CO9_MOUSE
ID CO9_MOUSE Reviewed; 548 AA.
AC P06683; Q91XA7;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Complement component C9;
DE Flags: Precursor;
GN Name=C9;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 21-548.
RX PubMed=2443347; DOI=10.1002/j.1460-2075.1987.tb02457.x;
RA Stanley K.K., Herz J.;
RT "Topological mapping of complement component C9 by recombinant DNA
RT techniques suggests a novel mechanism for its insertion into target
RT membranes.";
RL EMBO J. 6:1951-1957(1987).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-263.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=16944957; DOI=10.1021/pr060186m;
RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT "Proteome-wide characterization of N-glycosylation events by diagonal
RT chromatography.";
RL J. Proteome Res. 5:2438-2447(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5] {ECO:0007744|PDB:6CXO}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 21-548, AND DISULFIDE BONDS.
RX PubMed=30111885; DOI=10.1038/s41467-018-05717-0;
RA Spicer B.A., Law R.H.P., Caradoc-Davies T.T., Ekkel S.M., Bayly-Jones C.,
RA Pang S.S., Conroy P.J., Ramm G., Radjainia M., Venugopal H.,
RA Whisstock J.C., Dunstone M.A.;
RT "The first transmembrane region of complement component-9 acts as a brake
RT on its self-assembly.";
RL Nat. Commun. 9:3266-3266(2018).
CC -!- FUNCTION: Constituent of the membrane attack complex (MAC) that plays a
CC key role in the innate and adaptive immune response by forming pores in
CC the plasma membrane of target cells. C9 is the pore-forming subunit of
CC the MAC. {ECO:0000250|UniProtKB:P02748}.
CC -!- SUBUNIT: Component of the membrane attack complex (MAC). MAC assembly
CC is initiated by proteolytic cleavage of C5 into C5a and C5b. C5b binds
CC sequentially C6, C7, C8 and multiple copies of the pore-forming subunit
CC C9. About 20 C9 chains oligomerize to give rise to a huge beta-barrel
CC that forms a 100 Angstrom diameter pore in target membranes.
CC {ECO:0000250|UniProtKB:P02748}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02748}. Target
CC cell membrane {ECO:0000250|UniProtKB:P02748}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:P02748}. Note=Secreted as soluble
CC monomer. Oligomerizes at target membranes, forming a pre-pore. A
CC conformation change then leads to the formation of a 100 Angstrom
CC diameter pore. {ECO:0000250|UniProtKB:P02748}.
CC -!- PTM: Initially, positions and connectivity of disulfide bonds were
CC based on peptide sequencing done for the human protein. The high-
CC resolution crystal structure for the mouse protein corrected the
CC positions and connectivities of some disulfide bonds (PubMed:30111885).
CC The distance between Cys-55 and Cys-92 in the monomeric mouse protein
CC precludes formation of a disulfide bond, contrary to what is seen in
CC the structure of the human polymeric form of the protein (Probable).
CC {ECO:0000269|PubMed:30111885, ECO:0000305|PubMed:30111885}.
CC -!- SIMILARITY: Belongs to the complement C6/C7/C8/C9 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH11137.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC011137; AAH11137.1; ALT_INIT; mRNA.
DR EMBL; X05475; CAA29038.1; -; mRNA.
DR CCDS; CCDS27367.1; -.
DR PIR; A29677; A29677.
DR RefSeq; NP_038513.1; NM_013485.1.
DR PDB; 6CXO; X-ray; 2.20 A; A/B=21-548.
DR PDBsum; 6CXO; -.
DR AlphaFoldDB; P06683; -.
DR SMR; P06683; -.
DR BioGRID; 198425; 4.
DR ComplexPortal; CPX-6202; Membrane attack complex.
DR STRING; 10090.ENSMUSP00000022749; -.
DR GlyGen; P06683; 3 sites.
DR iPTMnet; P06683; -.
DR PhosphoSitePlus; P06683; -.
DR CPTAC; non-CPTAC-3779; -.
DR jPOST; P06683; -.
DR MaxQB; P06683; -.
DR PaxDb; P06683; -.
DR PeptideAtlas; P06683; -.
DR PRIDE; P06683; -.
DR ProteomicsDB; 283477; -.
DR Antibodypedia; 3685; 551 antibodies from 39 providers.
DR DNASU; 12279; -.
DR Ensembl; ENSMUST00000022749; ENSMUSP00000022749; ENSMUSG00000022149.
DR GeneID; 12279; -.
DR KEGG; mmu:12279; -.
DR UCSC; uc007vdh.1; mouse.
DR CTD; 735; -.
DR MGI; MGI:1098282; C9.
DR VEuPathDB; HostDB:ENSMUSG00000022149; -.
DR eggNOG; ENOG502QWHM; Eukaryota.
DR GeneTree; ENSGT00940000159777; -.
DR InParanoid; P06683; -.
DR OrthoDB; 787014at2759; -.
DR PhylomeDB; P06683; -.
DR TreeFam; TF330498; -.
DR Reactome; R-MMU-166665; Terminal pathway of complement.
DR Reactome; R-MMU-977606; Regulation of Complement cascade.
DR BioGRID-ORCS; 12279; 1 hit in 71 CRISPR screens.
DR ChiTaRS; C9; mouse.
DR PRO; PR:P06683; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P06683; protein.
DR Bgee; ENSMUSG00000022149; Expressed in left lobe of liver and 30 other tissues.
DR ExpressionAtlas; P06683; baseline and differential.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0005579; C:membrane attack complex; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0007596; P:blood coagulation; ISO:MGI.
DR GO; GO:0001906; P:cell killing; ISS:UniProtKB.
DR GO; GO:0006956; P:complement activation; IBA:GO_Central.
DR GO; GO:0006957; P:complement activation, alternative pathway; IEA:UniProtKB-KW.
DR GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0050778; P:positive regulation of immune response; IC:ComplexPortal.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR CDD; cd00112; LDLa; 1.
DR Gene3D; 2.20.100.10; -; 1.
DR Gene3D; 4.10.400.10; -; 1.
DR InterPro; IPR037567; Complement_C9.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR001862; MAC_perforin.
DR InterPro; IPR020864; MACPF.
DR InterPro; IPR020863; MACPF_CS.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR45742:SF3; PTHR45742:SF3; 1.
DR Pfam; PF00057; Ldl_recept_a; 1.
DR Pfam; PF01823; MACPF; 1.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR00764; COMPLEMENTC9.
DR SMART; SM00192; LDLa; 1.
DR SMART; SM00457; MACPF; 1.
DR SMART; SM00209; TSP1; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
DR SUPFAM; SSF57424; SSF57424; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 1.
DR PROSITE; PS00279; MACPF_1; 1.
DR PROSITE; PS51412; MACPF_2; 1.
DR PROSITE; PS50092; TSP1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complement alternate pathway; Complement pathway; Cytolysis;
KW Disulfide bond; EGF-like domain; Glycoprotein; Immunity; Innate immunity;
KW Membrane; Membrane attack complex; Reference proteome; Secreted; Signal;
KW Target cell membrane; Target membrane; Transmembrane;
KW Transmembrane beta strand.
FT SIGNAL 1..20
FT /evidence="ECO:0000250"
FT CHAIN 21..548
FT /note="Complement component C9"
FT /id="PRO_0000023605"
FT TRANSMEM 312..328
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..352
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT DOMAIN 40..93
FT /note="TSP type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 97..134
FT /note="LDL-receptor class A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 136..512
FT /note="MACPF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00745"
FT DOMAIN 513..543
FT /note="EGF-like"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..76
FT /evidence="ECO:0000269|PubMed:30111885,
FT ECO:0007744|PDB:6CXO"
FT DISULFID 52..86
FT /evidence="ECO:0000269|PubMed:30111885,
FT ECO:0007744|PDB:6CXO"
FT DISULFID 55..92
FT /evidence="ECO:0000250|UniProtKB:P02748"
FT DISULFID 99..110
FT /evidence="ECO:0000269|PubMed:30111885,
FT ECO:0007744|PDB:6CXO"
FT DISULFID 105..123
FT /evidence="ECO:0000269|PubMed:30111885,
FT ECO:0007744|PDB:6CXO"
FT DISULFID 117..132
FT /evidence="ECO:0000269|PubMed:30111885,
FT ECO:0007744|PDB:6CXO"
FT DISULFID 140..179
FT /evidence="ECO:0000269|PubMed:30111885,
FT ECO:0007744|PDB:6CXO"
FT DISULFID 378..407
FT /evidence="ECO:0000269|PubMed:30111885,
FT ECO:0007744|PDB:6CXO"
FT DISULFID 513..529
