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P06684

- CO5_MOUSE

UniProt

P06684 - CO5_MOUSE

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Protein

Complement C5

Gene

C5

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

  1. endopeptidase inhibitor activity Source: InterPro

GO - Biological processi

  1. cellular calcium ion homeostasis Source: Ensembl
  2. chemotaxis Source: Ensembl
  3. complement activation, alternative pathway Source: UniProtKB-KW
  4. complement activation, classical pathway Source: UniProtKB-KW
  5. cytolysis Source: UniProtKB-KW
  6. glucose homeostasis Source: Ensembl
  7. in utero embryonic development Source: MGI
  8. leukocyte migration involved in inflammatory response Source: Ensembl
  9. negative regulation of dopamine secretion Source: Ensembl
  10. negative regulation of macrophage chemotaxis Source: Ensembl
  11. negative regulation of norepinephrine secretion Source: Ensembl
  12. positive regulation of angiogenesis Source: BHF-UCL
  13. positive regulation of chemokine secretion Source: Ensembl
  14. positive regulation of chemotaxis Source: Ensembl
  15. positive regulation vascular endothelial growth factor production Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Complement alternate pathway, Complement pathway, Cytolysis, Immunity, Inflammatory response, Innate immunity

Enzyme and pathway databases

ReactomeiREACT_198562. Regulation of Complement cascade.
REACT_213087. Activation of C3 and C5.
REACT_215211. Terminal pathway of complement.

Protein family/group databases

MEROPSiI39.952.

Names & Taxonomyi

Protein namesi
Recommended name:
Complement C5
Alternative name(s):
Hemolytic complement
Cleaved into the following 4 chains:
Gene namesi
Name:C5
Synonyms:Hc
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:96031. Hc.

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: Ensembl
  2. extracellular vesicular exosome Source: Ensembl
  3. membrane attack complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane attack complex, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Add
BLAST
Chaini19 – 674656Complement C5 beta chainPRO_0000005991Add
BLAST
Propeptidei675 – 6784PRO_0000005992
Chaini679 – 16801002Complement C5 alpha chainPRO_0000005993Add
BLAST
Chaini679 – 75577C5a anaphylatoxinPRO_0000005994Add
BLAST
Chaini756 – 1680925Complement C5 alpha' chainPRO_0000005995Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi427 – 4271N-linked (GlcNAc...)2 Publications
Disulfide bondi702 ↔ 728By similarity
Disulfide bondi703 ↔ 735By similarity
Disulfide bondi715 ↔ 736By similarity
Glycosylationi915 – 9151N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1119 – 11191N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1536 ↔ 1609By similarity
Disulfide bondi1557 ↔ 1679By similarity
Glycosylationi1633 – 16331N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP06684.
PaxDbiP06684.
PRIDEiP06684.

PTM databases

PhosphoSiteiP06684.

Expressioni

Gene expression databases

BgeeiP06684.
CleanExiMM_HC.
ExpressionAtlasiP06684. baseline and differential.
GenevestigatoriP06684.

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 similarity

Protein-protein interaction databases

IntActiP06684. 2 interactions.
MINTiMINT-1857037.

Structurei

Secondary structure

1
1680
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi680 – 69112Combined sources
Beta strandi694 – 6963Combined sources
Helixi697 – 70711Combined sources
Helixi715 – 7195Combined sources
Helixi726 – 74419Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4P3AX-ray1.40A/B/C/D679-755[»]
4P3BX-ray2.10A/B/C/D679-754[»]
ProteinModelPortaliP06684.
SMRiP06684. Positions 22-673, 679-746.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini702 – 73635Anaphylatoxin-likePROSITE-ProRule annotationAdd
BLAST
Domaini1536 – 1679144NTRPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni696 – 72530Involved in C5AR1 bindingBy similarityAdd
BLAST

Sequence similaritiesi

Contains 1 anaphylatoxin-like domain.PROSITE-ProRule annotation
Contains 1 NTR domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG241555.
GeneTreeiENSGT00760000118982.
HOGENOMiHOG000231860.
HOVERGENiHBG098067.
InParanoidiP06684.
KOiK03994.
OMAiVFYVFHY.
OrthoDBiEOG77HDCX.
PhylomeDBiP06684.
TreeFamiTF313285.

Family and domain databases

Gene3Di1.20.91.20. 1 hit.
1.50.10.20. 1 hit.
2.60.40.690. 1 hit.
InterProiIPR009048. A-macroglobulin_rcpt-bd.
IPR011626. A2M_comp.
IPR002890. A2M_N.
IPR011625. A2M_N_2.
IPR000020. Anaphylatoxin/fibulin.
IPR018081. Anaphylatoxin_comp_syst.
IPR001599. Macroglobln_a2.
IPR001134. Netrin_domain.
IPR018933. Netrin_module_non-TIMP.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
IPR008993. TIMP-like_OB-fold.
[Graphical view]
PfamiPF00207. A2M. 1 hit.
PF07678. A2M_comp. 1 hit.
PF01835. A2M_N. 1 hit.
PF07703. A2M_N_2. 1 hit.
PF07677. A2M_recep. 1 hit.
PF01821. ANATO. 1 hit.
PF01759. NTR. 1 hit.
[Graphical view]
SMARTiSM00104. ANATO. 1 hit.
SM00643. C345C. 1 hit.
[Graphical view]
SUPFAMiSSF47686. SSF47686. 1 hit.
SSF48239. SSF48239. 1 hit.
SSF49410. SSF49410. 1 hit.
SSF50242. SSF50242. 1 hit.
PROSITEiPS01177. ANAPHYLATOXIN_1. 1 hit.
PS01178. ANAPHYLATOXIN_2. 1 hit.
PS50189. NTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P06684-1 [UniParc]FASTAAdd to Basket

