VCO31_AUSSU
ID VCO31_AUSSU Reviewed; 1652 AA.
AC Q0ZZJ6;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=A.superbus venom factor 1;
DE Short=AVF-1;
DE AltName: Full=CVF-like;
DE AltName: Full=Complement C3 homolog;
DE Contains:
DE RecName: Full=AVF-1 alpha chain;
DE Contains:
DE RecName: Full=AVF-1 gamma chain;
DE Contains:
DE RecName: Full=AVF-1 beta chain;
DE Flags: Precursor;
OS Austrelaps superbus (Lowland copperhead snake) (Hoplocephalus superbus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Acanthophiinae; Austrelaps.
OX NCBI_TaxID=29156;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 578-638, FUNCTION, SUBUNIT,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=17412383; DOI=10.1016/j.toxicon.2007.02.016;
RA Rehana S., Kini R.M.;
RT "Molecular isoforms of cobra venom factor-like proteins in the venom of
RT Austrelaps superbus.";
RL Toxicon 50:32-52(2007).
CC -!- FUNCTION: Complement-activating protein in snake venom. It is a
CC structural and functional analog of complement component C3b, the
CC activated form of C3. It binds factor B (CFB), which is subsequently
CC cleaved by factor D (CFD) to form the bimolecular complex AVF/Bb.
CC AVF/Bb is a C3 convertase that cleaves complement component C3, but not
CC C5 (as does CVF/Bb). {ECO:0000269|PubMed:17412383}.
CC -!- SUBUNIT: Heterotrimer of alpha, beta and gamma chains; disulfide-
CC linked. Is active with factor B in the presence of factor D.
CC {ECO:0000269|PubMed:17412383}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PTM: First processed by the removal of 4 Arg residues by furin-type
CC protease, forming two chains, alpha and gamma/beta precursor, linked by
CC a disulfide bond. This mature AVF is composed of three chains: alpha,
CC gamma and beta (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: Interestingly, a peptide (from position 1111 to position
CC 1125) coming from the pre-pro-protein has been identified by MS/MS,
CC suggesting a longer gamma-chain in AVF-1 than in CVF.
CC -!- SIMILARITY: Belongs to the venom complement C3 homolog family.
CC {ECO:0000305}.
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DR EMBL; DQ110889; AAZ81953.1; -; mRNA.
DR AlphaFoldDB; Q0ZZJ6; -.
DR SMR; Q0ZZJ6; -.
DR MEROPS; I39.950; -.
DR PRIDE; Q0ZZJ6; -.
DR TopDownProteomics; Q0ZZJ6; -.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006956; P:complement activation; IEA:InterPro.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR CDD; cd00017; ANATO; 1.
DR CDD; cd03583; NTR_complement_C3; 1.
DR Gene3D; 2.40.50.120; -; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 2.60.40.690; -; 1.
DR InterPro; IPR009048; A-macroglobulin_rcpt-bd.
DR InterPro; IPR036595; A-macroglobulin_rcpt-bd_sf.
DR InterPro; IPR011625; A2M_N_BRD.
DR InterPro; IPR011626; Alpha-macroglobulin_TED.
DR InterPro; IPR000020; Anaphylatoxin/fibulin.
DR InterPro; IPR018081; Anaphylatoxin_comp_syst.
DR InterPro; IPR001840; Anaphylatoxn_comp_syst_dom.
DR InterPro; IPR041425; C3/4/5_MG1.
DR InterPro; IPR035711; Complement_C3-like.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001599; Macroglobln_a2.
DR InterPro; IPR019742; MacrogloblnA2_CS.
DR InterPro; IPR002890; MG2.
DR InterPro; IPR041555; MG3.
DR InterPro; IPR040839; MG4.
DR InterPro; IPR001134; Netrin_domain.
DR InterPro; IPR018933; Netrin_module_non-TIMP.
DR InterPro; IPR035815; NTR_complement_C3.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR InterPro; IPR008993; TIMP-like_OB-fold.
DR PANTHER; PTHR11412:SF81; PTHR11412:SF81; 1.
