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P10643 (CO7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Complement component C7
Gene names
Name:C7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length843 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. C7 serves as a membrane anchor.

Subunit structure

Monomer or dimer; as a C5b-7 complex it can also form multimeric rosettes. 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.

Post-translational modification

C7 has 28 disulfide bridges.

O- and C-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans. Ref.4 Ref.7 Ref.8

Involvement in disease

Complement component 7 deficiency (C7D) [MIM:610102]: A rare defect of the complement classical pathway associated with susceptibility to severe recurrent infections, predominantly by Neisseria gonorrhoeae or Neisseria meningitidis.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.10 Ref.11 Ref.12

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 2 Sushi (CCP/SCR) domains.

Contains 2 TSP type-1 domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222
Chain23 – 843821Complement component C7
PRO_0000023583

Regions

Domain27 – 8054TSP type-1 1
Domain83 – 12139LDL-receptor class A
Domain124 – 456333MACPF
Domain457 – 48731EGF-like
Domain500 – 54950TSP type-1 2
Domain569 – 62860Sushi 1
Domain629 – 69062Sushi 2
Region545 – 61571CCP 1
Region616 – 69378CCP 2
Region695 – 77076Factor I module (FIM) 1
Region771 – 84373Factor I module (FIM) 2

Amino acid modifications

Glycosylation361C-linked (Man) Ref.4
Glycosylation2021N-linked (GlcNAc...) Ref.5 Ref.6
Glycosylation5031C-linked (Man); partial Ref.4
Glycosylation5061C-linked (Man); partial Ref.4
Glycosylation5091C-linked (Man); partial Ref.4
Glycosylation6961O-linked (GalNAc...) Ref.8
Glycosylation7541N-linked (GlcNAc...) (complex) Ref.6 Ref.7
Disulfide bond85 ↔ 96 By similarity
Disulfide bond91 ↔ 109 By similarity
Disulfide bond103 ↔ 119 By similarity
Disulfide bond128 ↔ 165 By similarity
Disulfide bond337 ↔ 353 Ref.9
Disulfide bond571 ↔ 613 By similarity
Disulfide bond599 ↔ 626 By similarity
Disulfide bond631 ↔ 673 By similarity
Disulfide bond659 ↔ 688 By similarity
Disulfide bond702 ↔ 713 Ref.9
Disulfide bond715 ↔ 750 Ref.9
Disulfide bond721 ↔ 743 Ref.9
Disulfide bond728 ↔ 763 Ref.9
Disulfide bond773 ↔ 782 Ref.9
Disulfide bond776 ↔ 789 Ref.9
Disulfide bond791 ↔ 825 Ref.9
Disulfide bond797 ↔ 818 Ref.9
Disulfide bond805 ↔ 838 Ref.9

Natural variations

Natural variant1281C → R.
Corresponds to variant rs2271708 [ dbSNP | Ensembl ].
VAR_050480
Natural variant2201R → Q in C7D. Ref.12
VAR_012643
Natural variant3791G → R in C7D. Ref.11
VAR_012644
Natural variant3891S → T Polymorphism confirmed at protein level. Ref.3 Ref.13
Corresponds to variant rs1063499 [ dbSNP | Ensembl ].
VAR_033798
Natural variant4201K → Q.
Corresponds to variant rs3792646 [ dbSNP | Ensembl ].
VAR_022023
Natural variant5211R → S in C7D. Ref.10
Corresponds to variant rs121964920 [ dbSNP | Ensembl ].
VAR_012645
Natural variant5871T → P Polymorphism confirmed at protein level. Ref.1 Ref.13
Corresponds to variant rs13157656 [ dbSNP | Ensembl ].
VAR_033799
Natural variant6821E → Q in C7D. Ref.12
VAR_012646
Natural variant6871R → H in C7D. Ref.12
VAR_012647

Experimental info

Sequence conflict1521R → V in CAA60121. Ref.3
Sequence conflict821 – 8222GA → AL Ref.3

Secondary structure

.............................. 843
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P10643 [UniParc].

