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Complement component C7

 CO7_HUMAN               Reviewed;         843 AA.
P10643; Q6P3T5; Q92489;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
15-MAR-2005, sequence version 2.
05-DEC-2018, entry version 192.
RecName: Full=Complement component C7;
Flags: Precursor;
Name=C7;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND VARIANT
PRO-587.
PubMed=3335508;
Discipio R.G., Chakravari D.N., Mueller-Eberhard H.J., Fey G.H.;
"The structure of human complement component C7 and the C5b-7
complex.";
J. Biol. Chem. 263:549-560(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=PNS;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-822, AND VARIANT THR-389.
PubMed=7730625;
Hobart M.J., Fernie B.A., DiScipio R.G.;
"Structure of the human C7 gene and comparison with the C6, C8A, C8B
and C9 genes.";
J. Immunol. 154:5188-5194(1995).
[4]
GLYCOSYLATION AT TRP-36; TRP-503; TRP-506 AND TRP-509.
PubMed=10551839; DOI=10.1074/jbc.274.46.32786;
Hofsteenge J., Blommers M., Hess D., Furmanek A., Miroshnichenko O.;
"The four terminal components of the complement system are C-
mannosylated on multiple tryptophan residues.";
J. Biol. Chem. 274:32786-32794(1999).
[5]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-202.
TISSUE=Plasma;
PubMed=14760718; DOI=10.1002/pmic.200300556;
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
"Screening for N-glycosylated proteins by liquid chromatography mass
spectrometry.";
Proteomics 4:454-465(2004).
[6]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-202 AND ASN-754.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[7]
GLYCOSYLATION AT ASN-754.
PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
"A strategy for precise and large scale identification of core
fucosylated glycoproteins.";
Mol. Cell. Proteomics 8:913-923(2009).
[8]
GLYCOSYLATION AT THR-696, STRUCTURE OF CARBOHYDRATES, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=22171320; DOI=10.1074/mcp.M111.013649;
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
"Human urinary glycoproteomics; attachment site specific analysis of
N-and O-linked glycosylations by CID and ECD.";
Mol. Cell. Proteomics 11:1-17(2012).
[9]
STRUCTURE BY NMR OF 693-843, AND DISULFIDE BONDS.
PubMed=19419965; DOI=10.1074/jbc.M901993200;
Phelan M.M., Thai C.-T., Soares D.C., Ogata R.T., Barlow P.N.,
Bramham J.;
"Solution structure of factor I-like modules from complement C7
reveals a pair of follistatin domains in compact pseudosymmetric
arrangement.";
J. Biol. Chem. 284:19637-19649(2009).
[10]
VARIANT C7D SER-521.
PubMed=8871666;
Fernie B.A., Wurzner R., Orren A., Morgan B.P., Potter P.C.,
Platonov A.E., Vershinina I.V., Shipulin G.A., Lachmann P.J.,
Hobart M.J.;
"Molecular bases of combined subtotal deficiencies of C6 and C7: their
effects in combination with other C6 and C7 deficiencies.";
J. Immunol. 157:3648-3657(1996).
[11]
VARIANT C7D ARG-379.
PubMed=9218625;
Fernie B.A., Orren A., Sheehan G., Schlesinger M., Hobart M.J.;
"Molecular bases of C7 deficiency: three different defects.";
J. Immunol. 159:1019-1026(1997).
[12]
VARIANTS C7D GLN-220; GLN-682 AND HIS-687.
PubMed=9856499; DOI=10.1007/s004390050859;
Fernie B.A., Hobart M.J.;
"Complement C7 deficiency: seven further molecular defects and their
associated marker haplotypes.";
Hum. Genet. 103:513-519(1998).
