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Protein

Complement component C8 alpha chain

Gene

C8A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells. C8A inserts into the target membrane, but does not form pores by itself.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei43 – 431Not glycosylated

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Complement alternate pathway, Complement pathway, Cytolysis, Immunity, Innate immunity

Enzyme and pathway databases

ReactomeiREACT_118707. Regulation of Complement cascade.
REACT_8028. Terminal pathway of complement.

Protein family/group databases

TCDBi1.C.39.3.1. the membrane attack complex/perforin (macpf) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Complement component C8 alpha chain
Alternative name(s):
Complement component 8 subunit alpha
Gene namesi
Name:C8A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:1352. C8A.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: ProtInc
  • membrane Source: ProtInc
  • membrane attack complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Membrane attack complex, Secreted

Pathology & Biotechi

Involvement in diseasei

Complement component 8 deficiency, 1 (C8D1)

Disease susceptibility is associated with variations affecting the gene represented in this entry.

Disease descriptionA rare defect of the complement classical pathway associated with susceptibility to severe recurrent infections, predominantly by Neisseria gonorrhoeae or Neisseria meningitidis.

See also OMIM:613790

Organism-specific databases

MIMi613790. phenotype.
Orphaneti169150. Immunodeficiency due to a late component of complements deficiency.
PharmGKBiPA25951.

Polymorphism and mutation databases

BioMutaiC8A.
DMDMi729167.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Propeptidei21 – 3010Sequence AnalysisPRO_0000023585
Chaini31 – 584554Complement component C8 alpha chainPRO_0000023586Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi39 ↔ 74By similarity
Glycosylationi44 – 441C-linked (Man)
Disulfide bondi50 ↔ 53By similarity
Disulfide bondi84 ↔ 90By similarity
Disulfide bondi96 ↔ 108By similarity
Disulfide bondi102 ↔ 121By similarity
Disulfide bondi115 ↔ 130By similarity
Disulfide bondi140 ↔ 177
Disulfide bondi194 – 194Interchain (with C-60 in C8-gamma chain)
Disulfide bondi375 ↔ 399
Glycosylationi437 – 4371N-linked (GlcNAc...)2 Publications
Glycosylationi542 – 5421C-linked (Man)
Glycosylationi545 – 5451C-linked (Man)
Glycosylationi548 – 5481C-linked (Man)

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP07357.
PaxDbiP07357.
PRIDEiP07357.

PTM databases

PhosphoSiteiP07357.

Expressioni

Gene expression databases

BgeeiP07357.
CleanExiHS_C8A.
GenevestigatoriP07357.

Interactioni

Subunit structurei

Heterotrimer of 3 chains: alpha, beta and gamma. The alpha and gamma chains are disulfide bonded. Component of the membrane attack complex (MAC). MAC assembly is initiated by protelytic cleavage of C5 into C5a and C5b. C5b binds sequentially C6, C7, C8 and multiple copies of the pore-forming subunit C9.3 Publications

Protein-protein interaction databases

BioGridi107192. 2 interactions.
DIPiDIP-1125N.
STRINGi9606.ENSP00000354458.

