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P07360

- CO8G_HUMAN

UniProt

P07360 - CO8G_HUMAN

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Protein
Complement component C8 gamma chain
Gene
C8G
Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. retinol binding Source: UniProtKB-KW

GO - Biological processi

  1. complement activation, alternative pathway Source: UniProtKB-KW
  2. complement activation, classical pathway Source: UniProtKB-KW
  3. cytolysis Source: UniProtKB-KW
  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

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: Chromosome 9

Organism-specific databases

HGNCiHGNC:1354. C8G.

Subcellular locationi

GO - Cellular componenti

  1. blood microparticle Source: UniProt
  2. extracellular region Source: Reactome
  3. extracellular vesicular exosome Source: UniProt
  4. 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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020
Add
BLAST
Chaini21 – 202182Complement component C8 gamma chain
PRO_0000017881Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei21 – 211Pyrrolidone carboxylic acid
Disulfide bondi60 – 60Interchain (with C-194 in C8-alpha chain)4 Publications
Disulfide bondi96 ↔ 1884 Publications

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Proteomic databases

PaxDbiP07360.
PeptideAtlasiP07360.
PRIDEiP07360.

PTM databases

PhosphoSiteiP07360.

Expressioni

Gene expression databases

ArrayExpressiP07360.
BgeeiP07360.
CleanExiHS_C8G.
GenevestigatoriP07360.

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

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP07360.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG39544.
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

MLPPGTATLL TLLLAAGSLG QKPQRPRRPA SPISTIQPKA NFDAQQFAGT    50
WLLVAVGSAC RFLQEQGHRA EATTLHVAPQ GTAMAVSTFR KLDGICWQVR 100
QLYGDTGVLG RFLLQARDAR GAVHVVVAET DYQSFAVLYL ERAGQLSVKL 150
YARSLPVSDS VLSGFEQRVQ EAHLTEDQIF YFPKYGFCEA ADQFHVLDEV 200
RR 202
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS7017.1.
PIRi A27487. C8HUG.
RefSeqi NP_000597.2. NM_000606.2.
UniGenei Hs.1285.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1IW2 X-ray 1.90 A 21-202 [» ]
1LF7 X-ray 1.20 A 21-202 [» ]
2OVA X-ray 1.50 A 21-202 [» ]
2OVD X-ray 1.80 A 21-202 [» ]
2OVE X-ray 2.00 A 21-202 [» ]
2QOS X-ray 1.81 C 30-202 [» ]
2RD7 X-ray 2.15 C 21-202 [» ]
3OJY X-ray 2.51 C 21-202 [» ]
ProteinModelPortali P07360.
SMRi P07360. Positions 30-202.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107194. 1 interaction.
STRINGi 9606.ENSP00000224181.

PTM databases

PhosphoSitei P07360.

Proteomic databases

PaxDbi P07360.
PeptideAtlasi P07360.
PRIDEi P07360.

Protocols and materials databases

DNASUi 733.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000224181 ; ENSP00000224181 ; ENSG00000176919 .
GeneIDi 733.
KEGGi hsa:733.
UCSCi uc004cka.2. human.

Organism-specific databases

CTDi 733.
GeneCardsi GC09P139839.
H-InvDB HIX0201411.
HGNCi HGNC:1354. C8G.
HPAi HPA046269.
MIMi 120930. gene.
neXtProti NX_P07360.
Orphaneti 169150. Immunodeficiency due to a late component of complements deficiency.
PharmGKBi PA25953.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG39544.
HOGENOMi HOG000111143.
HOVERGENi HBG005369.
InParanoidi P07360.
KOi K03999.
OMAi DAQQFAG.
PhylomeDBi P07360.
TreeFami TF336103.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTracei P07360.
GenomeRNAii 733.
NextBioi 2984.
PROi P07360.
SOURCEi Search...

Gene expression databases

ArrayExpressi P07360.
Bgeei P07360.
CleanExi HS_C8G.
Genevestigatori P07360.

Family and domain databases

Gene3Di 2.40.128.20. 1 hit.
InterProi IPR002968. A1-microglobln.
IPR012674. Calycin.
IPR011038. Calycin-like.
IPR002345. Lipocalin.
IPR022272. Lipocalin_CS.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view ]
Pfami PF00061. Lipocalin. 1 hit.
[Graphical view ]
PRINTSi PR01215. A1MCGLOBULIN.
PR00179. LIPOCALIN.
SUPFAMi SSF50814. SSF50814. 1 hit.
PROSITEi PS00213. LIPOCALIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. "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.
  11. "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.
  12. "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: September 3, 2014
This is version 156 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

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