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Protein

Cobra venom factor

Gene
N/A
Organism
Naja kaouthia (Monocled cobra) (Naja siamensis)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Complement-activating protein in cobra venom. It is a structural and functional analog of complement component C3b, the activated form of C3. It binds factor B (CFB), which is subsequently cleaved by factor D (CFD) to form the bimolecular complex CVF/Bb. CVF/Bb is a C3/C5 convertase that cleaves both complement components C3 and C5. Structurally, it resembles the C3b degradation product C3c, which is not able to form a C3/C5 convertase. Unlike C3b/Bb, CVF/Bb is a stable complex and completely resistant to the actions of complement regulatory factors H (CFH) and I (CFI). Therefore, CVF continuously activates complement resulting in the depletion of complement activity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi516 – 5161Magnesium; via carbonyl oxygen
Metal bindingi539 – 5391Magnesium
Metal bindingi540 – 5401Magnesium; via carbonyl oxygen
Metal bindingi542 – 5421Magnesium

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Complement system impairing toxin, Toxin

Keywords - Biological processi

Inflammatory response

Keywords - Ligandi

Metal-binding

Protein family/group databases

MEROPSiI39.950.

Names & Taxonomyi

Protein namesi
Recommended name:
Cobra venom factor
Short name:
CVF
Short name:
CVFk
Alternative name(s):
Complement C3 homolog
Cleaved into the following 3 chains:
OrganismiNaja kaouthia (Monocled cobra) (Naja siamensis)
Taxonomic identifieri8649 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeElapinaeNaja

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222By similarityAdd
BLAST
Chaini23 – 16421620Cobra venom factorPRO_0000005928Add
BLAST
Chaini23 – 649627Cobra venom factor alpha chainPRO_0000005929Add
BLAST
Propeptidei650 – 73283PRO_0000423372Add
BLAST
Chaini733 – 984252Cobra venom factor gamma chainPRO_0000005930Add
BLAST
Propeptidei985 – 1263279PRO_0000423373Add
BLAST
Chaini1264 – 1642379Cobra venom factor beta chainPRO_0000005931Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi153 – 1531N-linked (GlcNAc...)Sequence analysis
Glycosylationi158 – 1581N-linked (GlcNAc...)Sequence analysis
Glycosylationi209 – 2091N-linked (GlcNAc...)2 Publications
Disulfide bondi544 ↔ 801Interchain (between alpha and gamma chains)
Disulfide bondi609 ↔ 644
Disulfide bondi677 ↔ 704By similarity
Disulfide bondi678 ↔ 711By similarity
Disulfide bondi691 ↔ 712By similarity
Disulfide bondi857 ↔ 1492Interchain (between gamma and beta chains)
Cross-linki993 ↔ 996Isoglutamyl cysteine thioester (Cys-Gln)By similarity
Disulfide bondi1340 ↔ 1468
Glycosylationi1346 – 13461N-linked (GlcNAc...)2 Publications
Disulfide bondi1368 ↔ 1437
Disulfide bondi1485 ↔ 1490
Disulfide bondi1497 ↔ 1569
Disulfide bondi1516 ↔ 1640
Disulfide bondi1616 ↔ 1625

Post-translational modificationi

First processed by the removal of 4 Arg residues by furin-type protease, forming two chains, alpha and gamma/beta precursor, linked by a disulfide bond. Probably, the cobrin cleaves the C3a-like domain and then the C3d-like domain, generating the mature cobra venom factor (CVF). This mature CVF is composed of three chains: alpha, gamma and beta.
Contains 3 N-linked oligosaccharide chains, two in the alpha-chain and one in the beta-chain. Glycosylation is not required for the biological activity. However, it contributes to the immunogenicity of CVF. The carbohydrate content is 7.4. The major oligosaccharide is a symmetric fucosylated biantennary complex-type chain with an unusual alpha-galactosylated Le(x) structure at its non-reducing end.3 Publications

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Thioester bond

Proteomic databases

PRIDEiQ91132.

PTM databases

UniCarbKBiQ91132.

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Heterotrimer of alpha, beta and gamma chains; disulfide-linked. Is active with factor B in the presence of factor D.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
C5P010312EBI-7081824,EBI-8558308From a different organism.

