CO6_PANTR
ID CO6_PANTR Reviewed; 934 AA.
AC P61134;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Complement component C6;
DE Flags: Precursor;
GN Name=C6;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA Soejima M., Koda Y.;
RT "Sequence variation in C6 locus.";
RL Submitted (NOV-2003) 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. {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; AB126593; BAD02322.1; -; mRNA.
DR EMBL; AB126595; BAD02324.1; -; Genomic_DNA.
DR RefSeq; NP_001009015.1; NM_001009015.1.
DR AlphaFoldDB; P61134; -.
DR SMR; P61134; -.
DR STRING; 9598.ENSPTRP00000028843; -.
DR PaxDb; P61134; -.
DR GeneID; 449612; -.
DR KEGG; ptr:449612; -.
DR CTD; 729; -.
DR eggNOG; ENOG502QPIM; Eukaryota.
DR InParanoid; P61134; -.
DR OrthoDB; 100680at2759; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005579; C:membrane attack complex; 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:0045087; P:innate immune response; IEA:UniProtKB-KW.
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; 3.
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_0000023580"
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...) threonine"
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 CARBOHYD 855
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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; 104947 MW; 099A1130CD255B6A CRC64;
MARRSVLYFI LLNALINKGQ ACFCDHYAWT QWTSCSKTCN SGTQSRHRQI VVDKYYQENF
CEQICSKQET RECNWQRCPI NCLLGDFGPW SDCDPCVEKQ SKVRSVLRPS QFGGQPCTEP
LVAFQPCIPS KLCKIEEADC KNKFRCDSGR CIARKLECNG ENDCGDNSDE RDCGRTKAVC
TRKYNPIPSV QLMGNGFHFL AGEPRGEVLD NSFTGGICKT VKSSRTSNPY RVPANLENVG
FEVQTAEDDL KTDFYKDLTS LGHNENQQGS FSSQGGSSFS VPIFYSSKRS ENINHNSAFK
QAIQASHKKD SSFIRIHKVM KVLNFTTKAK DLHLSDVFLK ALNHLPLEYN SALYSRIFDD
FGTHYFTSGS LGGVYDLLYQ FSSEELKNSG LTEEEAKHCV RIETKKRVLF VKKTKVEHRC
TTNKLSEKHE GSFIQGAEKS ISLIRGGRSE YAAALAWEKG SSGLEEKTFS EWLESVKENP
AVIDFELAPI VDLVRNIPCA VTKRNNLRKA LQEYAAKFDP CQCAPCPNNG RPTLSGTECL
CVCQSGTYGE NCEKQSPDYK SNAVDGHWGC WSSWSTCDAT YKRSRTRECN NPVPQRGGKR
CEGEKRQEED CTFSIMENNG QPCINDDEEM KEVDLPEIEA DSGCPQPVPP ENGFIRNEKQ
LYSVGEDVEI SCLTGFETVG YQYFRCLPDG TWRQGDVECQ RRECIKPVVQ EVLTITPFQR
LYRIGESIEL TCPKGFVVAG PSRYTCQGNS WTPPISNSLT CEKDTLTKLR GHCQLGQKQS
GSECICMSPE EDCSHHSEDL CVFDTDSNDY FTSPACKFLA EKCLNNQQLH FLHIGSCQDG
HQLEWGLERT RLSSNSTKKE SCGYDTCYDW EKCSASTSKC VCLLPPQCFK GGNQLYCVKM
GSSTSEKTLN ICEVGTIRCA NRKMEILHPG KCLA
