Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Complement C5

Gene

C5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. Binding to the receptor C5AR1 induces a variety of responses including intracellular calcium release, contraction of smooth muscle, increased vascular permeability, and histamine release from mast cells and basophilic leukocytes (PubMed:8182049). C5a is also a potent chemokine which stimulates the locomotion of polymorphonuclear leukocytes and directs their migration toward sites of inflammation.1 Publication

GO - Molecular functioni

  • chemokine activity Source: ProtInc
  • endopeptidase inhibitor activity Source: InterPro
  • receptor binding Source: ProtInc

GO - Biological processi

  • activation of MAPK activity Source: ProtInc
  • cell surface receptor signaling pathway Source: ProtInc
  • chemotaxis Source: ProtInc
  • complement activation Source: Reactome
  • complement activation, alternative pathway Source: UniProtKB-KW
  • complement activation, classical pathway Source: UniProtKB-KW
  • cytolysis Source: UniProtKB-KW
  • G-protein coupled receptor signaling pathway Source: ProtInc
  • inflammatory response Source: ProtInc
  • in utero embryonic development Source: Ensembl
  • negative regulation of macrophage chemotaxis Source: BHF-UCL
  • positive regulation of angiogenesis Source: Ensembl
  • positive regulation of chemokine secretion Source: BHF-UCL
  • positive regulation of vascular endothelial growth factor production Source: BHF-UCL
  • regulation of complement activation Source: Reactome
  • response to stress Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

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

Enzyme and pathway databases

BioCyciMOUSE:MONOMER-12977.
ZFISH:ENSG00000106804-MONOMER.
BRENDAi3.4.21.43. 2681.
ReactomeiR-HSA-166665. Terminal pathway of complement.
R-HSA-174577. Activation of C3 and C5.
R-HSA-375276. Peptide ligand-binding receptors.
R-HSA-418594. G alpha (i) signalling events.
R-HSA-977606. Regulation of Complement cascade.
SIGNORiP01031.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:1331. C5.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: ProtInc
  • membrane attack complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane attack complex, Secreted

Pathology & Biotechi

Involvement in diseasei

Complement component 5 deficiency (C5D)
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare defect of the complement classical pathway associated with susceptibility to severe recurrent infections, predominantly by Neisseria gonorrhoeae or Neisseria meningitidis.
See also OMIM:609536

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.

Organism-specific databases

DisGeNETi727.
MalaCardsiC5.
MIMi609536. phenotype.
615749. phenotype.
OpenTargetsiENSG00000106804.
Orphaneti169150. Immunodeficiency due to a late component of complements deficiency.
PharmGKBiPA25911.

Chemistry databases

ChEMBLiCHEMBL2364163.
DrugBankiDB01257. Eculizumab.
DB00028. Intravenous Immunoglobulin.

Polymorphism and mutation databases

BioMutaiC5.
DMDMi166900096.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
ChainiPRO_000000598519 – 673Complement C5 beta chainAdd BLAST655
PropeptideiPRO_0000005986674 – 6771 Publication4
ChainiPRO_0000005987678 – 1676Complement C5 alpha chainAdd BLAST999
ChainiPRO_0000005988678 – 751C5a anaphylatoxinAdd BLAST74
ChainiPRO_0000005989752 – 1676Complement C5 alpha' chainAdd BLAST925

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi567 ↔ 810
Disulfide bondi634 ↔ 669
Disulfide bondi698 ↔ 724
Disulfide bondi699 ↔ 731
Disulfide bondi711 ↔ 732
Glycosylationi741N-linked (GlcNAc...)2 Publications1
Disulfide bondi856 ↔ 883
Disulfide bondi866 ↔ 1527
Glycosylationi911N-linked (GlcNAc...)3 Publications1
Disulfide bondi1101 ↔ 1159
Glycosylationi1115N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1375 ↔ 1505
Disulfide bondi1405 ↔ 1474
Disulfide bondi1520 ↔ 1525
Disulfide bondi1532 ↔ 1606
Disulfide bondi1553 ↔ 1676
Glycosylationi1630N-linked (GlcNAc...)1 Publication1
Disulfide bondi1654 ↔ 1657

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP01031.
PaxDbiP01031.
PeptideAtlasiP01031.
PRIDEiP01031.

PTM databases

iPTMnetiP01031.
PhosphoSitePlusiP01031.

Miscellaneous databases

PMAP-CutDBP01031.

Expressioni

Gene expression databases

BgeeiENSG00000106804.
CleanExiHS_C5.
GenevisibleiP01031. HS.

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). The C5a anaphylatoxin interacts with C5AR1. Interacts with tick complement inhibitor.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q911322EBI-8558308,EBI-7081824From a different organism.
CREB3L1Q96BA83EBI-8558308,EBI-6942903

GO - Molecular functioni

  • chemokine activity Source: ProtInc
  • receptor binding Source: ProtInc

Protein-protein interaction databases

BioGridi107188. 7 interactors.
IntActiP01031. 5 interactors.
STRINGi9606.ENSP00000223642.

Structurei

Secondary structure

11676
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi22 – 32Combined sources11
Beta strandi36 – 45Combined sources10
Beta strandi50 – 58Combined sources9
Turni59 – 61Combined sources3
Beta strandi64 – 73Combined sources10
Turni75 – 79Combined sources5
Beta strandi80 – 86Combined sources7
Helixi89 – 91Combined sources3
Beta strandi95 – 97Combined sources3
Beta strandi101 – 110Combined sources10
Beta strandi112 – 120Combined sources9
Beta strandi124 – 131Combined sources8
Beta strandi133 – 135Combined sources3
Beta strandi143 – 148Combined sources6
Beta strandi152 – 154Combined sources3
Beta strandi159 – 164Combined sources6
Beta strandi170 – 176Combined sources7
Beta strandi179 – 184Combined sources6
Beta strandi197 – 208Combined sources12
Beta strandi212 – 219Combined sources8
Beta strandi226 – 234Combined sources9
Beta strandi236 – 238Combined sources3
Turni241 – 244Combined sources4
Beta strandi246 – 254Combined sources9
Turni255 – 257Combined sources3
Beta strandi262 – 273Combined sources12
Beta strandi275 – 277Combined sources3
Beta strandi281 – 283Combined sources3
Beta strandi289 – 293Combined sources5
Beta strandi296 – 301Combined sources6
Helixi303 – 307Combined sources5
Turni308 – 310Combined sources3
Beta strandi314 – 318Combined sources5
Beta strandi322 – 331Combined sources10
Turni332 – 334Combined sources3
Beta strandi337 – 347Combined sources11
Beta strandi353 – 356Combined sources4
Beta strandi361 – 363Combined sources3
Beta strandi365 – 367Combined sources3
Beta strandi369 – 376Combined sources8
Beta strandi378 – 380Combined sources3
Beta strandi387 – 396Combined sources10
Beta strandi401 – 403Combined sources3
Beta strandi407 – 410Combined sources4
Turni413 – 415Combined sources3
Beta strandi416 – 422Combined sources7
Beta strandi428 – 437Combined sources10
Helixi444 – 446Combined sources3
Beta strandi449 – 456Combined sources8
Beta strandi464 – 468Combined sources5
Beta strandi472 – 476Combined sources5
Beta strandi480 – 492Combined sources13
Helixi493 – 495Combined sources3
Beta strandi498 – 505Combined sources8
Beta strandi508 – 516Combined sources9
Beta strandi519 – 522Combined sources4
Beta strandi524 – 529Combined sources6
Helixi532 – 534Combined sources3
Beta strandi536 – 546Combined sources11
Beta strandi548 – 550Combined sources3
Beta strandi553 – 563Combined sources11
Beta strandi571 – 577Combined sources7
Beta strandi580 – 582Combined sources3
Beta strandi587 – 606Combined sources20
Helixi607 – 610Combined sources4
Helixi614 – 616Combined sources3
Helixi623 – 627Combined sources5
Helixi628 – 630Combined sources3
Beta strandi635 – 637Combined sources3
Helixi642 – 648Combined sources7
Beta strandi651 – 657Combined sources7
Turni663 – 666Combined sources4
Helixi678 – 687Combined sources10
Turni689 – 692Combined sources4
Helixi693 – 703Combined sources11
Beta strandi707 – 709Combined sources3
Helixi711 – 715Combined sources5
Helixi722 – 740Combined sources19
Helixi744 – 757Combined sources14
Beta strandi764 – 767Combined sources4
Beta strandi777 – 789Combined sources13
Beta strandi795 – 805Combined sources11
Beta strandi808 – 811Combined sources4
Beta strandi815 – 819Combined sources5
Beta strandi822 – 828Combined sources7
Beta strandi838 – 847Combined sources10
Beta strandi849 – 851Combined sources3
Beta strandi853 – 859Combined sources7
Beta strandi863 – 869Combined sources7
Beta strandi874 – 877Combined sources4
Beta strandi886 – 888Combined sources3
Beta strandi892 – 902Combined sources11
Beta strandi906 – 916Combined sources11
Beta strandi919 – 930Combined sources12
Beta strandi932 – 945Combined sources14
Beta strandi949 – 952Combined sources4
Beta strandi956 – 959Combined sources4
Beta strandi974 – 982Combined sources9
Helixi985 – 992Combined sources8
Beta strandi993 – 996Combined sources4
Turni999 – 1002Combined sources4
Helixi1008 – 1013Combined sources6
Helixi1016 – 1027Combined sources12
Helixi1031 – 1033Combined sources3
Beta strandi1034 – 1036Combined sources3
Helixi1038 – 1054Combined sources17
Helixi1055 – 1059Combined sources5
Beta strandi1066 – 1069Combined sources4
Helixi1076 – 1089Combined sources14
Turni1090 – 1092Combined sources3
Helixi1097 – 1110Combined sources14
Beta strandi1121 – 1123Combined sources3
Helixi1133 – 1154Combined sources22
Helixi1155 – 1158Combined sources4
Helixi1162 – 1178Combined sources17
Helixi1185 – 1196Combined sources12
Helixi1203 – 1214Combined sources12
Beta strandi1217 – 1219Combined sources3
Turni1220 – 1223Combined sources4
Beta strandi1224 – 1227Combined sources4
Turni1233 – 1235Combined sources3
Helixi1245 – 1260Combined sources16
Helixi1264 – 1277Combined sources14
Beta strandi1280 – 1282Combined sources3
Helixi1287 – 1303Combined sources17
Beta strandi1310 – 1317Combined sources8
Beta strandi1324 – 1332Combined sources9
Beta strandi1338 – 1340Combined sources3
Beta strandi1342 – 1344Combined sources3
Beta strandi1346 – 1350Combined sources5
Beta strandi1357 – 1368Combined sources12
Beta strandi1371 – 1373Combined sources3
Beta strandi1376 – 1384Combined sources9
Beta strandi1401 – 1408Combined sources8
Beta strandi1420 – 1427Combined sources8
Beta strandi1432 – 1434Combined sources3
Helixi1436 – 1443Combined sources8
Beta strandi1451 – 1456Combined sources6
Beta strandi1459 – 1465Combined sources7
Beta strandi1469 – 1471Combined sources3
Beta strandi1473 – 1483Combined sources11
Beta strandi1485 – 1487Combined sources3
Beta strandi1491 – 1497Combined sources7
Beta strandi1500 – 1509Combined sources10
Beta strandi1522 – 1524Combined sources3
Turni1526 – 1529Combined sources4
Beta strandi1530 – 1532Combined sources3
Helixi1547 – 1550Combined sources4
Beta strandi1559 – 1571Combined sources13
Beta strandi1574 – 1590Combined sources17
Beta strandi1597 – 1605Combined sources9
Beta strandi1616 – 1622Combined sources7
Beta strandi1625 – 1629Combined sources5
Beta strandi1632 – 1638Combined sources7
Beta strandi1644 – 1647Combined sources4
Beta strandi1650 – 1652Combined sources3
Helixi1657 – 1672Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4UU9X-ray2.12C/D678-751[»]
5HCCX-ray2.59A679-1676[»]
B19-674[»]
5HCDX-ray2.98A679-1676[»]
B19-674[»]
5HCEX-ray3.12A679-1676[»]
B19-674[»]
5I5KX-ray4.20A/B1-1676[»]
ProteinModelPortaliP01031.
SMRiP01031.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01031.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini698 – 732Anaphylatoxin-likePROSITE-ProRule annotationAdd BLAST35
Domaini1532 – 1676NTRPROSITE-ProRule annotationAdd BLAST145

