GenomeNet

Database: UniProt
Entry: P07360
LinkDB: P07360
Original site: P07360 
ID   CO8G_HUMAN              Reviewed;         202 AA.
AC   P07360; Q14CT8; Q14CU0; Q5SQ07;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 3.
DT   29-SEP-2021, entry version 207.
DE   RecName: Full=Complement component C8 gamma chain;
DE   Flags: Precursor;
GN   Name=C8G;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, PYROGLUTAMATE
RP   FORMATION AT GLN-21, AND VARIANT GLY-118.
RX   PubMed=3676249; DOI=10.1021/bi00391a003;
RA   Ng S.C., Rao A.G., Howard O.M.Z., Sodetz J.M.;
RT   "The eighth component of human complement: evidence that it is an
RT   oligomeric serum protein assembled from products of three different
RT   genes.";
RL   Biochemistry 26:5229-5233(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLY-118.
RC   TISSUE=Liver;
RX   PubMed=2447883; DOI=10.1016/0006-291x(87)90431-1;
RA   Haefliger J.-A., Jenne D.E., Stanley K.K., Tschopp J.;
RT   "Structural homology of human complement component C8 gamma and plasma
RT   protein HC: identity of the cysteine bond pattern.";
RL   Biochem. Biophys. Res. Commun. 149:750-754(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLY-118.
RC   TISSUE=Blood;
RX   PubMed=8172891; DOI=10.1021/bi00183a020;
RA   Kaufman K.M., Sodetz J.M.;
RT   "Genomic structure of the human complement protein C8 gamma: homology to
RT   the lipocalin gene family.";
RL   Biochemistry 33:5162-5166(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLY-118.
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLY-118 AND ASN-124.
RC   TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   SIMILARITY TO LIPOCALINS.
RX   PubMed=2446620; DOI=10.1016/0006-291x(87)91636-6;
RA   Hunt L.T., Elzanowski A., Barker W.C.;
RT   "The homology of complement factor C8 gamma chain and alpha-1-
RT   microglobulin.";
RL   Biochem. Biophys. Res. Commun. 149:282-288(1987).
RN   [8]
RP   DISULFIDE BONDS, RETINOL-BINDING, AND 3D-STRUCTURE MODELING.
RX   PubMed=1707134; DOI=10.1016/0161-5890(91)90095-2;
RA   Haefliger J.-A., Peitsch M.C., Jenne D.E., Tschopp J.;
RT   "Structural and functional characterization of complement C8 gamma, a
RT   member of the lipocalin protein family.";
RL   Mol. Immunol. 28:123-131(1991).
RN   [9]
RP   REVIEW.
RX   PubMed=11058761; DOI=10.1016/s0167-4838(00)00155-2;
RA   Schreck S.F., Parker C., Plumb M.E., Sodetz J.M.;
RT   "Human complement protein C8 gamma.";
RL   Biochim. Biophys. Acta 1482:199-208(2000).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 21-202, AND DISULFIDE BOND.
RX   PubMed=12033936; DOI=10.1021/bi025696i;
RA   Ortlund E., Parker C.L., Schreck S.F., Ginell S., Minor W., Sodetz J.M.,
RA   Lebioda L.;
RT   "Crystal structure of human complement protein C8gamma at 1.2 A resolution
RT   reveals a lipocalin fold and a distinct ligand binding site.";
RL   Biochemistry 41:7030-7037(2002).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 21-202, AND DISULFIDE BOND.
RX   PubMed=17452033; DOI=10.1016/j.bbapap.2007.03.004;
RA   Chiswell B., Lovelace L.L., Brannen C., Ortlund E.A., Lebioda L.,
RA   Sodetz J.M.;
RT   "Structural features of the ligand binding site on human complement protein
RT   C8gamma: a member of the lipocalin family.";
RL   Biochim. Biophys. Acta 1774:637-644(2007).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 30-202, AND DISULFIDE BOND.
RX   PubMed=17692377; DOI=10.1016/j.molimm.2007.06.359;
RA   Lovelace L.L., Chiswell B., Slade D.J., Sodetz J.M., Lebioda L.;
RT   "Crystal structure of complement protein C8gamma in complex with a peptide
RT   containing the C8gamma binding site on C8alpha: implications for C8gamma
RT   ligand binding.";
RL   Mol. Immunol. 45:750-756(2008).
CC   -!- FUNCTION: C8 is a constituent of the membrane attack complex. C8 binds
CC       to the C5B-7 complex, forming the C5B-8 complex. C5-B8 binds C9 and
CC       acts as a catalyst in the polymerization of C9. The gamma subunit seems
CC       to be able to bind retinol.
CC   -!- SUBUNIT: C8 is composed of three chains: alpha, beta and gamma. The
CC       alpha and gamma chains are disulfide bonded.
