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P01031

- CO5_HUMAN

UniProt

P01031 - CO5_HUMAN

Protein

Complement C5

Gene

C5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 169 (01 Oct 2014)
      Sequence version 4 (05 Feb 2008)
      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. chemokine activity Source: ProtInc
    2. endopeptidase inhibitor activity Source: InterPro
    3. protein binding Source: IntAct
    4. receptor binding Source: ProtInc

    GO - Biological processi

    1. activation of MAPK activity Source: ProtInc
    2. cell chemotaxis Source: GOC
    3. cell surface receptor signaling pathway Source: ProtInc
    4. cellular calcium ion homeostasis Source: Ensembl
    5. chemotaxis Source: ProtInc
    6. complement activation Source: Reactome
    7. complement activation, alternative pathway Source: UniProtKB-KW
    8. complement activation, classical pathway Source: UniProtKB-KW
    9. cytolysis Source: UniProtKB-KW
    10. glucose homeostasis Source: Ensembl
    11. G-protein coupled receptor signaling pathway Source: ProtInc
    12. inflammatory response Source: ProtInc
    13. innate immune response Source: Reactome
    14. in utero embryonic development Source: Ensembl
    15. leukocyte migration involved in inflammatory response Source: Ensembl
    16. negative regulation of dopamine secretion Source: Ensembl
    17. negative regulation of macrophage chemotaxis Source: BHF-UCL
    18. negative regulation of norepinephrine secretion Source: Ensembl
    19. positive regulation of angiogenesis Source: Ensembl
    20. positive regulation of chemokine secretion Source: BHF-UCL
    21. positive regulation of chemotaxis Source: Ensembl
    22. positive regulation vascular endothelial growth factor production Source: BHF-UCL
    23. regulation of complement activation Source: Reactome
    24. response to stress Source: ProtInc

    Keywords - Biological processi

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

    Enzyme and pathway databases

    BioCyciMOUSE:MONOMER-12977.
    ReactomeiREACT_118707. Regulation of Complement cascade.
    REACT_14819. Peptide ligand-binding receptors.
    REACT_19231. G alpha (i) signalling events.
    REACT_7972. Activation of C3 and C5.
    REACT_8028. Terminal pathway of complement.

    Protein family/group databases

    MEROPSiI39.952.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Complement C5
    Alternative name(s):
    C3 and PZP-like alpha-2-macroglobulin domain-containing protein 4
    Cleaved into the following 4 chains:
    Gene namesi
    Name:C5
    Synonyms:CPAMD4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:1331. C5.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. extracellular space Source: ProtInc
    3. extracellular vesicular exosome Source: UniProt
    4. membrane attack complex Source: UniProtKB-KW

    Keywords - Cellular componenti

    Membrane attack complex, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Complement component 5 deficiency (C5D) [MIM:609536]: A rare defect of the complement classical pathway associated with susceptibility to severe recurrent infections, predominantly by Neisseria gonorrhoeae or Neisseria meningitidis.
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    An association study of C5 haplotypes and genotypes in individuals with chronic hepatitis C virus infection shows that individuals homozygous for the C5_1 haplotype have a significantly higher stage of liver fibrosis than individuals carrying at least 1 other allele.1 Publication

    Organism-specific databases

    MIMi609536. phenotype.
    615749. phenotype.
    Orphaneti169150. Immunodeficiency due to a late component of complements deficiency.
    PharmGKBiPA25911.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Chaini19 – 673655Complement C5 beta chainPRO_0000005985Add
    BLAST
    Propeptidei674 – 67741 PublicationPRO_0000005986
    Chaini678 – 1676999Complement C5 alpha chainPRO_0000005987Add
    BLAST
    Chaini678 – 75174C5a anaphylatoxinPRO_0000005988Add
    BLAST
    Chaini752 – 1676925Complement C5 alpha' chainPRO_0000005989Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi567 ↔ 810
    Disulfide bondi634 ↔ 669
    Disulfide bondi698 ↔ 724
    Disulfide bondi699 ↔ 731
    Disulfide bondi711 ↔ 732
    Glycosylationi741 – 7411N-linked (GlcNAc...)2 Publications
    Disulfide bondi856 ↔ 883
    Disulfide bondi866 ↔ 1527
    Glycosylationi911 – 9111N-linked (GlcNAc...)3 Publications
    Disulfide bondi1101 ↔ 1159
    Glycosylationi1115 – 11151N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1375 ↔ 1505
    Disulfide bondi1405 ↔ 1474
    Disulfide bondi1520 ↔ 1525
    Disulfide bondi1532 ↔ 1606
    Disulfide bondi1553 ↔ 1676
    Glycosylationi1630 – 16301N-linked (GlcNAc...)1 Publication
    Disulfide bondi1654 ↔ 1657

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP01031.
    PaxDbiP01031.
    PRIDEiP01031.