Structurei

Secondary structure

1
584
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni52 – 543Combined sources
Beta strandi56 – 605Combined sources
Beta strandi63 – 653Combined sources
Beta strandi78 – 836Combined sources
Beta strandi97 – 1015Combined sources
Beta strandi103 – 1053Combined sources
Helixi111 – 1133Combined sources
Beta strandi116 – 1183Combined sources
Beta strandi121 – 1233Combined sources
Beta strandi127 – 1293Combined sources
Beta strandi140 – 1434Combined sources
Helixi149 – 1524Combined sources
Beta strandi154 – 1574Combined sources
Turni158 – 1614Combined sources
Beta strandi162 – 1687Combined sources
Beta strandi179 – 1824Combined sources
Turni183 – 1864Combined sources
Beta strandi189 – 1913Combined sources
Turni192 – 1954Combined sources
Beta strandi196 – 1983Combined sources
Helixi201 – 2033Combined sources
Beta strandi204 – 2074Combined sources
Beta strandi212 – 2176Combined sources
Beta strandi226 – 2327Combined sources
Helixi233 – 24311Combined sources
Beta strandi246 – 2527Combined sources
Beta strandi260 – 2667Combined sources
Helixi273 – 2808Combined sources
Beta strandi287 – 30317Combined sources
Beta strandi305 – 3084Combined sources
Helixi312 – 3198Combined sources
Helixi327 – 33711Combined sources
Beta strandi339 – 35820Combined sources
Helixi359 – 3657Combined sources
Helixi369 – 37911Combined sources
Helixi398 – 4025Combined sources
Helixi408 – 4136Combined sources
Beta strandi416 – 4216Combined sources
Helixi443 – 4497Combined sources
Turni450 – 4523Combined sources
Beta strandi455 – 4639Combined sources
Helixi464 – 4707Combined sources
Helixi477 – 49115Combined sources
Helixi496 – 4983Combined sources
Turni503 – 5053Combined sources
Beta strandi508 – 5114Combined sources
Beta strandi514 – 5174Combined sources
Beta strandi525 – 5273Combined sources
Beta strandi552 – 5543Combined sources
Beta strandi556 – 5594Combined sources
Beta strandi578 – 5825Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QOSX-ray1.81A188-198[»]
2QQHX-ray2.50A133-366[»]
A410-492[»]
2RD7X-ray2.15A133-492[»]
3OJYX-ray2.51A31-584[»]
ProteinModelPortaliP07357.
SMRiP07357. Positions 32-582.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07357.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini38 – 9154TSP type-1 1PROSITE-ProRule annotationAdd
BLAST
Domaini94 – 13239LDL-receptor class APROSITE-ProRule annotationAdd
BLAST
Domaini135 – 498364MACPFPROSITE-ProRule annotationAdd
BLAST
Domaini499 – 52931EGF-likeAdd
BLAST
Domaini539 – 58345TSP type-1 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the complement C6/C7/C8/C9 family.Curated
Contains 1 EGF-like domain.Curated
Contains 1 LDL-receptor class A domain.PROSITE-ProRule annotation
Contains 1 MACPF domain.PROSITE-ProRule annotation
Contains 2 TSP type-1 domains.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane beta strand

Phylogenomic databases

eggNOGiNOG48024.
GeneTreeiENSGT00550000074478.
HOGENOMiHOG000231146.
HOVERGENiHBG005368.
InParanoidiP07357.
KOiK03997.
OMAiFMRIFTK.
OrthoDBiEOG7CRTPG.
PhylomeDBiP07357.
TreeFamiTF330498.

Family and domain databases

Gene3Di4.10.400.10. 1 hit.
InterProiIPR009030. Growth_fac_rcpt_N_dom.
IPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
IPR001862. MAC_perforin.
IPR020864. MACPF.
IPR020863. MACPF_CS.
IPR000884. Thrombospondin_1_rpt.
[Graphical view]
PfamiPF00057. Ldl_recept_a. 1 hit.
PF01823. MACPF. 1 hit.
PF00090. TSP_1. 1 hit.
[Graphical view]
PRINTSiPR00764. COMPLEMENTC9.
SMARTiSM00192. LDLa. 1 hit.
SM00457. MACPF. 1 hit.
SM00209. TSP1. 2 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 3 hits.
SSF82895. SSF82895. 2 hits.
PROSITEiPS00022. EGF_1. 1 hit.
PS01209. LDLRA_1. 1 hit.
PS50068. LDLRA_2. 1 hit.
PS00279. MACPF_1. 1 hit.
PS51412. MACPF_2. 1 hit.
PS50092. TSP1. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07357-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFAVVFFILS LMTCQPGVTA QEKVNQRVRR AATPAAVTCQ LSNWSEWTDC
60 70 80 90 100
FPCQDKKYRH RSLLQPNKFG GTICSGDIWD QASCSSSTTC VRQAQCGQDF
110 120 130 140 150
QCKETGRCLK RHLVCNGDQD CLDGSDEDDC EDVRAIDEDC SQYEPIPGSQ
160 170 180 190 200
KAALGYNILT QEDAQSVYDA SYYGGQCETV YNGEWRELRY DSTCERLYYG
210 220 230 240 250
DDEKYFRKPY NFLKYHFEAL ADTGISSEFY DNANDLLSKV KKDKSDSFGV
260 270 280 290 300
TIGIGPAGSP LLVGVGVSHS QDTSFLNELN KYNEKKFIFT RIFTKVQTAH
310 320 330 340 350
FKMRKDDIML DEGMLQSLME LPDQYNYGMY AKFINDYGTH YITSGSMGGI
360 370 380 390 400
YEYILVIDKA KMESLGITSR DITTCFGGSL GIQYEDKINV GGGLSGDHCK
410 420 430 440 450
KFGGGKTERA RKAMAVEDII SRVRGGSSGW SGGLAQNRST ITYRSWGRSL
460 470 480 490 500
KYNPVVIDFE MQPIHEVLRH TSLGPLEAKR QNLRRALDQY LMEFNACRCG
510 520 530 540 550
PCFNNGVPIL EGTSCRCQCR LGSLGAACEQ TQTEGAKADG SWSCWSSWSV
560 570 580
CRAGIQERRR ECDNPAPQNG GASCPGRKVQ TQAC
Length:584
Mass (Da):65,163
Last modified:February 1, 1995 - v2
Checksum:i9F61DDA51D2F3BBA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti575 – 5751P → S in AAA82124 (PubMed:7759071).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti93 – 931Q → K in allele C8A*B. 2 Publications
Corresponds to variant rs652785 [ dbSNP | Ensembl ].
VAR_011889
Natural varianti407 – 4071T → I.
Corresponds to variant rs706479 [ dbSNP | Ensembl ].
VAR_011890
Natural varianti458 – 4581D → N.
Corresponds to variant rs17114555 [ dbSNP | Ensembl ].
VAR_033800
Natural varianti485 – 4851R → L.
Corresponds to variant rs1620075 [ dbSNP | Ensembl ].
VAR_011891
Natural varianti561 – 5611E → Q.
Corresponds to variant rs1342440 [ dbSNP | Ensembl ].
VAR_011892
Natural varianti575 – 5751P → L.
Corresponds to variant rs17300936 [ dbSNP | Ensembl ].
VAR_033801