Protein-protein interaction databases

IntActiQ91132. 3 interactions.
MINTiMINT-7906427.

Structurei

Secondary structure

1
1642
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi24 – 3512Combined sources
Beta strandi42 – 476Combined sources
Beta strandi52 – 6110Combined sources
Beta strandi66 – 7510Combined sources
Helixi77 – 793Combined sources
Beta strandi81 – 833Combined sources
Helixi91 – 933Combined sources
Beta strandi103 – 1108Combined sources
Beta strandi113 – 12210Combined sources
Beta strandi128 – 1336Combined sources
Beta strandi135 – 1373Combined sources
Beta strandi145 – 1506Combined sources
Beta strandi161 – 1666Combined sources
Beta strandi172 – 1798Combined sources
Beta strandi195 – 2039Combined sources
Beta strandi210 – 2167Combined sources
Beta strandi223 – 23614Combined sources
Beta strandi243 – 2519Combined sources
Beta strandi259 – 26911Combined sources
Beta strandi272 – 2754Combined sources
Helixi277 – 2793Combined sources
Beta strandi281 – 2866Combined sources
Beta strandi289 – 2946Combined sources
Helixi296 – 3027Combined sources
Helixi306 – 3094Combined sources
Beta strandi313 – 32210Combined sources
Beta strandi328 – 34215Combined sources
Beta strandi344 – 3463Combined sources
Beta strandi352 – 3543Combined sources
Beta strandi360 – 3678Combined sources
Beta strandi378 – 3814Combined sources
Helixi382 – 3843Combined sources
Beta strandi386 – 3894Combined sources
Beta strandi394 – 4007Combined sources
Beta strandi407 – 4159Combined sources
Beta strandi418 – 4203Combined sources
Helixi422 – 4243Combined sources
Beta strandi427 – 4348Combined sources
Helixi438 – 4403Combined sources
Beta strandi444 – 4496Combined sources
Beta strandi459 – 46810Combined sources
Helixi470 – 4745Combined sources
Beta strandi478 – 4858Combined sources
Beta strandi488 – 4969Combined sources
Beta strandi502 – 5098Combined sources
Helixi512 – 5143Combined sources
Beta strandi516 – 52611Combined sources
Turni527 – 5293Combined sources
Beta strandi530 – 53910Combined sources
Beta strandi548 – 5514Combined sources
Beta strandi562 – 5709Combined sources
Beta strandi574 – 5818Combined sources
Helixi582 – 5876Combined sources
Helixi589 – 5913Combined sources
Helixi595 – 60410Combined sources
Beta strandi610 – 6123Combined sources
Helixi617 – 6237Combined sources
Beta strandi626 – 6305Combined sources
Helixi742 – 7443Combined sources
Beta strandi753 – 7553Combined sources
Beta strandi759 – 7613Combined sources
Beta strandi772 – 7798Combined sources
Beta strandi784 – 79512Combined sources
Turni796 – 7983Combined sources
Beta strandi799 – 8024Combined sources
Beta strandi806 – 8105Combined sources
Beta strandi813 – 8186Combined sources
Beta strandi830 – 8389Combined sources
Beta strandi840 – 8423Combined sources
Beta strandi844 – 8507Combined sources
Beta strandi856 – 8594Combined sources
Beta strandi862 – 8643Combined sources
Beta strandi866 – 8727Combined sources
Beta strandi876 – 88611Combined sources
Beta strandi888 – 90013Combined sources
Beta strandi906 – 91611Combined sources
Beta strandi918 – 93013Combined sources
Helixi932 – 9354Combined sources
Beta strandi937 – 9459Combined sources
Beta strandi959 – 9679Combined sources
Beta strandi1274 – 12807Combined sources
Beta strandi1282 – 12865Combined sources
Beta strandi1288 – 12936Combined sources
Helixi1294 – 12963Combined sources
Beta strandi1301 – 13077Combined sources
Beta strandi1311 – 13188Combined sources
Beta strandi1321 – 133111Combined sources
Beta strandi1342 – 135110Combined sources
Beta strandi1363 – 13719Combined sources
Beta strandi1373 – 13753Combined sources
Beta strandi1377 – 13859Combined sources
Beta strandi1390 – 13934Combined sources
Helixi1394 – 14018Combined sources
Beta strandi1406 – 14083Combined sources
Beta strandi1417 – 14193Combined sources
Beta strandi1421 – 143010Combined sources
Beta strandi1432 – 14343Combined sources
Beta strandi1436 – 14449Combined sources
Beta strandi1454 – 14607Combined sources
Beta strandi1469 – 14735Combined sources
Beta strandi1474 – 14763Combined sources
Beta strandi1483 – 14864Combined sources
Beta strandi1489 – 14924Combined sources
Helixi1508 – 15158Combined sources
Beta strandi1522 – 153413Combined sources
Beta strandi1537 – 154913Combined sources
Helixi1556 – 15583Combined sources
Beta strandi1561 – 15666Combined sources
Helixi1567 – 15693Combined sources
Helixi1570 – 15734Combined sources
Beta strandi1580 – 15856Combined sources
Helixi1587 – 15893Combined sources
Beta strandi1596 – 16005Combined sources
Beta strandi1602 – 16043Combined sources
Beta strandi1606 – 16105Combined sources
Helixi1614 – 16174Combined sources
Turni1619 – 16213Combined sources
Helixi1622 – 163817Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3FRPX-ray2.61A23-649[»]
B1264-1642[»]
G733-984[»]
3HRZX-ray2.20A23-649[»]
B733-984[»]
C1264-1642[»]
3HS0X-ray3.00A/F23-649[»]
B/G733-984[»]
C/H1264-1642[»]
3PRXX-ray4.30B/D1-1642[»]
3PVMX-ray4.30B/D1-1642[»]
ProteinModelPortaliQ91132.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ91132.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini677 – 71236Anaphylatoxin-likePROSITE-ProRule annotationAdd
BLAST
Domaini1497 – 1640144NTRPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni654 – 73279C3a-like domainBy similarityAdd
BLAST
Regioni736 – 74712Factor B binding siteBy similarityAdd
BLAST
Regioni985 – 1263279C3d-like domainBy similarityAdd
BLAST
Regioni1190 – 125364Factor H binding siteBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi650 – 6534Poly-Arg

