P07360 (CO8G_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Complement component C8 gamma chain

Gene names

Name:

C8G

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	202 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	C8 is composed of three chains: alpha, beta and gamma. The alpha and gamma chains are disulfide bonded.
Subcellular location	Secreted.
Sequence similarities	Belongs to the calycin superfamily. Lipocalin family.

Ontologies

Keywords
Biological process	Complement alternate pathway Complement pathway Cytolysis Immunity Innate immunity
Cellular component	Membrane attack complex Secreted
Coding sequence diversity	Polymorphism
Domain	Signal
Ligand	Retinol-binding
PTM	Disulfide bond Pyrrolidone carboxylic acid
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	complement activation, alternative pathway Inferred from electronic annotation. Source: UniProtKB-KW complement activation, classical pathway Inferred from electronic annotation. Source: UniProtKB-KW cytolysis Inferred from electronic annotation. Source: UniProtKB-KW innate immune response Traceable author statement. Source: Reactome
Cellular_component	extracellular region Traceable author statement. Source: Reactome extracellular space Inferred from electronic annotation. Source: Compara membrane attack complex Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	retinol binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

20

Chain

21 – 202

182

Complement component C8 gamma chain

PRO_0000017881

Amino acid modifications

Modified residue

21

1

Pyrrolidone carboxylic acid

Disulfide bond

60

Interchain (with C-194 in C8-alpha chain) Ref.8 Ref.10 Ref.11 Ref.12

Disulfide bond

96 ↔ 188

Ref.8 Ref.10 Ref.11 Ref.12

Natural variations

Natural variant

69

1

R → Q.
Corresponds to variant rs17614 [ dbSNP | Ensembl ].

VAR_014668

Natural variant

118

1

D → G. Ref.1 Ref.2 Ref.3 Ref.5 Ref.6
Corresponds to variant rs7850844 [ dbSNP | Ensembl ].

VAR_044319

Natural variant

124

1

H → N. Ref.6
Corresponds to variant rs17613 [ dbSNP | Ensembl ].

VAR_014669

Secondary structure

1

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202

Helix Strand Turn

Details...

Helix

32 – 35

4

Helix

44 – 47

4

Beta strand

49 – 57

9

Helix

61 – 66

6

Helix

67 – 69

3

Beta strand

73 – 80

8

Beta strand

83 – 92

10

Beta strand

95 – 105

11

Beta strand

111 – 114

4

Beta strand

117 – 121

5

Beta strand

123 – 130

8

Beta strand

132 – 142

11

Beta strand

145 – 156

12

Helix

159 – 171

13

Helix

176 – 178

3

Beta strand

179 – 181

3

Helix

193 – 195

3

Beta strand

196 – 198

3

Sequences

	Sequence		Length	Mass (Da)
	P07360 [UniParc]. Last modified October 3, 2006. Version 3. Checksum: 4E4F73140E607FFE	FASTA	202	22,277
	10 20 30 40 50 60 MLPPGTATLL TLLLAAGSLG QKPQRPRRPA SPISTIQPKA NFDAQQFAGT WLLVAVGSAC 70 80 90 100 110 120 RFLQEQGHRA EATTLHVAPQ GTAMAVSTFR KLDGICWQVR QLYGDTGVLG RFLLQARDAR 130 140 150 160 170 180 GAVHVVVAET DYQSFAVLYL ERAGQLSVKL YARSLPVSDS VLSGFEQRVQ EAHLTEDQIF 190 200 YFPKYGFCEA ADQFHVLDEV RR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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, 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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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]	"Human complement protein C8 gamma." Schreck S.F., Parker C., Plumb M.E., Sodetz J.M. Biochim. Biophys. Acta 1482:199-208(2000) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00011261.

PIR

C8HUG. A27487.

RefSeq

NP_000597.2. NM_000606.2.

UniGene

Hs.1285.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P07360.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000224181.

PTM databases

PhosphoSite

P07360.

Polymorphism databases

DMDM

115502373.

Proteomic databases

PaxDb

P07360.

PeptideAtlas

P07360.

PRIDE

P07360.

Protocols and materials databases

DNASU

733.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000224181; ENSP00000224181; ENSG00000176919.

GeneID

733.

KEGG

hsa:733.

UCSC

uc004cka.2. human.

Organism-specific databases

CTD

733.

GeneCards

GC09P139839.

H-InvDB

HIX0201411.

HGNC

HGNC:1354. C8G.

HPA

HPA046269.

MIM

120930. gene.

neXtProt

NX_P07360.

Orphanet

169150. Immunodeficiency due to a late component of complements deficiency.

PharmGKB

PA25953.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG39544.

HOGENOM

HOG000111143.

HOVERGEN

HBG005369.

InParanoid

P07360.

KO

K03999.

OMA

DAQQFAG.

PhylomeDB

P07360.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P07360.

Bgee

P07360.

CleanEx

HS_C8G.

Genevestigator

P07360.

GermOnline

ENSG00000176919. Homo sapiens.

Family and domain databases

Gene3D

2.40.128.20. 1 hit.

InterPro

IPR002968. A1-microglobln.
IPR012674. Calycin.
IPR011038. Calycin-like.
IPR002345. Lipocalin.
IPR022272. Lipocalin_CS.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]

Pfam

PF00061. Lipocalin. 1 hit.
[Graphical view]

PRINTS

PR01215. A1MCGLOBULIN.
PR00179. LIPOCALIN.

SUPFAM

SSF50814. Calycin. 1 hit.

PROSITE

PS00213. LIPOCALIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P07360.

GenomeRNAi

733.

NextBio

2984.

SOURCE

Search...

Entry information

Entry name

CO8G_HUMAN

Accession

Primary (citable) accession number: P07360
Secondary accession number(s): Q14CT8, Q14CU0, Q5SQ07

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	October 3, 2006
Last modified:	May 1, 2013
This is version 146 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.