    PTM databases

    PhosphoSiteiP01031.

    Miscellaneous databases

    PMAP-CutDBP01031.

    Expressioni

    Gene expression databases

    BgeeiP01031.
    CleanExiHS_C5.
    GenevestigatoriP01031.

    Organism-specific databases

    HPAiHPA029339.

    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). Interacts with tick complement inhibitor.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Q911322EBI-8558308,EBI-7081824From a different organism.

    Protein-protein interaction databases

    BioGridi107188. 7 interactions.
    IntActiP01031. 2 interactions.
    STRINGi9606.ENSP00000223642.

    Structurei

    Secondary structure

    1
    1676
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi23 – 3210
    Beta strandi41 – 433
    Beta strandi52 – 587
    Beta strandi61 – 666
    Turni75 – 795
    Beta strandi80 – 867
    Beta strandi93 – 975
    Beta strandi102 – 1109
    Beta strandi112 – 1176
    Beta strandi124 – 1318
    Beta strandi133 – 1353
    Beta strandi143 – 1486
    Beta strandi150 – 1534
    Beta strandi159 – 1646
    Beta strandi174 – 1763
    Beta strandi179 – 1846
    Beta strandi197 – 20812
    Beta strandi212 – 2198
    Beta strandi226 – 2294
    Beta strandi232 – 2343
    Beta strandi236 – 2383
    Turni241 – 2444
    Beta strandi247 – 2504
    Beta strandi252 – 2543
    Turni255 – 2573
    Beta strandi261 – 27313
    Beta strandi281 – 2855
    Beta strandi289 – 2935
    Beta strandi296 – 3005
    Turni303 – 3108
    Turni316 – 3183
    Beta strandi321 – 33414
    Beta strandi338 – 3425
    Beta strandi351 – 3544
    Beta strandi361 – 3633
    Beta strandi365 – 3673
    Beta strandi369 – 3779
    Beta strandi378 – 3803
    Beta strandi387 – 39610
    Beta strandi401 – 4033
    Beta strandi407 – 4104
    Beta strandi413 – 4153
    Beta strandi417 – 4226
    Beta strandi428 – 43710
    Helixi444 – 4463
    Beta strandi449 – 4568
    Beta strandi466 – 4694
    Beta strandi472 – 4765
    Beta strandi481 – 4877
    Beta strandi498 – 5058
    Beta strandi508 – 5169
    Beta strandi519 – 5224
    Beta strandi524 – 5296
    Helixi532 – 5343
    Beta strandi535 – 54612
    Beta strandi549 – 5513
    Beta strandi553 – 56311
    Beta strandi574 – 5774
    Beta strandi580 – 5823
    Beta strandi587 – 5937
    Beta strandi598 – 6025
    Beta strandi604 – 6063
    Turni607 – 6104
    Helixi614 – 6163
    Helixi620 – 6267
    Turni627 – 6304
    Beta strandi635 – 6373
    Beta strandi640 – 6423
    Helixi643 – 6486
    Beta strandi651 – 6544
    Beta strandi656 – 6583
    Beta strandi663 – 6653
    Helixi680 – 69011
    Helixi693 – 70311
    Beta strandi707 – 7093
    Helixi711 – 7166
    Helixi722 – 74120
    Helixi745 – 7484
    Beta strandi764 – 7663
    Beta strandi777 – 78913
    Beta strandi792 – 7998
    Beta strandi801 – 8055
    Beta strandi808 – 8114
    Beta strandi815 – 8195
    Beta strandi822 – 8287
    Beta strandi839 – 8479
    Beta strandi849 – 8513
    Beta strandi853 – 8619
    Beta strandi865 – 8695
    Beta strandi874 – 8774
    Beta strandi886 – 8883
    Beta strandi892 – 8954
    Beta strandi898 – 9025
    Beta strandi904 – 9063
    Beta strandi910 – 9167
    Beta strandi919 – 9257
    Beta strandi934 – 94512
    Turni949 – 9513
    Beta strandi957 – 9593
    Beta strandi974 – 9829
    Helixi985 – 9928
    Beta strandi993 – 9964
    Beta strandi1000 – 10023
    Helixi1009 – 10124
    Helixi1016 – 102712
    Helixi1031 – 10333
    Beta strandi1034 – 10363
    Helixi1038 – 105518
    Helixi1056 – 10594
    Beta strandi1064 – 10663
    Beta strandi1068 – 10725
    Helixi1076 – 109015
    Helixi1097 – 111014
    Helixi1133 – 115422
    Helixi1156 – 11583
    Helixi1162 – 117918
    Helixi1185 – 119511
    Helixi1203 – 121513
    Beta strandi1217 – 12193
    Turni1220 – 12234
    Beta strandi1224 – 12274
    Helixi1245 – 126016
    Helixi1264 – 127714
    Beta strandi1280 – 12823
    Turni1286 – 12894
    Helixi1290 – 130314
    Beta strandi1315 – 13206
    Beta strandi1322 – 13276
    Beta strandi1330 – 13323
    Beta strandi1338 – 13403
    Beta strandi1342 – 13443
    Beta strandi1346 – 13483
    Beta strandi1357 – 136812
    Beta strandi1371 – 13733
    Beta strandi1376 – 13849
    Beta strandi1401 – 14088
    Beta strandi1421 – 14277
    Beta strandi1432 – 14343
    Helixi1436 – 14438
    Beta strandi1449 – 14568
    Beta strandi1459 – 14657
    Beta strandi1469 – 14713
    Beta strandi1473 – 14808
    Beta strandi1491 – 14977
    Beta strandi1500 – 150910
    Turni1521 – 15244
    Helixi1525 – 15284
    Helixi1550 – 15534
    Beta strandi1559 – 15679
    Beta strandi1571 – 15733
    Beta strandi1576 – 158611
    Turni1589 – 15913
    Beta strandi1598 – 16014
    Beta strandi1618 – 16225
    Beta strandi1629 – 16324
    Beta strandi1644 – 16474
    Beta strandi1650 – 16567
    Helixi1659 – 16624
    Turni1663 – 16653
    Helixi1666 – 16716

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CFANMR-A679-747[»]
    1KJSNMR-A679-751[»]
    1XWENMR-A1530-1676[»]
    3CU7X-ray3.10A/B1-1676[»]
    3HQAX-ray2.59A/B679-750[»]
    3HQBX-ray3.30A/B679-750[»]
    3KLSX-ray3.60A/B1-1676[»]
    3KM9X-ray4.20A/B1-1676[»]
    3PRXX-ray4.30A/C1-1676[»]
    3PVMX-ray4.30A/C1-1676[»]
    4A5WX-ray3.50A19-1676[»]
    4E0SX-ray4.21A1-1676[»]
    4P39X-ray2.40A/B/C/D678-747[»]
    ProteinModelPortaliP01031.
    SMRiP01031. Positions 20-676, 679-743, 1530-1676.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP01031.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini698 – 73235Anaphylatoxin-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini1532 – 1676145NTRPROSITE-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

    eggNOGiCOG2373.
    HOGENOMiHOG000231860.
    HOVERGENiHBG098067.
    InParanoidiP01031.
    KOiK03994.
    OMAiVFYVFHY.
    OrthoDBiEOG77HDCX.
    PhylomeDBiP01031.
    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.
    IPR001840. Anaphylatoxn_comp_syst_dom.
    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]
    PRINTSiPR00004. ANAPHYLATOXN.
    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.