Sequence similaritiesi

Belongs to the venom complement C3 homolog family.Curated
Contains 1 anaphylatoxin-like domain.PROSITE-ProRule annotation
Contains 1 NTR domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG005110.

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.
IPR019742. MacrogloblnA2_CS.
IPR019565. MacrogloblnA2_thiol-ester-bond.
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.
PF10569. Thiol-ester_cl. 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.
PROSITEiPS00477. ALPHA_2_MACROGLOBULIN. 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.

Q91132-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MERMALYLVA ALLIGFPGSS HGALYTLITP AVLRTDTEEQ ILVEAHGDST
60 70 80 90 100
PKQLDIFVHD FPRKQKTLFQ TRVDMNPAGG MLVTPTIEIP AKEVSTDSRQ
110 120 130 140 150
NQYVVVQVTG PQVRLEKVVL LSYQSSFLFI QTDKGIYTPG SPVLYRVFSM
160 170 180 190 200
DHNTSKMNKT VIVEFQTPEG ILVSSNSVDL NFFWPYNLPD LVSLGTWRIV
210 220 230 240 250
AKYEHSPENY TAYFDVRKYV LPSFEVRLQP SEKFFYIDGN ENFHVSITAR
260 270 280 290 300
YLYGEEVEGV AFVLFGVKID DAKKSIPDSL TRIPIIDGDG KATLKRDTFR
310 320 330 340 350
SRFPNLNELV GHTLYASVTV MTESGSDMVV TEQSGIHIVA SPYQIHFTKT
360 370 380 390 400
PKYFKPGMPY ELTVYVTNPD GSPAAHVPVV SEAFHSMGTT LSDGTAKLIL
410 420 430 440 450
NIPLNAQSLP ITVRTNHGDL PRERQATKSM TAIAYQTQGG SGNYLHVAIT
460 470 480 490 500
STEIKPGDNL PVNFNVKGNA NSLKQIKYFT YLILNKGKIF KVGRQPRRDG
510 520 530 540 550
QNLVTMNLHI TPDLIPSFRF VAYYQVGNNE IVADSVWVDV KDTCMGTLVV
560 570 580 590 600
KGDNLIQMPG AAMKIKLEGD PGARVGLVAV DKAVYVLNDK YKISQAKIWD
610 620 630 640 650
TIEKSDFGCT AGSGQNNLGV FEDAGLALTT STNLNTKQRS AAKCPQPANR
660 670 680 690 700
RRRSSVLLLD SNASKAAEFQ DQDLRKCCED VMHENPMGYT CEKRAKYIQE
710 720 730 740 750
GDACKAAFLE CCRYIKGVRD ENQRESELFL ARDDNEDGFI ADSDIISRSD
760 770 780 790 800
FPKSWLWLTK DLTEEPNSQG ISSKTMSFYL RDSITTWVVL AVSFTPTKGI
810 820 830 840 850
CVAEPYEIRV MKVFFIDLQM PYSVVKNEQV EIRAILHNYV NEDIYVRVEL
860 870 880 890 900
LYNPAFCSAS TKGQRYRQQF PIKALSSRAV PFVIVPLEQG LHDVEIKASV
910 920 930 940 950