« Hide

        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
Length:1,680
Mass (Da):188,878
Last modified:November 1, 1990 - v2
Checksum:i81EB5A16FAC7D95C
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti216 – 2161Y → L in defective variant C5D.
Natural varianti217 – 16801464Missing in defective variant C5D.
Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M35525 mRNA. Translation: AAA37349.1.
M35526 mRNA. Translation: AAA37348.1.
AL845534 Genomic DNA. Translation: CAM17901.1.
CCDSiCCDS15957.1.
PIRiA35530. C5MS.
RefSeqiNP_034536.1. NM_010406.2.
UniGeneiMm.2168.

Genome annotation databases

EnsembliENSMUST00000028233; ENSMUSP00000028233; ENSMUSG00000026874.
GeneIDi15139.
KEGGimmu:15139.
UCSCiuc008jjn.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M35525 mRNA. Translation: AAA37349.1 .
M35526 mRNA. Translation: AAA37348.1 .
AL845534 Genomic DNA. Translation: CAM17901.1 .
CCDSi CCDS15957.1.
PIRi A35530. C5MS.
RefSeqi NP_034536.1. NM_010406.2.
UniGenei Mm.2168.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P06684.
SMRi P06684. Positions 22-673, 679-746.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P06684. 2 interactions.
MINTi MINT-1857037.

Protein family/group databases

MEROPSi I39.952.

PTM databases

PhosphoSitei P06684.

Proteomic databases

MaxQBi P06684.
PaxDbi P06684.
PRIDEi P06684.

Protocols and materials databases

Structural Biology Knowledgebase Search...

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 NOG241555.
GeneTreei ENSGT00760000118982.
HOGENOMi HOG000231860.
HOVERGENi HBG098067.
InParanoidi P06684.
KOi K03994.
OMAi VFYVFHY.
OrthoDBi EOG77HDCX.
PhylomeDBi P06684.
TreeFami TF313285.

Enzyme and pathway databases

Reactomei REACT_198562. Regulation of Complement cascade.
REACT_213087. Activation of C3 and C5.
REACT_215211. Terminal pathway of complement.

Miscellaneous databases

NextBioi 287602.
PROi P06684.
SOURCEi Search...

Gene expression databases

Bgeei P06684.
CleanExi MM_HC.
ExpressionAtlasi P06684. baseline and differential.
Genevestigatori P06684.

Family and domain databases

Gene3Di 1.20.91.20. 1 hit.
1.50.10.20. 1 hit.
2.60.40.690. 1 hit.
InterProi IPR009048. A-macroglobulin_rcpt-bd.
IPR011626. A2M_comp.
IPR002890. A2M_N.
IPR011625. A2M_N_2.
IPR000020. Anaphylatoxin/fibulin.
IPR018081. Anaphylatoxin_comp_syst.
IPR001599. Macroglobln_a2.
IPR001134. Netrin_domain.
IPR018933. Netrin_module_non-TIMP.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
IPR008993. TIMP-like_OB-fold.
[Graphical view ]
Pfami PF00207. A2M. 1 hit.
PF07678. A2M_comp. 1 hit.
PF01835. A2M_N. 1 hit.
PF07703. A2M_N_2. 1 hit.
PF07677. A2M_recep. 1 hit.
PF01821. ANATO. 1 hit.
PF01759. NTR. 1 hit.
[Graphical view ]
SMARTi SM00104. ANATO. 1 hit.
SM00643. C345C. 1 hit.
[Graphical view ]
SUPFAMi SSF47686. SSF47686. 1 hit.
SSF48239. SSF48239. 1 hit.
SSF49410. SSF49410. 1 hit.
SSF50242. SSF50242. 1 hit.
PROSITEi PS01177. ANAPHYLATOXIN_1. 1 hit.
PS01178. ANAPHYLATOXIN_2. 1 hit.
PS50189. NTR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Deficiency of the murine fifth complement component (C5). A 2-base pair gene deletion in a 5'-exon."
    Wetsel R.A., Fleischer D.T., Haviland D.L.
    J. Biol. Chem. 265:2435-2440(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "Primary structure of the fifth component of murine complement."
    Wetsel R.A., Ogata R.T., Tack B.F.
    Biochemistry 26:737-743(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 41-1680.
  4. "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."
    Haviland D.L., Haviland J.C., Fleischer D.T., Wetsel R.A.
    J. Biol. Chem. 266:11818-11825(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE STRUCTURE.
  5. "Proteome-wide characterization of N-glycosylation events by diagonal chromatography."
    Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.
    J. Proteome Res. 5:2438-2447(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-427.
    Strain: C57BL/6.
    Tissue: Plasma.
  6. "Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides."
    Bernhard O.K., Kapp E.A., Simpson R.J.
    J. Proteome Res. 6:987-995(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-427.
    Strain: C57BL/6.
    Tissue: Plasma.

Entry informationi

Entry nameiCO5_MOUSE
AccessioniPrimary (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: October 29, 2014
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3