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Protein

Complement component C8 gamma chain

Gene

C8G

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

Functioni

C8 is a constituent of the membrane attack complex. C8 binds to the C5B-7 complex, forming the C5B-8 complex. C5-B8 binds C9 and acts as a catalyst in the polymerization of C9. The gamma subunit seems to be able to bind retinol.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

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

Keywords - Ligandi

Retinol-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Complement component C8 gamma chain
Gene namesi
Name:C8G
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:1354. C8G.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • membrane attack complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane attack complex, Secreted

Pathology & Biotechi

Organism-specific databases

Orphaneti169150. Immunodeficiency due to a late component of complements deficiency.
PharmGKBiPA25953.

Polymorphism and mutation databases

BioMutaiC8G.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Add
BLAST
Chaini21 – 202182Complement component C8 gamma chainPRO_0000017881Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei21 – 211Pyrrolidone carboxylic acid1 Publication
Disulfide bondi60 – 60Interchain (with C-194 in C8-alpha chain)
Disulfide bondi96 ↔ 188

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Proteomic databases

PaxDbiP07360.
PeptideAtlasiP07360.
PRIDEiP07360.

PTM databases

PhosphoSiteiP07360.

Expressioni

Gene expression databases

BgeeiP07360.
CleanExiHS_C8G.
ExpressionAtlasiP07360. baseline and differential.
GenevisibleiP07360. HS.

Organism-specific databases

HPAiHPA046269.

Interactioni

Subunit structurei

C8 is composed of three chains: alpha, beta and gamma. The alpha and gamma chains are disulfide bonded.

Protein-protein interaction databases

BioGridi107194. 1 interaction.
STRINGi9606.ENSP00000224181.

Structurei

Secondary structure

1
202
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi32 – 354Combined sources
Helixi44 – 474Combined sources
Beta strandi49 – 579Combined sources
Helixi61 – 666Combined sources
Helixi67 – 693Combined sources
Beta strandi73 – 808Combined sources
Beta strandi83 – 9210Combined sources
Beta strandi95 – 10511Combined sources
Beta strandi111 – 1144Combined sources
Beta strandi117 – 1215Combined sources
Beta strandi123 – 1308Combined sources
Beta strandi132 – 14211Combined sources
Beta strandi145 – 15612Combined sources
Helixi159 – 17113Combined sources
Helixi176 – 1783Combined sources
Beta strandi179 – 1813Combined sources
Helixi193 – 1953Combined sources
Beta strandi196 – 1983Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IW2X-ray1.90A21-202[»]
1LF7X-ray1.20A21-202[»]
2OVAX-ray1.50A21-202[»]
2OVDX-ray1.80A21-202[»]
2OVEX-ray2.00A21-202[»]
2QOSX-ray1.81C30-202[»]
2RD7X-ray2.15C21-202[»]
3OJYX-ray2.51C21-202[»]
ProteinModelPortaliP07360.
SMRiP07360. Positions 30-202.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07360.

Family & Domainsi

Sequence similaritiesi

Belongs to the calycin superfamily. Lipocalin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG39544.
GeneTreeiENSGT00440000034309.
HOGENOMiHOG000111143.
HOVERGENiHBG005369.
InParanoidiP07360.
KOiK03999.
OMAiDAQQFAG.
PhylomeDBiP07360.
TreeFamiTF336103.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR002968. A1-microglobln.
IPR012674. Calycin.
IPR011038. Calycin-like.
IPR002345. Lipocalin.
IPR022272. Lipocalin_CS.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR01215. A1MCGLOBULIN.
PR00179. LIPOCALIN.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00213. LIPOCALIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P07360-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPPGTATLL TLLLAAGSLG QKPQRPRRPA SPISTIQPKA NFDAQQFAGT
60 70 80 90 100
WLLVAVGSAC RFLQEQGHRA EATTLHVAPQ GTAMAVSTFR KLDGICWQVR
110 120 130 140 150
QLYGDTGVLG RFLLQARDAR GAVHVVVAET DYQSFAVLYL ERAGQLSVKL
160 170 180 190 200
YARSLPVSDS VLSGFEQRVQ EAHLTEDQIF YFPKYGFCEA ADQFHVLDEV

RR
Length:202
Mass (Da):22,277
Last modified:October 3, 2006 - v3
Checksum:i4E4F73140E607FFE
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti69 – 691R → Q.
Corresponds to variant rs17614 [ dbSNP | Ensembl ].
VAR_014668
Natural varianti118 – 1181D → G.5 Publications
Corresponds to variant rs7850844 [ dbSNP | Ensembl ].
VAR_044319
Natural varianti124 – 1241H → N.1 Publication
Corresponds to variant rs17613 [ dbSNP | Ensembl ].
VAR_014669

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17263 mRNA. Translation: AAA51888.1.
M17999 mRNA. Translation: AAA51863.1.
X06465 mRNA. Translation: CAA29773.1.
U08198 Genomic DNA. Translation: AAA18482.1.
AL807752 Genomic DNA. Translation: CAI12749.1.
CH471090 Genomic DNA. Translation: EAW88316.1.
BC113624 mRNA. Translation: AAI13625.1.
BC113626 mRNA. Translation: AAI13627.1.
CCDSiCCDS7017.1.
PIRiA27487. C8HUG.
RefSeqiNP_000597.2. NM_000606.2.
UniGeneiHs.1285.