Last modified March 15, 2005. Version 2.
Checksum: DBD5D7C92DF71FA5

FASTA84393,518
        10         20         30         40         50         60 
MKVISLFILV GFIGEFQSFS SASSPVNCQW DFYAPWSECN GCTKTQTRRR SVAVYGQYGG 

        70         80         90        100        110        120 
QPCVGNAFET QSCEPTRGCP TEEGCGERFR CFSGQCISKS LVCNGDSDCD EDSADEDRCE 

       130        140        150        160        170        180 
DSERRPSCDI DKPPPNIELT GNGYNELTGQ FRNRVINTKS FGGQCRKVFS GDGKDFYRLS 

       190        200        210        220        230        240 
GNVLSYTFQV KINNDFNYEF YNSTWSYVKH TSTEHTSSSR KRSFFRSSSS SSRSYTSHTN 

       250        260        270        280        290        300 
EIHKGKSYQL LVVENTVEVA QFINNNPEFL QLAEPFWKEL SHLPSLYDYS AYRRLIDQYG 

       310        320        330        340        350        360 
THYLQSGSLG GEYRVLFYVD SEKLKQNDFN SVEEKKCKSS GWHFVVKFSS HGCKELENAL 

       370        380        390        400        410        420 
KAASGTQNNV LRGEPFIRGG GAGFISGLSY LELDNPAGNK RRYSAWAESV TNLPQVIKQK 

       430        440        450        460        470        480 
LTPLYELVKE VPCASVKKLY LKWALEEYLD EFDPCHCRPC QNGGLATVEG THCLCHCKPY 

       490        500        510        520        530        540 
TFGAACEQGV LVGNQAGGVD GGWSCWSSWS PCVQGKKTRS RECNNPPPSG GGRSCVGETT 

       550        560        570        580        590        600 
ESTQCEDEEL EHLRLLEPHC FPLSLVPTEF CPSPPALKDG FVQDEGTMFP VGKNVVYTCN 

       610        620        630        640        650        660 
EGYSLIGNPV ARCGEDLRWL VGEMHCQKIA CVLPVLMDGI QSHPQKPFYT VGEKVTVSCS 

       670        680        690        700        710        720 
GGMSLEGPSA FLCGSSLKWS PEMKNARCVQ KENPLTQAVP KCQRWEKLQN SRCVCKMPYE 

       730        740        750        760        770        780 
CGPSLDVCAQ DERSKRILPL TVCKMHVLHC QGRNYTLTGR DSCTLPASAE KACGACPLWG 

       790        800        810        820        830        840 
KCDAESSKCV CREASECEEE GFSICVEVNG KEQTMSECEA GALRCRGQSI SVTSIRPCAA 


ETQ 

« Hide

References

« Hide 'large scale' references
[1]"The structure of human complement component C7 and the C5b-7 complex."
Discipio R.G., Chakravari D.N., Mueller-Eberhard H.J., Fey G.H.
J. Biol. Chem. 263:549-560(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, VARIANT PRO-587.
[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: PNS.
[3]"Structure of the human C7 gene and comparison with the C6, C8A, C8B and C9 genes."
Hobart M.J., Fernie B.A., DiScipio R.G.
J. Immunol. 154:5188-5194(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-822, VARIANT THR-389.
[4]"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-36; TRP-503; TRP-506 AND TRP-509.
[5]"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-202.
Tissue: Plasma.
[6]"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-202 AND ASN-754.
Tissue: Plasma.
[7]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-754.
[8]"Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD."
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.
Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT THR-696, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.
[9]"Solution structure of factor I-like modules from complement C7 reveals a pair of follistatin domains in compact pseudosymmetric arrangement."
Phelan M.M., Thai C.-T., Soares D.C., Ogata R.T., Barlow P.N., Bramham J.
J. Biol. Chem. 284:19637-19649(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 693-843, DISULFIDE BONDS.
[10]"Molecular bases of combined subtotal deficiencies of C6 and C7: their effects in combination with other C6 and C7 deficiencies."
Fernie B.A., Wurzner R., Orren A., Morgan B.P., Potter P.C., Platonov A.E., Vershinina I.V., Shipulin G.A., Lachmann P.J., Hobart M.J.
J. Immunol. 157:3648-3657(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT C7D SER-521.
[11]"Molecular bases of C7 deficiency: three different defects."
Fernie B.A., Orren A., Sheehan G., Schlesinger M., Hobart M.J.
J. Immunol. 159:1019-1026(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT C7D ARG-379.
[12]"Complement C7 deficiency: seven further molecular defects and their associated marker haplotypes."
Fernie B.A., Hobart M.J.
Hum. Genet. 103:513-519(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS C7D GLN-220; GLN-682 AND HIS-687.
[13]"Quantitative detection of single amino acid polymorphisms by targeted proteomics."
Su Z.D., Sun L., Yu D.X., Li R.X., Li H.X., Yu Z.J., Sheng Q.H., Lin X., Zeng R., Wu J.R.
J. Mol. Cell Biol. 3:309-315(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS THR-389 AND PRO-587, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Web resources

