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Complement C5 (Hemolytic complement) [Cleaved into: Complement C5 beta chain; Complement C5 alpha chain; C5a anaphylatoxin; Complement C5 alpha' chain]

 CO5_MOUSE               Reviewed;        1680 AA.
P06684; A2AS36;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-NOV-1990, sequence version 2.
20-JUN-2018, entry version 169.
RecName: Full=Complement C5;
AltName: Full=Hemolytic complement;
Contains:
RecName: Full=Complement C5 beta chain;
Contains:
RecName: Full=Complement C5 alpha chain;
Contains:
RecName: Full=C5a anaphylatoxin;
Contains:
RecName: Full=Complement C5 alpha' chain;
Flags: Precursor;
Name=C5; Synonyms=Hc;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND INVOLVEMENT IN C5 DEFICIENCY.
PubMed=2303408;
Wetsel R.A., Fleischer D.T., Haviland D.L.;
"Deficiency of the murine fifth complement component (C5). A 2-base
pair gene deletion in a 5'-exon.";
J. Biol. Chem. 265:2435-2440(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 41-1680.
PubMed=2436653; DOI=10.1021/bi00377a013;
Wetsel R.A., Ogata R.T., Tack B.F.;
"Primary structure of the fifth component of murine complement.";
Biochemistry 26:737-743(1987).
[4]
GENE STRUCTURE.
PubMed=1711041;
Haviland D.L., Haviland J.C., Fleischer D.T., Wetsel R.A.;
"Structure of the murine fifth complement component (C5) gene. A
large, highly interrupted gene with a variant donor splice site and
organizational homology with the third and fourth complement component
genes.";
J. Biol. Chem. 266:11818-11825(1991).
[5]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-427.
STRAIN=C57BL/6J; TISSUE=Plasma;
PubMed=16944957; DOI=10.1021/pr060186m;
Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,
Gevaert K.;
"Proteome-wide characterization of N-glycosylation events by diagonal
chromatography.";
J. Proteome Res. 5:2438-2447(2006).
[6]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-427.
STRAIN=C57BL/6J; TISSUE=Plasma;
PubMed=17330941; DOI=10.1021/pr0604559;
Bernhard O.K., Kapp E.A., Simpson R.J.;
"Enhanced analysis of the mouse plasma proteome using cysteine-
containing tryptic glycopeptides.";
J. Proteome Res. 6:987-995(2007).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Activation of C5 by a C5 convertase initiates the
spontaneous assembly of the late complement components, C5-C9,
into the membrane attack complex. C5b has a transient binding site
for C6. The C5b-C6 complex is the foundation upon which the lytic
complex is assembled.
-!- FUNCTION: Derived from proteolytic degradation of complement C5,
C5 anaphylatoxin is a mediator of local inflammatory process.
Binding to the receptor C5AR1 induces a variety of responses
including intracellular calcium release, contraction of smooth
muscle, increased vascular permeability, and histamine release
from mast cells and basophilic leukocytes. C5a is also a potent
chemokine which stimulates the locomotion of polymorphonuclear
leukocytes and directs their migration toward sites of
inflammation. {ECO:0000250|UniProtKB:P01031}.
-!- SUBUNIT: C5 precursor is first processed by the removal of 4 basic
residues, forming two chains, beta and alpha, linked by a
disulfide bond. C5 convertase activates C5 by cleaving the alpha
chain, releasing C5a anaphylatoxin and generating C5b (beta chain
+ alpha' chain). The C5a anaphylatoxin interacts with C5AR1.
{ECO:0000250|UniProtKB:P01031}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- DISEASE: Note=Murine C5 deficiency is caused by a 2 base-pairs
deletion resulting in frameshift and premature truncation. All C5-
deficient strains contain this mutation.
{ECO:0000269|PubMed:2303408}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M35525; AAA37349.1; -; mRNA.
EMBL; M35526; AAA37348.1; -; mRNA.
EMBL; AL845534; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PIR; A35530; C5MS.
RefSeq; NP_034536.2; NM_010406.2.
UniGene; Mm.2168; -.
PDB; 4P3A; X-ray; 1.40 A; A/B/C/D=679-755.
PDB; 4P3B; X-ray; 2.10 A; A/B/C/D=679-754.
PDB; 4WB2; X-ray; 1.80 A; A/B/C=679-755.
PDB; 4WB3; X-ray; 2.00 A; A/B/C=679-754.
PDBsum; 4P3A; -.
PDBsum; 4P3B; -.
PDBsum; 4WB2; -.
PDBsum; 4WB3; -.
ProteinModelPortal; P06684; -.
SMR; P06684; -.
BioGrid; 200226; 1.
CORUM; P06684; -.
IntAct; P06684; 3.
STRING; 10090.ENSMUSP00000028233; -.
MEROPS; I39.952; -.
iPTMnet; P06684; -.
PhosphoSitePlus; P06684; -.
MaxQB; P06684; -.
PaxDb; P06684; -.
