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P01031 (CO5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 164. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Complement C5
Alternative name(s):
C3 and PZP-like alpha-2-macroglobulin domain-containing protein 4
Gene names
Name:C5
Synonyms:CPAMD4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1676 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). Interacts with tick complement inhibitor. Ref.20

Subcellular location

Secreted.

Involvement in disease

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 (Ref.18).

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
   Coding sequence diversityPolymorphism
   DomainSignal
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Traceable author statement PubMed 8898085. Source: ProtInc

activation of MAPK activity

Traceable author statement PubMed 7649993. Source: ProtInc

cell chemotaxis

Traceable author statement PubMed 10820279. Source: GOC

cell surface receptor signaling pathway

Traceable author statement PubMed 10820279. Source: ProtInc

cellular calcium ion homeostasis

Inferred from electronic annotation. Source: Ensembl

chemotaxis

Traceable author statement PubMed 10820279. Source: ProtInc

complement activation

Traceable author statement. Source: Reactome

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 electronic annotation. Source: Ensembl

inflammatory response

Traceable author statement PubMed 8759757. Source: ProtInc

innate immune response

Traceable author statement. Source: Reactome

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 direct assay PubMed 14566334. Source: BHF-UCL

negative regulation of norepinephrine secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of angiogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of chemokine secretion

Inferred from direct assay PubMed 14566334. Source: BHF-UCL

positive regulation of chemotaxis

Inferred from electronic annotation. Source: Ensembl

positive regulation vascular endothelial growth factor production

Inferred from direct assay PubMed 14566334PubMed 16452172. Source: BHF-UCL

regulation of complement activation

Traceable author statement. Source: Reactome

response to stress

Traceable author statement PubMed 9590258. Source: ProtInc

   Cellular_componentextracellular region

Traceable author statement. Source: Reactome

extracellular space

Traceable author statement PubMed 9218605. Source: ProtInc

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

membrane attack complex

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionchemokine activity

Traceable author statement PubMed 10820279. Source: ProtInc

endopeptidase inhibitor activity

Inferred from electronic annotation. Source: InterPro

receptor binding

Traceable author statement PubMed 10820279PubMed 9590258. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Q911322EBI-8558308,EBI-7081824From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 673655Complement C5 beta chain
PRO_0000005985
Propeptide674 – 6774
PRO_0000005986
Chain678 – 1676999Complement C5 alpha chain
PRO_0000005987
Chain678 – 75174C5a anaphylatoxin
PRO_0000005988
Chain752 – 1676925Complement C5 alpha' chain
PRO_0000005989

Regions

Domain698 – 73235Anaphylatoxin-like
Domain1532 – 1676145NTR

Amino acid modifications

Glycosylation7411N-linked (GlcNAc...) Ref.9 Ref.20
Glycosylation9111N-linked (GlcNAc...) Ref.9 Ref.20 Ref.21
Glycosylation11151N-linked (GlcNAc...) Potential
Glycosylation16301N-linked (GlcNAc...) Ref.9
Disulfide bond567 ↔ 810 Ref.13 Ref.14 Ref.19 Ref.20 Ref.21
Disulfide bond634 ↔ 669 Ref.13 Ref.14 Ref.19 Ref.20 Ref.21
Disulfide bond698 ↔ 724 Ref.13 Ref.14 Ref.19 Ref.20 Ref.21
Disulfide bond699 ↔ 731 Ref.13 Ref.14 Ref.19 Ref.20 Ref.21
Disulfide bond711 ↔ 732 Ref.13 Ref.14 Ref.19 Ref.20 Ref.21
Disulfide bond856 ↔ 883 Ref.13 Ref.14 Ref.19 Ref.20 Ref.21
Disulfide bond866 ↔ 1527 Ref.13 Ref.14 Ref.19 Ref.20 Ref.21
Disulfide bond1101 ↔ 1159 Ref.13 Ref.14 Ref.19 Ref.20 Ref.21
Disulfide bond1375 ↔ 1505 Ref.13 Ref.14 Ref.19 Ref.20 Ref.21
Disulfide bond1405 ↔ 1474 Ref.13 Ref.14 Ref.19 Ref.20 Ref.21
Disulfide bond1520 ↔ 1525 Ref.13 Ref.14 Ref.19 Ref.20 Ref.21
Disulfide bond1532 ↔ 1606 Ref.13 Ref.14 Ref.19 Ref.20 Ref.21
Disulfide bond1553 ↔ 1676 Ref.13 Ref.14 Ref.19 Ref.20 Ref.21
Disulfide bond1654 ↔ 1657 Ref.13 Ref.14 Ref.19 Ref.20 Ref.21

