
RefSeq	NP_001728.1. NM_001737.3.
UniGene	Hs.654443.
3D structure databases
ProteinModelPortal	P02748.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1124N.
STRING	9606.ENSP00000263408.
PTM databases
PhosphoSite	P02748.
Polymorphism databases
DMDM	1352108.
Proteomic databases
PaxDb	P02748.
PeptideAtlas	P02748.
PRIDE	P02748.
Protocols and materials databases
DNASU	735.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000263408; ENSP00000263408; ENSG00000113600.
GeneID	735.
KEGG	hsa:735.
UCSC	uc003jlv.4. human.
Organism-specific databases
CTD	735.
GeneCards	GC05M039320.
HGNC	HGNC:1358. C9.
HPA	CAB002151. HPA029577.
MIM	120940. gene. 613825. phenotype.
neXtProt	NX_P02748.
Orphanet	169150. Immunodeficiency due to a late component of complements deficiency.
PharmGKB	PA25968.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG46204.
HOGENOM	HOG000111869.
HOVERGEN	HBG106792.
InParanoid	P02748.
KO	K04000.
OMA	DFVNWAS.
OrthoDB	EOG4XPQFJ.
PhylomeDB	P02748.
Enzyme and pathway databases
Reactome	REACT_6900. Immune System.
Gene expression databases
ArrayExpress	P02748.
Bgee	P02748.
CleanEx	HS_C9.
Genevestigator	P02748.
GermOnline	ENSG00000113600. Homo sapiens.
Family and domain databases
Gene3D	4.10.400.10. 1 hit.
InterPro	IPR023415. LDLR_class-A_CS. IPR002172. LDrepeatLR_classA_rpt. IPR001862. MAC_perforin. IPR020864. MACPF. IPR020863. MACPF_CS. IPR000884. Thrombospondin_1_rpt. [Graphical view]
Pfam	PF00057. Ldl_recept_a. 1 hit. PF01823. MACPF. 1 hit. PF00090. TSP_1. 1 hit. [Graphical view]
PRINTS	PR00764. COMPLEMENTC9.
SMART	SM00192. LDLa. 1 hit. SM00457. MACPF. 1 hit. SM00209. TSP1. 1 hit. [Graphical view]
SUPFAM	SSF57424. LDL_rcpt_classA_cys-rich. 1 hit. SSF82895. TSP1. 1 hit.
PROSITE	PS00022. EGF_1. 1 hit. PS01186. EGF_2. 1 hit. PS50026. EGF_3. False negative. 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]
ProtoNet	Search...
Other
GenomeRNAi	735.
NextBio	2992.
SOURCE	Search...

Entry information

Entry name

CO9_HUMAN

Accession

Primary (citable) accession number: P02748

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	February 1, 1996
Last modified:	May 1, 2013
This is version 142 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.

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Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following 2 chains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents