CO9_BOVIN
ID CO9_BOVIN Reviewed; 548 AA.
AC Q3MHN2;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Complement component C9;
DE Flags: Precursor;
GN Name=C9;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) 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: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. {ECO:0000250}.
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; BC105174; AAI05175.1; -; mRNA.
DR RefSeq; NP_001030441.1; NM_001035364.2.
DR RefSeq; XP_015314577.1; XM_015459091.1.
DR AlphaFoldDB; Q3MHN2; -.
DR SMR; Q3MHN2; -.
DR STRING; 9913.ENSBTAP00000021495; -.
DR PaxDb; Q3MHN2; -.
DR PeptideAtlas; Q3MHN2; -.
DR PRIDE; Q3MHN2; -.
DR Ensembl; ENSBTAT00000021495; ENSBTAP00000021495; ENSBTAG00000016149.
DR GeneID; 526766; -.
DR KEGG; bta:526766; -.
DR VEuPathDB; HostDB:ENSBTAG00000016149; -.
DR VGNC; VGNC:26647; C9.
DR eggNOG; ENOG502QWHM; Eukaryota.
DR GeneTree; ENSGT00940000159777; -.
DR HOGENOM; CLU_032453_2_0_1; -.
DR InParanoid; Q3MHN2; -.
DR OMA; WASSIND; -.
DR OrthoDB; 787014at2759; -.
DR TreeFam; TF330498; -.
DR Proteomes; UP000009136; Chromosome 20.
DR Bgee; ENSBTAG00000016149; Expressed in liver and 47 other tissues.
DR ExpressionAtlas; Q3MHN2; baseline.
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: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; 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; 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 PRINTS; PR00764; COMPLEMENTC9.
DR SMART; SM00192; LDLa; 1.
DR SMART; SM00457; MACPF; 1.
DR SMART; SM00209; TSP1; 1.
DR SUPFAM; SSF57184; SSF57184; 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 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; Reference proteome; Secreted; Signal;
KW Target cell membrane; Target membrane; Transmembrane;
KW Transmembrane beta strand.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..548
FT /note="Complement component C9"
FT /id="PRO_0000045783"
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 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..514
FT /note="MACPF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00745"
FT DOMAIN 515..545
FT /note="EGF-like"
FT CARBOHYD 456
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 515..531
FT /evidence="ECO:0000250|UniProtKB:P02748"
FT DISULFID 518..533
FT /evidence="ECO:0000250|UniProtKB:P02748"
FT DISULFID 535..544
FT /evidence="ECO:0000250|UniProtKB:P02748"
SQ SEQUENCE 548 AA; 61998 MW; 69402AB0B20237F9 CRC64;
MSAGQRFAFA ICILEISLLR AGPTPSYDPA ERQGTPLPID CRMSSWSEWS KCDPCLKQMF
RSRSIEIFGQ FNGRKCVDAV GDRQQCVPTE ACEDPEEGCG NDFQCGTGRC IKNRLLCNED
NDCGDYSDED NCEQDPRPPC RNRVVEESEL ARTAGFGINI LGMDPLSTPF DNQYYNGLCD
RVWDGNTLTY YRRPWNVASL TYDTKADKNF RTENHEESIQ ILRTIIEEKK LNFNAGLSVK
YTPVEAIEKN KCVDLEHSDK GSTSSPSKLA AEAKFRFTYS KDDIYRLLSS YSAKQEKMFL
HVKGKVHLGR FVMRSRDVML QTTFLDSINT LPTTYEKGEY FAFLETYGTH YSSSGSLGGL
YELIYVLDKK SMEQKDIELR DVQRCLGFDL DLSLKVGVEV TGNFDSKLCS KKGMGQTETN
PEADLFDDVI TFIRGGTRKY ATELKEKLLR GARMINVTDF VNWAASLNHA PVLISQKLVP
IYDLIPVKMK DAHLKKQNLE RAIEDYINEF SVRKCQPCQN GGTVVLLDGE CVCSCPKEFK
GVACEIKK