PeptideAtlas; P06684; -.
PRIDE; P06684; -.
Ensembl; ENSMUST00000028233; ENSMUSP00000028233; ENSMUSG00000026874.
GeneID; 15139; -.
KEGG; mmu:15139; -.
UCSC; uc008jjn.2; mouse.
CTD; 15139; -.
MGI; MGI:96031; Hc.
eggNOG; KOG1366; Eukaryota.
eggNOG; ENOG410XRED; LUCA.
GeneTree; ENSGT00760000118982; -.
HOGENOM; HOG000231860; -.
HOVERGEN; HBG098067; -.
InParanoid; P06684; -.
KO; K03994; -.
OMA; YYIVTGE; -.
OrthoDB; EOG091G00BU; -.
PhylomeDB; P06684; -.
TreeFam; TF313285; -.
Reactome; R-MMU-166665; Terminal pathway of complement.
Reactome; R-MMU-174577; Activation of C3 and C5.
Reactome; R-MMU-375276; Peptide ligand-binding receptors.
Reactome; R-MMU-418594; G alpha (i) signalling events.
Reactome; R-MMU-977606; Regulation of Complement cascade.
PRO; PR:P06684; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000026874; -.
CleanEx; MM_HC; -.
ExpressionAtlas; P06684; baseline and differential.
Genevisible; P06684; MM.
GO; GO:0005615; C:extracellular space; IEA:InterPro.
GO; GO:0005579; C:membrane attack complex; ISO:MGI.
GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
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:0001701; P:in utero embryonic development; IGI:MGI.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0010760; P:negative regulation of macrophage chemotaxis; ISO:MGI.
GO; GO:0045766; P:positive regulation of angiogenesis; IMP:BHF-UCL.
GO; GO:0090197; P:positive regulation of chemokine secretion; ISO:MGI.
GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; ISO:MGI.
Gene3D; 2.60.40.10; -; 2.
Gene3D; 2.60.40.690; -; 1.
InterPro; IPR009048; A-macroglobulin_rcpt-bd.
InterPro; IPR036595; A-macroglobulin_rcpt-bd_sf.
InterPro; IPR011626; A2M_comp.
InterPro; IPR002890; A2M_N.
InterPro; IPR011625; A2M_N_2.
InterPro; IPR000020; Anaphylatoxin/fibulin.
InterPro; IPR018081; Anaphylatoxin_comp_syst.
InterPro; IPR037562; Complement_C5.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR001599; Macroglobln_a2.
InterPro; IPR001134; Netrin_domain.
InterPro; IPR018933; Netrin_module_non-TIMP.
InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
InterPro; IPR008993; TIMP-like_OB-fold.
PANTHER; PTHR11412:SF83; PTHR11412:SF83; 1.
Pfam; PF00207; A2M; 1.
Pfam; PF07678; A2M_comp; 1.
Pfam; PF01835; A2M_N; 1.
Pfam; PF07703; A2M_N_2; 1.
Pfam; PF07677; A2M_recep; 1.
Pfam; PF01821; ANATO; 1.
Pfam; PF01759; NTR; 1.
SMART; SM01360; A2M; 1.
SMART; SM01359; A2M_N_2; 1.
SMART; SM01361; A2M_recep; 1.
SMART; SM00104; ANATO; 1.
SMART; SM00643; C345C; 1.
SUPFAM; SSF47686; SSF47686; 1.
SUPFAM; SSF48239; SSF48239; 1.
SUPFAM; SSF49410; SSF49410; 1.
SUPFAM; SSF50242; SSF50242; 1.
PROSITE; PS01177; ANAPHYLATOXIN_1; 1.
PROSITE; PS01178; ANAPHYLATOXIN_2; 1.
PROSITE; PS50189; NTR; 1.
1: Evidence at protein level;
3D-structure; Cleavage on pair of basic residues;
Complement alternate pathway; Complement pathway; Complete proteome;
Cytolysis; Disulfide bond; Glycoprotein; Immunity;
Inflammatory response; Innate immunity; Membrane attack complex;
Reference proteome; Secreted; Signal.
SIGNAL 1 18
CHAIN 19 674 Complement C5 beta chain.
/FTId=PRO_0000005991.
PROPEP 675 678
/FTId=PRO_0000005992.
CHAIN 679 1680 Complement C5 alpha chain.
/FTId=PRO_0000005993.
CHAIN 679 755 C5a anaphylatoxin.
/FTId=PRO_0000005994.
CHAIN 756 1680 Complement C5 alpha' chain.
/FTId=PRO_0000005995.
DOMAIN 702 736 Anaphylatoxin-like. {ECO:0000255|PROSITE-
ProRule:PRU00022}.
DOMAIN 1536 1679 NTR. {ECO:0000255|PROSITE-
ProRule:PRU00295}.
REGION 696 725 Involved in C5AR1 binding.
{ECO:0000250|UniProtKB:P01031}.
CARBOHYD 427 427 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16944957,
ECO:0000269|PubMed:17330941}.
