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P01031

- CO5_HUMAN

UniProt

P01031 - CO5_HUMAN

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Protein

Complement C5

Gene

C5

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. chemokine activity Source: ProtInc
  2. endopeptidase inhibitor activity Source: InterPro
  3. 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
Complete GO annotation...

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: UniProtKB
  4. 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) [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). 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.

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 – 3210Combined sources
Beta strandi41 – 433Combined sources
Beta strandi52 – 587Combined sources
Beta strandi61 – 666Combined sources
Turni75 – 795Combined sources
Beta strandi80 – 867Combined sources
Beta strandi93 – 975Combined sources
Beta strandi102 – 1109Combined sources
Beta strandi112 – 1176Combined sources
Beta strandi124 – 1318Combined sources
Beta strandi133 – 1353Combined sources
Beta strandi143 – 1486Combined sources
Beta strandi150 – 1534Combined sources
Beta strandi159 – 1646Combined sources
Beta strandi174 – 1763Combined sources
Beta strandi179 – 1846Combined sources
Beta strandi197 – 20812Combined sources
Beta strandi212 – 2198Combined sources
Beta strandi226 – 2294Combined sources
Beta strandi232 – 2343Combined sources
Beta strandi236 – 2383Combined sources
Turni241 – 2444Combined sources
Beta strandi247 – 2504Combined sources
Beta strandi252 – 2543Combined sources
Turni255 – 2573Combined sources
Beta strandi261 – 27313Combined sources
Beta strandi281 – 2855Combined sources
Beta strandi289 – 2935Combined sources
Beta strandi296 – 3005Combined sources
Turni303 – 3108Combined sources
Turni316 – 3183Combined sources
Beta strandi321 – 33414Combined sources
Beta strandi338 – 3425Combined sources
Beta strandi351 – 3544Combined sources
Beta strandi361 – 3633Combined sources
Beta strandi365 – 3673Combined sources
Beta strandi369 – 3779Combined sources
Beta strandi378 – 3803Combined sources
Beta strandi387 – 39610Combined sources
Beta strandi401 – 4033Combined sources
Beta strandi407 – 4104Combined sources
Beta strandi413 – 4153Combined sources
Beta strandi417 – 4226Combined sources
Beta strandi428 – 43710Combined sources
Helixi444 – 4463Combined sources
Beta strandi449 – 4568Combined sources
Beta strandi466 – 4694Combined sources
Beta strandi472 – 4765Combined sources
Beta strandi481 – 4877Combined sources
Beta strandi498 – 5058Combined sources
Beta strandi508 – 5169Combined sources
Beta strandi519 – 5224Combined sources
Beta strandi524 – 5296Combined sources
Helixi532 – 5343Combined sources
Beta strandi535 – 54612Combined sources
Beta strandi549 – 5513Combined sources
Beta strandi553 – 56311Combined sources
Beta strandi574 – 5774Combined sources
Beta strandi580 – 5823Combined sources
Beta strandi587 – 5937Combined sources
Beta strandi598 – 6025Combined sources
Beta strandi604 – 6063Combined sources
Turni607 – 6104Combined sources
Helixi614 – 6163Combined sources
Helixi620 – 6267Combined sources
Turni627 – 6304Combined sources
Beta strandi635 – 6373Combined sources
Beta strandi640 – 6423Combined sources
Helixi643 – 6486Combined sources
Beta strandi651 – 6544Combined sources
Beta strandi656 – 6583Combined sources
Beta strandi663 – 6653Combined sources
Helixi679 – 70224Combined sources
Beta strandi707 – 7093Combined sources
Helixi711 – 7155Combined sources
Helixi722 – 74019Combined sources
Helixi745 – 7484Combined sources
Beta strandi764 – 7663Combined sources
Beta strandi777 – 78913Combined sources
Beta strandi792 – 7998Combined sources
Beta strandi801 – 8055Combined sources
Beta strandi808 – 8114Combined sources
Beta strandi815 – 8195Combined sources
Beta strandi822 – 8287Combined sources
Beta strandi839 – 8479Combined sources
Beta strandi849 – 8513Combined sources
Beta strandi853 – 8619Combined sources
Beta strandi865 – 8695Combined sources
Beta strandi874 – 8774Combined sources
Beta strandi886 – 8883Combined sources
Beta strandi892 – 8954Combined sources
Beta strandi898 – 9025Combined sources
Beta strandi904 – 9063Combined sources
Beta strandi910 – 9167Combined sources
Beta strandi919 – 9257Combined sources
Beta strandi934 – 94512Combined sources
Turni949 – 9513Combined sources
Beta strandi957 – 9593Combined sources
Beta strandi974 – 9829Combined sources
Helixi985 – 9928Combined sources
Beta strandi993 – 9964Combined sources
Beta strandi1000 – 10023Combined sources
Helixi1009 – 10124Combined sources
Helixi1016 – 102712Combined sources
Helixi1031 – 10333Combined sources
Beta strandi1034 – 10363Combined sources
Helixi1038 – 105518Combined sources
Helixi1056 – 10594Combined sources
Beta strandi1064 – 10663Combined sources
Beta strandi1068 – 10725Combined sources
Helixi1076 – 109015Combined sources
Helixi1097 – 111014Combined sources
Helixi1133 – 115422Combined sources
Helixi1156 – 11583Combined sources
Helixi1162 – 117918Combined sources
Helixi1185 – 119511Combined sources
Helixi1203 – 121513Combined sources
Beta strandi1217 – 12193Combined sources
Turni1220 – 12234Combined sources
Beta strandi1224 – 12274Combined sources
Helixi1245 – 126016Combined sources
Helixi1264 – 127714Combined sources
Beta strandi1280 – 12823Combined sources
Turni1286 – 12894Combined sources
Helixi1290 – 130314Combined sources
Beta strandi1315 – 13206Combined sources
Beta strandi1322 – 13276Combined sources
Beta strandi1330 – 13323Combined sources
Beta strandi1338 – 13403Combined sources
Beta strandi1342 – 13443Combined sources
Beta strandi1346 – 13483Combined sources
Beta strandi1357 – 136812Combined sources
Beta strandi1371 – 13733Combined sources
Beta strandi1376 – 13849Combined sources
Beta strandi1401 – 14088Combined sources
Beta strandi1421 – 14277Combined sources
Beta strandi1432 – 14343Combined sources
Helixi1436 – 14438Combined sources
Beta strandi1449 – 14568Combined sources
Beta strandi1459 – 14657Combined sources
Beta strandi1469 – 14713Combined sources
Beta strandi1473 – 14808Combined sources
Beta strandi1491 – 14977Combined sources
Beta strandi1500 – 150910Combined sources
Turni1521 – 15244Combined sources
Helixi1525 – 15284Combined sources
Helixi1550 – 15534Combined sources
Beta strandi1559 – 15679Combined sources
Beta strandi1571 – 15733Combined sources
Beta strandi1576 – 158611Combined sources
Turni1589 – 15913Combined sources
Beta strandi1598 – 16014Combined sources
Beta strandi1618 – 16225Combined sources
Beta strandi1629 – 16324Combined sources
Beta strandi1644 – 16474Combined sources
Beta strandi1650 – 16567Combined sources
Helixi1659 – 16624Combined sources
Turni1663 – 16653Combined sources
Helixi1666 – 16716Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni692 – 72130Involved in C5AR1 binding1 PublicationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2373.
GeneTreeiENSGT00760000118982.
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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        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.

