CO9_TAKRU
ID CO9_TAKRU Reviewed; 586 AA.
AC P79755;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Complement component C9;
DE Flags: Precursor;
GN Name=c9;
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9373156; DOI=10.1016/s0378-1119(97)00423-x;
RA Yeo G.S.H., Elgar G., Sandford R., Brenner S.;
RT "Cloning and sequencing of complement component C9 and its linkage to DOC-2
RT in the pufferfish Fugu rubripes.";
RL Gene 200:203-211(1997).
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). About 20 C9
CC chains oligomerize to give rise to a huge beta-barrel that forms a 100
CC 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: 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; U87241; AAC60288.1; -; Genomic_DNA.
DR RefSeq; XP_003965317.1; XM_003965268.2.
DR AlphaFoldDB; P79755; -.
DR SMR; P79755; -.
DR STRING; 31033.ENSTRUP00000047561; -.
DR TCDB; 1.C.39.3.6; the membrane attack complex/perforin (macpf) family.
DR GeneID; 101068974; -.
DR KEGG; tru:101068974; -.
DR CTD; 735; -.
DR eggNOG; ENOG502QWHM; Eukaryota.
DR InParanoid; P79755; -.
DR OrthoDB; 787014at2759; -.
DR Proteomes; UP000005226; 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; 4.10.400.10; -; 1.
DR InterPro; IPR037567; Complement_C9.
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; SSF57424; SSF57424; 1.
DR SUPFAM; SSF82895; SSF82895; 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; 2.
PE 3: Inferred from homology;
KW Complement alternate pathway; Complement pathway; Cytolysis;
KW Disulfide bond; EGF-like domain; Glycoprotein; Immunity; Innate immunity;
KW Membrane; Membrane attack complex; Reference proteome; Repeat; Secreted;
KW Signal; Target cell membrane; Target membrane; Transmembrane;
KW Transmembrane beta strand.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..586
FT /note="Complement component C9"
FT /id="PRO_0000023608"
FT DOMAIN 36..89
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 94..131
FT /note="LDL-receptor class A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 132..493
FT /note="MACPF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00745"
FT DOMAIN 494..524
FT /note="EGF-like"
FT DOMAIN 543..585
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 545
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 37..72
FT /evidence="ECO:0000250|UniProtKB:P02748"
FT DISULFID 48..82
FT /evidence="ECO:0000250|UniProtKB:P02748"
FT DISULFID 51..88
FT /evidence="ECO:0000250|UniProtKB:P02748"
FT DISULFID 96..108
FT /evidence="ECO:0000250|UniProtKB:P02748"
FT DISULFID 103..121
FT /evidence="ECO:0000250|UniProtKB:P02748"
FT DISULFID 115..129
FT /evidence="ECO:0000250|UniProtKB:P02748"
FT DISULFID 136..175
FT /evidence="ECO:0000250|UniProtKB:P02748"
FT DISULFID 494..510
FT /evidence="ECO:0000250|UniProtKB:P02748"
FT DISULFID 497..512
FT /evidence="ECO:0000250|UniProtKB:P02748"
FT DISULFID 514..523
FT /evidence="ECO:0000250|UniProtKB:P02748"
SQ SEQUENCE 586 AA; 65198 MW; 8466EB7B8B8FDC18 CRC64;
MRTEAALQLG FCALCVMLAL LGEGMGRELP DPPAVNCVWS RWAPWSSCDP CTNTRRRSRG
VEVFGQFAGI ACQGSVGDRE YCITNAKCNL PPPRECSDSE FQCESGSCIK LRLKCNGDYD
CEDGSDEDCE PLRKTCPPTV LDTNEQGRTA GYGINILGAD PRMNPFNNDF FNGRCDKVRN
PNTLQLDRLP WNIGVLNYQT LVEETASREI YEDSYSLLRE MLKEMSIKVD AGLSFKFKST
EPSMSNNSLK LDASLEYEKK TMIKDVSELT NIKNKSFMRV KGRLQLSTYR MRSHQLQVAD
EFVAHVKSLP LEYEKGIYYA FLEDYGTHYT KNGKSGGEYE LVYVLNQDTI KAKNLTERKI
QECLKIGIEA EFATTSVQDG KAHAKLNKCD DVTTKSQGDV EGKAVVDNVM TSVKGGSLES
AVTMRAKLNK EGVMDIATYQ NWARTIASAP ALINSEPEPI YMLIPTDIPG ANSRIANLKQ
ATADYVAEYN VCKCRPCHNG GTLALLDGKC ICMCSNLFEG LGCQNFKGDK ARVPAARPAV
TQEGNWSCWS SWSNCQGQKR SRTRYCNTEG VLGAECRGEI RSEEYC