QEALWSDGVR KKLKVVPEGV QKSIVTIVKL DPRAKGVGGT QLEVIKARKL
960 970 980 990 1000
DDRVPDTEIE TKIIIQGDPV AQIIENSIDG SKLNHLIITP SGCGEQNMIR
1010 1020 1030 1040 1050
MAAPVIATYY LDTTEQWETL GINRRTEAVN QIVTGYAQQM VYKKADHSYA
1060 1070 1080 1090 1100
AFTNRASSSW LTAYVVKVFA MAAKMVAGIS HEIICGGVRW LILNRQQPDG
1110 1120 1130 1140 1150
AFKENAPVLS GTMQGGIQGA EEEVYLTAFI LVALLESKTI CNDYVNSLDS
1160 1170 1180 1190 1200
SIKKATNYLL KKYEKLQRPY TTALTAYALA AADQLNDDRV LMAASTGRDH
1210 1220 1230 1240 1250
WEEYNAHTHN IEGTSYALLA LLKMKKFDQT GPIVRWLTDQ NFYGETYGQT
1260 1270 1280 1290 1300
QATVMAFQAL AEYEIQMPTH KDLNLDITIE LPDREVPIRY RINYENALLA
1310 1320 1330 1340 1350
RTVETKLNQD ITVTASGDGK ATMTILTFYN AQLQEKANVC NKFHLNVSVE
1360 1370 1380 1390 1400
NIHLNAMGAK GALMLKICTR YLGEVDSTMT IIDISMLTGF LPDAEDLTRL
1410 1420 1430 1440 1450
SKGVDRYISR YEVDNNMAQK VAVIIYLNKV SHSEDECLHF KILKHFEVGF
1460 1470 1480 1490 1500
IQPGSVKVYS YYNLDEKCTK FYHPDKGTGL LNKICIGNVC RCAGETCSSL
1510 1520 1530 1540 1550
NHQERIDVPL QIEKACETNV DYVYKTKLLR IEEQDGNDIY VMDVLEVIKQ
1560 1570 1580 1590 1600
GTDENPRAKT HQYISQRKCQ EALNLKVNDD YLIWGSRSDL LPTKDKISYI
1610 1620 1630 1640
ITKNTWIERW PHEDECQEEE FQKLCDDFAQ FSYTLTEFGC PT
Length:1,642
Mass (Da):184,518
Last modified:November 1, 1996 - v1
Checksum:i2A71B2BD61D612A3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09969 mRNA. Translation: AAA68989.1.
AY497579 Genomic DNA. Translation: AAR89520.1.
AY586272 Genomic DNA. Translation: AAS97956.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09969 mRNA. Translation: AAA68989.1.
AY497579 Genomic DNA. Translation: AAR89520.1.
AY586272 Genomic DNA. Translation: AAS97956.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3FRPX-ray2.61A23-649[»]
B1264-1642[»]
G733-984[»]
3HRZX-ray2.20A23-649[»]
B733-984[»]
C1264-1642[»]
3HS0X-ray3.00A/F23-649[»]
B/G733-984[»]
C/H1264-1642[»]
3PRXX-ray4.30B/D1-1642[»]
3PVMX-ray4.30B/D1-1642[»]
ProteinModelPortaliQ91132.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ91132. 3 interactions.
MINTiMINT-7906427.