FT /evidence="ECO:0000269|PubMed:30111885,
FT ECO:0007744|PDB:6CXO"
FT DISULFID 516..531
FT /evidence="ECO:0000269|PubMed:30111885,
FT ECO:0007744|PDB:6CXO"
FT DISULFID 533..542
FT /evidence="ECO:0000269|PubMed:30111885,
FT ECO:0007744|PDB:6CXO"
FT CONFLICT 88
FT /note="P -> T (in Ref. 2; CAA29038)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="T -> R (in Ref. 2; CAA29038)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="A -> P (in Ref. 2; CAA29038)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="E -> Q (in Ref. 2; CAA29038)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="P -> A (in Ref. 2; CAA29038)"
FT /evidence="ECO:0000305"
FT CONFLICT 269..270
FT /note="KF -> TI (in Ref. 2; CAA29038)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="F -> L (in Ref. 2; CAA29038)"
FT /evidence="ECO:0000305"
FT CONFLICT 547
FT /note="K -> T (in Ref. 2; CAA29038)"
FT /evidence="ECO:0000305"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:6CXO"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:6CXO"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:6CXO"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:6CXO"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:6CXO"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:6CXO"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:6CXO"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:6CXO"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:6CXO"
FT HELIX 149..153
FT /evidence="ECO:0007829|PDB:6CXO"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:6CXO"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:6CXO"
FT STRAND 195..204
FT /evidence="ECO:0007829|PDB:6CXO"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:6CXO"
FT HELIX 216..226
FT /evidence="ECO:0007829|PDB:6CXO"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:6CXO"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:6CXO"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:6CXO"
FT HELIX 274..282
FT /evidence="ECO:0007829|PDB:6CXO"
FT STRAND 289..306
FT /evidence="ECO:0007829|PDB:6CXO"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:6CXO"
FT HELIX 315..322
FT /evidence="ECO:0007829|PDB:6CXO"
FT HELIX 330..340
FT /evidence="ECO:0007829|PDB:6CXO"
FT STRAND 342..361
FT /evidence="ECO:0007829|PDB:6CXO"
FT HELIX 362..367
FT /evidence="ECO:0007829|PDB:6CXO"
FT HELIX 372..379
FT /evidence="ECO:0007829|PDB:6CXO"
FT TURN 418..422
FT /evidence="ECO:0007829|PDB:6CXO"
FT STRAND 424..429
FT /evidence="ECO:0007829|PDB:6CXO"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:6CXO"
FT HELIX 436..448
FT /evidence="ECO:0007829|PDB:6CXO"
FT HELIX 455..463
FT /evidence="ECO:0007829|PDB:6CXO"
FT TURN 464..467
FT /evidence="ECO:0007829|PDB:6CXO"
FT STRAND 470..478
FT /evidence="ECO:0007829|PDB:6CXO"
FT HELIX 479..482
FT /evidence="ECO:0007829|PDB:6CXO"
FT HELIX 490..507
FT /evidence="ECO:0007829|PDB:6CXO"
FT HELIX 510..512
FT /evidence="ECO:0007829|PDB:6CXO"
FT STRAND 521..525
FT /evidence="ECO:0007829|PDB:6CXO"
FT STRAND 528..532
FT /evidence="ECO:0007829|PDB:6CXO"
SQ SEQUENCE 548 AA; 62002 MW; 8F1D16184E4781BE CRC64;
MASGMAITLA LAIFALGVNA QMPIPVSREE QEQHYPIPID CRMSPWSNWS ECDPCLKQRF
RSRSILAFGQ FNGKSCVDVL GDRQGCEPTQ ECEEIQENCG NDFQCETGRC IKRRLLCNGD
NDCGDYSDEN DCDDDPRTPC RDRVAEESEL GLTAGYGINI LGMEPLRTPF DNEFYNGLCD
RVRDEKTYYR KPWNVVSLIY ETKADKSFRT ENYDEHLEVF KAINREKTSN FNADFALKFS
ATEVPEKGAG EVSPAEHSSK PTNISAKFKF SYFMGKNFRR LSSYFSQSKK MFVHLRGVVQ
LGRFVMRNRD VVLRSTFLDD VKALPTSYEK GEYFGFLETY GTHYSTSGSL GGQYEIVYVL
DKASMKEKGV DLNDVKHCLG FNMDLRIPLQ DDLKDASVTA SVNADGCIKT DNGKTVNITR
DNIIDDVISF IRGGTREQAI LLKEKILRGD KTFDKTDFAN WASSLANAPA LISQRMSPIY
NLIPLKIKDA YIKKQNLEKA VEDYIDEFST KRCYPCLNGG TIILLDGQCL CSCPMMFRGM
ACEIHQKI
