UniProtKB - P06684 (CO5_MOUSE)
Protein
Complement C5
Gene
C5
Organism
Mus musculus (Mouse)
Status
Functioni
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.
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.By similarity
GO - Molecular functioni
- endopeptidase inhibitor activity Source: InterPro
GO - Biological processi
- complement activation, alternative pathway Source: UniProtKB-KW
- complement activation, classical pathway Source: UniProtKB-KW
- cytolysis Source: UniProtKB-KW
- inflammatory response Source: UniProtKB-KW
- in utero embryonic development Source: MGI
- negative regulation of macrophage chemotaxis Source: MGI
- positive regulation of angiogenesis Source: BHF-UCL
- positive regulation of chemokine secretion Source: MGI
- positive regulation of vascular endothelial growth factor production Source: MGI
Keywordsi
Biological process | Complement alternate pathway, Complement pathway, Cytolysis, Immunity, Inflammatory response, Innate immunity |
Enzyme and pathway databases
Reactomei | R-MMU-166665, Terminal pathway of complement R-MMU-174577, Activation of C3 and C5 R-MMU-375276, Peptide ligand-binding receptors R-MMU-418594, G alpha (i) signalling events R-MMU-977606, Regulation of Complement cascade |
Protein family/group databases
MEROPSi | I39.952 |
Names & Taxonomyi
Protein namesi | Recommended name: Complement C5Alternative name(s): Hemolytic complement Cleaved into the following 4 chains: |
Gene namesi | Name:C5 Synonyms:Hc |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:96031, Hc |
Subcellular locationi
Extracellular region or secreted
Extracellular region or secreted
- extracellular space Source: InterPro
Plasma Membrane
- membrane attack complex Source: MGI
Keywords - Cellular componenti
Membrane attack complex, SecretedPathology & Biotechi
Involvement in diseasei
Murine C5 deficiency is caused by a 2 base-pairs deletion resulting in frameshift and premature truncation. All C5-deficient strains contain this mutation.1 Publication
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 18 | Add BLAST | 18 | |
ChainiPRO_0000005991 | 19 – 674 | Complement C5 beta chainAdd BLAST | 656 | |
PropeptideiPRO_0000005992 | 675 – 678 | 4 | ||
ChainiPRO_0000005993 | 679 – 1680 | Complement C5 alpha chainAdd BLAST | 1002 | |
ChainiPRO_0000005994 | 679 – 755 | C5a anaphylatoxinAdd BLAST | 77 | |
ChainiPRO_0000005995 | 756 – 1680 | Complement C5 alpha' chainAdd BLAST | 925 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 427 | N-linked (GlcNAc...) asparagine2 Publications | 1 | |
Disulfide bondi | 702 ↔ 728 | By similarity | ||
Disulfide bondi | 703 ↔ 735 | By similarity | ||
Disulfide bondi | 715 ↔ 736 | By similarity | ||
Glycosylationi | 915 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1119 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1536 ↔ 1609 | By similarity | ||
Disulfide bondi | 1557 ↔ 1679 | By similarity | ||
Glycosylationi | 1633 | N-linked (GlcNAc...) asparagineSequence analysis | 1 |
Keywords - PTMi
Cleavage on pair of basic residues, Disulfide bond, GlycoproteinProteomic databases
CPTACi | non-CPTAC-3698 non-CPTAC-4025 |
MaxQBi | P06684 |
PaxDbi | P06684 |
PeptideAtlasi | P06684 |
PRIDEi | P06684 |
PTM databases
GlyGeni | P06684, 4 sites |
iPTMneti | P06684 |
PhosphoSitePlusi | P06684 |
Expressioni
Gene expression databases
Bgeei | ENSMUSG00000026874, Expressed in lung and 97 other tissues |
ExpressionAtlasi | P06684, baseline and differential |
Genevisiblei | P06684, MM |
Interactioni
Subunit structurei
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.