    P01031-1 [UniParc]FASTAAdd to Basket

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    MGLLGILCFL IFLGKTWGQE QTYVISAPKI FRVGASENIV IQVYGYTEAF     50
    DATISIKSYP DKKFSYSSGH VHLSSENKFQ NSAILTIQPK QLPGGQNPVS 100
    YVYLEVVSKH FSKSKRMPIT YDNGFLFIHT DKPVYTPDQS VKVRVYSLND 150
    DLKPAKRETV LTFIDPEGSE VDMVEEIDHI GIISFPDFKI PSNPRYGMWT 200
    IKAKYKEDFS TTGTAYFEVK EYVLPHFSVS IEPEYNFIGY KNFKNFEITI 250
    KARYFYNKVV TEADVYITFG IREDLKDDQK EMMQTAMQNT MLINGIAQVT 300
    FDSETAVKEL SYYSLEDLNN KYLYIAVTVI ESTGGFSEEA EIPGIKYVLS 350
    PYKLNLVATP LFLKPGIPYP IKVQVKDSLD QLVGGVPVTL NAQTIDVNQE 400
    TSDLDPSKSV TRVDDGVASF VLNLPSGVTV LEFNVKTDAP DLPEENQARE 450
    GYRAIAYSSL SQSYLYIDWT DNHKALLVGE HLNIIVTPKS PYIDKITHYN 500
    YLILSKGKII HFGTREKFSD ASYQSINIPV TQNMVPSSRL LVYYIVTGEQ 550
    TAELVSDSVW LNIEEKCGNQ LQVHLSPDAD AYSPGQTVSL NMATGMDSWV 600
    ALAAVDSAVY GVQRGAKKPL ERVFQFLEKS DLGCGAGGGL NNANVFHLAG 650
    LTFLTNANAD DSQENDEPCK EILRPRRTLQ KKIEEIAAKY KHSVVKKCCY 700
    DGACVNNDET CEQRAARISL GPRCIKAFTE CCVVASQLRA NISHKDMQLG 750
    RLHMKTLLPV SKPEIRSYFP ESWLWEVHLV PRRKQLQFAL PDSLTTWEIQ 800
    GVGISNTGIC VADTVKAKVF KDVFLEMNIP YSVVRGEQIQ LKGTVYNYRT 850
    SGMQFCVKMS AVEGICTSES PVIDHQGTKS SKCVRQKVEG SSSHLVTFTV 900
    LPLEIGLHNI NFSLETWFGK EILVKTLRVV PEGVKRESYS GVTLDPRGIY 950
    GTISRRKEFP YRIPLDLVPK TEIKRILSVK GLLVGEILSA VLSQEGINIL 1000
    THLPKGSAEA ELMSVVPVFY VFHYLETGNH WNIFHSDPLI EKQKLKKKLK 1050
    EGMLSIMSYR NADYSYSVWK GGSASTWLTA FALRVLGQVN KYVEQNQNSI 1100
    CNSLLWLVEN YQLDNGSFKE NSQYQPIKLQ GTLPVEAREN SLYLTAFTVI 1150
    GIRKAFDICP LVKIDTALIK ADNFLLENTL PAQSTFTLAI SAYALSLGDK 1200
    THPQFRSIVS ALKREALVKG NPPIYRFWKD NLQHKDSSVP NTGTARMVET 1250
    TAYALLTSLN LKDINYVNPV IKWLSEEQRY GGGFYSTQDT INAIEGLTEY 1300
    SLLVKQLRLS MDIDVSYKHK GALHNYKMTD KNFLGRPVEV LLNDDLIVST 1350
    GFGSGLATVH VTTVVHKTST SEEVCSFYLK IDTQDIEASH YRGYGNSDYK 1400
    RIVACASYKP SREESSSGSS HAVMDISLPT GISANEEDLK ALVEGVDQLF 1450
    TDYQIKDGHV ILQLNSIPSS DFLCVRFRIF ELFEVGFLSP ATFTVYEYHR 1500
    PDKQCTMFYS TSNIKIQKVC EGAACKCVEA DCGQMQEELD LTISAETRKQ 1550
    TACKPEIAYA YKVSITSITV ENVFVKYKAT LLDIYKTGEA VAEKDSEITF 1600
    IKKVTCTNAE LVKGRQYLIM GKEALQIKYN FSFRYIYPLD SLTWIEYWPR 1650
    DTTCSSCQAF LANLDEFAED IFLNGC 1676
    Length:1,676
    Mass (Da):188,305
    Last modified:February 5, 2008 - v4
    Checksum:iA7589E352F74672A
    GO

    Polymorphismi

    C5 variants are responsible for poor response to eculizumab [MIMi:615749]. Eculizumab is a monoclonal antibody highly effective in reducing intravascular hemolysis in patients with paroxysmal nocturnal hemoglobinuria. It specifically binds to the terminal complement protein C5, inhibits its cleavage into C5a and C5b, and prevents the formations of the cytolytic complement pore.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti145 – 1451V → I.1 Publication
    Corresponds to variant rs17216529 [ dbSNP | Ensembl ].
    VAR_038735
    Natural varianti354 – 3541L → M.
    Corresponds to variant rs34552775 [ dbSNP | Ensembl ].
    VAR_048822
    Natural varianti389 – 3891T → I.2 Publications
    VAR_023946
    Natural varianti449 – 4491R → G.1 Publication
    Corresponds to variant rs2230213 [ dbSNP | Ensembl ].
    VAR_038736
    Natural varianti518 – 5181F → S.
    VAR_001996
    Natural varianti802 – 8021V → I.7 Publications
    Corresponds to variant rs17611 [ dbSNP | Ensembl ].
    VAR_014574
    Natural varianti885 – 8851R → C Polymorphism associated with poor response to eculizumab in PNH patients. 1 Publication
    Corresponds to variant rs373359894 [ dbSNP | Ensembl ].
    VAR_071067
    Natural varianti885 – 8851R → H Polymorphism associated with poor response to eculizumab in PNH patients. 1 Publication
    Corresponds to variant rs56040400 [ dbSNP | Ensembl ].
    VAR_071068
    Natural varianti928 – 9281R → Q.1 Publication
    Corresponds to variant rs41309892 [ dbSNP | Ensembl ].
    VAR_038737
    Natural varianti933 – 9331G → V.1 Publication
    Corresponds to variant rs41309902 [ dbSNP | Ensembl ].
    VAR_038738
    Natural varianti966 – 9661D → Y Polymorphism confirmed at protein level. 1 Publication
    Corresponds to variant rs2230212 [ dbSNP | Ensembl ].
    VAR_048823
    Natural varianti1033 – 10331I → T.1 Publication
    Corresponds to variant rs41311881 [ dbSNP | Ensembl ].
    VAR_038739
    Natural varianti1037 – 10371D → N.1 Publication
    Corresponds to variant rs41311883 [ dbSNP | Ensembl ].
    VAR_038740
    Natural varianti1043 – 10431Q → K.1 Publication
    Corresponds to variant rs41311887 [ dbSNP | Ensembl ].
    VAR_038741
    Natural varianti1053 – 10531M → L.
    Corresponds to variant rs17609 [ dbSNP | Ensembl ].
    VAR_014575
    Natural varianti1310 – 13101S → N.1 Publication
    Corresponds to variant rs17610 [ dbSNP | Ensembl ].
    VAR_014576
    Natural varianti1365 – 13651V → A.
    Corresponds to variant rs16910245 [ dbSNP | Ensembl ].
    VAR_048824
    Natural varianti1437 – 14371E → D.1 Publication
    Corresponds to variant rs17612 [ dbSNP | Ensembl ].
    VAR_014577

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M57729 mRNA. Translation: AAA51925.1.
    DQ400449 Genomic DNA. Translation: ABD48959.1.
    CH471090 Genomic DNA. Translation: EAW87480.1.
    BC113738 mRNA. Translation: AAI13739.1.
    BC113740 mRNA. Translation: AAI13741.1.
    M65134 mRNA. Translation: AAA51856.1.
    CCDSiCCDS6826.1.
    PIRiA40075. C5HU.
    RefSeqiNP_001726.2. NM_001735.2.
    UniGeneiHs.494997.

    Genome annotation databases

    EnsembliENST00000223642; ENSP00000223642; ENSG00000106804.
    GeneIDi727.
    KEGGihsa:727.
    UCSCiuc004bkv.3. human.

    Polymorphism databases

    DMDMi166900096.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    C5base

    C5 mutation db

    Wikipedia

    Complement C5 entry

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M57729 mRNA. Translation: AAA51925.1 .
    DQ400449 Genomic DNA. Translation: ABD48959.1 .
    CH471090 Genomic DNA. Translation: EAW87480.1 .
    BC113738 mRNA. Translation: AAI13739.1 .
    BC113740 mRNA. Translation: AAI13741.1 .
    M65134 mRNA. Translation: AAA51856.1 .
    CCDSi CCDS6826.1.
    PIRi A40075. C5HU.
    RefSeqi NP_001726.2. NM_001735.2.
    UniGenei Hs.494997.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CFA NMR - A 679-747 [» ]
    1KJS NMR - A 679-751 [» ]
    1XWE NMR - A 1530-1676 [» ]
    3CU7 X-ray 3.10 A/B 1-1676 [» ]
    3HQA X-ray 2.59 A/B 679-750 [» ]
    3HQB X-ray 3.30 A/B 679-750 [» ]
    3KLS X-ray 3.60 A/B 1-1676 [» ]
    3KM9 X-ray 4.20 A/B 1-1676 [» ]
    3PRX X-ray 4.30 A/C 1-1676 [» ]
    3PVM X-ray 4.30 A/C 1-1676 [» ]
    4A5W X-ray 3.50 A 19-1676 [» ]
    4E0S X-ray 4.21 A 1-1676 [» ]
    4P39 X-ray 2.40 A/B/C/D 678-747 [» ]
    ProteinModelPortali P01031.
    SMRi P01031. Positions 20-676, 679-743, 1530-1676.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107188. 7 interactions.
    IntActi P01031. 2 interactions.
    STRINGi 9606.ENSP00000223642.

    Chemistry

    ChEMBLi CHEMBL2364163.
    DrugBanki DB01257. Eculizumab.

    Protein family/group databases

    MEROPSi I39.952.

    PTM databases

    PhosphoSitei P01031.

    Polymorphism databases

    DMDMi 166900096.

    Proteomic databases

    MaxQBi P01031.
    PaxDbi P01031.
    PRIDEi P01031.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000223642 ; ENSP00000223642 ; ENSG00000106804 .
    GeneIDi 727.
    KEGGi hsa:727.
    UCSCi uc004bkv.3. human.

    Organism-specific databases

    CTDi 727.
    GeneCardsi GC09M123714.
    H-InvDB HIX0025739.
    HGNCi HGNC:1331. C5.
    HPAi HPA029339.
    MIMi 120900. gene.
    609536. phenotype.
    615749. phenotype.
    neXtProti NX_P01031.
    Orphaneti 169150. Immunodeficiency due to a late component of complements deficiency.
    PharmGKBi PA25911.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2373.
    HOGENOMi HOG000231860.
    HOVERGENi HBG098067.
    InParanoidi P01031.
    KOi K03994.
    OMAi VFYVFHY.
    OrthoDBi EOG77HDCX.
    PhylomeDBi P01031.
    TreeFami TF313285.

    Enzyme and pathway databases

    BioCyci MOUSE:MONOMER-12977.
    Reactomei REACT_118707. Regulation of Complement cascade.
    REACT_14819. Peptide ligand-binding receptors.
    REACT_19231. G alpha (i) signalling events.
    REACT_7972. Activation of C3 and C5.
    REACT_8028. Terminal pathway of complement.

    Miscellaneous databases

    EvolutionaryTracei P01031.
    GeneWikii Complement_component_5.
    GenomeRNAii 727.
    NextBioi 2960.
    PMAP-CutDB P01031.
    PROi P01031.
    SOURCEi Search...

    Gene expression databases

    Bgeei P01031.
    CleanExi HS_C5.
    Genevestigatori P01031.

