CO9_RABIT
ID CO9_RABIT Reviewed; 557 AA.
AC P48747;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Complement component C9;
DE Flags: Precursor;
GN Name=C9;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 22-34.
RC STRAIN=New Zealand white; TISSUE=Liver;
RX PubMed=7533152; DOI=10.1074/jbc.270.8.3483;
RA Huesler T., Lockert D.H., Kaufman K.M., Sodetz J.M., Sims P.J.;
RT "Chimeras of human complement C9 reveal the site recognized by complement
RT regulatory protein CD59.";
RL J. Biol. Chem. 270:3483-3486(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; U20055; AAC48459.1; -; mRNA.
DR RefSeq; NP_001075815.1; NM_001082346.1.
DR AlphaFoldDB; P48747; -.
DR SMR; P48747; -.
DR CORUM; P48747; -.
DR STRING; 9986.ENSOCUP00000010939; -.
DR PRIDE; P48747; -.
DR GeneID; 100009197; -.
DR KEGG; ocu:100009197; -.
DR CTD; 735; -.
DR eggNOG; ENOG502QWHM; Eukaryota.
DR InParanoid; P48747; -.
DR OrthoDB; 787014at2759; -.
DR Proteomes; UP000001811; 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; IPR000742; EGF-like_dom.
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; SSF57424; SSF57424; 1.
DR SUPFAM; SSF82895; SSF82895; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 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 Direct protein sequencing; Disulfide bond; EGF-like domain; Glycoprotein;
KW Immunity; Innate immunity; Membrane; Membrane attack complex;
KW Reference proteome; Secreted; Signal; Target cell membrane;
KW Target membrane; Transmembrane; Transmembrane beta strand.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:7533152"
FT CHAIN 22..557
FT /note="Complement component C9"
FT /id="PRO_0000023606"
FT TRANSMEM 319..335
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..359
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..137
FT /note="LDL-receptor class A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 139..519
FT /note="MACPF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00745"
FT DOMAIN 520..550
FT /note="EGF-like"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 424
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..113
FT /evidence="ECO:0000250|UniProtKB:P02748"
FT DISULFID 108..126
FT /evidence="ECO:0000250|UniProtKB:P02748"
FT DISULFID 120..135
FT /evidence="ECO:0000250|UniProtKB:P02748"
FT DISULFID 143..182
FT /evidence="ECO:0000250|UniProtKB:P02748"
FT DISULFID 520..536
FT /evidence="ECO:0000250|UniProtKB:P02748"
FT DISULFID 523..538
FT /evidence="ECO:0000250|UniProtKB:P02748"
FT DISULFID 540..549
FT /evidence="ECO:0000250|UniProtKB:P02748"
SQ SEQUENCE 557 AA; 62662 MW; FF4E65FF8D1AB417 CRC64;
MAASHSFAFV VCVLEIGALT AGPTPSYVHE PIQRSDPLQP IDCRMSPWSE WSHCDPCLRQ
MFRSRSIEVF GQFHGKSCVD ALGDRRACIP TEACEDAEED CEKDEFHCGT GRCIKRRLLC
NGDNDCGDFS DEDDCETEPR LTCRNREVQE SELARTAGYG INILGMDPLA TPFDNEYYHG
LCDRVWDGNT LTHYRKPWNV AVLAYETKID KNFRTEYYEE QMQAFKSIIE EETSNFNANL
ALKFTPTEAK ASKAEEASPK NKSLDDNDKG FSSKFQFSYS KNETYQLFLS YSSQKEKMFL
LVKGIIQLGR FVMKNRGVML TNTFLDDIKS LPTTYEKGEY FAFLETYGTH YSSSGSLGGR
YELIYVLDKA SMKEKGIELN DIKKCLGFDL DLSLNIPGKS AGLSLTGQAN KNNCLKSGHG
NAVNITRANL IDDVISLIRG GTQKFAFELK EKLLTKAKMV DVTDFINWAS SLSDAPVLIN
QKLSPIYNLI PVKIKDAHQK RQNLERGIED YINEFSTKKC SPCQNGGTAL LMDGQCLCTC
PFMFEGIACE ISKRKLA
