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P06684 (CO5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Complement C5
Alternative name(s):
Hemolytic complement
Gene names
Name:C5
Synonyms:Hc
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1680 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

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).

Subunit structure

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).

Subcellular location

Secreted.

Sequence similarities

Contains 1 anaphylatoxin-like domain.

Contains 1 NTR domain.

Ontologies

Keywords
   Biological processComplement alternate pathway
Complement pathway
Cytolysis
Immunity
Inflammatory response
Innate immunity
   Cellular componentMembrane attack complex
Secreted
   DomainSignal
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular calcium ion homeostasis

Inferred from electronic annotation. Source: Ensembl

chemotaxis

Inferred from electronic annotation. Source: Ensembl

complement activation, alternative pathway

Inferred from electronic annotation. Source: UniProtKB-KW

complement activation, classical pathway

Inferred from electronic annotation. Source: UniProtKB-KW

cytolysis

Inferred from electronic annotation. Source: UniProtKB-KW

glucose homeostasis

Inferred from electronic annotation. Source: Ensembl

in utero embryonic development

Inferred from genetic interaction PubMed 18947875. Source: MGI

leukocyte migration involved in inflammatory response

Inferred from electronic annotation. Source: Ensembl

negative regulation of dopamine secretion

Inferred from electronic annotation. Source: Ensembl

negative regulation of macrophage chemotaxis

Inferred from electronic annotation. Source: Ensembl

negative regulation of norepinephrine secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of angiogenesis

Inferred from mutant phenotype PubMed 16452172. Source: BHF-UCL

positive regulation of chemokine secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of chemotaxis

Inferred from electronic annotation. Source: Ensembl

positive regulation vascular endothelial growth factor production

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentextracellular space

Inferred from electronic annotation. Source: Ensembl

membrane attack complex

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionendopeptidase inhibitor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818
Chain19 – 674656Complement C5 beta chain
PRO_0000005991
Propeptide675 – 6784
PRO_0000005992
Chain679 – 16801002Complement C5 alpha chain
PRO_0000005993
Chain679 – 75577C5a anaphylatoxin
PRO_0000005994
Chain756 – 1680925Complement C5 alpha' chain
PRO_0000005995

Regions

Domain702 – 73635Anaphylatoxin-like
Domain1536 – 1679144NTR

Amino acid modifications

Glycosylation4271N-linked (GlcNAc...) Ref.5 Ref.6
Glycosylation9151N-linked (GlcNAc...) Potential
Glycosylation11191N-linked (GlcNAc...) Potential
Glycosylation16331N-linked (GlcNAc...) Potential
Disulfide bond702 ↔ 728 By similarity
Disulfide bond703 ↔ 735 By similarity
Disulfide bond715 ↔ 736 By similarity
Disulfide bond1536 ↔ 1609 By similarity
Disulfide bond1557 ↔ 1679 By similarity

Natural variations

Natural variant2161Y → L in defective variant C5D.
Natural variant217 – 16801464Missing in defective variant C5D.

Sequences

Sequence LengthMass (Da)Tools
P06684 [UniParc].

Last modified November 1, 1990. Version 2.
Checksum: 81EB5A16FAC7D95C

FASTA1,680188,878
        10         20         30         40         50         60 
MGLWGILCLL IFLDKTWGQE QTYVISAPKI LRVGSSENVV IQVHGYTEAF DATLSLKSYP 

        70         80         90        100        110        120 
DKKVTFSSGY VNLSPENKFQ NAALLTLQPN QVPREESPVS HVYLEVVSKH FSKSKKIPIT 

       130        140        150        160        170        180 
YNNGILFIHT DKPVYTPDQS VKIRVYSLGD DLKPAKRETV LTFIDPEGSE VDIVEENDYT 

       190        200        210        220        230        240 
GIISFPDFKI PSNPKYGVWT IKANYKKDFT TTGTAYFEIK EYVLPRFSVS IELERTFIGY 

       250        260        270        280        290        300 
KNFKNFEITV KARYFYNKVV PDAEVYAFFG LREDIKDEEK QMMHKATQAA KLVDGVAQIS 

       310        320        330        340        350        360 
FDSETAVKEL SYNSLEDLNN KYLYIAVTVT ESSGGFSEEA EIPGVKYVLS PYTLNLVATP 

       370        380        390        400        410        420 
LFVKPGIPFS IKAQVKDSLE QAVGGVPVTL MAQTVDVNQE TSDLETKRSI THDTDGVAVF 

       430        440        450        460        470        480 
VLNLPSNVTV LKFEIRTDDP ELPEENQASK EYEAVAYSSL SQSYIYIAWT ENYKPMLVGE 

       490        500        510        520        530        540 
YLNIMVTPKS PYIDKITHYN YLILSKGKIV QYGTREKLFS STYQNINIPV TQNMVPSARL 

       550        560        570        580        590        600 
LVYYIVTGEQ TAELVADAVW INIEEKCGNQ LQVHLSPDEY VYSPGQTVSL DMVTEADSWV 

       610        620        630        640        650        660 
ALSAVDRAVY KVQGNAKRAM QRVFQALDEK SDLGCGAGGG HDNADVFHLA GLTFLTNANA 

       670        680        690        700        710        720 
DDSHYRDDSC KEILRSKRNL HLLRQKIEEQ AAKYKHSVPK KCCYDGARVN FYETCEERVA 

       730        740        750        760        770        780 
RVTIGPLCIR AFNECCTIAN KIRKESPHKP VQLGRIHIKT LLPVMKADIR SYFPESWLWE 

       790        800        810        820        830        840 
IHRVPKRKQL QVTLPDSLTT WEIQGIGISD NGICVADTLK AKVFKEVFLE MNIPYSVVRG 

       850        860        870        880        890        900 
EQIQLKGTVY NYMTSGTKFC VKMSAVEGIC TSGSSAASLH TSRPSRCVFQ RIEGSSSHLV 

       910        920        930        940        950        960 
TFTLLPLEIG LHSINFSLET SFGKDILVKT LRVVPEGVKR ESYAGVILDP KGIRGIVNRR 

       970        980        990       1000       1010       1020 
KEFPYRIPLD LVPKTKVERI LSVKGLLVGE FLSTVLSKEG INILTHLPKG SAEAELMSIA 

      1030       1040       1050       1060       1070       1080 
PVFYVFHYLE AGNHWNIFYP DTLSKRQSLE KKIKQGVVSV MSYRNADYSY SMWKGASAST 

      1090       1100       1110       1120       1130       1140 
WLTAFALRVL GQVAKYVKQD ENSICNSLLW LVEKCQLENG SFKENSQYLP IKLQGTLPAE 

      1150       1160       1170       1180       1190       1200 
AQEKTLYLTA FSVIGIRKAV DICPTMKIHT ALDKADSFLL ENTLPSKSTF TLAIVAYALS 

      1210       1220       1230       1240       1250       1260 
LGDRTHPRFR LIVSALRKEA FVKGDPPIYR YWRDTLKRPD SSVPSSGTAG MVETTAYALL 

      1270       1280       1290       1300       1310       1320 
ASLKLKDMNY ANPIIKWLSE EQRYGGGFYS TQDTINAIEG LTEYSLLLKQ IHLDMDINVA 

      1330       1340       1350       1360       1370       1380 
YKHEGDFHKY KVTEKHFLGR PVEVSLNDDL VVSTGYSSGL ATVYVKTVVH KISVSEEFCS 

      1390       1400       1410       1420       1430       1440 
FYLKIDTQDI EASSHFRLSD SGFKRIIACA SYKPSKEEST SGSSHAVMDI SLPTGIGANE 

      1450       1460       1470       1480       1490       1500 
EDLRALVEGV DQLLTDYQIK DGHVILQLNS IPSRDFLCVR FRIFELFQVG FLNPATFTVY 

      1510       1520       1530       1540       1550       1560 
EYHRPDKQCT MIYSISDTRL QKVCEGAACT CVEADCAQLQ AEVDLAISAD SRKEKACKPE 

      1570       1580       1590       1600       1610       1620 
TAYAYKVRIT SATEENVFVK YTATLLVTYK TGEAADENSE VTFIKKMSCT NANLVKGKQY 

      1630       1640       1650       1660       1670       1680 
LIMGKEVLQI KHNFSFKYIY PLDSSTWIEY WPTDTTCPSC QAFVENLNNF AEDLFLNSCE 

« Hide

References

« Hide 'large scale' references
[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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
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. expand/collapse author list , 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.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M35525 mRNA. Translation: AAA37349.1.
M35526 mRNA. Translation: AAA37348.1.
AL845534 Genomic DNA. Translation: CAM17901.1.
CCDSCCDS15957.1.
PIRC5MS. A35530.
RefSeqNP_034536.1. NM_010406.2.
UniGeneMm.2168.

3D structure databases

ProteinModelPortalP06684.
SMRP06684. Positions 22-673, 683-743.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP06684. 2 interactions.
MINTMINT-1857037.

Protein family/group databases

MEROPSI39.952.

PTM databases

PhosphoSiteP06684.

Proteomic databases

MaxQBP06684.
PaxDbP06684.
PRIDEP06684.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028233; ENSMUSP00000028233; ENSMUSG00000026874.
GeneID15139.
KEGGmmu:15139.
UCSCuc008jjn.2. mouse.

Organism-specific databases

CTD15139.
MGIMGI:96031. Hc.

Phylogenomic databases

eggNOGNOG241555.
GeneTreeENSGT00560000077078.
HOGENOMHOG000231860.
HOVERGENHBG098067.
InParanoidA2AS36.
KOK03994.
OMAVFYVFHY.
OrthoDBEOG77HDCX.
PhylomeDBP06684.
TreeFamTF313285.

Gene expression databases

BgeeP06684.
CleanExMM_HC.
GenevestigatorP06684.

Family and domain databases

Gene3D1.20.91.20. 1 hit.
1.50.10.20. 1 hit.
2.60.40.690. 1 hit.
InterProIPR009048. 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]
PfamPF00207. 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]
SMARTSM00104. ANATO. 1 hit.
SM00643. C345C. 1 hit.
[Graphical view]
SUPFAMSSF47686. SSF47686. 1 hit.
SSF48239. SSF48239. 1 hit.
SSF49410. SSF49410. 1 hit.
SSF50242. SSF50242. 1 hit.
PROSITEPS01177. ANAPHYLATOXIN_1. 1 hit.
PS01178. ANAPHYLATOXIN_2. 1 hit.
PS50189. NTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio287602.
PROP06684.
SOURCESearch...

Entry information

Entry nameCO5_MOUSE
AccessionPrimary (citable) accession number: P06684
Secondary accession number(s): A2AS36
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: November 1, 1990
Last modified: July 9, 2014
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot