CO8G_RABIT
ID CO8G_RABIT Reviewed; 202 AA.
AC Q28679;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Complement component C8 gamma chain;
DE Flags: Precursor;
GN Name=C8G;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New Zealand white; TISSUE=Liver;
RX PubMed=7510745;
RA White R.V., Kaufman K.M., Letson C.S., Platteborze P.L., Sodetz J.M.;
RT "Characterization of rabbit complement component C8. Functional evidence
RT for the species-selective recognition of C8 alpha by homologous restriction
RT factor (CD59).";
RL J. Immunol. 152:2501-2508(1994).
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; L26979; AAA31193.1; -; mRNA.
DR PIR; I46688; I46688.
DR RefSeq; NP_001075723.1; NM_001082254.1.
DR AlphaFoldDB; Q28679; -.
DR SMR; Q28679; -.
DR PRIDE; Q28679; -.
DR GeneID; 100009075; -.
DR KEGG; ocu:100009075; -.
DR CTD; 733; -.
DR InParanoid; Q28679; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005579; C:membrane attack complex; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Complement alternate pathway; Complement pathway; Cytolysis;
KW Disulfide bond; Glycoprotein; Immunity; Innate immunity;
KW Membrane attack complex; Reference proteome; Retinol-binding; Secreted;
KW Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..202
FT /note="Complement component C8 gamma chain"
FT /id="PRO_0000017883"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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; 21901 MW; E6E82B677E126A5B CRC64;
MVLRGRAVLL AVLLAAGSLG RWAQKPRGAP SAISAIQPKA NFDAQQFAGT WLLAAVGSAC
HFLQEQGHRA EATALHVAPQ GAAMAVSTFR KLDGICWQVS QRYGATGVPG RFLLPARGPR
GAVHVVAAET DYHSFAVLYL ERARQLSVKL YVRSLPVSDS VLGAFEQRVA QANLTQDQVL
FFPTYGFCEA ADQFHILDEV RR