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:
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_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:
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 .
CCDSi CCDS6826.1.
PIRi A40075. C5HU.
RefSeqi NP_001726.2. NM_001735.2.
UniGenei Hs.494997.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
DB00028. Intravenous Immunoglobulin.

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.
GeneTreei ENSGT00760000118982.
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

« Hide 'large scale' publications
  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. "The amino terminus of the human C5a receptor is required for high affinity C5a binding and for receptor activation by C5a but not C5a analogs."
    DeMartino J.A., Van Riper G., Siciliano S.J., Molineaux C.J., Konteatis Z.D., Rosen H., Springer M.S.
    J. Biol. Chem. 269:14446-14450(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH C5AR1.
  10. "Residues 21-30 within the extracellular N-terminal region of the C5a receptor represent a binding domain for the C5a anaphylatoxin."
    Chen Z., Zhang X., Gonnella N.C., Pellas T.C., Boyar W.C., Ni F.
    J. Biol. Chem. 273:10411-10419(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH C5AR1.
  11. "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.
  12. "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.
  13. "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.
  14. "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.
  15. "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.
  16. "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.
  17. "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.
  18. Cited for: INVOLVEMENT IN COMPLEMENT C5 DEFICIENCY.
  19. "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.
  20. Cited for: ASSOCIATION WITH SUSCEPTIBILITY TO LIVER FIBROSIS.
  21. "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.
  22. Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS), INTERACTION WITH TICK COMPLEMENT INHIBITOR, GLYCOSYLATION AT ASN-741 AND ASN-911, DISULFIDE BONDS.
  23. "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.
  24. "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.
  25. 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: November 26, 2014
This is version 171 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

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