By similarityProtein-protein interaction databases
BioGRIDi | 200226, 4 interactors |
IntActi | P06684, 3 interactors |
STRINGi | 10090.ENSMUSP00000028233 |
Miscellaneous databases
RNActi | P06684, protein |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P06684 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 702 – 736 | Anaphylatoxin-likePROSITE-ProRule annotationAdd BLAST | 35 | |
Domaini | 1536 – 1679 | NTRPROSITE-ProRule annotationAdd BLAST | 144 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 696 – 725 | Involved in C5AR1 bindingBy similarityAdd BLAST | 30 |
Keywords - Domaini
SignalPhylogenomic databases
eggNOGi | KOG1366, Eukaryota |
GeneTreei | ENSGT00940000155670 |
HOGENOMi | CLU_001634_4_2_1 |
InParanoidi | P06684 |
OMAi | LTWIEYW |
OrthoDBi | 20179at2759 |
PhylomeDBi | P06684 |
TreeFami | TF313285 |
Family and domain databases
CDDi | cd00017, ANATO, 1 hit |
Gene3Di | 2.40.50.120, 1 hit 2.60.40.10, 2 hits 2.60.40.690, 1 hit |
InterProi | View protein in InterPro IPR009048, A-macroglobulin_rcpt-bd IPR036595, A-macroglobulin_rcpt-bd_sf IPR011625, A2M_N_BRD IPR011626, Alpha-macroglobulin_TED IPR000020, Anaphylatoxin/fibulin IPR018081, Anaphylatoxin_comp_syst IPR041425, C3/4/5_MG1 IPR037562, Complement_C5 IPR013783, Ig-like_fold IPR001599, Macroglobln_a2 IPR002890, MG2 IPR041555, MG3 IPR040839, MG4 IPR001134, Netrin_domain IPR018933, Netrin_module_non-TIMP IPR008930, Terpenoid_cyclase/PrenylTrfase IPR008993, TIMP-like_OB-fold |
PANTHERi | PTHR11412:SF83, PTHR11412:SF83, 1 hit |
Pfami | View protein in Pfam PF00207, A2M, 1 hit PF07703, A2M_BRD, 1 hit PF07677, A2M_recep, 1 hit PF01821, ANATO, 1 hit PF17790, MG1, 1 hit PF01835, MG2, 1 hit PF17791, MG3, 1 hit PF17789, MG4, 1 hit PF01759, NTR, 1 hit PF07678, TED_complement, 1 hit |
SMARTi | View protein in SMART SM01360, A2M, 1 hit SM01359, A2M_N_2, 1 hit SM01361, A2M_recep, 1 hit SM00104, ANATO, 1 hit SM00643, C345C, 1 hit |
SUPFAMi | SSF47686, SSF47686, 1 hit SSF48239, SSF48239, 1 hit SSF49410, SSF49410, 1 hit SSF50242, SSF50242, 1 hit |
PROSITEi | View protein in PROSITE PS01177, ANAPHYLATOXIN_1, 1 hit PS01178, ANAPHYLATOXIN_2, 1 hit PS50189, NTR, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All
P06684-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MGLWGILCLL IFLDKTWGQE QTYVISAPKI LRVGSSENVV IQVHGYTEAF
60 70 80 90 100
DATLSLKSYP DKKVTFSSGY VNLSPENKFQ NAALLTLQPN QVPREESPVS
110 120 130 140 150
HVYLEVVSKH FSKSKKIPIT YNNGILFIHT DKPVYTPDQS VKIRVYSLGD
160 170 180 190 200
DLKPAKRETV LTFIDPEGSE VDIVEENDYT GIISFPDFKI PSNPKYGVWT
210 220 230 240 250
IKANYKKDFT TTGTAYFEIK EYVLPRFSVS IELERTFIGY KNFKNFEITV
260 270 280 290 300
KARYFYNKVV PDAEVYAFFG LREDIKDEEK QMMHKATQAA KLVDGVAQIS
310 320 330 340 350
FDSETAVKEL SYNSLEDLNN KYLYIAVTVT ESSGGFSEEA EIPGVKYVLS
360 370 380 390 400
PYTLNLVATP LFVKPGIPFS IKAQVKDSLE QAVGGVPVTL MAQTVDVNQE
410 420 430 440 450
TSDLETKRSI THDTDGVAVF VLNLPSNVTV LKFEIRTDDP ELPEENQASK
460 470 480 490 500
EYEAVAYSSL SQSYIYIAWT ENYKPMLVGE YLNIMVTPKS PYIDKITHYN
510 520 530 540 550
YLILSKGKIV QYGTREKLFS STYQNINIPV TQNMVPSARL LVYYIVTGEQ
560 570 580 590 600
TAELVADAVW INIEEKCGNQ LQVHLSPDEY VYSPGQTVSL DMVTEADSWV
610 620 630 640 650
ALSAVDRAVY KVQGNAKRAM QRVFQALDEK SDLGCGAGGG HDNADVFHLA
660 670 680 690 700
GLTFLTNANA DDSHYRDDSC KEILRSKRNL HLLRQKIEEQ AAKYKHSVPK
710 720 730 740 750
KCCYDGARVN FYETCEERVA RVTIGPLCIR AFNECCTIAN KIRKESPHKP
760 770 780 790 800
VQLGRIHIKT LLPVMKADIR SYFPESWLWE IHRVPKRKQL QVTLPDSLTT
810 820 830 840 850
WEIQGIGISD NGICVADTLK AKVFKEVFLE MNIPYSVVRG EQIQLKGTVY
860 870 880 890 900
NYMTSGTKFC VKMSAVEGIC TSGSSAASLH TSRPSRCVFQ RIEGSSSHLV
910 920 930 940 950
TFTLLPLEIG LHSINFSLET SFGKDILVKT LRVVPEGVKR ESYAGVILDP
960 970 980 990 1000
KGIRGIVNRR KEFPYRIPLD LVPKTKVERI LSVKGLLVGE FLSTVLSKEG
1010 1020 1030 1040 1050
INILTHLPKG SAEAELMSIA PVFYVFHYLE AGNHWNIFYP DTLSKRQSLE
1060 1070 1080 1090 1100
KKIKQGVVSV MSYRNADYSY SMWKGASAST WLTAFALRVL GQVAKYVKQD
1110 1120 1130 1140 1150
ENSICNSLLW LVEKCQLENG SFKENSQYLP IKLQGTLPAE AQEKTLYLTA
1160 1170 1180 1190 1200
FSVIGIRKAV DICPTMKIHT ALDKADSFLL ENTLPSKSTF TLAIVAYALS
1210 1220 1230 1240 1250
LGDRTHPRFR LIVSALRKEA FVKGDPPIYR YWRDTLKRPD SSVPSSGTAG
1260 1270 1280 1290 1300
MVETTAYALL ASLKLKDMNY ANPIIKWLSE EQRYGGGFYS TQDTINAIEG
1310 1320 1330 1340 1350
LTEYSLLLKQ IHLDMDINVA YKHEGDFHKY KVTEKHFLGR PVEVSLNDDL
1360 1370 1380 1390 1400
VVSTGYSSGL ATVYVKTVVH KISVSEEFCS FYLKIDTQDI EASSHFRLSD
1410 1420 1430 1440 1450
SGFKRIIACA SYKPSKEEST SGSSHAVMDI SLPTGIGANE EDLRALVEGV
1460 1470 1480 1490 1500
DQLLTDYQIK DGHVILQLNS IPSRDFLCVR FRIFELFQVG FLNPATFTVY
1510 1520 1530 1540 1550
EYHRPDKQCT MIYSISDTRL QKVCEGAACT CVEADCAQLQ AEVDLAISAD
1560 1570 1580 1590 1600
SRKEKACKPE TAYAYKVRIT SATEENVFVK YTATLLVTYK TGEAADENSE
1610 1620 1630 1640 1650
VTFIKKMSCT NANLVKGKQY LIMGKEVLQI KHNFSFKYIY PLDSSTWIEY
1660 1670 1680
WPTDTTCPSC QAFVENLNNF AEDLFLNSCE
Computationally mapped potential isoform sequencesi
There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basketA0A0J9YUU3 | A0A0J9YUU3_MOUSE | Hemolytic complement | Hc | 193 | Annotation score: |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M35525 mRNA Translation: AAA37349.1 M35526 mRNA Translation: AAA37348.1 AL845534 Genomic DNA No translation available. |
CCDSi | CCDS15957.1 |
PIRi | A35530, C5MS |
RefSeqi | NP_034536.2, NM_010406.2 |
Genome annotation databases
Ensembli | ENSMUST00000028233; ENSMUSP00000028233; ENSMUSG00000026874 |
GeneIDi | 15139 |
KEGGi | mmu:15139 |
UCSCi | uc008jjn.2, mouse |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M35525 mRNA Translation: AAA37349.1 M35526 mRNA Translation: AAA37348.1 AL845534 Genomic DNA No translation available. |
CCDSi | CCDS15957.1 |
PIRi | A35530, C5MS |
RefSeqi | NP_034536.2, NM_010406.2 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
4P3A | X-ray | 1.40 | A/B/C/D | 679-755 | [»] | |
4P3B | X-ray | 2.10 | A/B/C/D | 679-754 | [»] | |
4WB2 | X-ray | 1.80 | A/B/C | 679-755 | [»] | |
4WB3 | X-ray | 2.00 | A/B/C | 679-754 | [»] | |
SMRi | P06684 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 200226, 4 interactors |
IntActi | P06684, 3 interactors |
STRINGi | 10090.ENSMUSP00000028233 |
Protein family/group databases
MEROPSi | I39.952 |
