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P06684

- CO5_MOUSE

UniProt

P06684 - CO5_MOUSE

Protein

Complement C5

Gene

C5

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 2 (01 Nov 1990)
      Previous versions | rss
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    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

    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

    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.
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

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

    Sequence similaritiesi

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

    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

    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 1, 2014
    This is version 136 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