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P07360

- CO8G_HUMAN

UniProt

P07360 - CO8G_HUMAN

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
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    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 3 (03 Oct 2006)
      Previous versions | rss
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    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

    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

    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 – 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

    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

    1
    202
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07360.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the calycin superfamily. Lipocalin family.Curated

    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

    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: October 1, 2014
    This is version 157 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