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni692 – 721Involved in C5AR1 binding1 PublicationAdd BLAST30

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1366. Eukaryota.
ENOG410XRED. LUCA.
GeneTreeiENSGT00760000118982.
HOGENOMiHOG000231860.
HOVERGENiHBG098067.
InParanoidiP01031.
KOiK03994.
OMAiVFYVFHY.
OrthoDBiEOG091G00BU.
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.
SMARTiSM01360. A2M. 1 hit.
SM01359. A2M_N_2. 1 hit.
SM01361. A2M_recep. 1 hit.
SM00104. 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

« Hide

        10         20         30         40         50
MGLLGILCFL IFLGKTWGQE QTYVISAPKI FRVGASENIV IQVYGYTEAF
60 70 80 90 100
DATISIKSYP DKKFSYSSGH VHLSSENKFQ NSAILTIQPK QLPGGQNPVS
110 120 130 140 150
YVYLEVVSKH FSKSKRMPIT YDNGFLFIHT DKPVYTPDQS VKVRVYSLND
160 170 180 190 200
DLKPAKRETV LTFIDPEGSE VDMVEEIDHI GIISFPDFKI PSNPRYGMWT
210 220 230 240 250
IKAKYKEDFS TTGTAYFEVK EYVLPHFSVS IEPEYNFIGY KNFKNFEITI
260 270 280 290 300
KARYFYNKVV TEADVYITFG IREDLKDDQK EMMQTAMQNT MLINGIAQVT
310 320 330 340 350
FDSETAVKEL SYYSLEDLNN KYLYIAVTVI ESTGGFSEEA EIPGIKYVLS
360 370 380 390 400
PYKLNLVATP LFLKPGIPYP IKVQVKDSLD QLVGGVPVTL NAQTIDVNQE
410 420 430 440 450
TSDLDPSKSV TRVDDGVASF VLNLPSGVTV LEFNVKTDAP DLPEENQARE
460 470 480 490 500
GYRAIAYSSL SQSYLYIDWT DNHKALLVGE HLNIIVTPKS PYIDKITHYN
510 520 530 540 550
YLILSKGKII HFGTREKFSD ASYQSINIPV TQNMVPSSRL LVYYIVTGEQ
560 570 580 590 600
TAELVSDSVW LNIEEKCGNQ LQVHLSPDAD AYSPGQTVSL NMATGMDSWV
610 620 630 640 650
ALAAVDSAVY GVQRGAKKPL ERVFQFLEKS DLGCGAGGGL NNANVFHLAG
660 670 680 690 700
LTFLTNANAD DSQENDEPCK EILRPRRTLQ KKIEEIAAKY KHSVVKKCCY
710 720 730 740 750
DGACVNNDET CEQRAARISL GPRCIKAFTE CCVVASQLRA NISHKDMQLG
760 770 780 790 800
RLHMKTLLPV SKPEIRSYFP ESWLWEVHLV PRRKQLQFAL PDSLTTWEIQ
810 820 830 840 850
GVGISNTGIC VADTVKAKVF KDVFLEMNIP YSVVRGEQIQ LKGTVYNYRT
860 870 880 890 900
SGMQFCVKMS AVEGICTSES PVIDHQGTKS SKCVRQKVEG SSSHLVTFTV
910 920 930 940 950
LPLEIGLHNI NFSLETWFGK EILVKTLRVV PEGVKRESYS GVTLDPRGIY
960 970 980 990 1000
GTISRRKEFP YRIPLDLVPK TEIKRILSVK GLLVGEILSA VLSQEGINIL
1010 1020 1030 1040 1050
THLPKGSAEA ELMSVVPVFY VFHYLETGNH WNIFHSDPLI EKQKLKKKLK
1060 1070 1080 1090 1100
EGMLSIMSYR NADYSYSVWK GGSASTWLTA FALRVLGQVN KYVEQNQNSI
1110 1120 1130 1140 1150
CNSLLWLVEN YQLDNGSFKE NSQYQPIKLQ GTLPVEAREN SLYLTAFTVI
1160 1170 1180 1190 1200
GIRKAFDICP LVKIDTALIK ADNFLLENTL PAQSTFTLAI SAYALSLGDK
1210 1220 1230 1240 1250
THPQFRSIVS ALKREALVKG NPPIYRFWKD NLQHKDSSVP NTGTARMVET
1260 1270 1280 1290 1300
TAYALLTSLN LKDINYVNPV IKWLSEEQRY GGGFYSTQDT INAIEGLTEY
1310 1320 1330 1340 1350
