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P06684

- CO5_MOUSE

UniProt

P06684 - CO5_MOUSE

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Protein
Complement C5
Gene
C5, Hc
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. It induces the contraction of smooth muscle, increases vascular permeability and causes histamine release from mast cells and basophilic leukocytes. C5a also stimulates the locomotion of polymorphonuclear leukocytes (chemokinesis) and direct their migration toward sites of inflammation (chemotaxis).

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. 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 – 1818
Add
BLAST
Chaini19 – 674656Complement C5 beta chain
PRO_0000005991Add
BLAST
Propeptidei675 – 6784
PRO_0000005992
Chaini679 – 16801002Complement C5 alpha chain
PRO_0000005993Add
BLAST
Chaini679 – 75577C5a anaphylatoxin
PRO_0000005994Add
BLAST
Chaini756 – 1680925Complement C5 alpha' chain
PRO_0000005995Add
BLAST

Amino acid modifications

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

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.
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).

Protein-protein interaction databases

IntActiP06684. 2 interactions.
MINTiMINT-1857037.

Structurei

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, 683-743.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini702 – 73635Anaphylatoxin-like
Add
BLAST
Domaini1536 – 1679144NTR
Add
BLAST

Sequence similaritiesi

Contains 1 NTR domain.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG241555.
GeneTreeiENSGT00560000077078.
HOGENOMiHOG000231860.
HOVERGENiHBG098067.
InParanoidiA2AS36.
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

MGLWGILCLL IFLDKTWGQE QTYVISAPKI LRVGSSENVV IQVHGYTEAF     50
DATLSLKSYP DKKVTFSSGY VNLSPENKFQ NAALLTLQPN QVPREESPVS 100
HVYLEVVSKH FSKSKKIPIT YNNGILFIHT DKPVYTPDQS VKIRVYSLGD 150
DLKPAKRETV LTFIDPEGSE VDIVEENDYT GIISFPDFKI PSNPKYGVWT 200
IKANYKKDFT TTGTAYFEIK EYVLPRFSVS IELERTFIGY KNFKNFEITV 250
KARYFYNKVV PDAEVYAFFG LREDIKDEEK QMMHKATQAA KLVDGVAQIS 300
FDSETAVKEL SYNSLEDLNN KYLYIAVTVT ESSGGFSEEA EIPGVKYVLS 350
PYTLNLVATP LFVKPGIPFS IKAQVKDSLE QAVGGVPVTL MAQTVDVNQE 400
TSDLETKRSI THDTDGVAVF VLNLPSNVTV LKFEIRTDDP ELPEENQASK 450
EYEAVAYSSL SQSYIYIAWT ENYKPMLVGE YLNIMVTPKS PYIDKITHYN 500
YLILSKGKIV QYGTREKLFS STYQNINIPV TQNMVPSARL LVYYIVTGEQ 550
TAELVADAVW INIEEKCGNQ LQVHLSPDEY VYSPGQTVSL DMVTEADSWV 600
ALSAVDRAVY KVQGNAKRAM QRVFQALDEK SDLGCGAGGG HDNADVFHLA 650
GLTFLTNANA DDSHYRDDSC KEILRSKRNL HLLRQKIEEQ AAKYKHSVPK 700
KCCYDGARVN FYETCEERVA RVTIGPLCIR AFNECCTIAN KIRKESPHKP 750
VQLGRIHIKT LLPVMKADIR SYFPESWLWE IHRVPKRKQL QVTLPDSLTT 800
WEIQGIGISD NGICVADTLK AKVFKEVFLE MNIPYSVVRG EQIQLKGTVY 850
NYMTSGTKFC VKMSAVEGIC TSGSSAASLH TSRPSRCVFQ RIEGSSSHLV 900
TFTLLPLEIG LHSINFSLET SFGKDILVKT LRVVPEGVKR ESYAGVILDP 950
KGIRGIVNRR KEFPYRIPLD LVPKTKVERI LSVKGLLVGE FLSTVLSKEG 1000
INILTHLPKG SAEAELMSIA PVFYVFHYLE AGNHWNIFYP DTLSKRQSLE 1050
KKIKQGVVSV MSYRNADYSY SMWKGASAST WLTAFALRVL GQVAKYVKQD 1100
ENSICNSLLW LVEKCQLENG SFKENSQYLP IKLQGTLPAE AQEKTLYLTA 1150
FSVIGIRKAV DICPTMKIHT ALDKADSFLL ENTLPSKSTF TLAIVAYALS 1200
LGDRTHPRFR LIVSALRKEA FVKGDPPIYR YWRDTLKRPD SSVPSSGTAG 1250
MVETTAYALL ASLKLKDMNY ANPIIKWLSE EQRYGGGFYS TQDTINAIEG 1300
LTEYSLLLKQ IHLDMDINVA YKHEGDFHKY KVTEKHFLGR PVEVSLNDDL 1350
VVSTGYSSGL ATVYVKTVVH KISVSEEFCS FYLKIDTQDI EASSHFRLSD 1400
SGFKRIIACA SYKPSKEEST SGSSHAVMDI SLPTGIGANE EDLRALVEGV 1450
DQLLTDYQIK DGHVILQLNS IPSRDFLCVR FRIFELFQVG FLNPATFTVY 1500
EYHRPDKQCT MIYSISDTRL QKVCEGAACT CVEADCAQLQ AEVDLAISAD 1550
SRKEKACKPE TAYAYKVRIT SATEENVFVK YTATLLVTYK TGEAADENSE 1600
VTFIKKMSCT NANLVKGKQY LIMGKEVLQI KHNFSFKYIY PLDSSTWIEY 1650
WPTDTTCPSC QAFVENLNNF AEDLFLNSCE 1680
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, 683-743.
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 ENSGT00560000077078.
HOGENOMi HOG000231860.
HOVERGENi HBG098067.
InParanoidi A2AS36.
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.
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: September 3, 2014
This is version 135 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

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