[13]
VARIANTS THR-389 AND PRO-587, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=22028381; DOI=10.1093/jmcb/mjr024;
Su Z.D., Sun L., Yu D.X., Li R.X., Li H.X., Yu Z.J., Sheng Q.H.,
Lin X., Zeng R., Wu J.R.;
"Quantitative detection of single amino acid polymorphisms by targeted
proteomics.";
J. Mol. Cell Biol. 3:309-315(2011).
-!- FUNCTION: Constituent of the membrane attack complex (MAC) that
plays a key role in the innate and adaptive immune response by
forming pores in the plasma membrane of target cells. C7 serves as
a membrane anchor.
-!- SUBUNIT: Monomer or dimer; as a C5b-7 complex it can also form
multimeric rosettes. MAC assembly is initiated by proteolytic
cleavage of C5 into C5a and C5b. C5b binds sequentially C6, C7, C8
and multiple copies of the pore-forming subunit C9.
-!- SUBCELLULAR LOCATION: Secreted.
-!- PTM: C7 has 28 disulfide bridges.
-!- PTM: C-, N- and O-glycosylated. O-glycosylated with core 1 or
possibly core 8 glycans. {ECO:0000269|PubMed:10551839,
ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:22171320}.
-!- DISEASE: Complement component 7 deficiency (C7D) [MIM:610102]: A
rare defect of the complement classical pathway associated with
susceptibility to severe recurrent infections, predominantly by
Neisseria gonorrhoeae or Neisseria meningitidis.
{ECO:0000269|PubMed:8871666, ECO:0000269|PubMed:9218625,
ECO:0000269|PubMed:9856499}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the complement C6/C7/C8/C9 family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=C7base; Note=C7 mutation db;
URL="http://structure.bmc.lu.se/idbase/C7base/";
-----------------------------------------------------------------------
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EMBL; J03507; AAA51861.1; -; mRNA.
EMBL; BC063851; AAH63851.1; -; mRNA.
EMBL; X86328; CAA60121.1; -; Genomic_DNA.
EMBL; X86329; CAA60121.1; JOINED; Genomic_DNA.
EMBL; X86330; CAA60121.1; JOINED; Genomic_DNA.
EMBL; X86331; CAA60121.1; JOINED; Genomic_DNA.
EMBL; X86332; CAA60121.1; JOINED; Genomic_DNA.
EMBL; X86333; CAA60121.1; JOINED; Genomic_DNA.
EMBL; X86334; CAA60121.1; JOINED; Genomic_DNA.
EMBL; X86335; CAA60121.1; JOINED; Genomic_DNA.
EMBL; X86336; CAA60121.1; JOINED; Genomic_DNA.
EMBL; X86337; CAA60121.1; JOINED; Genomic_DNA.
EMBL; X86338; CAA60121.1; JOINED; Genomic_DNA.
EMBL; X86339; CAA60121.1; JOINED; Genomic_DNA.
EMBL; X86340; CAA60121.1; JOINED; Genomic_DNA.
EMBL; X86341; CAA60121.1; JOINED; Genomic_DNA.
EMBL; X86342; CAA60121.1; JOINED; Genomic_DNA.
EMBL; X86343; CAA60121.1; JOINED; Genomic_DNA.
EMBL; X86344; CAA60121.1; JOINED; Genomic_DNA.
CCDS; CCDS47201.1; -.
PIR; A27340; A27340.
RefSeq; NP_000578.2; NM_000587.3.
UniGene; Hs.669878; -.
UniGene; Hs.78065; -.
PDB; 2WCY; NMR; -; A=693-843.
PDBsum; 2WCY; -.
ProteinModelPortal; P10643; -.
SMR; P10643; -.
BioGrid; 107191; 4.
IntAct; P10643; 3.
MINT; P10643; -.
STRING; 9606.ENSP00000322061; -.
GlyConnect; 807; -.
iPTMnet; P10643; -.
PhosphoSitePlus; P10643; -.
UniCarbKB; P10643; -.
BioMuta; C7; -.
DMDM; 61252057; -.
PaxDb; P10643; -.
PeptideAtlas; P10643; -.
PRIDE; P10643; -.
