GenomeNet

Database: UniProt
Entry: P61135
LinkDB: P61135
Original site: P61135 
ID   CO6_PONPY               Reviewed;         934 AA.
AC   P61135;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 1.
DT   23-MAY-2018, entry version 81.
DE   RecName: Full=Complement component C6;
DE   Flags: Precursor;
GN   Name=C6;
OS   Pongo pygmaeus (Bornean orangutan).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pongo.
OX   NCBI_TaxID=9600;
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
CC       plays a key role in the innate and adaptive immune response by
CC       forming pores in the plasma membrane of target cells.
CC       {ECO:0000250}.
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 12-14 copies of the
CC       pore-forming subunit C9 (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
CC       within the same module (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the complement C6/C7/C8/C9 family.
CC       {ECO:0000305}.
DR   EMBL; AB126594; BAD02323.1; -; mRNA.
DR   EMBL; AB126596; BAD02325.1; -; Genomic_DNA.
DR   ProteinModelPortal; P61135; -.
DR   SMR; P61135; -.
DR   PRIDE; P61135; -.
DR   HOGENOM; HOG000111865; -.
DR   HOVERGEN; HBG005366; -.
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   InterPro; IPR037563; Complement_C6.
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   PANTHER; PTHR19325:SF23; PTHR19325:SF23; 1.
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   Repeat; Secreted; Signal; Sushi.
FT   SIGNAL        1     21       {ECO:0000250}.
FT   CHAIN        22    934       Complement component C6.
FT                                /FTId=PRO_0000023581.
FT   DOMAIN       22     79       TSP type-1 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN       81    134       TSP type-1 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN      138    175       LDL-receptor class A.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      176    522       MACPF. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00745}.
FT   DOMAIN      523    553       EGF-like.
FT   DOMAIN      565    612       TSP type-1 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN      642    701       Sushi 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      702    763       Sushi 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      780    839       Kazal-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00798}.
FT   DOMAIN      876    934       Kazal-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00798}.
FT   REGION      611    688       CCP 1.
FT   REGION      642    934       C5b-binding domain.
FT   REGION      689    765       CCP 2.
FT   REGION      766    840       Factor I module (FIM) 1.
FT   REGION      858    934       Factor I module (FIM) 2.
FT   CARBOHYD     29     29       C-linked (Man) tryptophan.
FT                                {ECO:0000250|UniProtKB:P13671}.
FT   CARBOHYD     32     32       C-linked (Man) tryptophan.
FT                                {ECO:0000250|UniProtKB:P13671}.
FT   CARBOHYD     38     38       O-linked (Fuc...) threonine.
FT                                {ECO:0000250|UniProtKB:P13671}.
FT   CARBOHYD     90     90       C-linked (Man) tryptophan.
FT                                {ECO:0000250|UniProtKB:P13671}.
FT   CARBOHYD    324    324       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    392    392       O-linked (Fuc...) threonine.
FT                                {ECO:0000250|UniProtKB:P13671}.
FT   CARBOHYD    568    568       C-linked (Man) tryptophan.
FT                                {ECO:0000250|UniProtKB:P13671}.
FT   CARBOHYD    571    571       C-linked (Man) tryptophan.
FT                                {ECO:0000250|UniProtKB:P13671}.
FT   CARBOHYD    574    574       C-linked (Man) tryptophan.
FT                                {ECO:0000250|UniProtKB:P13671}.
FT   CARBOHYD    855    855       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     22     61       {ECO:0000250}.
FT   DISULFID     24     65       {ECO:0000250}.
FT   DISULFID     35     73       {ECO:0000250}.
FT   DISULFID     39     78       {ECO:0000250}.
FT   DISULFID     82    117       {ECO:0000250}.
FT   DISULFID     93    127       {ECO:0000250}.
FT   DISULFID     96    133       {ECO:0000250}.
FT   DISULFID    140    151       {ECO:0000250}.
FT   DISULFID    146    164       {ECO:0000250}.
FT   DISULFID    158    173       {ECO:0000250}.
FT   DISULFID    180    218       {ECO:0000250}.
FT   DISULFID    399    420       {ECO:0000250}.
FT   DISULFID    499    623       {ECO:0000250}.
FT   DISULFID    521    570       {ECO:0000250}.
FT   DISULFID    523    539       {ECO:0000250}.
FT   DISULFID    526    541       {ECO:0000250}.
FT   DISULFID    543    552       {ECO:0000250}.
FT   DISULFID    577    611       {ECO:0000250}.
FT   DISULFID    589    601       {ECO:0000250}.
FT   DISULFID    644    686       {ECO:0000250}.
FT   DISULFID    672    699       {ECO:0000250}.
FT   DISULFID    704    746       {ECO:0000250}.
FT   DISULFID    732    761       {ECO:0000250}.
FT   DISULFID    773    823       {ECO:0000250}.
FT   DISULFID    784    801       {ECO:0000250}.
FT   DISULFID    786    837       {ECO:0000250}.
FT   DISULFID    793    816       {ECO:0000250}.
FT   DISULFID    862    873       {ECO:0000250}.
FT   DISULFID    867    919       {ECO:0000250}.
FT   DISULFID    880    897       {ECO:0000250}.
FT   DISULFID    882    932       {ECO:0000250}.
FT   DISULFID    888    912       {ECO:0000250}.
SQ   SEQUENCE   934 AA;  104959 MW;  6F1D7D6F15A093BF CRC64;
     MARCSVLYFI LLSALINKGQ ACFCDHYPWT QWTSCSKTCN SGTQSRHRQI VVDKYYQENF
     CEQICSKQET RECNWQRCPI NCLLGDFGPW SDCDPCVEKQ SKVRSVLRPS QFGGQPCTEP
     LVAFQPCIPS KLCKIEEADC KNKFRCDSGR CIARKLECNG ENDCGDNSDE RDCGRTKAVC
     TRKYDPIPSV QLMGSGFHFL AGEPRGEVLD NSFTGGICKT VKSSRTSNPY RVPANLENVG
     FEVQTAEDDL KTDFYKDLTS LGHNENQQGS FSSQGGSSFS VPIFYSSKRS ENINHNSAFK
     QAIQASHKKD SSFIRIHKVM KVLNFTTKAK DLHLSDIFLK ALNHLPLEYN SALYSRIFDD
     FGTHYFTSGS LGGVYDLLYQ FSSEELKNSG LTEEEAKHCV RIETKKRVLF AKKTKVEHRC
     TTNKLSEKHE GSFIEGAEKS ISLIRGGRSE YAAALAWEKG SSGLEEKTFS EWLESVKENP
     AVIDFELAPI VDLVRNIPCA VTKRNNLRKA FQEYAAKFDP CQCAPCPNNG RPTLSGTECL
     CVCQSGTYGE NCERRSPDYK SNAVDGHWGC WSSWSTCDAT YKRSRTRECN NPAPQRGGKH
     CEGEKRQEED CTFSIMENNG QPCINDDEEM KEIDLPEIEA DSGCPQPIPP ENGFIRNEKK
     LYSVGEDVEI LCLTGFETVG YQYFRCLPDG TWRQGDVECQ RTECIKPVVQ EVLTITPFQR
     LYRIGESIEL TCPKGFVVAG PSRYTCQGNS WTPPISNSLT CEKDTLIKLK GHCQPGQKQS
     GSECICMYPE EDCSHYSEDL CVFDTDSNDY FTSPACKFLA EKCLNNQQLH FLHIGSCQDG
     RQLEWGLERA RFSSNSTKKE SCGYDTCYDW EKCSASTSKC VCLLPPQCFK GGNQLYCVKM
     GSSTSEKTLN ICEVGAIRCA NRKMEILHPG KCLA
//
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