Natural variations

Natural variant1451V → I. Ref.2
Corresponds to variant rs17216529 [ dbSNP | Ensembl ].
VAR_038735
Natural variant3541L → M.
Corresponds to variant rs34552775 [ dbSNP | Ensembl ].
VAR_048822
Natural variant3891T → I. Ref.1 Ref.17
VAR_023946
Natural variant4491R → G. Ref.2
Corresponds to variant rs2230213 [ dbSNP | Ensembl ].
VAR_038736
Natural variant5181F → S.
VAR_001996
Natural variant8021V → I. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.17
Corresponds to variant rs17611 [ dbSNP | Ensembl ].
VAR_014574
Natural variant9281R → Q. Ref.2
Corresponds to variant rs41309892 [ dbSNP | Ensembl ].
VAR_038737
Natural variant9331G → V. Ref.2
Corresponds to variant rs41309902 [ dbSNP | Ensembl ].
VAR_038738
Natural variant9661D → Y Polymorphism confirmed at protein level. Ref.22
Corresponds to variant rs2230212 [ dbSNP | Ensembl ].
VAR_048823
Natural variant10331I → T. Ref.2
Corresponds to variant rs41311881 [ dbSNP | Ensembl ].
VAR_038739
Natural variant10371D → N. Ref.2
Corresponds to variant rs41311883 [ dbSNP | Ensembl ].
VAR_038740
Natural variant10431Q → K. Ref.2
Corresponds to variant rs41311887 [ dbSNP | Ensembl ].
VAR_038741
Natural variant10531M → L.
Corresponds to variant rs17609 [ dbSNP | Ensembl ].
VAR_014575
Natural variant13101S → N. Ref.2
Corresponds to variant rs17610 [ dbSNP | Ensembl ].
VAR_014576
Natural variant13651V → A.
Corresponds to variant rs16910245 [ dbSNP | Ensembl ].
VAR_048824
Natural variant14371E → D. Ref.2
Corresponds to variant rs17612 [ dbSNP | Ensembl ].
VAR_014577

Secondary structure

................................................................................................................................................................................................................................................................................................................. 1676
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P01031 [UniParc].

Last modified February 5, 2008. Version 4.
Checksum: A7589E352F74672A

FASTA1,676188,305
        10         20         30         40         50         60 
MGLLGILCFL IFLGKTWGQE QTYVISAPKI FRVGASENIV IQVYGYTEAF DATISIKSYP 

        70         80         90        100        110        120 
DKKFSYSSGH VHLSSENKFQ NSAILTIQPK QLPGGQNPVS YVYLEVVSKH FSKSKRMPIT 

       130        140        150        160        170        180 
YDNGFLFIHT DKPVYTPDQS VKVRVYSLND DLKPAKRETV LTFIDPEGSE VDMVEEIDHI 

       190        200        210        220        230        240 
GIISFPDFKI PSNPRYGMWT IKAKYKEDFS TTGTAYFEVK EYVLPHFSVS IEPEYNFIGY 

       250        260        270        280        290        300 
KNFKNFEITI KARYFYNKVV TEADVYITFG IREDLKDDQK EMMQTAMQNT MLINGIAQVT 