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16974 mRNA. Translation: AAA52200.1.
U08006
, U07996, U07997, U07998, U07999, U08000, U08001, U08002, U08003, U08004, U08005 Genomic DNA. Translation: AAA82124.1.
AL121998 Genomic DNA. Translation: CAI19172.1.
BC132911 mRNA. Translation: AAI32912.1.
BC132913 mRNA. Translation: AAI32914.1.
CCDSiCCDS606.1.
PIRiI37213. C8HUA.
RefSeqiNP_000553.1. NM_000562.2.
UniGeneiHs.93210.

Genome annotation databases

EnsembliENST00000361249; ENSP00000354458; ENSG00000157131.
GeneIDi731.
KEGGihsa:731.
UCSCiuc001cyo.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16974 mRNA. Translation: AAA52200.1.
U08006
, U07996, U07997, U07998, U07999, U08000, U08001, U08002, U08003, U08004, U08005 Genomic DNA. Translation: AAA82124.1.
AL121998 Genomic DNA. Translation: CAI19172.1.
BC132911 mRNA. Translation: AAI32912.1.
BC132913 mRNA. Translation: AAI32914.1.
CCDSiCCDS606.1.
PIRiI37213. C8HUA.
RefSeqiNP_000553.1. NM_000562.2.
UniGeneiHs.93210.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QOSX-ray1.81A188-198[»]
2QQHX-ray2.50A133-366[»]
A410-492[»]
2RD7X-ray2.15A133-492[»]
3OJYX-ray2.51A31-584[»]
ProteinModelPortaliP07357.
SMRiP07357. Positions 32-582.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107192. 2 interactions.
DIPiDIP-1125N.
STRINGi9606.ENSP00000354458.

Protein family/group databases

TCDBi1.C.39.3.1. the membrane attack complex/perforin (macpf) family.

PTM databases

PhosphoSiteiP07357.

Polymorphism and mutation databases

BioMutaiC8A.
DMDMi729167.

Proteomic databases

MaxQBiP07357.
PaxDbiP07357.
PRIDEiP07357.

Protocols and materials databases

DNASUi731.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000361249; ENSP00000354458; ENSG00000157131.
GeneIDi731.
KEGGihsa:731.
UCSCiuc001cyo.2. human.

Organism-specific databases

CTDi731.
GeneCardsiGC01P057237.
HGNCiHGNC:1352. C8A.
MIMi120950. gene.
613790. phenotype.
neXtProtiNX_P07357.
Orphaneti169150. Immunodeficiency due to a late component of complements deficiency.
PharmGKBiPA25951.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG48024.
GeneTreeiENSGT00550000074478.
HOGENOMiHOG000231146.
HOVERGENiHBG005368.
InParanoidiP07357.
KOiK03997.
OMAiFMRIFTK.
OrthoDBiEOG7CRTPG.
PhylomeDBiP07357.
TreeFamiTF330498.

Enzyme and pathway databases

ReactomeiREACT_118707. Regulation of Complement cascade.
REACT_8028. Terminal pathway of complement.

Miscellaneous databases

ChiTaRSiC8A. human.
EvolutionaryTraceiP07357.
GenomeRNAii731.
NextBioi2976.
PROiP07357.
SOURCEiSearch...

Gene expression databases

BgeeiP07357.
CleanExiHS_C8A.
GenevestigatoriP07357.

Family and domain databases

Gene3Di4.10.400.10. 1 hit.
InterProiIPR009030. Growth_fac_rcpt_N_dom.
IPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
IPR001862. MAC_perforin.
IPR020864. MACPF.
IPR020863. MACPF_CS.
IPR000884. Thrombospondin_1_rpt.
[Graphical view]
PfamiPF00057. Ldl_recept_a. 1 hit.
PF01823. MACPF. 1 hit.
PF00090. TSP_1. 1 hit.
[Graphical view]
PRINTSiPR00764. COMPLEMENTC9.
SMARTiSM00192. LDLa. 1 hit.
SM00457. MACPF. 1 hit.
SM00209. TSP1. 2 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 3 hits.
SSF82895. SSF82895. 2 hits.
PROSITEiPS00022. EGF_1. 1 hit.
PS01209. LDLRA_1. 1 hit.
PS50068. LDLRA_2. 1 hit.
PS00279. MACPF_1. 1 hit.
PS51412. MACPF_2. 1 hit.
PS50092. TSP1. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complementary DNA and derived amino acid sequence of the alpha subunit of human complement protein C8: evidence for the existence of a separate alpha subunit messenger RNA."
    Rao A.G., Howard O.M.Z., Ng S.C., Whitehead A.S., Colten H.R., Sodetz J.M.
    Biochemistry 26:3556-3564(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Liver.
  2. Sodetz J.M.
    Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 467-479.
  3. "Genomic organization of human complement protein C8 alpha and further examination of its linkage to C8 beta."
    Michelotti G.A., Snider J.V., Sodetz J.M.
    Hum. Genet. 95:513-518(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Blood.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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], VARIANT LYS-93.
  6. "The eighth component of human complement. Purification and physicochemical characterization of its unusual subunit structure."
    Steckel E.W., York R.G., Monahan J.B., Sodetz J.M.
    J. Biol. Chem. 255:11997-12005(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBUNIT.
  7. "The four terminal components of the complement system are C-mannosylated on multiple tryptophan residues."
    Hofsteenge J., Blommers M., Hess D., Furmanek A., Miroshnichenko O.
    J. Biol. Chem. 274:32786-32794(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT TRP-44; TRP-542; TRP-545 AND TRP-548.
  8. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-437.
    Tissue: Plasma.
  9. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-437.
    Tissue: Liver.
  10. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. "Structure of C8alpha-MACPF reveals mechanism of membrane attack in complement immune defense."
    Hadders M.A., Beringer D.X., Gros P.
    Science 317:1552-1554(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 133-492, FUNCTION.
  12. "Crystal structure of the MACPF domain of human complement protein C8 alpha in complex with the C8 gamma subunit."
    Slade D.J., Lovelace L.L., Chruszcz M., Minor W., Lebioda L., Sodetz J.M.
    J. Mol. Biol. 379:331-342(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 133-492 IN COMPLEX WITH C8G, INTERCHAIN DISULFIDE BOND.
  13. "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 188-198 IN COMPLEX WITH C8G.
  14. "The eighth component of human complement: molecular basis of C8A (C81) polymorphism."
    Zhang L., Rittner C., Sodetz J.M., Schneider P.M., Kaufmann T.
    Hum. Genet. 96:281-284(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT C8A*B LYS-93.

Entry informationi

Entry nameiCO8A_HUMAN
AccessioniPrimary (citable) accession number: P07357
Secondary accession number(s): A2RUI4
, A2RUI5, Q13668, Q9H130
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: February 1, 1995
Last modified: May 27, 2015
This is version 166 of the entry and version 2 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 1
    Human chromosome 1: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.