CO8G_MOUSE
ID CO8G_MOUSE Reviewed; 202 AA.
AC Q8VCG4;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Complement component C8 gamma chain;
DE Flags: Precursor;
GN Name=C8g;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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 [2]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-158 AND ASN-173.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=16944957; DOI=10.1021/pr060186m;
RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT "Proteome-wide characterization of N-glycosylation events by diagonal
RT chromatography.";
RL J. Proteome Res. 5:2438-2447(2006).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: C8 is composed of three chains: alpha, beta and gamma. The
CC alpha and gamma chains are disulfide bonded (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000305}.
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DR EMBL; BC019967; AAH19967.1; -; mRNA.
DR CCDS; CCDS15777.1; -.
DR RefSeq; NP_081338.1; NM_027062.2.
DR AlphaFoldDB; Q8VCG4; -.
DR SMR; Q8VCG4; -.
DR BioGRID; 213399; 2.
DR ComplexPortal; CPX-6202; Membrane attack complex.
DR STRING; 10090.ENSMUSP00000041855; -.
DR GlyGen; Q8VCG4; 3 sites.
DR iPTMnet; Q8VCG4; -.
DR PhosphoSitePlus; Q8VCG4; -.
DR CPTAC; non-CPTAC-3301; -.
DR CPTAC; non-CPTAC-5591; -.
DR jPOST; Q8VCG4; -.
DR MaxQB; Q8VCG4; -.
DR PaxDb; Q8VCG4; -.
DR PeptideAtlas; Q8VCG4; -.
DR PRIDE; Q8VCG4; -.
DR ProteomicsDB; 283673; -.
DR Antibodypedia; 18835; 83 antibodies from 20 providers.
DR DNASU; 69379; -.
DR Ensembl; ENSMUST00000040042; ENSMUSP00000041855; ENSMUSG00000015083.
DR GeneID; 69379; -.
DR KEGG; mmu:69379; -.
DR UCSC; uc008isi.2; mouse.
DR CTD; 733; -.
DR MGI; MGI:88237; C8g.
DR VEuPathDB; HostDB:ENSMUSG00000015083; -.
DR eggNOG; ENOG502S0KX; Eukaryota.
DR GeneTree; ENSGT00440000034309; -.
DR HOGENOM; CLU_094061_0_0_1; -.
DR InParanoid; Q8VCG4; -.
DR OMA; LMCVCLW; -.
DR OrthoDB; 1331491at2759; -.
DR PhylomeDB; Q8VCG4; -.
DR TreeFam; TF336103; -.
DR Reactome; R-MMU-166665; Terminal pathway of complement.
DR Reactome; R-MMU-977606; Regulation of Complement cascade.
DR BioGRID-ORCS; 69379; 0 hits in 72 CRISPR screens.
DR ChiTaRS; C8g; mouse.
DR PRO; PR:Q8VCG4; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8VCG4; protein.
DR Bgee; ENSMUSG00000015083; Expressed in left lobe of liver and 118 other tissues.
DR ExpressionAtlas; Q8VCG4; baseline and differential.
DR Genevisible; Q8VCG4; MM.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005579; C:membrane attack complex; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IC:ComplexPortal.
DR GO; GO:0001848; F:complement binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
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 GO; GO:0050778; P:positive regulation of immune response; IC:ComplexPortal.
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 Complement alternate pathway; Complement pathway; Cytolysis;
KW Disulfide bond; Glycoprotein; Immunity; Innate immunity;
KW Membrane attack complex; Pyrrolidone carboxylic acid; Reference proteome;
KW Retinol-binding; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..202
FT /note="Complement component C8 gamma chain"
FT /id="PRO_0000017882"
FT MOD_RES 21
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P07360"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT DISULFID 60
FT /note="Interchain (with C-194 in C8-alpha chain)"
FT /evidence="ECO:0000250"
FT DISULFID 96..188
FT /evidence="ECO:0000250"
SQ SEQUENCE 202 AA; 22508 MW; CA7E08B1B663CE50 CRC64;
MLSPGAVLFF TLLLTASSLG QRTRKPIGST SPISTIQAQV NFSAQKFAGT WLLVAVGSSC
RFLQEQGHRA EATTLHAAPQ GAAMAVSTFR KLDGICWQVR QLFENTGVPG RFLFQVSRAR
GPVHMVVAET DYQSFAILYL EQGRKLSVKL YVRSLPVNDS VLDVFERRVR EANLTEDQIL
FFPKYGFCET ADQLHILNEV PR