DR Pfam; PF00207; A2M; 1.
DR Pfam; PF07703; A2M_BRD; 1.
DR Pfam; PF07677; A2M_recep; 1.
DR Pfam; PF01821; ANATO; 1.
DR Pfam; PF17790; MG1; 1.
DR Pfam; PF01835; MG2; 1.
DR Pfam; PF17791; MG3; 1.
DR Pfam; PF17789; MG4; 1.
DR Pfam; PF01759; NTR; 1.
DR Pfam; PF07678; TED_complement; 1.
DR PRINTS; PR00004; ANAPHYLATOXN.
DR SMART; SM01360; A2M; 1.
DR SMART; SM01359; A2M_N_2; 1.
DR SMART; SM01361; A2M_recep; 1.
DR SMART; SM00104; ANATO; 1.
DR SMART; SM00643; C345C; 1.
DR SUPFAM; SSF47686; SSF47686; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
DR SUPFAM; SSF49410; SSF49410; 1.
DR SUPFAM; SSF50242; SSF50242; 1.
DR PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1.
DR PROSITE; PS01177; ANAPHYLATOXIN_1; 1.
DR PROSITE; PS01178; ANAPHYLATOXIN_2; 1.
DR PROSITE; PS50189; NTR; 1.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Complement system impairing toxin;
KW Direct protein sequencing; Disulfide bond; Inflammatory response;
KW Magnesium; Metal-binding; Secreted; Signal; Thioester bond; Toxin.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1652
FT /note="A.superbus venom factor 1"
FT /id="PRO_0000418036"
FT CHAIN 23..656
FT /note="AVF-1 alpha chain"
FT /id="PRO_0000418037"
FT PROPEP 657..739
FT /evidence="ECO:0000250"
FT /id="PRO_0000423374"
FT CHAIN 740..991
FT /note="AVF-1 gamma chain"
FT /id="PRO_0000418038"
FT PROPEP 992..1270
FT /evidence="ECO:0000250"
FT /id="PRO_0000423375"
FT CHAIN 1271..1652
FT /note="AVF-1 beta chain"
FT /id="PRO_0000418039"
FT DOMAIN 684..719
FT /note="Anaphylatoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00022"
FT DOMAIN 1507..1650
FT /note="NTR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT REGION 661..739
FT /note="C3a-like domain"
FT /evidence="ECO:0000250"
FT REGION 743..754
FT /note="Factor B binding site"
FT /evidence="ECO:0000250"
FT REGION 992..1270
FT /note="C3d-like domain"
FT /evidence="ECO:0000250"
FT REGION 1197..1260
FT /note="Factor H binding site"
FT /evidence="ECO:0000250"
FT BINDING 519
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 542
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 543
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 545
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT DISULFID 547..808
FT /note="Interchain (between alpha and gamma chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00022,
FT ECO:0000255|PROSITE-ProRule:PRU00295"
FT DISULFID 616..651
FT /evidence="ECO:0000250"
FT DISULFID 684..711
FT /evidence="ECO:0000250"
FT DISULFID 685..718
