CO9_RAT
ID CO9_RAT Reviewed; 554 AA.
AC Q62930; Q62957;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Complement component C9;
DE Flags: Precursor;
GN Name=C9;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Sprague-Dawley;
RX PubMed=9212048; DOI=10.1203/00006450-199707000-00021;
RA Lassiter H.A., Walz B.M., Wilson J.L., Jung E., Calisi C.R.,
RA Goldsmith L.J., Wilson R.A., Morgan B.P., Feldhoff R.C.;
RT "The administration of complement component C9 enhances the survival of
RT neonatal rats with Escherichia coli sepsis.";
RL Pediatr. Res. 42:128-136(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Hinchliffe S.J., Van den Berg C.W., Rushmere N.K., Morgan B.P.;
RT "Cloning of rat C9: consequences for homologous restriction of
RT complement.";
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
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:0000269|PubMed:9212048}.
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:0000269|PubMed:9212048}. Target
CC cell membrane {ECO:0000269|PubMed:9212048}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P02748}. Note=Secreted as soluble monomer.
CC Oligomerizes at target membranes, forming a pre-pore. A conformation
CC change then leads to the formation of a 100 Angstrom diameter pore.
CC {ECO:0000250|UniProtKB:P02748}.
CC -!- TISSUE SPECIFICITY: Detected in blood serum (at protein level).
CC {ECO:0000269|PubMed:9212048}.
CC -!- DEVELOPMENTAL STAGE: Detected at low levels in neonate blood serum.
CC Levels increase throughout the first three weeks after birth.
CC {ECO:0000269|PubMed:9212048}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA96528.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U49071; AAB38023.1; -; mRNA.
DR EMBL; U52948; AAA96528.1; ALT_INIT; mRNA.
DR RefSeq; NP_476487.1; NM_057146.1.
DR AlphaFoldDB; Q62930; -.
DR SMR; Q62930; -.
DR BioGRID; 250734; 1.
DR STRING; 10116.ENSRNOP00000018545; -.
DR GlyGen; Q62930; 3 sites.
DR iPTMnet; Q62930; -.
DR PhosphoSitePlus; Q62930; -.
DR PaxDb; Q62930; -.
DR PRIDE; Q62930; -.
DR GeneID; 117512; -.
DR KEGG; rno:117512; -.
DR CTD; 735; -.
DR RGD; 620319; C9.
DR eggNOG; ENOG502QWHM; Eukaryota.
DR InParanoid; Q62930; -.
DR OrthoDB; 787014at2759; -.
DR Reactome; R-RNO-166665; Terminal pathway of complement.
DR Reactome; R-RNO-977606; Regulation of Complement cascade.
DR PRO; PR:Q62930; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0005579; C:membrane attack complex; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0007596; P:blood coagulation; IMP:RGD.
DR GO; GO:0001906; P:cell killing; ISO:RGD.
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:0051260; P:protein homooligomerization; ISO:RGD.
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 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; 1.
PE 1: Evidence at protein 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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..554
FT /note="Complement component C9"
FT /id="PRO_0000023607"
FT TRANSMEM 316..332
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..356
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..518
FT /note="MACPF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00745"
FT DOMAIN 519..549
FT /note="EGF-like"
FT SITE 267..268
FT /note="Cleavage; by thrombin"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..76
FT /evidence="ECO:0000250|UniProtKB:P02748"
FT DISULFID 52..86
FT /evidence="ECO:0000250|UniProtKB:P02748"
FT DISULFID 55..92
FT /evidence="ECO:0000250|UniProtKB:P02748"
FT DISULFID 99..110
FT /evidence="ECO:0000250|UniProtKB:P02748"
FT DISULFID 105..123
FT /evidence="ECO:0000250|UniProtKB:P02748"
FT DISULFID 117..132
FT /evidence="ECO:0000250|UniProtKB:P02748"
FT DISULFID 140..179
FT /evidence="ECO:0000250|UniProtKB:P02748"
FT DISULFID 519..535
FT /evidence="ECO:0000250|UniProtKB:P02748"
FT DISULFID 522..537
FT /evidence="ECO:0000250|UniProtKB:P02748"
FT DISULFID 539..548
FT /evidence="ECO:0000250|UniProtKB:P02748"
FT CONFLICT 65
FT /note="I -> M (in Ref. 2; AAA96528)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="K -> R (in Ref. 2; AAA96528)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 554 AA; 62281 MW; 9C885F76A1275649 CRC64;
MASGVTITLA IAIFALEINA QAPEPTPREE PSADALLPID CRMSTWSQWS QCDPCLKQRF
RSRSIEVFGQ FQGKSCADAL GDRQHCEPTQ ECEEVQENCG NDFQCETGRC IKRKLLCNGD
NDCGDFSDES DCESDPRLPC RDRVVEESEL GRTAGYGINI LGMDPLGTPF DNEFYNGLCD
RVRDGNTLTY YRKPWNVAFL AYETKADKNF RTENYEEQFE MFKTIVRDRT TSFNANLALK
FTITEAPIKK VGVDEVSPEK NSSKPKDSSV DFQFSYFKKE NFQRLSSYLS QTKKMFLHVK
GMIQLGRFVM RNRGVMLTTT FLDDVKALPV SYEKGEYFGF LETYGTHYSS SGSLGGLYEL
IYVLDKASMK EKGVELSDVK RCLGFNLDVS LYTPLQTALE GPSLTANVNH SDCLKTGDGK
VVNISRDHII DDVISFIRGG TRKQAVLLKE KLLRGAKTID VNDFINWASS LDDAPALISQ
KLSPIYNLIP LTMKDAYAKK QNMEKAIEDY VNEFSARKCY PCQNGGTAIL LDGQCMCSCT
IKFKGIACEI SKQR