CARBOHYD 915 915 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1119 1119 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1633 1633 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 702 728 {ECO:0000250}.
DISULFID 703 735 {ECO:0000250}.
DISULFID 715 736 {ECO:0000250}.
DISULFID 1536 1609 {ECO:0000250}.
DISULFID 1557 1679 {ECO:0000250}.
HELIX 680 691 {ECO:0000244|PDB:4P3A}.
STRAND 694 696 {ECO:0000244|PDB:4P3A}.
HELIX 697 707 {ECO:0000244|PDB:4P3A}.
STRAND 711 713 {ECO:0000244|PDB:4WB2}.
HELIX 715 719 {ECO:0000244|PDB:4P3A}.
HELIX 726 744 {ECO:0000244|PDB:4P3A}.
SEQUENCE 1680 AA; 188878 MW; 81EB5A16FAC7D95C CRC64;
MGLWGILCLL IFLDKTWGQE QTYVISAPKI LRVGSSENVV IQVHGYTEAF DATLSLKSYP
DKKVTFSSGY VNLSPENKFQ NAALLTLQPN QVPREESPVS HVYLEVVSKH FSKSKKIPIT
YNNGILFIHT DKPVYTPDQS VKIRVYSLGD DLKPAKRETV LTFIDPEGSE VDIVEENDYT
GIISFPDFKI PSNPKYGVWT IKANYKKDFT TTGTAYFEIK EYVLPRFSVS IELERTFIGY
KNFKNFEITV KARYFYNKVV PDAEVYAFFG LREDIKDEEK QMMHKATQAA KLVDGVAQIS
FDSETAVKEL SYNSLEDLNN KYLYIAVTVT ESSGGFSEEA EIPGVKYVLS PYTLNLVATP
LFVKPGIPFS IKAQVKDSLE QAVGGVPVTL MAQTVDVNQE TSDLETKRSI THDTDGVAVF
VLNLPSNVTV LKFEIRTDDP ELPEENQASK EYEAVAYSSL SQSYIYIAWT ENYKPMLVGE
YLNIMVTPKS PYIDKITHYN YLILSKGKIV QYGTREKLFS STYQNINIPV TQNMVPSARL
LVYYIVTGEQ TAELVADAVW INIEEKCGNQ LQVHLSPDEY VYSPGQTVSL DMVTEADSWV
ALSAVDRAVY KVQGNAKRAM QRVFQALDEK SDLGCGAGGG HDNADVFHLA GLTFLTNANA
DDSHYRDDSC KEILRSKRNL HLLRQKIEEQ AAKYKHSVPK KCCYDGARVN FYETCEERVA
RVTIGPLCIR AFNECCTIAN KIRKESPHKP VQLGRIHIKT LLPVMKADIR SYFPESWLWE
IHRVPKRKQL QVTLPDSLTT WEIQGIGISD NGICVADTLK AKVFKEVFLE MNIPYSVVRG
EQIQLKGTVY NYMTSGTKFC VKMSAVEGIC TSGSSAASLH TSRPSRCVFQ RIEGSSSHLV
TFTLLPLEIG LHSINFSLET SFGKDILVKT LRVVPEGVKR ESYAGVILDP KGIRGIVNRR
KEFPYRIPLD LVPKTKVERI LSVKGLLVGE FLSTVLSKEG INILTHLPKG SAEAELMSIA
PVFYVFHYLE AGNHWNIFYP DTLSKRQSLE KKIKQGVVSV MSYRNADYSY SMWKGASAST
WLTAFALRVL GQVAKYVKQD ENSICNSLLW LVEKCQLENG SFKENSQYLP IKLQGTLPAE
AQEKTLYLTA FSVIGIRKAV DICPTMKIHT ALDKADSFLL ENTLPSKSTF TLAIVAYALS
LGDRTHPRFR LIVSALRKEA FVKGDPPIYR YWRDTLKRPD SSVPSSGTAG MVETTAYALL
ASLKLKDMNY ANPIIKWLSE EQRYGGGFYS TQDTINAIEG LTEYSLLLKQ IHLDMDINVA
YKHEGDFHKY KVTEKHFLGR PVEVSLNDDL VVSTGYSSGL ATVYVKTVVH KISVSEEFCS
FYLKIDTQDI EASSHFRLSD SGFKRIIACA SYKPSKEEST SGSSHAVMDI SLPTGIGANE
EDLRALVEGV DQLLTDYQIK DGHVILQLNS IPSRDFLCVR FRIFELFQVG FLNPATFTVY
EYHRPDKQCT MIYSISDTRL QKVCEGAACT CVEADCAQLQ AEVDLAISAD SRKEKACKPE
TAYAYKVRIT SATEENVFVK YTATLLVTYK TGEAADENSE VTFIKKMSCT NANLVKGKQY
LIMGKEVLQI KHNFSFKYIY PLDSSTWIEY WPTDTTCPSC QAFVENLNNF AEDLFLNSCE


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