ProteomicsDB; 52633; -.
Ensembl; ENST00000313164; ENSP00000322061; ENSG00000112936.
GeneID; 730; -.
KEGG; hsa:730; -.
UCSC; uc003jmh.5; human.
CTD; 730; -.
DisGeNET; 730; -.
EuPathDB; HostDB:ENSG00000112936.18; -.
GeneCards; C7; -.
HGNC; HGNC:1346; C7.
HPA; HPA001465; -.
MalaCards; C7; -.
MIM; 217070; gene.
MIM; 610102; phenotype.
neXtProt; NX_P10643; -.
OpenTargets; ENSG00000112936; -.
Orphanet; 169150; Immunodeficiency due to a late component of complement deficiency.
PharmGKB; PA25941; -.
eggNOG; ENOG410IDXP; Eukaryota.
eggNOG; ENOG410YJ70; LUCA.
GeneTree; ENSGT00940000156804; -.
HOGENOM; HOG000111868; -.
HOVERGEN; HBG005367; -.
InParanoid; P10643; -.
KO; K03996; -.
OMA; YNSSWSY; -.
OrthoDB; EOG091G07LK; -.
PhylomeDB; P10643; -.
TreeFam; TF330498; -.
Reactome; R-HSA-166665; Terminal pathway of complement.
Reactome; R-HSA-977606; Regulation of Complement cascade.
ChiTaRS; C7; human.
EvolutionaryTrace; P10643; -.
GenomeRNAi; 730; -.
PRO; PR:P10643; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000112936; Expressed in 195 organ(s), highest expression level in adrenal cortex.
CleanEx; HS_C7; -.
Genevisible; P10643; HS.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005579; C:membrane attack complex; IDA:UniProtKB.
GO; GO:0006883; P:cellular sodium ion homeostasis; IEA:Ensembl.
GO; GO:0006956; P:complement activation; TAS:ProtInc.
GO; GO:0006957; P:complement activation, alternative pathway; IEA:UniProtKB-KW.
GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
GO; GO:0030449; P:regulation of complement activation; TAS:Reactome.
CDD; cd00033; CCP; 2.
CDD; cd00112; LDLa; 1.
Gene3D; 2.20.100.10; -; 2.
InterPro; IPR037564; Complement_C7.
InterPro; IPR003884; FacI_MAC.
InterPro; IPR023415; LDLR_class-A_CS.
InterPro; IPR002172; LDrepeatLR_classA_rpt.
InterPro; IPR001862; MAC_perforin.
InterPro; IPR020864; MACPF.
InterPro; IPR020863; MACPF_CS.
InterPro; IPR035976; Sushi/SCR/CCP_sf.
InterPro; IPR000436; Sushi_SCR_CCP_dom.
InterPro; IPR000884; TSP1_rpt.
InterPro; IPR036383; TSP1_rpt_sf.
PANTHER; PTHR19325:SF389; PTHR19325:SF389; 1.
Pfam; PF00057; Ldl_recept_a; 1.
Pfam; PF01823; MACPF; 1.
Pfam; PF00084; Sushi; 2.
Pfam; PF00090; TSP_1; 2.
PRINTS; PR00764; COMPLEMENTC9.
SMART; SM00032; CCP; 2.
SMART; SM00057; FIMAC; 2.
SMART; SM00192; LDLa; 1.
SMART; SM00457; MACPF; 1.
SMART; SM00209; TSP1; 2.
SUPFAM; SSF57535; SSF57535; 2.
SUPFAM; SSF82895; SSF82895; 2.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS01209; LDLRA_1; 1.
PROSITE; PS50068; LDLRA_2; 1.
PROSITE; PS00279; MACPF_1; 1.
PROSITE; PS51412; MACPF_2; 1.
PROSITE; PS50923; SUSHI; 2.
PROSITE; PS50092; TSP1; 2.
