VCO32_AUSSU
ID VCO32_AUSSU Reviewed; 1651 AA.
AC A0RZC6;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=A.superbus venom factor 2;
DE Short=AVF-2;
DE AltName: Full=CVF-like;
DE AltName: Full=Complement C3 homolog;
DE Contains:
DE RecName: Full=AVF-2 alpha chain;
DE Contains:
DE RecName: Full=AVF-2 gamma chain;
DE Contains:
DE RecName: Full=AVF-2 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].
RC TISSUE=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 do CVF/Bb) (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterotrimer of alpha, beta and gamma chains; disulfide-
CC linked. Is active with factor B in the presence of factor D (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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: Is expressed in small quantities.
CC -!- SIMILARITY: Belongs to the venom complement C3 homolog family.
CC {ECO:0000305}.
CC -!- CAUTION: Lacks the typical Cys at position 1000 required for the
CC thioester bond formation. {ECO:0000305}.
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DR EMBL; DQ110890; AAZ81954.1; -; mRNA.
DR AlphaFoldDB; A0RZC6; -.
DR SMR; A0RZC6; -.
DR MEROPS; I39.950; -.
DR PRIDE; A0RZC6; -.
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; 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; PS01177; ANAPHYLATOXIN_1; 1.
DR PROSITE; PS01178; ANAPHYLATOXIN_2; 1.
DR PROSITE; PS50189; NTR; 1.
PE 2: Evidence at transcript level;
KW Cleavage on pair of basic residues; Complement system impairing toxin;
KW Disulfide bond; Glycoprotein; Inflammatory response; Magnesium;
KW Metal-binding; Secreted; Signal; Toxin.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1651
FT /note="A.superbus venom factor 2"
FT /id="PRO_0000418040"
FT CHAIN 23..656
FT /note="AVF-2 alpha chain"
FT /id="PRO_0000418041"
FT PROPEP 657..739
FT /evidence="ECO:0000250"
FT /id="PRO_0000418042"
FT CHAIN 740..991
FT /note="AVF-2 gamma chain"
FT /id="PRO_0000418043"
FT PROPEP 992..1269
FT /evidence="ECO:0000250"
FT /id="PRO_0000418044"
FT CHAIN 1270..1651
FT /note="AVF-2 beta chain"
FT /id="PRO_0000418045"
FT DOMAIN 684..719
FT /note="Anaphylatoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00022"
FT DOMAIN 1506..1649
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..1269
FT /note="C3d-like domain"
FT /evidence="ECO:0000250"
FT REGION 1197..1259
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 CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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..1501
FT /note="Interchain (between gamma and beta chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00022,
FT ECO:0000255|PROSITE-ProRule:PRU00295"
FT DISULFID 1346..1477
FT /evidence="ECO:0000250"
FT DISULFID 1377..1446
FT /evidence="ECO:0000250"
FT DISULFID 1494..1499
FT /evidence="ECO:0000250"
FT DISULFID 1506..1578
FT /evidence="ECO:0000250"
FT DISULFID 1525..1649
FT /evidence="ECO:0000250"
FT DISULFID 1625..1634
FT /evidence="ECO:0000250"
SQ SEQUENCE 1651 AA; 184576 MW; D04E126410AA51AD CRC64;
MEGMALYLVA ALLIGFPGSS HGALYTLITP GVLRTDTEEQ ILVEAHGDSA PKQPVISIHD
FPRRQKILFQ IRVDMNPAGG MLVTPTIKIP AKELNKESRQ NQYVVVKVSG LPLELEKVVL
LSSQSGFVFI QTDKGIYTPG SLVRYRVFSM DYNMHRMDKT VIVEFQTPEG VVVSSNPINP
SSVLIRHYNL SELVSFGTWK AVAKYEHSPE ESYTAYFDVR EYVLPSFEVR LQPSDKFLYI
DGNKNFHVSI TARYLYGKKV EGVAFVLFGV KIDDAKKSIP DSLTRIPIID GDGEAILKRD
ILRSRFQNLN ELVGHTLYAS VTVMTESGSD MVVTEQSGIH IVTSPYQIYF TKPPKYFKPG
MPYELTVYVT NPDGSPAANV PVVSEAIHSE GTTLSDGTAK LILNTPLNTQ SLPITVRTNH
RDLPRERQAT KSMTATAYQT QGGSGNYLHV AITSTEIKAG DNLPVSFNVR GNANSLNQIK
YFTYLILTKG KIFKVGRQPR GEGQNLVTMN LRITPDLIPA FRFVAYYQVG NNEIVADSVW
VDVKDTCMGM LVVKGASSRD NRIQKPGAAM KIKLEGDPGA RVGLVAVDKA VYVLNDKYKI
SQAKIWDTIE KSDFGCTAGG GQDNLGVFED AGLALTTSTN LNTKQRSVAT CPQPTNRRRR
SSVLLLDSKA SKAAQFQEQN LHKCCEDGMH ENPMGYTCEK RAKYTQEGDA CKAAFLECCR
YIKGIRDENQ RESELFLARS DFEDEFFEED NIISRSDFPD SWLWLTEDLN EPPNSQGISS
KTLSFYLKDS ITTWEVLAVS IAPTKGICVA EPYEITVMKD FFIDLRVPYS VVKNEQVEIR
AVLYNYADED IYVRVELLYN PAFCSASAEG QRYRVQVPVR ALSSWAVPFV IVPLEQGLHD
VEVKASVRGE LASDGVRKKL KVVPEGERKN IVTVIELDPS VKGVGGTQEQ TVVANKLDDK
VPETEIETKF SVLGDPVAQI IENSIDGSKL SHLIITPSGS GEQNMITMTP SVIATYYLDA
TGQWENLGVD RRTEAVKQIM KGYAQQMVYK KADHSYASFV NRASSSWLTA YVVKVFAMAA
KMVKDINHEI ICGGVKWLIL NRQQSDGVFK ENAPVILGGM MGGTQGAEPE VSLTAFILVA
LLESRSVCNE HINILDNSIN KATDYLLKKY EKLQRPYTTA LTAYALAAAE RLNDDRVLMA
ASTGRDRWEE HARTHNIEGT SYALLALLKM KKFAEAGPVV KWLIDQKYYG GTYGQTQATV
MVFQALAEYE IQIPTHKDLN LNISINLPER EVPLRYSINY GNALVARTAE TKLNEDFTVS
ASGDGKATMT ILTVYNAQLR EDANVCNKFH LNVSVENAQL NSKQAKGAKD TLRLKICTRY
LGEVDSTMTI IDVSMLTGFL PDTEDLTRLS KGVDRYISKF EIDNNMVQKG TVVIYLDKVS
HSEVECLNFK IHKHFEVGFI QPGPVKVYSY YNLDEQCTKF YHPDKGTGLL NKICHGNICR
CAEQSCSLLN QQKKIDLPLR IQKACAPNVD YVYKAKLLRI EEKDGNDIYV MDVLEVIKGG
TDRNPQAKAR QYVSQRKCQE ALNLNLNNDY LIWGLSSDLW PMKNDISYLI TKNTWIERWP
NEDECQDEEF QNLCDDFAQL SNTLTIFGCP T