       310        320        330        340        350        360 
FDSETAVKEL SYYSLEDLNN KYLYIAVTVI ESTGGFSEEA EIPGIKYVLS PYKLNLVATP 

       370        380        390        400        410        420 
LFLKPGIPYP IKVQVKDSLD QLVGGVPVTL NAQTIDVNQE TSDLDPSKSV TRVDDGVASF 

       430        440        450        460        470        480 
VLNLPSGVTV LEFNVKTDAP DLPEENQARE GYRAIAYSSL SQSYLYIDWT DNHKALLVGE 

       490        500        510        520        530        540 
HLNIIVTPKS PYIDKITHYN YLILSKGKII HFGTREKFSD ASYQSINIPV TQNMVPSSRL 

       550        560        570        580        590        600 
LVYYIVTGEQ TAELVSDSVW LNIEEKCGNQ LQVHLSPDAD AYSPGQTVSL NMATGMDSWV 

       610        620        630        640        650        660 
ALAAVDSAVY GVQRGAKKPL ERVFQFLEKS DLGCGAGGGL NNANVFHLAG LTFLTNANAD 

       670        680        690        700        710        720 
DSQENDEPCK EILRPRRTLQ KKIEEIAAKY KHSVVKKCCY DGACVNNDET CEQRAARISL 

       730        740        750        760        770        780 
GPRCIKAFTE CCVVASQLRA NISHKDMQLG RLHMKTLLPV SKPEIRSYFP ESWLWEVHLV 

       790        800        810        820        830        840 
PRRKQLQFAL PDSLTTWEIQ GVGISNTGIC VADTVKAKVF KDVFLEMNIP YSVVRGEQIQ 

       850        860        870        880        890        900 
LKGTVYNYRT SGMQFCVKMS AVEGICTSES PVIDHQGTKS SKCVRQKVEG SSSHLVTFTV 

       910        920        930        940        950        960 
LPLEIGLHNI NFSLETWFGK EILVKTLRVV PEGVKRESYS GVTLDPRGIY GTISRRKEFP 

       970        980        990       1000       1010       1020 
YRIPLDLVPK TEIKRILSVK GLLVGEILSA VLSQEGINIL THLPKGSAEA ELMSVVPVFY 

      1030       1040       1050       1060       1070       1080 
VFHYLETGNH WNIFHSDPLI EKQKLKKKLK EGMLSIMSYR NADYSYSVWK GGSASTWLTA 

      1090       1100       1110       1120       1130       1140 
FALRVLGQVN KYVEQNQNSI CNSLLWLVEN YQLDNGSFKE NSQYQPIKLQ GTLPVEAREN 

      1150       1160       1170       1180       1190       1200 
SLYLTAFTVI GIRKAFDICP LVKIDTALIK ADNFLLENTL PAQSTFTLAI SAYALSLGDK 

      1210       1220       1230       1240       1250       1260 
THPQFRSIVS ALKREALVKG NPPIYRFWKD NLQHKDSSVP NTGTARMVET TAYALLTSLN 

      1270       1280       1290       1300       1310       1320 
LKDINYVNPV IKWLSEEQRY GGGFYSTQDT INAIEGLTEY SLLVKQLRLS MDIDVSYKHK 

      1330       1340       1350       1360       1370       1380 
GALHNYKMTD KNFLGRPVEV LLNDDLIVST GFGSGLATVH VTTVVHKTST SEEVCSFYLK 

      1390       1400       1410       1420       1430       1440 
IDTQDIEASH YRGYGNSDYK RIVACASYKP SREESSSGSS HAVMDISLPT GISANEEDLK 

      1450       1460       1470       1480       1490       1500 
ALVEGVDQLF TDYQIKDGHV ILQLNSIPSS DFLCVRFRIF ELFEVGFLSP ATFTVYEYHR 

      1510       1520       1530       1540       1550       1560 
PDKQCTMFYS TSNIKIQKVC EGAACKCVEA DCGQMQEELD LTISAETRKQ TACKPEIAYA 