FT /evidence="ECO:0000250"
FT DISULFID 698..719
FT /evidence="ECO:0000250"
FT DISULFID 864..1502
FT /note="Interchain (between gamma and beta chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00022,
FT ECO:0000255|PROSITE-ProRule:PRU00295"
FT DISULFID 1347..1478
FT /evidence="ECO:0000250"
FT DISULFID 1378..1447
FT /evidence="ECO:0000250"
FT DISULFID 1495..1500
FT /evidence="ECO:0000250"
FT DISULFID 1507..1579
FT /evidence="ECO:0000250"
FT DISULFID 1526..1650
FT /evidence="ECO:0000250"
FT DISULFID 1626..1635
FT /evidence="ECO:0000250"
FT CROSSLNK 1000..1003
FT /note="Isoglutamyl cysteine thioester (Cys-Gln)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1652 AA; 184726 MW; D216045157ACE9C4 CRC64;
MEGMALYLVA ALLIGFPGSS HGALYTLITP GVLRTDTEEQ ILVEAHGDSV PKQAVISIHD
FPRRQKTLFQ TRVDMNPAGG MLVTPTIKIP AKELNKESRQ NQYVVVKVSG LPLELEKVVL
LSYQSGFVFI QTDKGIYTPG SPVRYRVFSM DYNMHRMDKT VIVEFQTPEG VVVSSNPVNP
SSVLIRPYNL PELVSFGTWK AVAKYEHSPE ESYTAYFDVR EYVLPSFEVR LQPSDKFLYI
DGNKNFHVSI TARYLYGKKV EGVAFVLFGV KIDDAKKSIP DSLTRIPIID GDGEAILKRD
TLRSRFQNLN ELVGHTLYAS VTVMTESGSD MVVTEQSGIH IVTSPYQIYF TKTPKYFKPG
MPYELTVYVT NPDGSPAANV PVVSEAIRSE GTTLSDGTAK LILNTPLNTQ SLPITVRTNH
RDLPSERQAT KSMTATAYQT QGGSGNYLHV AITSAEIKAG DNLPVNFNVR GNANSLNQIK
YFTYLILTKG KIFKVGRQPK GEGQNLVTMN LRITPDLIPA FRFVAYYQVG NNEIVADSVW
VDVKDTCMGT LVVKGASSRD NRIQKPGAAM KIKLEGDPGA RVGLVAVDKA VYVLNDKYKI
SQAKIWDTIE KSDFGCTAGG GQNNLGVFED AGLALTTSTN LNTKQRSVAT CPQPTNRRRR
SSVLLLDSKA NKAAQFQDQN LRKCCEDGMH ENPMGYTCEK RAKYIQEGDA CKAAFLECCR
YIKGIRDENQ RESELFLARS DFEDELFGED NIISRSDFPE SWLWLTEDLK EPPNSQGISS
KTLSFYLRDS ITTWEVLAVS IAPTKGICVA EPYEITVMKD FFIDLRVPYS VVKNEQVEIR
AVLYNYADED IYVRVELLYN PAFCSASTEG QRYRVQVPVK ALSSWAVPFV IVPLEQGLHD
VEVKASVRGE LASDGVRKKL KVVPEGERKN IVTVIELDPS VKGVDGTQEQ TVIANKLDDK
VPETEIETKI SVLGDPVAQI IENSIDGSKL NHLIITPSGC GEQNMITMTP SVIATYYLDA
TGQWENLGVD RRTEAVKQIM KGYAQQMVYK KADHSYAAFP NRASSSWLTA YVVKVFAMAA
KIVKDIKHEI ICGGVKWLIL NRQQPDGVFK ENAPVIHGEM LGGTKGAEPE VSLTAFILTA
LLESRSVCNE HINILDSSIN KAIDYLLKKY EKLQRPYTTA LTAYALAAAE RLNDDRVLMA
ASTGRDRWEE HNARTHNIEG TSYALLALLK MKKFAEAGPV VKWLIDQKYY GGTYGQTQAT
VMVFQALAEY EIQIPTHKDL NLDISINLPE REVPLRYSIN YGNALVARTA ETKLNEDFTV
SASGDGKATM TILTVYNAQL REDANVCNKF HLDVSVENAQ LNSKQAKGAK DTLRLKICTR
YLGEVDSTMT IIDVSMLTGF LADAEDLTRL SKGVDRYISK FEIDNNMVQK GTVVIYLDKV
SHSEVECLHF KIHKHFEVGF IQPGSVKVYS YYNLDEQCTK FYHPDKGTGL LNKICHGNIC
RCAEESCSLL NQQKKIDLQL RIQKACAPNV DYVYKTKLLQ IEEKDGNDIY VMDVLEVIKG
GTDRNPQAKA RQYVSQRKCQ EALNLKLNND YLIWGLSSDL WPRKNDISYL ITKNTWIERW
PNEDECQDEE FQNLCDDFAQ LSNTLTIFGC PT