Genome annotation databases

EnsembliENST00000224181; ENSP00000224181; ENSG00000176919.
GeneIDi733.
KEGGihsa:733.
UCSCiuc004cka.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17263 mRNA. Translation: AAA51888.1.
M17999 mRNA. Translation: AAA51863.1.
X06465 mRNA. Translation: CAA29773.1.
U08198 Genomic DNA. Translation: AAA18482.1.
AL807752 Genomic DNA. Translation: CAI12749.1.
CH471090 Genomic DNA. Translation: EAW88316.1.
BC113624 mRNA. Translation: AAI13625.1.
BC113626 mRNA. Translation: AAI13627.1.
CCDSiCCDS7017.1.
PIRiA27487. C8HUG.
RefSeqiNP_000597.2. NM_000606.2.
UniGeneiHs.1285.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IW2X-ray1.90A21-202[»]
1LF7X-ray1.20A21-202[»]
2OVAX-ray1.50A21-202[»]
2OVDX-ray1.80A21-202[»]
2OVEX-ray2.00A21-202[»]
2QOSX-ray1.81C30-202[»]
2RD7X-ray2.15C21-202[»]
3OJYX-ray2.51C21-202[»]
ProteinModelPortaliP07360.
SMRiP07360. Positions 30-202.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107194. 1 interaction.
STRINGi9606.ENSP00000224181.

PTM databases

PhosphoSiteiP07360.

Polymorphism and mutation databases

BioMutaiC8G.

Proteomic databases

PaxDbiP07360.
PeptideAtlasiP07360.
PRIDEiP07360.

Protocols and materials databases

DNASUi733.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000224181; ENSP00000224181; ENSG00000176919.
GeneIDi733.
KEGGihsa:733.
UCSCiuc004cka.2. human.

Organism-specific databases

CTDi733.
GeneCardsiGC09P139839.
H-InvDBHIX0201411.
HGNCiHGNC:1354. C8G.
HPAiHPA046269.
MIMi120930. gene.
neXtProtiNX_P07360.
Orphaneti169150. Immunodeficiency due to a late component of complements deficiency.
PharmGKBiPA25953.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG39544.
GeneTreeiENSGT00440000034309.
HOGENOMiHOG000111143.
HOVERGENiHBG005369.
InParanoidiP07360.
KOiK03999.
OMAiDAQQFAG.
PhylomeDBiP07360.
TreeFamiTF336103.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP07360.
GenomeRNAii733.
NextBioi2984.
PROiP07360.
SOURCEiSearch...

Gene expression databases

BgeeiP07360.
CleanExiHS_C8G.
ExpressionAtlasiP07360. baseline and differential.
GenevisibleiP07360. HS.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR002968. A1-microglobln.
IPR012674. Calycin.
IPR011038. Calycin-like.
IPR002345. Lipocalin.
IPR022272. Lipocalin_CS.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR01215. A1MCGLOBULIN.
PR00179. LIPOCALIN.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00213. LIPOCALIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The eighth component of human complement: evidence that it is an oligomeric serum protein assembled from products of three different genes."
    Ng S.C., Rao A.G., Howard O.M.Z., Sodetz J.M.
    Biochemistry 26:5229-5233(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, PYROGLUTAMATE FORMATION AT GLN-21, VARIANT GLY-118.
  2. "Structural homology of human complement component C8 gamma and plasma protein HC: identity of the cysteine bond pattern."
    Haefliger J.-A., Jenne D.E., Stanley K.K., Tschopp J.
    Biochem. Biophys. Res. Commun. 149:750-754(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLY-118.
    Tissue: Liver.
  3. "Genomic structure of the human complement protein C8 gamma: homology to the lipocalin gene family."
    Kaufman K.M., Sodetz J.M.
    Biochemistry 33:5162-5166(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLY-118.
    Tissue: Blood.
  4. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLY-118.
  6. "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], VARIANTS GLY-118 AND ASN-124.
    Tissue: Colon.
  7. "The homology of complement factor C8 gamma chain and alpha-1-microglobulin."
    Hunt L.T., Elzanowski A., Barker W.C.
    Biochem. Biophys. Res. Commun. 149:282-288(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: SIMILARITY TO LIPOCALINS.
  8. "Structural and functional characterization of complement C8 gamma, a member of the lipocalin protein family."
    Haefliger J.-A., Peitsch M.C., Jenne D.E., Tschopp J.
    Mol. Immunol. 28:123-131(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS, RETINOL-BINDING, 3D-STRUCTURE MODELING.
  9. Cited for: REVIEW.
  10. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. "Crystal structure of human complement protein C8gamma at 1.2 A resolution reveals a lipocalin fold and a distinct ligand binding site."
    Ortlund E., Parker C.L., Schreck S.F., Ginell S., Minor W., Sodetz J.M., Lebioda L.
    Biochemistry 41:7030-7037(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 21-202, DISULFIDE BOND.
  12. "Structural features of the ligand binding site on human complement protein C8gamma: a member of the lipocalin family."
    Chiswell B., Lovelace L.L., Brannen C., Ortlund E.A., Lebioda L., Sodetz J.M.
    Biochim. Biophys. Acta 1774:637-644(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 21-202, DISULFIDE BOND.
  13. "Crystal structure of complement protein C8gamma in complex with a peptide containing the C8gamma binding site on C8alpha: implications for C8gamma ligand binding."
    Lovelace L.L., Chiswell B., Slade D.J., Sodetz J.M., Lebioda L.
    Mol. Immunol. 45:750-756(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 30-202, DISULFIDE BOND.

Entry informationi

Entry nameiCO8G_HUMAN
AccessioniPrimary (citable) accession number: P07360
Secondary accession number(s): Q14CT8, Q14CU0, Q5SQ07
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: October 3, 2006
Last modified: June 24, 2015
This is version 165 of the entry and version 3 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: 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

External Data

Dasty 3

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 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.