C9
entrez
12279
canonical
uniprot
P06683
canonical
ensembl
ENSMUSG00000022149
resolver
ensp
ENSMUSP00000022749
resolver
ensp
ENSMUSP00000159308
resolver
ensp
ENSMUSP00000363883
resolver
enst
ENSMUST00000022749
resolver
enst
ENSMUST00000239466
resolver
genesymbol
C9
resolver
uniprot
A0A0R4J032
resolver
uniprot
Q91XA7
resolver
uniprot_entry
A0A0R4J032_MOUSE
resolver
uniprot_entry
CO9_MOUSE
resolver
uniprot_sec
Q91XA7
resolver
activity_regulation
ACTIVITY REGULATION: Membrane attack complex (MAC) assembly is inhibited by CD59, thereby protecting self-cells from damage during complement activation. CD59 acts by preventing incorporation of the multiple copies of C9 required for complete formation of the osmolytic pore. MAC assembly is also inhibited by clusterin (CLU) chaperones that inhibit polymerization of C9. {ECO:0000250|UniProtKB:P02748}.
uniprot
proteins
amino_acid_sequence
MASGMAITLALAIFALGVNAQMPIPVSREEQEQHYPIPIDCRMSPWSNWSECDPCLKQRFRSRSILAFGQFNGKSCVDVLGDRQGCEPTQECEEIQENCGNDFQCETGRCIKRRLLCNGDNDCGDYSDENDCDDDPRTPCRDRVAEESELGLTAGYGINILGMEPLRTPFDNEFYNGLCDRVRDEKTYYRKPWNVVSLIYETKADKSFRTENYDEHLEVFKAINREKTSNFNADFALKFSATEVPEKGAGEVSPAEHSSKPTNISAKFKFSYFMGKNFRRLSSYFSQSKKMFVHLRGVVQLGRFVMRNRDVVLRSTFLDDVKALPTSYEKGEYFGFLETYGTHYSTSGSLGGQYEIVYVLDKASMKEKGVDLNDVKHCLGFNMDLRIPLQDDLKDASVTASVNADGCIKTDNGKTVNITRDNIIDDVISFIRGGTREQAILLKEKILRGDKTFDKTDFANWASSLANAPALISQRMSPIYNLIPLKIKDAYIKKQNLEKAVEDYIDEFSTKRCYPCLNGGTIILLDGQCLCSCPMMFRGMACEIHQKI
uniprot
proteins
function
FUNCTION: Pore-forming component of the membrane attack complex (MAC), a multiprotein complex activated by the complement cascade, which inserts into a target cell membrane and forms a pore, leading to target cell membrane rupture and cell lysis. The MAC is initiated by proteolytic cleavage of C5 into complement C5b in response to the classical, alternative, lectin and GZMK complement pathways. The complement pathways consist in a cascade of proteins that leads to phagocytosis and breakdown of pathogens and signaling that strengthens the adaptive immune system. Constitutes the pore-forming subunit of the MAC complex: during MAC assembly, C9 associates with the C5b8 intermediate complex, and polymerizes to complete the pore. {ECO:0000250|UniProtKB:P02748}.
uniprot
proteins
mass_dalton
62002
uniprot
proteins
post_translational_modification
PTM: Initially, positions and connectivity of disulfide bonds were based on peptide sequencing done for the human protein. The high-resolution crystal structure for the mouse protein corrected the positions and connectivities of some disulfide bonds (PubMed:30111885). The distance between Cys-55 and Cys-92 in the monomeric mouse protein precludes formation of a disulfide bond, contrary to what is seen in the structure of the human polymeric form of the protein (PubMed:30111885). {ECO:0000269|PubMed:30111885}.
uniprot
proteins
protein_family
Complement C6/C7/C8/C9 family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
2443347
uniprot
proteins
pubmed
30111885
uniprot
proteins
sequence_length
548
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02748}. Target cell membrane {ECO:0000250|UniProtKB:P02748}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P02748}. Note=Secreted as soluble monomer. Oligomerizes at target membranes, forming a pre-pore. A conformation change then leads to the formation of a 100 Angstrom diameter pore. {ECO:0000250|UniProtKB:P02748}.
uniprot
proteins
transmembrane_region
TRANSMEM 231..238; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:P02748"; TRANSMEM 263..270; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:P02748"; TRANSMEM 372..379; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:P02748
uniprot
proteins