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P01031

- CO5_HUMAN

UniProt

P01031 - CO5_HUMAN

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Protein
Complement C5
Gene
C5, CPAMD4
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. 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
Complete GO annotation...

GO - Biological processi

  1. G-protein coupled receptor signaling pathway Source: ProtInc
  2. activation of MAPK activity Source: ProtInc
  3. cell chemotaxis Source: GOC
  4. cell surface receptor signaling pathway Source: ProtInc
  5. cellular calcium ion homeostasis Source: Ensembl
  6. chemotaxis Source: ProtInc
  7. complement activation Source: Reactome
  8. complement activation, alternative pathway Source: UniProtKB-KW
  9. complement activation, classical pathway Source: UniProtKB-KW
  10. cytolysis Source: UniProtKB-KW
  11. glucose homeostasis Source: Ensembl
  12. in utero embryonic development Source: Ensembl
  13. inflammatory response Source: ProtInc
  14. innate immune response Source: Reactome
  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: UniProt
  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 – 1818 Reviewed prediction
Add
BLAST
Chaini19 – 673655Complement C5 beta chain
PRO_0000005985Add
BLAST
Propeptidei674 – 6774
PRO_0000005986
Chaini678 – 1676999Complement C5 alpha chain
PRO_0000005987Add
BLAST
Chaini678 – 75174C5a anaphylatoxin
PRO_0000005988Add
BLAST
Chaini752 – 1676925Complement C5 alpha' chain
PRO_0000005989Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi567 ↔ 8105 Publications
Disulfide bondi634 ↔ 6695 Publications
Disulfide bondi698 ↔ 7245 Publications
Disulfide bondi699 ↔ 7315 Publications
Disulfide bondi711 ↔ 7325 Publications
Glycosylationi741 – 7411N-linked (GlcNAc...)2 Publications
Disulfide bondi856 ↔ 8835 Publications
Disulfide bondi866 ↔ 15275 Publications
Glycosylationi911 – 9111N-linked (GlcNAc...)3 Publications
Disulfide bondi1101 ↔ 11595 Publications
Glycosylationi1115 – 11151N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1375 ↔ 15055 Publications
Disulfide bondi1405 ↔ 14745 Publications
Disulfide bondi1520 ↔ 15255 Publications
Disulfide bondi1532 ↔ 16065 Publications
Disulfide bondi1553 ↔ 16765 Publications
Glycosylationi1630 – 16301N-linked (GlcNAc...)1 Publication
Disulfide bondi1654 ↔ 16575 Publications

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.1 Publication

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

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.

Miscellaneous databases

EvolutionaryTraceiP01031.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini698 – 73235Anaphylatoxin-like
Add
BLAST
Domaini1532 – 1676145NTR
Add
BLAST

Sequence similaritiesi

Contains 1 NTR domain.

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.
Corresponds to variant rs373359894 [ dbSNP | Ensembl ].
VAR_071067
Natural varianti885 – 8851R → H Polymorphism associated with poor response to eculizumab in PNH patients.
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...

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

« 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. "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: September 3, 2014
This is version 168 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

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