CO7_PIG
ID CO7_PIG Reviewed; 843 AA.
AC Q9TUQ3;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Complement component C7;
DE Flags: Precursor;
GN Name=C7;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 640-651, FUNCTION,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Lung;
RX PubMed=10878384; DOI=10.4049/jimmunol.165.2.1059;
RA Agah A., Montalto M.C., Kiesecker C.L., Morrissey M., Grover M.,
RA Whoolery K.L., Rother R.P., Stahl G.L.;
RT "Isolation, characterization, and cloning of porcine complement component
RT C7.";
RL J. Immunol. 165:1059-1065(2000).
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.
CC {ECO:0000269|PubMed:10878384}.
CC -!- SUBUNIT: Monomer or dimer; as a C5b-7 complex it can also form
CC multimeric rosettes. MAC assembly is initiated by proteolytic cleavage
CC of C5 into C5a and C5b. C5b binds sequentially C6, C7, C8 and multiple
CC copies of the pore-forming subunit C9 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10878384}.
CC -!- TISSUE SPECIFICITY: Detected in plasma (at protein level). Bone marrow,
CC heart, intestine, lung, spleen, kidney, liver and thymus.
CC {ECO:0000269|PubMed:10878384}.
CC -!- PTM: C7 has 28 disulfide bridges. {ECO:0000250}.
CC -!- PTM: C- and N-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; AF162274; AAD45918.1; -; mRNA.
DR RefSeq; NP_999447.1; NM_214282.1.
DR AlphaFoldDB; Q9TUQ3; -.
DR SMR; Q9TUQ3; -.
DR STRING; 9823.ENSSSCP00000017865; -.
DR PaxDb; Q9TUQ3; -.
DR PeptideAtlas; Q9TUQ3; -.
DR PRIDE; Q9TUQ3; -.
DR GeneID; 397526; -.
DR KEGG; ssc:397526; -.
DR CTD; 730; -.
DR eggNOG; ENOG502QU3G; Eukaryota.
DR InParanoid; Q9TUQ3; -.
DR OrthoDB; 100680at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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 1: Evidence at protein level;
KW Complement alternate pathway; Complement pathway; Cytolysis;
KW Direct protein sequencing; Disulfide bond; EGF-like domain; Glycoprotein;
KW Immunity; Innate immunity; Membrane attack complex; Reference proteome;
KW Repeat; Secreted; Signal; Sushi.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..843
FT /note="Complement component C7"
FT /id="PRO_0000023584"
FT DOMAIN 27..80
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 83..121
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 105..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..539
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 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 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 337..353
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; 93062 MW; 0B703D93C3E5C83D CRC64;
MKAMSLVFLV GLIGEFQVFS SASSPVNCQW DSYAPWSECN GCTKTQTRRR PVAVYGQYGG
HPCVGSTFET QSCEPTRGCP TEEGCGERFR CFSGQCISKS LVCNGDSDCE EDSADEDRCE
DSESRPSCDL SKPPPNIELT GNGYNALTGQ FRNRVLNTKS FGGQCRKVFS GDGRDFYRLS
GNVLSYTFQV KVNNDFNYEF YNSTWSYAKH TSTEHTSSSK GRVFIFSSSS SSSSYYAKTY
EILKKKSYQL LVVQNTVEVA QFINNNPEFL QLAESFWKEL SYLPPLYDYS AYRRLIDQYG
THYLQSGSLG GEYKVLFYVD SEKVAESDLG SEDKKKCASS HISFLFKSSK HKCKAMEEAL
KSASGTQSNV LRGVPFVRGG RPGFVSGLSY LELDNPDGNK QRYSSWAGSV TDLPQVIKQK
LTPLYELVKE VPCASVKRLY LKRALEEYLD EFDSCHCQPC QNGGMASVEG TQCQCHCKPN
TFGVACEQGV LVGDHAGGID GGWSCWSSWG PCAQGKKTRS RKCNNPPPSG GGKSCIGETS
ESRQCEDEDL EHLRLLEPHC FPLSLVPTEF CPSPPALKDG FVQNEETTFP VGKNIVYSCN
EGYSLVGDPV ARCGEDLQWT VGKMHCQKIA CVLPTLMRGL QSHPQKPFYT VGEKVTFSCS
SGMSLEGPST FLCGSSLKWS PEMKNVQCVR KEAPLAKKVP ECQLWEKLQN SKCVCKMPYE
CGSSLDVCAR DERSKRILRL TVCKMHVLQC QGRNYTLSVG ETCTLPGSAE KACGACPLWE
KCDAQSSKCV CRAASECEEA GFRVCVEVNG REQTMTECEA GVLRCLGLSI TVTSIRPCAP
EAP