C7base

C7 mutation db

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03507 mRNA. Translation: AAA51861.1.
BC063851 mRNA. Translation: AAH63851.1.
X86328 expand/collapse EMBL AC list , X86329, X86330, X86331, X86332, X86333, X86334, X86335, X86336, X86337, X86338, X86339, X86340, X86341, X86342, X86343, X86344 Genomic DNA. Translation: CAA60121.1.
PIRA27340.
RefSeqNP_000578.2. NM_000587.2.
UniGeneHs.78065.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2WCYNMR-A693-843[»]
ProteinModelPortalP10643.
SMRP10643. Positions 25-843.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107191. 3 interactions.
IntActP10643. 2 interactions.
MINTMINT-7032139.
STRING9606.ENSP00000322061.

PTM databases

PhosphoSiteP10643.

Polymorphism databases

DMDM61252057.

Proteomic databases

PaxDbP10643.
PRIDEP10643.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000313164; ENSP00000322061; ENSG00000112936.
GeneID730.
KEGGhsa:730.
UCSCuc003jmh.3. human.

Organism-specific databases

CTD730.
GeneCardsGC05P040909.
HGNCHGNC:1346. C7.
HPAHPA001465.
MIM217070. gene.
610102. phenotype.
neXtProtNX_P10643.
Orphanet169150. Immunodeficiency due to a late component of complements deficiency.
PharmGKBPA25941.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG145238.
HOGENOMHOG000111868.
HOVERGENHBG005367.
InParanoidP10643.
KOK03996.
OMALLEPHCF.
OrthoDBEOG7ZSHS9.
PhylomeDBP10643.
TreeFamTF330498.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

BgeeP10643.
CleanExHS_C7.
GenevestigatorP10643.

Family and domain databases

Gene3D4.10.400.10. 1 hit.
InterProIPR003884. FacI_MAC.
IPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
IPR001862. MAC_perforin.
IPR020864. MACPF.
IPR020863. MACPF_CS.
IPR000436. Sushi_SCR_CCP.
IPR000884. Thrombospondin_1_rpt.
[Graphical view]
PfamPF00057. Ldl_recept_a. 1 hit.
PF01823. MACPF. 1 hit.
PF00084. Sushi. 2 hits.
PF00090. TSP_1. 2 hits.
[Graphical view]
PRINTSPR00764. COMPLEMENTC9.
SMARTSM00032. CCP. 2 hits.
SM00057. FIMAC. 2 hits.
SM00192. LDLa. 1 hit.
SM00457. MACPF. 1 hit.
SM00209. TSP1. 2 hits.
[Graphical view]
SUPFAMSSF57535. SSF57535. 2 hits.
SSF82895. SSF82895. 2 hits.
PROSITEPS00022. 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.
PS50923. SUSHI. 2 hits.
PS50092. TSP1. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSC7. human.
EvolutionaryTraceP10643.
GenomeRNAi730.
NextBio2972.
PROP10643.
SOURCESearch...

Entry information

Entry nameCO7_HUMAN
AccessionPrimary (citable) accession number: P10643
Secondary accession number(s): Q6P3T5, Q92489
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: March 15, 2005
Last modified: April 16, 2014
This is version 154 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

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