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Database: UniProt
Entry: P48747
LinkDB: P48747
Original site: P48747 
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   16-JAN-2019, entry version 108.
DE   RecName: Full=Complement component C9;
DE   Flags: Precursor;
GN   Name=C9;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
OC   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
RT   complement regulatory protein CD59.";
RL   J. Biol. Chem. 270:3483-3486(1995).
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). MAC
CC       assembly is initiated by proteolytic cleavage of C5 into C5a and
CC       C5b. C5b binds sequentially C6, C7, C8 and multiple copies of the
CC       pore-forming subunit C9. About 20 C9 chains oligomerize to give
CC       rise to a huge beta-barrel that forms a 100 Angstrom diameter pore
CC       in target membranes. {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: Thrombin cleaves factor C9 to produce C9a and C9b.
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; U20055; AAC48459.1; -; mRNA.
DR   RefSeq; NP_001075815.1; NM_001082346.1.
DR   UniGene; Ocu.2269; -.
DR   ProteinModelPortal; 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; ENOG410IH3C; Eukaryota.
DR   eggNOG; ENOG410XT9A; LUCA.
DR   HOGENOM; HOG000111869; -.
DR   HOVERGEN; HBG106792; -.
DR   InParanoid; P48747; -.
DR   KO; K04000; -.
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: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   Gene3D; 2.20.100.10; -; 1.
DR   InterPro; IPR037567; Complement_C9.
DR   InterPro; IPR013032; EGF-like_CS.
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   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; Complete proteome;
KW   Cytolysis; Direct protein sequencing; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Immunity; Innate immunity; Membrane;
KW   Membrane attack complex; Reference proteome; Secreted; Signal;
KW   Target cell membrane; Target membrane; Transmembrane;
KW   Transmembrane beta strand.
FT   SIGNAL        1     21       {ECO:0000269|PubMed:7533152}.
FT   CHAIN        22    557       Complement component C9.
FT                                /FTId=PRO_0000023606.
FT   TRANSMEM    319    335       Beta stranded. {ECO:0000255}.
FT   TRANSMEM    340    359       Beta stranded. {ECO:0000255}.
FT   DOMAIN       42     95       TSP type-1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN       99    137       LDL-receptor class A.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      139    519       MACPF. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00745}.
FT   DOMAIN      520    550       EGF-like.
FT   CARBOHYD    261    261       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    282    282       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    424    424       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     43     78       {ECO:0000250|UniProtKB:P02748}.
FT   DISULFID     54     88       {ECO:0000250|UniProtKB:P02748}.
FT   DISULFID     57     94       {ECO:0000250|UniProtKB:P02748}.
FT   DISULFID    101    113       {ECO:0000250|UniProtKB:P02748}.
FT   DISULFID    108    126       {ECO:0000250|UniProtKB:P02748}.
FT   DISULFID    120    135       {ECO:0000250|UniProtKB:P02748}.
FT   DISULFID    143    182       {ECO:0000250|UniProtKB:P02748}.
FT   DISULFID    520    536       {ECO:0000250|UniProtKB:P02748}.
FT   DISULFID    523    538       {ECO:0000250|UniProtKB:P02748}.
FT   DISULFID    540    549       {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
//
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