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Protein

Complement component C9

Gene

C9

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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. C9 is the pore-forming subunit of the MAC.

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Complement component C9
Gene namesi
Name:C9
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1098282. C9.

Subcellular locationi

  • Secreted By similarity
  • Cell membrane By similarity; Multi-pass membrane protein By similarity

  • 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 (By similarity).By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei312 – 32817Beta strandedSequence analysisAdd
BLAST
Transmembranei333 – 35220Beta strandedSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Membrane attack complex, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020By similarityAdd
BLAST
Chaini21 – 548528Complement component C9PRO_0000023605Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi41 ↔ 76By similarity
Glycosylationi48 – 481N-linked (GlcNAc...)Sequence analysis
Disulfide bondi52 ↔ 55By similarity
Disulfide bondi86 ↔ 92By similarity
Disulfide bondi99 ↔ 110By similarity
Disulfide bondi105 ↔ 123By similarity
Disulfide bondi117 ↔ 132By similarity
Disulfide bondi140 ↔ 179By similarity
Glycosylationi263 – 2631N-linked (GlcNAc...)1 Publication
Disulfide bondi378 ↔ 407By similarity
Glycosylationi417 – 4171N-linked (GlcNAc...)Sequence analysis
Disulfide bondi513 ↔ 529By similarity
Disulfide bondi516 ↔ 531By similarity
Disulfide bondi533 ↔ 542By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiP06683.
MaxQBiP06683.
PaxDbiP06683.
PRIDEiP06683.

PTM databases

iPTMnetiP06683.
PhosphoSiteiP06683.

Expressioni

Gene expression databases

BgeeiP06683.
CleanExiMM_C9.

Interactioni

Subunit structurei

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 (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000022749.

Structurei

3D structure databases

ProteinModelPortaliP06683.
SMRiP06683. Positions 36-543.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini40 – 9354TSP type-1PROSITE-ProRule annotationAdd
BLAST
Domaini97 – 13438LDL-receptor class APROSITE-ProRule annotationAdd
BLAST
Domaini136 – 512377MACPFPROSITE-ProRule annotationAdd
BLAST
Domaini513 – 54331EGF-likeAdd
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 1 TSP type-1 domain.PROSITE-ProRule annotation

Keywords - Domaini

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

Phylogenomic databases

eggNOGiENOG410IH3C. Eukaryota.
ENOG410XT9A. LUCA.
HOGENOMiHOG000111869.
HOVERGENiHBG106792.
InParanoidiP06683.
KOiK04000.
OrthoDBiEOG7D85W9.
PhylomeDBiP06683.
TreeFamiTF330498.

Family and domain databases

Gene3Di4.10.400.10. 1 hit.
InterProiIPR009030. Growth_fac_rcpt_.
IPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
IPR001862. MAC_perforin.
IPR020864. MACPF.
IPR020863. MACPF_CS.
IPR000884. TSP1_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. 1 hit.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 2 hits.
SSF57424. SSF57424. 1 hit.
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. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P06683-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASGMAITLA LAIFALGVNA QMPIPVSREE QEQHYPIPID CRMSPWSNWS
60 70 80 90 100
ECDPCLKQRF RSRSILAFGQ FNGKSCVDVL GDRQGCEPTQ ECEEIQENCG
110 120 130 140 150
NDFQCETGRC IKRRLLCNGD NDCGDYSDEN DCDDDPRTPC RDRVAEESEL
160 170 180 190 200
GLTAGYGINI LGMEPLRTPF DNEFYNGLCD RVRDEKTYYR KPWNVVSLIY
210 220 230 240 250
ETKADKSFRT ENYDEHLEVF KAINREKTSN FNADFALKFS ATEVPEKGAG
260 270 280 290 300
EVSPAEHSSK PTNISAKFKF SYFMGKNFRR LSSYFSQSKK MFVHLRGVVQ
310 320 330 340 350
LGRFVMRNRD VVLRSTFLDD VKALPTSYEK GEYFGFLETY GTHYSTSGSL
360 370 380 390 400
GGQYEIVYVL DKASMKEKGV DLNDVKHCLG FNMDLRIPLQ DDLKDASVTA
410 420 430 440 450
SVNADGCIKT DNGKTVNITR DNIIDDVISF IRGGTREQAI LLKEKILRGD
460 470 480 490 500
KTFDKTDFAN WASSLANAPA LISQRMSPIY NLIPLKIKDA YIKKQNLEKA
510 520 530 540
VEDYIDEFST KRCYPCLNGG TIILLDGQCL CSCPMMFRGM ACEIHQKI
Length:548
Mass (Da):62,002
Last modified:January 23, 2002 - v2
Checksum:i8F1D16184E4781BE
GO

