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Database: UniProt
Entry: P79755
LinkDB: P79755
Original site: P79755 
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   16-JAN-2019, entry version 104.
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;
OC   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
RT   DOC-2 in the pufferfish Fugu rubripes.";
RL   Gene 200:203-211(1997).
CC   -!- FUNCTION: Constituent of the membrane attack complex (MAC) that
CC       plays a key role in the innate and adaptive immune response by
CC       forming pores in the plasma membrane of target cells. C9 is the
CC       pore-forming subunit of the MAC. {ECO:0000250|UniProtKB:P02748}.
CC   -!- SUBUNIT: Component of the membrane attack complex (MAC). About 20
CC       C9 chains oligomerize to give rise to a huge beta-barrel that
CC       forms a 100 Angstrom diameter pore in target membranes.
CC       {ECO:0000250|UniProtKB:P02748}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02748}.
CC       Target cell membrane {ECO:0000250|UniProtKB:P02748}; Multi-pass
CC       membrane protein {ECO:0000250|UniProtKB:P02748}. Note=Secreted as
CC       soluble monomer. Oligomerizes at target membranes, forming a pre-
CC       pore. A conformation change then leads to the formation of a 100
CC       Angstrom diameter pore. {ECO:0000250|UniProtKB:P02748}.
CC   -!- PTM: The structure of the human polymeric form indicates the
CC       existence of an additional disulfide bond compared to the mouse
CC       monomeric form. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the complement C6/C7/C8/C9 family.
CC       {ECO:0000305}.
DR   EMBL; U87241; AAC60288.1; -; Genomic_DNA.
DR   RefSeq; XP_003965317.1; XM_003965268.2.
DR   ProteinModelPortal; 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; ENOG410IH3C; Eukaryota.
DR   eggNOG; ENOG410XT9A; LUCA.
DR   InParanoid; P79755; -.
DR   KO; K04000; -.
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:0044218; C:other organism cell membrane; IEA:UniProtKB-SubCell.
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   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; PTHR19325:SF362; PTHR19325:SF362; 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; Complete proteome;
KW   Cytolysis; Disulfide bond; EGF-like domain; Glycoprotein; Immunity;
KW   Innate immunity; Membrane; Membrane attack complex;
KW   Reference proteome; Repeat; Secreted; Signal; Target cell membrane;
KW   Target membrane; Transmembrane; Transmembrane beta strand.
FT   SIGNAL        1     26       {ECO:0000255}.
FT   CHAIN        27    586       Complement component C9.
FT                                /FTId=PRO_0000023608.
FT   DOMAIN       36     89       TSP type-1 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN       94    131       LDL-receptor class A.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      132    493       MACPF. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00745}.
FT   DOMAIN      494    524       EGF-like.
FT   DOMAIN      543    585       TSP type-1 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   CARBOHYD    246    246       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    274    274       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    354    354       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    545    545       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     37     72       {ECO:0000250|UniProtKB:P02748}.
FT   DISULFID     48     82       {ECO:0000250|UniProtKB:P02748}.
FT   DISULFID     51     88       {ECO:0000250|UniProtKB:P02748}.
FT   DISULFID     96    108       {ECO:0000250|UniProtKB:P02748}.
FT   DISULFID    103    121       {ECO:0000250|UniProtKB:P02748}.
FT   DISULFID    115    129       {ECO:0000250|UniProtKB:P02748}.
FT   DISULFID    136    175       {ECO:0000250|UniProtKB:P02748}.
FT   DISULFID    494    510       {ECO:0000250|UniProtKB:P02748}.
FT   DISULFID    497    512       {ECO:0000250|UniProtKB:P02748}.
FT   DISULFID    514    523       {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
//
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