    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.
    IPR001840. Anaphylatoxn_comp_syst_dom.
    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 ]
    PRINTSi PR00004. ANAPHYLATOXN.
    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. "Complete cDNA sequence of human complement pro-C5. Evidence of truncated transcripts derived from a single copy gene."
      Haviland D.L., Haviland J.C., Fleischer D.T., Hunt A., Wetsel R.A.
      J. Immunol. 146:362-368(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ILE-389 AND ILE-802.
    2. SeattleSNPs variation discovery resource
      Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ILE-145; GLY-449; ILE-802; GLN-928; VAL-933; THR-1033; ASN-1037; LYS-1043; ASN-1310 AND ASP-1437.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ILE-802.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ILE-802.
    5. "Molecular analysis of human complement component C5: localization of the structural gene to chromosome 9."
      Wetsel R.A., Lemons R.S., Lebeau M.M., Barnum S.R., Noack D., Tack B.F.
      Biochemistry 27:1474-1482(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 412-1676, VARIANT ILE-802.
    6. "Isolation and sequence analysis of a cDNA clone encoding the fifth complement component."
      Lundwall A.B., Wetsel R.A., Kristensen T., Whitehead A.S., Woods D.E., Ogden R.C., Colten H.R., Tack B.F.
      J. Biol. Chem. 260:2108-2112(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 412-1676, VARIANT ILE-802.
    7. "Primary structural analysis of the polypeptide portion of human C5a anaphylatoxin. Polypeptide sequence determination and assignment of the oligosaccharide attachment site in C5a."
      Fernandez H.N., Hugli T.E.
      J. Biol. Chem. 253:6955-6964(1978) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 678-751.
    8. "Group B streptococci inactivate complement component C5a by enzymic cleavage at the C-terminus."
      Bohnsack J.F., Mollison K.W., Buko A.M., Ashworth J.C., Hill H.R.
      Biochem. J. 273:635-640(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 678-751.
    9. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-741; ASN-911 AND ASN-1630.
      Tissue: Plasma.
    10. "Sequence-specific assignments in the 1H NMR spectrum of the human inflammatory protein C5a."
      Zuiderweg E.R.P., Mollison K.W., Henkin J., Carter G.W.
      Biochemistry 27:3568-3580(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF C5A.
    11. "Tertiary structure of human complement component C5a in solution from nuclear magnetic resonance data."
      Zuiderweg E.R.P., Nettesheim D.G., Mollison K.W., Carter G.W.
      Biochemistry 28:172-185(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF C5A.
    12. "Heteronuclear three-dimensional NMR spectroscopy of the inflammatory protein C5a."
      Zuiderweg E.R.P., Fesik S.W.
      Biochemistry 28:2387-2391(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF C5A.
    13. "Solution structure of a unique C5a semi-synthetic antagonist: implications in receptor binding."
      Zhang X., Boyar W., Galakatos N., Gonnella N.C.
      Protein Sci. 6:65-72(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 679-747 OF C5A, DISULFIDE BONDS.
    14. "Structural definition of the C5a C-terminus by two-dimensional nuclear magnetic resonance spectroscopy."
      Zhang X., Boyar W., Toth M.J., Wennogle L., Gonnella N.C.
      Proteins 28:261-267(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 679-751 OF C5A, DISULFIDE BONDS.
    15. "Inherited human complement C5 deficiency. Nonsense mutations in exons 1 (Gln1 to Stop) and 36 (Arg1458 to Stop) and compound heterozygosity in three African-American families."
      Wang X., Fleischer D.T., Whitehead W.T., Haviland D.L., Rosenfeld S.I., Leddy J.P., Snyderman R., Wetsel R.A.
      J. Immunol. 154:5464-5471(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN COMPLEMENT C5 DEFICIENCY.
    16. Cited for: INVOLVEMENT IN COMPLEMENT C5 DEFICIENCY.
    17. "C5 complement deficiency in a Spanish family. Molecular characterization of the double mutation responsible for the defect."
      Delgado-Cervino E., Fontan G., Lopez-Trascasa M.
      Mol. Immunol. 42:105-111(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN COMPLEMENT C5 DEFICIENCY, VARIANTS ILE-389 AND ILE-802.
    18. Cited for: ASSOCIATION WITH SUSCEPTIBILITY TO LIVER FIBROSIS.
    19. "Functional insights from the structure of the multifunctional C345C domain of C5 of complement."
      Bramham J., Thai C.-T., Soares D.C., Uhrin D., Ogata R.T., Barlow P.N.
      J. Biol. Chem. 280:10636-10645(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1530-1676, DISULFIDE BONDS.
    20. Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS), INTERACTION WITH TICK COMPLEMENT INHIBITOR, GLYCOSYLATION AT ASN-741 AND ASN-911, DISULFIDE BONDS.
    21. "Substrate recognition by complement convertases revealed in the C5-cobra venom factor complex."
      Laursen N.S., Andersen K.R., Braren I., Spillner E., Sottrup-Jensen L., Andersen G.R.
      EMBO J. 30:606-616(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (4.30 ANGSTROMS) OF 20-1676 IN COMPLEX WITH COBRA VENOM FACTOR, GLYCOSYLATION AT ASN-911, DISULFIDE BONDS.
    22. "Quantitative detection of single amino acid polymorphisms by targeted proteomics."
      Su Z.D., Sun L., Yu D.X., Li R.X., Li H.X., Yu Z.J., Sheng Q.H., Lin X., Zeng R., Wu J.R.
      J. Mol. Cell Biol. 3:309-315(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT TYR-966, IDENTIFICATION BY MASS SPECTROMETRY.
    23. Cited for: VARIANTS CYS-885 AND HIS-885, INVOLVEMENT IN POOR RESPONSE TO ECULIZUMAB.

    Entry informationi

    Entry nameiCO5_HUMAN
    AccessioniPrimary (citable) accession number: P01031
    Secondary accession number(s): Q14CJ0, Q27I61
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: February 5, 2008
    Last modified: October 1, 2014
    This is version 169 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3