Sequence cautioni

The sequence AAH11137.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti88 – 881P → T in CAA29038 (PubMed:2443347).Curated
Sequence conflicti153 – 1531T → R in CAA29038 (PubMed:2443347).Curated
Sequence conflicti241 – 2411A → P in CAA29038 (PubMed:2443347).Curated
Sequence conflicti246 – 2461E → Q in CAA29038 (PubMed:2443347).Curated
Sequence conflicti261 – 2611P → A in CAA29038 (PubMed:2443347).Curated
Sequence conflicti269 – 2702KF → TI in CAA29038 (PubMed:2443347).Curated
Sequence conflicti285 – 2851F → L in CAA29038 (PubMed:2443347).Curated
Sequence conflicti547 – 5471K → T in CAA29038 (PubMed:2443347).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC011137 mRNA. Translation: AAH11137.1. Different initiation.
X05475 mRNA. Translation: CAA29038.1.
PIRiA29677.
RefSeqiNP_038513.1. NM_013485.1.
UniGeneiMm.29095.

Genome annotation databases

GeneIDi12279.
KEGGimmu:12279.
UCSCiuc007vdh.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC011137 mRNA. Translation: AAH11137.1. Different initiation.
X05475 mRNA. Translation: CAA29038.1.
PIRiA29677.
RefSeqiNP_038513.1. NM_013485.1.
UniGeneiMm.29095.

3D structure databases

ProteinModelPortaliP06683.
SMRiP06683. Positions 36-543.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000022749.

PTM databases

iPTMnetiP06683.
PhosphoSiteiP06683.

Proteomic databases

EPDiP06683.
MaxQBiP06683.
PaxDbiP06683.
PRIDEiP06683.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi12279.
KEGGimmu:12279.
UCSCiuc007vdh.1. mouse.

Organism-specific databases

CTDi735.
MGIiMGI:1098282. C9.

Phylogenomic databases

eggNOGiENOG410IH3C. Eukaryota.
ENOG410XT9A. LUCA.
HOGENOMiHOG000111869.
HOVERGENiHBG106792.
InParanoidiP06683.
KOiK04000.
OrthoDBiEOG7D85W9.
PhylomeDBiP06683.
TreeFamiTF330498.

Miscellaneous databases

PROiP06683.
SOURCEiSearch...

Gene expression databases

BgeeiP06683.
CleanExiMM_C9.

Family and domain databases

Gene3Di4.10.400.10. 1 hit.
InterProiIPR009030. Growth_fac_rcpt_.
IPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
IPR001862. MAC_perforin.
IPR020864. MACPF.
IPR020863. MACPF_CS.
IPR000884. TSP1_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. 1 hit.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 2 hits.
SSF57424. SSF57424. 1 hit.
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. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
    Tissue: Liver.
  2. "Topological mapping of complement component C9 by recombinant DNA techniques suggests a novel mechanism for its insertion into target membranes."
    Stanley K.K., Herz J.
    EMBO J. 6:1951-1957(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 21-548.
  3. "Proteome-wide characterization of N-glycosylation events by diagonal chromatography."
    Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.
    J. Proteome Res. 5:2438-2447(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-263.
    Strain: C57BL/6J.
    Tissue: Plasma.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart, Kidney, Liver and Lung.

Entry informationi

Entry nameiCO9_MOUSE
AccessioniPrimary (citable) accession number: P06683
Secondary accession number(s): Q91XA7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2002
Last modified: June 8, 2016
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.