ID   CO9_HORSE               Reviewed;         547 AA.
AC   P48770;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 117.
DE   RecName: Full=Complement component C9;
DE   Flags: Precursor;
GN   Name=C9;
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7541424;
RA   Tomlinson S., Wang Y., Ueda E., Esser A.F.;
RT   "Chimeric horse/human recombinant C9 proteins identify the amino acid
RT   sequence in horse C9 responsible for restriction of hemolysis.";
RL   J. Immunol. 155:436-444(1995).
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: Thrombin cleaves factor C9 to produce C9a and C9b.
CC   -!- PTM: The structure of the human polymeric form indicates the existence
CC       of an additional disulfide bond compared to the mouse monomeric form.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the complement C6/C7/C8/C9 family.
CC       {ECO:0000305}.
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DR   EMBL; U19381; AAB16820.1; -; mRNA.
DR   RefSeq; NP_001075419.1; NM_001081950.1.
DR   AlphaFoldDB; P48770; -.
DR   SMR; P48770; -.
DR   STRING; 9796.ENSECAP00000006188; -.
DR   TCDB; 1.C.39.3.5; the membrane attack complex/perforin (macpf) family.
DR   PaxDb; P48770; -.
DR   GeneID; 100034183; -.
DR   KEGG; ecb:100034183; -.
DR   CTD; 735; -.
DR   InParanoid; P48770; -.
DR   OrthoDB; 787014at2759; -.
DR   Proteomes; UP000002281; Unplaced.
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:0001906; P:cell killing; ISS:UniProtKB.
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: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   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   2: Evidence at transcript level;
KW   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..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..547
FT                   /note="Complement component C9"
FT                   /id="PRO_0000023601"
FT   TRANSMEM        314..330
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        335..354
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          42..95
FT                   /note="TSP type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          99..136
FT                   /note="LDL-receptor class A"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          138..509
FT                   /note="MACPF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00745"
FT   DOMAIN          510..540
FT                   /note="EGF-like"
FT   CARBOHYD        260
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        277
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        451
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        43..78
FT                   /evidence="ECO:0000250|UniProtKB:P02748"
FT   DISULFID        54..88
FT                   /evidence="ECO:0000250|UniProtKB:P02748"
FT   DISULFID        57..94
FT                   /evidence="ECO:0000250|UniProtKB:P02748"
FT   DISULFID        101..112
FT                   /evidence="ECO:0000250|UniProtKB:P02748"
FT   DISULFID        107..125
FT                   /evidence="ECO:0000250|UniProtKB:P02748"
FT   DISULFID        119..134
FT                   /evidence="ECO:0000250|UniProtKB:P02748"
FT   DISULFID        142..181
FT                   /evidence="ECO:0000250|UniProtKB:P02748"
FT   DISULFID        510..526
FT                   /evidence="ECO:0000250|UniProtKB:P02748"
FT   DISULFID        513..528
FT                   /evidence="ECO:0000250|UniProtKB:P02748"
FT   DISULFID        530..539
FT                   /evidence="ECO:0000250|UniProtKB:P02748"
SQ   SEQUENCE   547 AA;  62014 MW;  75E5FE961DE873B6 CRC64;
     MSAGRTFAFA ICILEVSVLT AGPTPNYAPE PEQQSGTPLP IDCRMSSWSE WSECDPCLRQ
     MFRSRSIEVF GQFNGQRCVD AVGDRRQCVP TEACEEVEDD CGNDFQCGTG RCIKKRLLCN
     GDNDCGDFSD EDDCENDPRP PCRERVVEES ELARTAGYGI NILGMDPLST PFDNEYYNGL
     CDRVRDGNTL TYYRKPWNLA SLAYETKADK NFRIEHYEQQ IQAFRSVIEE RRSHFNADFT
     LKFTPTEAKK CKQEPEESCN GTDSSENRIF RFAYSKNETY QLFLSYSSKK EKMFLHVKGV
     IQLGKFVMRS RDVVLTTTFL DDIKALPTAY EKGEYIAFLE TYGTHYSSSG SLGGLYELIY
     VLDKASMDQK GVELRDIQRC LGFNLDLSLK DKYEVTAKID KNDCLKRNEK EIVNIMDGSL
     IDDVISLIRG GTRKYAFELK EKLLKGAKTV NVTDFVNWAS SLNDAPVLIS QRLSPIYNLI
     PVKMKDAHQK KQNLERAIED YINEFSVRKC HPCQNGGTVI QIDGQCLCSC PIAFEGIACE
     TGKKKIS