CO7_BOVIN
ID CO7_BOVIN Reviewed; 843 AA.
AC Q29RQ1;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Complement component C7;
DE Flags: Precursor;
GN Name=C7;
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=Heart ventricle;
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. C7 serves as a membrane anchor (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer or dimer; as a C5b-7 complex it can also form
CC multimeric rosettes (By similarity). Component of the membrane attack
CC complex (MAC). MAC assembly is initiated by proteolytic cleavage of C5
CC into C5a and C5b. C5b binds sequentially C6, C7, C8 and multiple copies
CC of the pore-forming subunit C9 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- PTM: C7 has 28 disulfide bridges. {ECO:0000250}.
CC -!- PTM: C-, N- and O-glycosylated. {ECO:0000250|UniProtKB:P10643}.
CC -!- SIMILARITY: Belongs to the complement C6/C7/C8/C9 family.
CC {ECO:0000305}.
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DR EMBL; BC114076; AAI14077.1; -; mRNA.
DR RefSeq; NP_001039431.1; NM_001045966.1.
DR AlphaFoldDB; Q29RQ1; -.
DR SMR; Q29RQ1; -.
DR STRING; 9913.ENSBTAP00000047583; -.
DR PaxDb; Q29RQ1; -.
DR PRIDE; Q29RQ1; -.
DR GeneID; 507339; -.
DR KEGG; bta:507339; -.
DR CTD; 730; -.
DR eggNOG; ENOG502QU3G; Eukaryota.
DR InParanoid; Q29RQ1; -.
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: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 CDD; cd00033; CCP; 2.
DR CDD; cd00112; LDLa; 1.
DR Gene3D; 2.20.100.10; -; 2.
DR Gene3D; 4.10.400.10; -; 1.
DR InterPro; IPR037564; Complement_C7.
DR InterPro; IPR003884; FacI_MAC.
DR InterPro; IPR040729; Kazal_3.
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; PTHR45742:SF2; PTHR45742:SF2; 1.
DR Pfam; PF18434; Kazal_3; 1.
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; 2.
DR SUPFAM; SSF57424; SSF57424; 1.
DR SUPFAM; SSF57535; SSF57535; 2.
DR SUPFAM; SSF82895; SSF82895; 2.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 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; PS50923; SUSHI; 2.
DR PROSITE; PS50092; TSP1; 2.
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 attack complex; Reference proteome; Repeat; Secreted; Signal;
KW Sushi.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..843
FT /note="Complement component C7"
FT /id="PRO_0000254015"
FT DOMAIN 27..80
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 84..120
FT /note="LDL-receptor class A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 124..456
FT /note="MACPF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00745"
FT DOMAIN 457..487
FT /note="EGF-like"
FT DOMAIN 500..549
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 569..628
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 629..690
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 114..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..615
FT /note="CCP 1"
FT REGION 616..693
FT /note="CCP 2"
FT REGION 695..770
FT /note="Factor I module (FIM) 1"
FT REGION 771..843
FT /note="Factor I module (FIM) 2"
FT COMPBIAS 119..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 36
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P10643"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 503
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P10643"
FT CARBOHYD 506
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P10643"
FT CARBOHYD 509
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P10643"
FT CARBOHYD 696
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P10643"
FT CARBOHYD 754
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 85..96
FT /evidence="ECO:0000250"
FT DISULFID 91..109
FT /evidence="ECO:0000250"
FT DISULFID 103..119
FT /evidence="ECO:0000250"
FT DISULFID 128..165
FT /evidence="ECO:0000250"
FT DISULFID 571..613
FT /evidence="ECO:0000250"
FT DISULFID 599..626
FT /evidence="ECO:0000250"
FT DISULFID 631..673
FT /evidence="ECO:0000250"
FT DISULFID 659..688
FT /evidence="ECO:0000250"
FT DISULFID 702..713
FT /evidence="ECO:0000250"
FT DISULFID 715..750
FT /evidence="ECO:0000250"
FT DISULFID 721..743
FT /evidence="ECO:0000250"
FT DISULFID 728..763
FT /evidence="ECO:0000250"
FT DISULFID 773..782
FT /evidence="ECO:0000250"
FT DISULFID 776..789
FT /evidence="ECO:0000250"
FT DISULFID 791..825
FT /evidence="ECO:0000250"
FT DISULFID 797..818
FT /evidence="ECO:0000250"
FT DISULFID 805..838
FT /evidence="ECO:0000250"
SQ SEQUENCE 843 AA; 93090 MW; 7CCC4B1DA34D6A07 CRC64;
MKAITLLFLV GFIGEFQVFS SASSPINCQW GSYAPWSECN GCTKTQTRRR SIAVYGQYGG
HSCVGSAFET QPCQPTRGCP TEDGCGERFR CFSGQCISKS LVCNGDSDCE EDGADEDRCE
DAESRPACDK DKPPPNIELT GRGYNALTGQ FRNQVLNTKS FGGQCRKVYS GDGRDFYRLS
GNILSYTFQV KINNDFNNEF YNSTWAYVKE TSTEHSSSSK GRFLFFSSSS SSHGYSSNTN
ILTKKKSYQL LVLQNTVEVA QFINNNPEFL QLAESFWKEL SYLPSLYDYS AYRRLIDQYG
THYLQSGSLG GEYKVIFHMD SEKVKKFDFH SEDKRKCASS HFQFLFTSSK QKCTTMEEVL
KSVSENEGNL LRGVPFVRGG HSGFLAGLSY LDLNNPAGNK RRYSQWAGSV PDLPEVIKQK
LTPLYELVKE VPCASVKKLY LKRAIEEYLD EFDPCHCRPC HNGGMATVQG SQCQCYCKPK
TSGVACEQGV LLGDQAGGVD GGWNCWSSWG PCVQGKKTRS RQCNNPSPSA GGKSCIGETS
ETRQCEDEEL EHLRLLEPHC FPLSLVPTKF CSSPPALKDG FVQDEGATFP VGKNIMYTCK
EGYSLVGDPV ARCGEDLQWL VGNMHCQKIA CVLPALMDGI QSHPHKPFYT IGEKVTISCS
GGRSLEGPST FLCSSSLKWS PEVKDVQCVQ REAPLTPKVP KCQPWEKLQN SRCVCKMPYE
CGSSLGVCAR DERSKRILPL TVCKMHVLQC QGRNYTVAGR ESCTLPASAE KACGVCPLWE
KCDAEGSECV CRAASECEEA GFSVCVEVNG REQTMTECEA GVLRCRGLSI SVTGIRPCVA
EAA