SLLVKQLRLS MDIDVSYKHK GALHNYKMTD KNFLGRPVEV LLNDDLIVST
1360 1370 1380 1390 1400
GFGSGLATVH VTTVVHKTST SEEVCSFYLK IDTQDIEASH YRGYGNSDYK
1410 1420 1430 1440 1450
RIVACASYKP SREESSSGSS HAVMDISLPT GISANEEDLK ALVEGVDQLF
1460 1470 1480 1490 1500
TDYQIKDGHV ILQLNSIPSS DFLCVRFRIF ELFEVGFLSP ATFTVYEYHR
1510 1520 1530 1540 1550
PDKQCTMFYS TSNIKIQKVC EGAACKCVEA DCGQMQEELD LTISAETRKQ
1560 1570 1580 1590 1600
TACKPEIAYA YKVSITSITV ENVFVKYKAT LLDIYKTGEA VAEKDSEITF
1610 1620 1630 1640 1650
IKKVTCTNAE LVKGRQYLIM GKEALQIKYN FSFRYIYPLD SLTWIEYWPR
1660 1670
DTTCSSCQAF LANLDEFAED IFLNGC
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 (PubMed:24521109).1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_038735145V → I.1 PublicationCorresponds to variant rs17216529dbSNPEnsembl.1
Natural variantiVAR_048822354L → M.Corresponds to variant rs34552775dbSNPEnsembl.1
Natural variantiVAR_023946389T → I.2 Publications1
Natural variantiVAR_038736449R → G.1 PublicationCorresponds to variant rs2230213dbSNPEnsembl.1
Natural variantiVAR_001996518F → S.1
Natural variantiVAR_014574802V → I.7 PublicationsCorresponds to variant rs17611dbSNPEnsembl.1
Natural variantiVAR_071067885R → C Polymorphism associated with poor response to eculizumab in PNH patients. 1 PublicationCorresponds to variant rs373359894dbSNPEnsembl.1
Natural variantiVAR_071068885R → H Polymorphism associated with poor response to eculizumab in PNH patients. 1 PublicationCorresponds to variant rs56040400dbSNPEnsembl.1
Natural variantiVAR_038737928R → Q.1 PublicationCorresponds to variant rs41309892dbSNPEnsembl.1
Natural variantiVAR_038738933G → V.1 PublicationCorresponds to variant rs41309902dbSNPEnsembl.1
Natural variantiVAR_048823966D → Y Polymorphism; confirmed at protein level. 1 PublicationCorresponds to variant rs2230212dbSNPEnsembl.1
Natural variantiVAR_0387391033I → T.1 PublicationCorresponds to variant rs41311881dbSNPEnsembl.1
Natural variantiVAR_0387401037D → N.1 PublicationCorresponds to variant rs41311883dbSNPEnsembl.1
Natural variantiVAR_0387411043Q → K.1 PublicationCorresponds to variant rs41311887dbSNPEnsembl.1
Natural variantiVAR_0145751053M → L.Corresponds to variant rs17609dbSNPEnsembl.1
Natural variantiVAR_0145761310S → N.1 PublicationCorresponds to variant rs17610dbSNPEnsembl.1
Natural variantiVAR_0488241365V → A.Corresponds to variant rs16910245dbSNPEnsembl.1
Natural variantiVAR_0145771437E → D.1 PublicationCorresponds to variant rs17612dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001304092.1. NM_001317163.1.
NP_001726.2. NM_001735.2.
UniGeneiHs.494997.