1: Evidence at protein level;
3D-structure; Complement alternate pathway; Complement pathway;
Complete proteome; Cytolysis; Direct protein sequencing;
Disease mutation; Disulfide bond; EGF-like domain; Glycoprotein;
Immunity; Innate immunity; Membrane attack complex; Polymorphism;
Reference proteome; Repeat; Secreted; Signal; Sushi.
SIGNAL 1 22
CHAIN 23 843 Complement component C7.
/FTId=PRO_0000023583.
DOMAIN 27 80 TSP type-1 1. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 83 121 LDL-receptor class A.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 124 456 MACPF. {ECO:0000255|PROSITE-
ProRule:PRU00745}.
DOMAIN 457 487 EGF-like.
DOMAIN 500 549 TSP type-1 2. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 569 628 Sushi 1. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 629 690 Sushi 2. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
REGION 545 615 CCP 1.
REGION 616 693 CCP 2.
REGION 695 770 Factor I module (FIM) 1.
REGION 771 843 Factor I module (FIM) 2.
CARBOHYD 36 36 C-linked (Man) tryptophan.
{ECO:0000269|PubMed:10551839}.
CARBOHYD 202 202 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:16335952}.
CARBOHYD 503 503 C-linked (Man) tryptophan; partial.
{ECO:0000269|PubMed:10551839}.
CARBOHYD 506 506 C-linked (Man) tryptophan; partial.
{ECO:0000269|PubMed:10551839}.
CARBOHYD 509 509 C-linked (Man) tryptophan; partial.
{ECO:0000269|PubMed:10551839}.
CARBOHYD 696 696 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:22171320}.
CARBOHYD 754 754 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19139490}.
DISULFID 85 96 {ECO:0000250}.
DISULFID 91 109 {ECO:0000250}.
DISULFID 103 119 {ECO:0000250}.
DISULFID 128 165 {ECO:0000250}.
DISULFID 337 353 {ECO:0000269|PubMed:19419965}.
DISULFID 571 613 {ECO:0000250}.
DISULFID 599 626 {ECO:0000250}.
DISULFID 631 673 {ECO:0000250}.
DISULFID 659 688 {ECO:0000250}.
DISULFID 702 713 {ECO:0000269|PubMed:19419965}.
DISULFID 715 750 {ECO:0000269|PubMed:19419965}.
DISULFID 721 743 {ECO:0000269|PubMed:19419965}.
DISULFID 728 763 {ECO:0000269|PubMed:19419965}.
DISULFID 773 782 {ECO:0000269|PubMed:19419965}.
DISULFID 776 789 {ECO:0000269|PubMed:19419965}.
DISULFID 791 825 {ECO:0000269|PubMed:19419965}.
DISULFID 797 818 {ECO:0000269|PubMed:19419965}.
DISULFID 805 838 {ECO:0000269|PubMed:19419965}.
VARIANT 128 128 C -> R (in dbSNP:rs2271708).
/FTId=VAR_050480.
VARIANT 220 220 R -> Q (in C7D; dbSNP:rs369349760).
{ECO:0000269|PubMed:9856499}.
/FTId=VAR_012643.
VARIANT 379 379 G -> R (in C7D; dbSNP:rs121964921).
{ECO:0000269|PubMed:9218625}.
/FTId=VAR_012644.
VARIANT 389 389 S -> T (polymorphism; confirmed at
protein level; dbSNP:rs1063499).
{ECO:0000269|PubMed:22028381,
ECO:0000269|PubMed:7730625}.
/FTId=VAR_033798.
VARIANT 420 420 K -> Q (in dbSNP:rs3792646).
/FTId=VAR_022023.
VARIANT 521 521 R -> S (in C7D; dbSNP:rs121964920).
{ECO:0000269|PubMed:8871666}.
/FTId=VAR_012645.
VARIANT 587 587 T -> P (polymorphism; confirmed at
protein level; dbSNP:rs13157656).
{ECO:0000269|PubMed:22028381,
ECO:0000269|PubMed:3335508}.
/FTId=VAR_033799.
VARIANT 682 682 E -> Q (in C7D; dbSNP:rs541873000).
{ECO:0000269|PubMed:9856499}.
/FTId=VAR_012646.
VARIANT 687 687 R -> H (in C7D; dbSNP:rs113187203).
{ECO:0000269|PubMed:9856499}.
/FTId=VAR_012647.
CONFLICT 152 152 R -> V (in Ref. 3; CAA60121).
{ECO:0000305}.
CONFLICT 821 822 GA -> AL (in Ref. 3). {ECO:0000305}.
STRAND 706 709 {ECO:0000244|PDB:2WCY}.
STRAND 712 715 {ECO:0000244|PDB:2WCY}.
HELIX 718 720 {ECO:0000244|PDB:2WCY}.
STRAND 726 731 {ECO:0000244|PDB:2WCY}.
TURN 732 734 {ECO:0000244|PDB:2WCY}.
STRAND 737 741 {ECO:0000244|PDB:2WCY}.
HELIX 742 750 {ECO:0000244|PDB:2WCY}.
STRAND 755 757 {ECO:0000244|PDB:2WCY}.
STRAND 766 769 {ECO:0000244|PDB:2WCY}.
STRAND 778 782 {ECO:0000244|PDB:2WCY}.
STRAND 784 791 {ECO:0000244|PDB:2WCY}.
HELIX 794 796 {ECO:0000244|PDB:2WCY}.
STRAND 803 808 {ECO:0000244|PDB:2WCY}.
STRAND 811 816 {ECO:0000244|PDB:2WCY}.
HELIX 817 826 {ECO:0000244|PDB:2WCY}.
STRAND 831 836 {ECO:0000244|PDB:2WCY}.
SEQUENCE 843 AA; 93518 MW; DBD5D7C92DF71FA5 CRC64;
MKVISLFILV GFIGEFQSFS SASSPVNCQW DFYAPWSECN GCTKTQTRRR SVAVYGQYGG
QPCVGNAFET QSCEPTRGCP TEEGCGERFR CFSGQCISKS LVCNGDSDCD EDSADEDRCE
DSERRPSCDI DKPPPNIELT GNGYNELTGQ FRNRVINTKS FGGQCRKVFS GDGKDFYRLS
GNVLSYTFQV KINNDFNYEF YNSTWSYVKH TSTEHTSSSR KRSFFRSSSS SSRSYTSHTN
EIHKGKSYQL LVVENTVEVA QFINNNPEFL QLAEPFWKEL SHLPSLYDYS AYRRLIDQYG
THYLQSGSLG GEYRVLFYVD SEKLKQNDFN SVEEKKCKSS GWHFVVKFSS HGCKELENAL
KAASGTQNNV LRGEPFIRGG GAGFISGLSY LELDNPAGNK RRYSAWAESV TNLPQVIKQK
LTPLYELVKE VPCASVKKLY LKWALEEYLD EFDPCHCRPC QNGGLATVEG THCLCHCKPY
TFGAACEQGV LVGNQAGGVD GGWSCWSSWS PCVQGKKTRS RECNNPPPSG GGRSCVGETT
ESTQCEDEEL EHLRLLEPHC FPLSLVPTEF CPSPPALKDG FVQDEGTMFP VGKNVVYTCN
EGYSLIGNPV ARCGEDLRWL VGEMHCQKIA CVLPVLMDGI QSHPQKPFYT VGEKVTVSCS
GGMSLEGPSA FLCGSSLKWS PEMKNARCVQ KENPLTQAVP KCQRWEKLQN SRCVCKMPYE
CGPSLDVCAQ DERSKRILPL TVCKMHVLHC QGRNYTLTGR DSCTLPASAE KACGACPLWG
KCDAESSKCV CREASECEEE GFSICVEVNG KEQTMSECEA GALRCRGQSI SVTSIRPCAA
ETQ


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