CO6_RAT
ID CO6_RAT Reviewed; 934 AA.
AC Q811M5;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Complement component C6;
DE Flags: Precursor;
GN Name=C6;
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].
RC STRAIN=PVG.RT1L;
RX PubMed=15568620; DOI=10.1016/j.imbio.2004.08.001;
RA Bhole D., Stahl G.L.;
RT "Molecular basis for complement component 6 (C6) deficiency in rats and
RT mice.";
RL Immunobiology 209:559-568(2004).
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. {ECO:0000250}.
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 12-14 copies of the pore-forming subunit C9
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- PTM: All cysteine residues are assumed to be cross-linked to one
CC another. Individual modules containing an even number of conserved
CC cysteine residues are supposed to have disulfide linkages only within
CC the same module (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the complement C6/C7/C8/C9 family.
CC {ECO:0000305}.
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DR EMBL; AY230250; AAO40768.1; -; mRNA.
DR RefSeq; NP_788263.1; NM_176074.3.
DR AlphaFoldDB; Q811M5; -.
DR SMR; Q811M5; -.
DR BioGRID; 246424; 1.
DR STRING; 10116.ENSRNOP00000029891; -.
DR CarbonylDB; Q811M5; -.
DR GlyGen; Q811M5; 9 sites.
DR PRIDE; Q811M5; -.
DR GeneID; 24237; -.
DR KEGG; rno:24237; -.
DR CTD; 729; -.
DR RGD; 2238; C6.
DR eggNOG; ENOG502QPIM; Eukaryota.
DR InParanoid; Q811M5; -.
DR OrthoDB; 100680at2759; -.
DR PhylomeDB; Q811M5; -.
DR Reactome; R-RNO-166665; Terminal pathway of complement.
DR Reactome; R-RNO-977606; Regulation of Complement cascade.
DR PRO; PR:Q811M5; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005579; C:membrane attack complex; ISO:RGD.
DR GO; GO:0006956; P:complement activation; ISO:RGD.
DR GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0001970; P:positive regulation of activation of membrane attack complex; ISO:RGD.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
DR GO; GO:0045917; P:positive regulation of complement activation; ISO:RGD.
DR CDD; cd00033; CCP; 2.
DR CDD; cd00112; LDLa; 1.
DR Gene3D; 2.20.100.10; -; 3.
DR Gene3D; 4.10.400.10; -; 1.
DR InterPro; IPR003884; FacI_MAC.
DR InterPro; IPR002350; Kazal_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; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR Pfam; PF00057; Ldl_recept_a; 1.
DR Pfam; PF01823; MACPF; 1.
DR Pfam; PF00084; Sushi; 2.
DR Pfam; PF00090; TSP_1; 2.
DR PRINTS; PR00764; COMPLEMENTC9.
DR SMART; SM00032; CCP; 2.
DR SMART; SM00057; FIMAC; 2.
DR SMART; SM00192; LDLa; 1.
DR SMART; SM00457; MACPF; 1.
DR SMART; SM00209; TSP1; 3.
DR SUPFAM; SSF57424; SSF57424; 1.
DR SUPFAM; SSF57535; SSF57535; 2.
DR SUPFAM; SSF82895; SSF82895; 3.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS51465; KAZAL_2; 2.
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; PS50923; SUSHI; 2.
DR PROSITE; PS50092; TSP1; 3.
PE 2: Evidence at transcript level;
KW Complement pathway; Cytolysis; Disulfide bond; EGF-like domain;
KW Glycoprotein; Immunity; Innate immunity; Membrane attack complex;
KW Reference proteome; Repeat; Secreted; Signal; Sushi.
FT SIGNAL 1..21
FT /evidence="ECO:0000250"
FT CHAIN 22..934
FT /note="Complement component C6"
FT /id="PRO_0000023582"
FT DOMAIN 22..79
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 81..134
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 138..175
FT /note="LDL-receptor class A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 176..522
FT /note="MACPF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00745"
FT DOMAIN 523..553
FT /note="EGF-like"
FT DOMAIN 565..612
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 642..701
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 702..763
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 780..839
FT /note="Kazal-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 876..934
FT /note="Kazal-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT REGION 611..688
FT /note="CCP 1"
FT REGION 642..934
FT /note="C5B-binding domain"
FT REGION 689..765
FT /note="CCP 2"
FT REGION 766..840
FT /note="Factor I module (FIM) 1"
FT REGION 858..934
FT /note="Factor I module (FIM) 2"
FT CARBOHYD 29
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P13671"
FT CARBOHYD 32
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P13671"
FT CARBOHYD 38
FT /note="O-linked (Fuc...) serine"
FT /evidence="ECO:0000250|UniProtKB:P13671"
FT CARBOHYD 90
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P13671"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 392
FT /note="O-linked (Fuc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P13671"
FT CARBOHYD 568
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P13671"
FT CARBOHYD 571
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P13671"
FT CARBOHYD 574
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P13671"
FT DISULFID 22..61
FT /evidence="ECO:0000250"
FT DISULFID 24..65
FT /evidence="ECO:0000250"
FT DISULFID 35..73
FT /evidence="ECO:0000250"
FT DISULFID 39..78
FT /evidence="ECO:0000250"
FT DISULFID 82..117
FT /evidence="ECO:0000250"
FT DISULFID 93..127
FT /evidence="ECO:0000250"
FT DISULFID 96..133
FT /evidence="ECO:0000250"
FT DISULFID 140..151
FT /evidence="ECO:0000250"
FT DISULFID 146..164
FT /evidence="ECO:0000250"
FT DISULFID 158..173
FT /evidence="ECO:0000250"
FT DISULFID 180..218
FT /evidence="ECO:0000250"
FT DISULFID 399..420
FT /evidence="ECO:0000250"
FT DISULFID 499..623
FT /evidence="ECO:0000250"
FT DISULFID 521..570
FT /evidence="ECO:0000250"
FT DISULFID 523..539
FT /evidence="ECO:0000250"
FT DISULFID 526..541
FT /evidence="ECO:0000250"
FT DISULFID 543..552
FT /evidence="ECO:0000250"
FT DISULFID 577..611
FT /evidence="ECO:0000250"
FT DISULFID 589..601
FT /evidence="ECO:0000250"
FT DISULFID 644..686
FT /evidence="ECO:0000250"
FT DISULFID 672..699
FT /evidence="ECO:0000250"
FT DISULFID 704..746
FT /evidence="ECO:0000250"
FT DISULFID 732..761
FT /evidence="ECO:0000250"
FT DISULFID 773..823
FT /evidence="ECO:0000250"
FT DISULFID 784..801
FT /evidence="ECO:0000250"
FT DISULFID 786..837
FT /evidence="ECO:0000250"
FT DISULFID 793..816
FT /evidence="ECO:0000250"
FT DISULFID 862..873
FT /evidence="ECO:0000250"
FT DISULFID 867..919
FT /evidence="ECO:0000250"
FT DISULFID 880..897
FT /evidence="ECO:0000250"
FT DISULFID 882..932
FT /evidence="ECO:0000250"
FT DISULFID 888..912
FT /evidence="ECO:0000250"
SQ SEQUENCE 934 AA; 105114 MW; 90C219EEFF03AE15 CRC64;
MTRHLTLCFI LLIILIDKSE ACFCDHYPWT HWSSCSKSCN SGTQSRQRQI VVNDYYRDNS
CDQLCTKQET RQCNVETCPI NCVLGDYGTW SDCDPCIRKQ VKVRSVLRPS QFGGQPCTEP
LVTFQPCVPS ELCKIEETDC KNKFLCDSGR CIPSKLKCNG ENDCGDNSDE RNCGRTKPVC
SRTYTPIPSV QLMGAGFHFL AGEPRGDVPD NSFTGGICKS VRSSRTSNPH RVPANLENVN
FEVQTIEDDL KTDFYKDLAT IGKNKNEDRS LSGEKKDSFY VPIFYSSKKS ENFQRNSGFK
NAIEASHKKD SSFVRIHKVI KVLNFTMKTT DLQLSDVFLK ALIHLPLEYN FALYSRIFDD
FGTHYFTSGS LGGKYDLLYQ FSRQELQNSG LTEEETRNCV RYETKKRFLF FTKTYKEDRC
TTNRLSEKYK GSFLQGSEKS ISLVQGGRSQ QAAALAWEKG SSGPEANVFS EWLESVKENP
AVVDYELAPI IDLVRNIPCA VTKRNNLRKA LQEYAAKFDP CQCAPCPNNG RPRLSGTECL
CVCQSGTYGE NCEKRSPDYK SNAVDGNWGC WSSWSACNAA YRRSRSRECN NPEPQRGGQR
CEGKHWQEED CTFSIMEKVG QPCISDDEEI KEVDLAEPEA DSGCPQPPLP ENAFVWNEKK
LYSVGEEVEI SCLTGFKAVG YQYFRCLPDR TWRQGDVECQ RTECLKPVVQ DVLTISPFQS
VYKIGESIEL TCPRGFVVAG PSRYTCKGDS WTPPIPNSLS CEKDILTKSK GLCQPGQKQS
GSECVCMSPE EDCSSYSEDL CIFDEGSSQY FTSSACKFLA EKCLNSNQFH FVHAGSCQEG
PQLEWGLERL KLAMKSTKRV PCGYDTCYDW EKCSAHTSNC VCLLPPQCPK DENQLHCVKM
GSSMRGKTVN ICTLGAVRCA NRKVEILNPG RCLD