PTM databases
GlyGeni | P06684, 4 sites |
iPTMneti | P06684 |
PhosphoSitePlusi | P06684 |
Proteomic databases
CPTACi | non-CPTAC-3698 non-CPTAC-4025 |
MaxQBi | P06684 |
PaxDbi | P06684 |
PeptideAtlasi | P06684 |
PRIDEi | P06684 |
Protocols and materials databases
ABCDi | P06684, 2 sequenced antibodies |
Genome annotation databases
Ensembli | ENSMUST00000028233; ENSMUSP00000028233; ENSMUSG00000026874 |
GeneIDi | 15139 |
KEGGi | mmu:15139 |
UCSCi | uc008jjn.2, mouse |
Organism-specific databases
CTDi | 15139 |
MGIi | MGI:96031, Hc |
Phylogenomic databases
eggNOGi | KOG1366, Eukaryota |
GeneTreei | ENSGT00940000155670 |
HOGENOMi | CLU_001634_4_2_1 |
InParanoidi | P06684 |
OMAi | LTWIEYW |
OrthoDBi | 20179at2759 |
PhylomeDBi | P06684 |
TreeFami | TF313285 |
Enzyme and pathway databases
Reactomei | R-MMU-166665, Terminal pathway of complement R-MMU-174577, Activation of C3 and C5 R-MMU-375276, Peptide ligand-binding receptors R-MMU-418594, G alpha (i) signalling events R-MMU-977606, Regulation of Complement cascade |
Miscellaneous databases
BioGRID-ORCSi | 15139, 2 hits in 17 CRISPR screens |
ChiTaRSi | Hc, mouse |
PROi | PR:P06684 |
RNActi | P06684, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSMUSG00000026874, Expressed in lung and 97 other tissues |
ExpressionAtlasi | P06684, baseline and differential |
Genevisiblei | P06684, MM |
Family and domain databases
CDDi | cd00017, ANATO, 1 hit |
Gene3Di | 2.40.50.120, 1 hit 2.60.40.10, 2 hits 2.60.40.690, 1 hit |
InterProi | View protein in InterPro IPR009048, A-macroglobulin_rcpt-bd IPR036595, A-macroglobulin_rcpt-bd_sf IPR011625, A2M_N_BRD IPR011626, Alpha-macroglobulin_TED IPR000020, Anaphylatoxin/fibulin IPR018081, Anaphylatoxin_comp_syst IPR041425, C3/4/5_MG1 IPR037562, Complement_C5 IPR013783, Ig-like_fold IPR001599, Macroglobln_a2 IPR002890, MG2 IPR041555, MG3 IPR040839, MG4 IPR001134, Netrin_domain IPR018933, Netrin_module_non-TIMP IPR008930, Terpenoid_cyclase/PrenylTrfase IPR008993, TIMP-like_OB-fold |
PANTHERi | PTHR11412:SF83, PTHR11412:SF83, 1 hit |
Pfami | View protein in Pfam PF00207, A2M, 1 hit PF07703, A2M_BRD, 1 hit PF07677, A2M_recep, 1 hit PF01821, ANATO, 1 hit PF17790, MG1, 1 hit PF01835, MG2, 1 hit PF17791, MG3, 1 hit PF17789, MG4, 1 hit PF01759, NTR, 1 hit PF07678, TED_complement, 1 hit |
SMARTi | View protein in SMART SM01360, A2M, 1 hit SM01359, A2M_N_2, 1 hit SM01361, A2M_recep, 1 hit SM00104, ANATO, 1 hit SM00643, C345C, 1 hit |
SUPFAMi | SSF47686, SSF47686, 1 hit SSF48239, SSF48239, 1 hit SSF49410, SSF49410, 1 hit SSF50242, SSF50242, 1 hit |
PROSITEi | View protein in PROSITE PS01177, ANAPHYLATOXIN_1, 1 hit PS01178, ANAPHYLATOXIN_2, 1 hit PS50189, NTR, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | CO5_MOUSE | |
Accessioni | P06684Primary (citable) accession number: P06684 Secondary accession number(s): A2AS36 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | January 1, 1988 |
Last sequence update: | November 1, 1990 | |
Last modified: | December 2, 2020 | |
This is version 183 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references