CO9_ONCMY
ID CO9_ONCMY Reviewed; 574 AA.
AC P06682;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 2.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Complement component C9;
DE Flags: Fragment;
GN Name=c9;
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [2]
RP SEQUENCE REVISION.
RX PubMed=2808363; DOI=10.1016/s0021-9258(19)84676-8;
RA Haefliger J.-A., Tschopp J., Vial N., Jenne D.E.;
RT "Complete primary structure and functional characterization of the sixth
RT component of the human complement system. Identification of the C5b-binding
RT domain in complement C6.";
RL J. Biol. Chem. 264:18041-18051(1989).
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; X05474; CAA29037.1; ALT_SEQ; mRNA.
DR PIR; B29677; B29677.
DR AlphaFoldDB; P06682; -.
DR SMR; P06682; -.
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; 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; 2.
DR SUPFAM; SSF57424; SSF57424; 1.
DR SUPFAM; SSF82895; SSF82895; 2.
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 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; Repeat; Secreted; Target cell membrane;
KW Target membrane; Transmembrane; Transmembrane beta strand.
FT CHAIN <1..574
FT /note="Complement component C9"
FT /id="PRO_0000162510"
FT TRANSMEM 284..300
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..324
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT DOMAIN 18..72
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 77..117
FT /note="LDL-receptor class A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 115..480
FT /note="MACPF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00745"
FT DOMAIN 481..511
FT /note="EGF-like"
FT DOMAIN 531..572
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT CARBOHYD 3
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 533
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 19..54
FT /evidence="ECO:0000250|UniProtKB:P02748"
FT DISULFID 30..65
FT /evidence="ECO:0000250|UniProtKB:P02748"
FT DISULFID 33..71
FT /evidence="ECO:0000250|UniProtKB:P02748"
FT DISULFID 79..91
FT /evidence="ECO:0000250|UniProtKB:P02748"
FT DISULFID 86..104
FT /evidence="ECO:0000250|UniProtKB:P02748"
FT DISULFID 98..112
FT /evidence="ECO:0000250|UniProtKB:P02748"
FT DISULFID 119..158
FT /evidence="ECO:0000250|UniProtKB:P02748"
FT DISULFID 481..497
FT /evidence="ECO:0000250|UniProtKB:P02748"
FT DISULFID 484..499
FT /evidence="ECO:0000250|UniProtKB:P02748"
FT DISULFID 501..510
FT /evidence="ECO:0000250|UniProtKB:P02748"
FT NON_TER 1
SQ SEQUENCE 574 AA; 64033 MW; CB516A9F76824D59 CRC64;
QANGTLGRSR WLPLDPVDCV WSRWSEWTPC NSCTKIRHRS RSVEVFGQFG GKPCQGQPIG
EQQRCTSDAV CEQALPSECS SIEFTCESGA CIKLRLSCNG DYDCEDGSDE DCEPVRKPCG
TKLYDTNEQG RTAGYGINIL GMEPRINPFN NDYFNGMCNK VKNINNNEYN RLPWNVGLLN
YETIAEETVS KEIYEDTYTL LRELMTETKL TVSAGLNLKF TPTEKSMAKS NTTVSGGVGL
DAEYDRTQMI KEVSEYTTIK NKSFMRVNGR VQLSTYRMRS RDLQVAGEFL EHVKSLPLEY
EKGQYFSFLE DYGTHYTRNG KSGGEHQLVY VLNQDTIKDK KLTERKLQDC IKVGISANFD
TNIGIGGDAH IRPGHCKDTV NKNTAEKEGK ALVDKVITVV RGGTLEAAVA MRTQITKEGL
MDVKTYQNWA RTVGDAPALL SSEPEPIQTL IPLSMPDANT RRLNMQRATQ EYEAEYSVCK
CKPCHNGGSL ALLDGKCLCL CLPQFEGLAC QDAKADNNKN TKTPVRVFLE KGNWSCWAAW
SGCSGGKRIR TRSCNTQGLS DATCRGDIVT EDYC