Genome annotation databases

EnsembliENST00000223642; ENSP00000223642; ENSG00000106804.
GeneIDi727.
KEGGihsa:727.
UCSCiuc004bkv.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

C5base

C5 mutation db

Wikipedia

Complement C5 entry

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001304092.1. NM_001317163.1.
NP_001726.2. NM_001735.2.
UniGeneiHs.494997.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4UU9X-ray2.12C/D678-751[»]
5HCCX-ray2.59A679-1676[»]
B19-674[»]
5HCDX-ray2.98A679-1676[»]
B19-674[»]
5HCEX-ray3.12A679-1676[»]
B19-674[»]
5I5KX-ray4.20A/B1-1676[»]
ProteinModelPortaliP01031.
SMRiP01031.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107188. 7 interactors.
IntActiP01031. 5 interactors.
STRINGi9606.ENSP00000223642.

Chemistry databases

ChEMBLiCHEMBL2364163.
DrugBankiDB01257. Eculizumab.
DB00028. Intravenous Immunoglobulin.

Protein family/group databases

MEROPSiI39.952.

PTM databases

iPTMnetiP01031.
PhosphoSitePlusiP01031.

Polymorphism and mutation databases

BioMutaiC5.
DMDMi166900096.

Proteomic databases

MaxQBiP01031.
PaxDbiP01031.
PeptideAtlasiP01031.
PRIDEiP01031.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000223642; ENSP00000223642; ENSG00000106804.
GeneIDi727.
KEGGihsa:727.
UCSCiuc004bkv.4. human.

Organism-specific databases

CTDi727.
DisGeNETi727.
GeneCardsiC5.
H-InvDBHIX0025739.
HGNCiHGNC:1331. C5.
HPAiHPA029339.
MalaCardsiC5.
MIMi120900. gene.
609536. phenotype.
615749. phenotype.
neXtProtiNX_P01031.
OpenTargetsiENSG00000106804.
Orphaneti169150. Immunodeficiency due to a late component of complements deficiency.
PharmGKBiPA25911.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1366. Eukaryota.
ENOG410XRED. LUCA.
GeneTreeiENSGT00760000118982.
HOGENOMiHOG000231860.
HOVERGENiHBG098067.
InParanoidiP01031.
KOiK03994.
OMAiVFYVFHY.
OrthoDBiEOG091G00BU.
PhylomeDBiP01031.
TreeFamiTF313285.

Enzyme and pathway databases

BioCyciMOUSE:MONOMER-12977.
ZFISH:ENSG00000106804-MONOMER.
BRENDAi3.4.21.43. 2681.
ReactomeiR-HSA-166665. Terminal pathway of complement.
R-HSA-174577. Activation of C3 and C5.
R-HSA-375276. Peptide ligand-binding receptors.
R-HSA-418594. G alpha (i) signalling events.
R-HSA-977606. Regulation of Complement cascade.
SIGNORiP01031.

Miscellaneous databases

EvolutionaryTraceiP01031.
GeneWikiiComplement_component_5.
GenomeRNAii727.
PMAP-CutDBP01031.
PROiP01031.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000106804.
CleanExiHS_C5.
GenevisibleiP01031. HS.

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.
SMARTiSM01360. A2M. 1 hit.
SM01359. A2M_N_2. 1 hit.
SM01361. A2M_recep. 1 hit.
SM00104. 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]
ProtoNetiSearch...

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: November 30, 2016
This is version 191 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.