TCDB is operated by the Saier Lab Bioinformatics Group
« See all members of the family


1.C.39.3.1
Pore-forming, membrane attack, complement component 8, α-polypeptide precursor; C8α-MACPF (structure solved to 2.5 Å resolution; Hadders et al., 2007; Rosado et al., 2007).  β-Hairpins in C8α and C9 play a direct role in MAC membrane penetration and pore formation (Weiland et al. 2014).

Accession Number:P07357
Protein Name:Complement component C8 alpha chain
Length:584
Molecular Weight:65163.00
Species:Homo sapiens (Human) [9606]
Location1 / Topology2 / Orientation3: Secreted1 / Multi-pass membrane protein2
Substrate small molecules, large molecules

Cross database links:

Genevestigator: P07357
eggNOG: prNOG05734
HEGENOM: HBG446019
DIP: DIP-1125N
RefSeq: NP_000553.1   
Entrez Gene ID: 731   
Pfam: PF00057    PF01823    PF00090   
OMIM: 120950  gene+phenotype
KEGG: hsa:731   

Gene Ontology

GO:0005615 C:extracellular space
GO:0005579 C:membrane attack complex
GO:0006957 P:complement activation, alternative pathway
GO:0006958 P:complement activation, classical pathway
GO:0019835 P:cytolysis

References (12)

[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.et.al.   2820471
[2] “Genomic organization of human complement protein C8 alpha and further examination of its linkage to C8 beta.”  Michelotti G.A.et.al.   7759071
[3] “The DNA sequence and biological annotation of human chromosome 1.”  Gregory S.G.et.al.   16710414
[4] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”  The MGC Project Teamet.al.   15489334
[5] “The eighth component of human complement. Purification and physicochemical characterization of its unusual subunit structure.”  Steckel E.W.et.al.   7440581
[6] “The four terminal components of the complement system are C-mannosylated on multiple tryptophan residues.”  Hofsteenge J.et.al.   10551839
[7] “Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.”  Liu T.et.al.   16335952
[8] “Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.”  Chen R.et.al.   19159218
[9] “Structure of C8alpha-MACPF reveals mechanism of membrane attack in complement immune defense.”  Hadders M.A.et.al.   17872444
[10] “Crystal structure of the MACPF domain of human complement protein C8 alpha in complex with the C8 gamma subunit.”  Slade D.J.et.al.   18440555
[11] “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.et.al.   17692377
[12] “The eighth component of human complement: molecular basis of C8A (C81) polymorphism.”  Zhang L.et.al.   7649542
Structure:
2QOS   2QQH   2RD7   3OJY     

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
Window Size: Angle:  
Window Size: Angle:  
FASTA formatted sequence
1:	MFAVVFFILS LMTCQPGVTA QEKVNQRVRR AATPAAVTCQ LSNWSEWTDC FPCQDKKYRH 
61:	RSLLQPNKFG GTICSGDIWD QASCSSSTTC VRQAQCGQDF QCKETGRCLK RHLVCNGDQD 
121:	CLDGSDEDDC EDVRAIDEDC SQYEPIPGSQ KAALGYNILT QEDAQSVYDA SYYGGQCETV 
181:	YNGEWRELRY DSTCERLYYG DDEKYFRKPY NFLKYHFEAL ADTGISSEFY DNANDLLSKV 
241:	KKDKSDSFGV TIGIGPAGSP LLVGVGVSHS QDTSFLNELN KYNEKKFIFT RIFTKVQTAH 
301:	FKMRKDDIML DEGMLQSLME LPDQYNYGMY AKFINDYGTH YITSGSMGGI YEYILVIDKA 
361:	KMESLGITSR DITTCFGGSL GIQYEDKINV GGGLSGDHCK KFGGGKTERA RKAMAVEDII 
421:	SRVRGGSSGW SGGLAQNRST ITYRSWGRSL KYNPVVIDFE MQPIHEVLRH TSLGPLEAKR 
481:	QNLRRALDQY LMEFNACRCG PCFNNGVPIL EGTSCRCQCR LGSLGAACEQ TQTEGAKADG 
541:	SWSCWSSWSV CRAGIQERRR ECDNPAPQNG GASCPGRKVQ TQAC