      1570       1580       1590       1600       1610       1620 
YKVSITSITV ENVFVKYKAT LLDIYKTGEA VAEKDSEITF IKKVTCTNAE LVKGRQYLIM 

      1630       1640       1650       1660       1670 
GKEALQIKYN FSFRYIYPLD SLTWIEYWPR DTTCSSCQAF LANLDEFAED IFLNGC 

« Hide

References

« Hide 'large scale' references
[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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Linking C5 deficiency to an exonic splicing enhancer mutation."
Pfarr N., Prawitt D., Kirschfink M., Schroff C., Knuf M., Habermehl P., Mannhardt W., Zepp F., Fairbrother W., Loos M., Burge C.B., Pohlenz J.
J. Immunol. 174:4172-4177(2005) [PubMed] [Europe PMC] [Abstract]
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]"Complement factor 5 is a quantitative trait gene that modifies liver fibrogenesis in mice and humans."
Hillebrandt S., Wasmuth H.E., Weiskirchen R., Hellerbrand C., Keppeler H., Werth A., Schirin-Sokhan R., Wilkens G., Geier A., Lorenzen J., Koehl J., Gressner A.M., Matern S., Lammert F.
Nat. Genet. 37:835-843(2005) [PubMed] [Europe PMC] [Abstract]
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]"Structure of and influence of a tick complement inhibitor on human complement component 5."
Fredslund F., Laursen N.S., Roversi P., Jenner L., Oliveira C.L.P., Pedersen J.S., Nunn M.A., Lea S.M., Discipio R., Sottrup-Jensen L., Andersen G.R.
Nat. Immunol. 9:753-760(2008) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

C5base

C5 mutation db

Wikipedia

Complement C5 entry

SeattleSNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRC5HU. A40075.
RefSeqNP_001726.2. NM_001735.2.
UniGeneHs.494997.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP01031.
SMRP01031. Positions 20-676, 679-743, 1530-1676.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107188. 7 interactions.
IntActP01031. 2 interactions.
STRING9606.ENSP00000223642.

Chemistry

ChEMBLCHEMBL2364163.
DrugBankDB01257. Eculizumab.

Protein family/group databases

MEROPSI39.952.

PTM databases

PhosphoSiteP01031.

Polymorphism databases

DMDM166900096.

Proteomic databases

PaxDbP01031.
PRIDEP01031.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000223642; ENSP00000223642; ENSG00000106804.
GeneID727.
KEGGhsa:727.
UCSCuc004bkv.3. human.

Organism-specific databases

CTD727.
GeneCardsGC09M123714.
H-InvDBHIX0025739.
HGNCHGNC:1331. C5.
HPAHPA029339.
MIM120900. gene.
609536. phenotype.
neXtProtNX_P01031.
Orphanet169150. Immunodeficiency due to a late component of complements deficiency.
PharmGKBPA25911.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2373.
HOGENOMHOG000231860.
HOVERGENHBG098067.
InParanoidP01031.
KOK03994.
OMAFIHTDKP.
OrthoDBEOG77HDCX.
PhylomeDBP01031.
TreeFamTF313285.

Enzyme and pathway databases

BioCycMOUSE:MONOMER-12977.
ReactomeREACT_111102. Signal Transduction.
REACT_6900. Immune System.

Gene expression databases

BgeeP01031.
CleanExHS_C5.
GenevestigatorP01031.

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.
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]
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]
PRINTSPR00004. ANAPHYLATOXN.
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

EvolutionaryTraceP01031.
GeneWikiComplement_component_5.
GenomeRNAi727.
NextBio2960.
PMAP-CutDBP01031.
PROP01031.
SOURCESearch...

Entry information

Entry nameCO5_HUMAN
AccessionPrimary (citable) accession number: P01031
Secondary accession number(s): Q14CJ0, Q27I61
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 5, 2008
Last modified: April 16, 2014
This is version 164 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM