CO6_BOVIN
ID CO6_BOVIN Reviewed; 932 AA.
AC Q29RU4;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Complement component C6;
DE Flags: Precursor;
GN Name=C6;
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 (FEB-2006) 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; BC114014; AAI14015.1; -; mRNA.
DR RefSeq; NP_001039444.1; NM_001045979.1.
DR AlphaFoldDB; Q29RU4; -.
DR SMR; Q29RU4; -.
DR STRING; 9913.ENSBTAP00000018845; -.
DR PaxDb; Q29RU4; -.
DR PRIDE; Q29RU4; -.
DR GeneID; 507749; -.
DR KEGG; bta:507749; -.
DR CTD; 729; -.
DR eggNOG; ENOG502QPIM; Eukaryota.
DR InParanoid; Q29RU4; -.
DR OrthoDB; 100680at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005579; C:membrane attack complex; IBA:GO_Central.
DR GO; GO:0006956; P:complement activation; IBA:GO_Central.
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:0000255"
FT CHAIN 22..932
FT /note="Complement component C6"
FT /id="PRO_0000254014"
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 139..174
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..932
FT /note="Kazal-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT REGION 611..688
FT /note="CCP 1"
FT REGION 642..932
FT /note="C5b-binding domain"
FT /evidence="ECO:0000250"
FT REGION 689..765
FT /note="CCP 2"
FT REGION 766..840
FT /note="Factor I module (FIM) 1"
FT REGION 858..932
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 859
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 932 AA; 104541 MW; ABB3401C467E5E83 CRC64;
MARHSVMYFI LLSALIDKSQ ACFCDHYPWS QWSSCSKTCN SGTQTRQRRI VTDKYYFENF
CGQLCTKQES RECNWQTCPI NCRLGDYGPW SDCDPCVQKR FKVRSILRPS QFGGQPCTEP
LMTFQPCIPS KLCKIEEIDC KNKFRCDSGR CIASKLECNG ENDCGDNSDE RNCGRKKTVC
SRSHNPIPGV QLMGMGFHFL AGEPRGEVLD NSFTGGVCRT VKSSRASNPY RVPANLENVN
FEVQTKEDDL EADFYDDLIP LEDNKDQEAL GSGLATSSFR VPIFYSSKRS QSSSHSSAFK
QAIQASQKKA SSFIRIHKVI KVLNFTMKTK DLQLSDVFLK ALNHLPLEYN SALYSRIFDD
FGTHYFTSGS LGGVYDLLYQ FSKEELKNSG LTQEEAKNCI RIETKKRFLF VKKTKVEHRC
TTNKLSEKYE GSFMQGSEKS ISLVQGGRSA YAAALAWEKG SPVPEERVFS DWLESVKENP
SVIDFALAPI TDLVRNIPCA VTRRNNLRRA FREYAAKFDP CQCARCPNSG RPVLSGTECL
CVCQSGTYGE NCERRSPDYK SNAVDGNWGC WSSWSSCDAT YRRSRTRECN NPAPQQGGKR
CEGERRQEEH CTFSIMQNDG QPCISDDEDM KETDLPELES DSGCPQPVPP ENGFIRNEKK
QYSVGEEVEI LCFTGFKAVG YQYFRCLPDR SWRQGDVECQ RTECLKPIVP EGLTLSPFQT
LYKIGDSIEL TCPRGLVVNG PSRYTCSGDS WTPPISDSLS CEKDVLTGLR GHCQPGQKQL
GSECVCMSPE EDCGHYSEEI CVLDTTSSDY FTSSACKLLA EKCLNNQQLH FVHIGSCEEG
PQLKWGLERI KLSSSSTKNE SCGYDTCYNW EKCSATTSKC VCLLPSQCTK GGDQLFCVQI
GSSANGKTMN ICEVGAVKCA KREMEILHSG RC