Protein family/group databases

MEROPSiI39.950.

PTM databases

UniCarbKBiQ91132.

Proteomic databases

PRIDEiQ91132.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG005110.

Miscellaneous databases

EvolutionaryTraceiQ91132.

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.
IPR019742. MacrogloblnA2_CS.
IPR019565. MacrogloblnA2_thiol-ester-bond.
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.
PF10569. Thiol-ester_cl. 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.
PROSITEiPS00477. ALPHA_2_MACROGLOBULIN. 1 hit.
PS01178. ANAPHYLATOXIN_2. 1 hit.
PS50189. NTR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning and derived primary structure of cobra venom factor."
    Fritzinger D.C., Bredehorst R., Vogel C.-W.
    Proc. Natl. Acad. Sci. U.S.A. 91:12775-12779(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Venom gland.
  2. "Genomic structure of cobra venom factor (CVF)."
    Bammert H., Kunze B., Li Y., Fritzinger D.C., Bredehorst R., Vogel C.-W.
    Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24 AND 1608-1642.
    Tissue: Liver.
  3. "Cobra venom factor: Structure, function, and humanization for therapeutic complement depletion."
    Vogel C.-W., Fritzinger D.C.
    Toxicon 56:1198-1222(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  4. "N-linked oligosaccharides of cobra venom factor contain novel alpha(1-3)galactosylated Le(x) structures."
    Gowda D.C., Glushka J., van Halbeek H., Thotakura R.N., Bredehorst R., Vogel C.-W.
    Glycobiology 11:195-208(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION.
  5. "Structure and function of recombinant cobra venom factor."
    Kock M.A., Hew B.E., Bammert H., Fritzinger D.C., Vogel C.-W.
    J. Biol. Chem. 279:30836-30843(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE.
  6. "Insights into complement convertase formation based on the structure of the factor B-cobra venom factor complex."
    Janssen B.J., Gomes L., Koning R.I., Svergun D.I., Koster A.J., Fritzinger D.C., Vogel C.-W., Gros P.
    EMBO J. 28:2469-2478(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 23-649; 733-984 AND 1264-1642 IN COMPLEX WITH HUMAN COMPLEMENT FACTOR B, METAL-BINDING SITES, GLYCOSYLATION AT ASN-209 AND ASN-1346, DISULFIDE BONDS.
  7. "The crystal structure of cobra venom factor, a cofactor for C3- and C5-convertase CVFBb."
    Krishnan V., Ponnuraj K., Xu Y., Macon K., Volanakis J.E., Narayana S.V.
    Structure 17:611-619(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 23-649; 733-984 AND 1264-1642, METAL-BINDING SITES, DISULFIDE BONDS.
  8. "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 23-1642 IN COMPLEX WITH HUMAN COMPLEMENT C5, GLYCOSYLATION AT ASN-209 AND ASN-1346, DISULFIDE BONDS.

Entry informationi

Entry nameiVCO3_NAJKA
AccessioniPrimary (citable) accession number: Q91132
Secondary accession number(s): Q6PQH3, Q6RHR7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Miscellaneous

CVF has been used to study the complement pathways and to investigate the role of complement in disease pathophysiology. It has also been used to consume complement to prevent the hyperactive rejection of organs in xenotransplantation and for targeted complement-mediated cell killing. CVF can be safely administered to laboratory animals for temporary depletion of complement activity. Interestingly, it is able to deplete complement in serum from all vertebrates tested, except cobras. The only side effect from massive activation of complement in vivo by CVF has been an acute and fleeting inflammatory injury of the lungs (PubMed:20417224).1 Publication

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.