CC   -!- INTERACTION:
CC       P07360; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-9021652, EBI-947187;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M17263; AAA51888.1; -; mRNA.
DR   EMBL; M17999; AAA51863.1; -; mRNA.
DR   EMBL; X06465; CAA29773.1; -; mRNA.
DR   EMBL; U08198; AAA18482.1; -; Genomic_DNA.
DR   EMBL; AL807752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471090; EAW88316.1; -; Genomic_DNA.
DR   EMBL; BC113624; AAI13625.1; -; mRNA.
DR   EMBL; BC113626; AAI13627.1; -; mRNA.
DR   CCDS; CCDS7017.1; -.
DR   PIR; A27487; C8HUG.
DR   RefSeq; NP_000597.2; NM_000606.2.
DR   PDB; 1IW2; X-ray; 1.90 A; A=21-202.
DR   PDB; 1LF7; X-ray; 1.20 A; A=21-202.
DR   PDB; 2OVA; X-ray; 1.50 A; A=21-202.
DR   PDB; 2OVD; X-ray; 1.80 A; A=21-202.
DR   PDB; 2OVE; X-ray; 2.00 A; A=21-202.
DR   PDB; 2QOS; X-ray; 1.81 A; C=30-202.
DR   PDB; 2RD7; X-ray; 2.15 A; C=21-202.
DR   PDB; 3OJY; X-ray; 2.51 A; C=21-202.
DR   PDB; 6H03; EM; 5.60 A; E=21-202.
DR   PDB; 6H04; EM; 5.60 A; E=21-202.
DR   PDBsum; 1IW2; -.
DR   PDBsum; 1LF7; -.
DR   PDBsum; 2OVA; -.
DR   PDBsum; 2OVD; -.
DR   PDBsum; 2OVE; -.
DR   PDBsum; 2QOS; -.
DR   PDBsum; 2RD7; -.
DR   PDBsum; 3OJY; -.
DR   PDBsum; 6H03; -.
DR   PDBsum; 6H04; -.
DR   SMR; P07360; -.
DR   BioGRID; 107194; 7.
DR   ComplexPortal; CPX-6159; Membrane attack complex.
DR   IntAct; P07360; 7.
DR   STRING; 9606.ENSP00000224181; -.
DR   DrugBank; DB04272; Citric acid.
DR   DrugBank; DB03017; Lauric acid.
DR   DrugBank; DB01593; Zinc.
DR   DrugBank; DB14487; Zinc acetate.
DR   iPTMnet; P07360; -.
DR   PhosphoSitePlus; P07360; -.
DR   BioMuta; C8G; -.
DR   jPOST; P07360; -.
DR   MassIVE; P07360; -.
DR   PaxDb; P07360; -.
DR   PeptideAtlas; P07360; -.
DR   PRIDE; P07360; -.
DR   ProteomicsDB; 52000; -.
DR   Antibodypedia; 18835; 82 antibodies.
DR   DNASU; 733; -.
DR   Ensembl; ENST00000371634; ENSP00000360697; ENSG00000176919.
DR   GeneID; 733; -.
DR   KEGG; hsa:733; -.
DR   UCSC; uc004cka.3; human.
DR   CTD; 733; -.
DR   DisGeNET; 733; -.
DR   GeneCards; C8G; -.
DR   HGNC; HGNC:1354; C8G.
DR   HPA; ENSG00000176919; Tissue enriched (liver).
DR   MalaCards; C8G; -.
DR   MIM; 120930; gene.
DR   neXtProt; NX_P07360; -.
DR   OpenTargets; ENSG00000176919; -.
DR   Orphanet; 169150; Immunodeficiency due to a late component of complement deficiency.
DR   PharmGKB; PA25953; -.
DR   VEuPathDB; HostDB:ENSG00000176919; -.
DR   eggNOG; ENOG502S0KX; Eukaryota.
DR   GeneTree; ENSGT00440000034309; -.
DR   HOGENOM; CLU_094061_0_0_1; -.
DR   InParanoid; P07360; -.
DR   OMA; YLINHGT; -.
DR   OrthoDB; 1227818at2759; -.
DR   PhylomeDB; P07360; -.
DR   TreeFam; TF336103; -.
DR   PathwayCommons; P07360; -.
DR   Reactome; R-HSA-166665; Terminal pathway of complement.
DR   Reactome; R-HSA-977606; Regulation of Complement cascade.
DR   SIGNOR; P07360; -.
DR   BioGRID-ORCS; 733; 4 hits in 1005 CRISPR screens.
DR   EvolutionaryTrace; P07360; -.
DR   GenomeRNAi; 733; -.
DR   Pharos; P07360; Tbio.
DR   PRO; PR:P07360; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; P07360; protein.
DR   Bgee; ENSG00000176919; Expressed in right lobe of liver and 115 other tissues.
DR   ExpressionAtlas; P07360; baseline and differential.
DR   Genevisible; P07360; HS.
DR   GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005579; C:membrane attack complex; IEA:UniProtKB-KW.
DR   GO; GO:0001848; F:complement binding; IBA:GO_Central.
DR   GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR   GO; GO:0019841; F:retinol binding; IEA:UniProtKB-KW.
DR   GO; GO:0006957; P:complement activation, alternative pathway; IEA:UniProtKB-KW.
DR   GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.128.20; -; 1.
DR   InterPro; IPR002968; A1-microglobln.
DR   InterPro; IPR043245; C8G.
DR   InterPro; IPR012674; Calycin.
DR   InterPro; IPR022272; Lipocalin_CS.
DR   InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR   PANTHER; PTHR47304; PTHR47304; 1.
DR   Pfam; PF00061; Lipocalin; 1.
DR   PRINTS; PR01215; A1MCGLOBULIN.
DR   SUPFAM; SSF50814; SSF50814; 1.
DR   PROSITE; PS00213; LIPOCALIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complement alternate pathway; Complement pathway; Cytolysis;
KW   Direct protein sequencing; Disulfide bond; Immunity; Innate immunity;
KW   Membrane attack complex; Pyrrolidone carboxylic acid; Reference proteome;
KW   Retinol-binding; Secreted; Signal.
FT   SIGNAL          1..20
FT   CHAIN           21..202
FT                   /note="Complement component C8 gamma chain"
FT                   /id="PRO_0000017881"
FT   MOD_RES         21
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:3676249"
FT   DISULFID        60
FT                   /note="Interchain (with C-194 in C8-alpha chain)"
FT   DISULFID        96..188
FT   VARIANT         69
FT                   /note="R -> Q (in dbSNP:rs17614)"
FT                   /id="VAR_014668"
FT   VARIANT         118
FT                   /note="D -> G (in dbSNP:rs7850844)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:2447883, ECO:0000269|PubMed:3676249,
FT                   ECO:0000269|PubMed:8172891, ECO:0000269|Ref.5"
FT                   /id="VAR_044319"
FT   VARIANT         124
FT                   /note="H -> N (in dbSNP:rs17613)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_014669"
FT   HELIX           32..35
FT                   /evidence="ECO:0007829|PDB:1LF7"
FT   HELIX           44..47
FT                   /evidence="ECO:0007829|PDB:1LF7"
FT   STRAND          49..57
FT                   /evidence="ECO:0007829|PDB:1LF7"
FT   HELIX           61..66
FT                   /evidence="ECO:0007829|PDB:2QOS"
FT   HELIX           67..69
FT                   /evidence="ECO:0007829|PDB:2QOS"
FT   STRAND          73..80
FT                   /evidence="ECO:0007829|PDB:1LF7"
FT   STRAND          83..92
FT                   /evidence="ECO:0007829|PDB:1LF7"
FT   STRAND          95..105
FT                   /evidence="ECO:0007829|PDB:1LF7"
FT   STRAND          111..114
FT                   /evidence="ECO:0007829|PDB:1LF7"
FT   STRAND          117..121
FT                   /evidence="ECO:0007829|PDB:1LF7"
FT   STRAND          123..130
FT                   /evidence="ECO:0007829|PDB:1LF7"
FT   STRAND          132..142
FT                   /evidence="ECO:0007829|PDB:1LF7"
FT   STRAND          145..156
FT                   /evidence="ECO:0007829|PDB:1LF7"
FT   HELIX           159..171
FT                   /evidence="ECO:0007829|PDB:1LF7"
FT   HELIX           176..178
FT                   /evidence="ECO:0007829|PDB:1LF7"
FT   STRAND          179..181
FT                   /evidence="ECO:0007829|PDB:1LF7"
FT   HELIX           193..195
FT                   /evidence="ECO:0007829|PDB:1LF7"
FT   STRAND          196..198
FT                   /evidence="ECO:0007829|PDB:1LF7"
SQ   SEQUENCE   202 AA;  22277 MW;  4E4F73140E607FFE CRC64;
     MLPPGTATLL TLLLAAGSLG QKPQRPRRPA SPISTIQPKA NFDAQQFAGT WLLVAVGSAC
     RFLQEQGHRA EATTLHVAPQ GTAMAVSTFR KLDGICWQVR QLYGDTGVLG RFLLQARDAR
     GAVHVVVAET DYQSFAVLYL ERAGQLSVKL YARSLPVSDS VLSGFEQRVQ EAHLTEDQIF
     YFPKYGFCEA ADQFHVLDEV RR
//
DBGET integrated database retrieval system