VBP2_ASCSS
ID VBP2_ASCSS Reviewed; 120 AA.
AC Q86BW2;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 53.
DE RecName: Full=Vanadium-binding protein 2 {ECO:0000312|EMBL:BAC76458.1};
DE EC=1.13.-.-;
DE Flags: Precursor;
GN Name=VANABIN2 {ECO:0000312|EMBL:BAC76458.1};
OS Ascidia sydneiensis samea (Vanadium-rich ascidian).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC Ascidiidae; Ascidia.
OX NCBI_TaxID=79730;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAC76458.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 30-49, AND FUNCTION.
RC TISSUE=Blood {ECO:0000312|EMBL:BAC76458.1};
RX PubMed=12697328; DOI=10.1016/s0167-4781(03)00036-8;
RA Ueki T., Adachi T., Kawano S., Aoshima M., Yamaguchi N., Kanamori K.,
RA Michibata H.;
RT "Vanadium-binding proteins (vanabins) from a vanadium-rich ascidian Ascidia
RT sydneiensis samea.";
RL Biochim. Biophys. Acta 1626:43-50(2003).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 30-41, AND FUNCTION.
RX PubMed=18466774; DOI=10.1016/j.bbagen.2008.04.001;
RA Ueki T., Satake M., Kamino K., Michibata H.;
RT "Sequence variation of Vanabin2-like vanadium-binding proteins in blood
RT cells of the vanadium-accumulating ascidian Ascidia sydneiensis samea.";
RL Biochim. Biophys. Acta 1780:1010-1015(2008).
RN [3] {ECO:0000305}
RP FUNCTION.
RX PubMed=14602598; DOI=10.1128/aem.69.11.6442-6446.2003;
RA Ueki T., Sakamoto Y., Yamaguchi N., Michibata H.;
RT "Bioaccumulation of copper ions by Escherichia coli expressing vanabin
RT genes from the vanadium-rich ascidian Ascidia sydneiensis samea.";
RL Appl. Environ. Microbiol. 69:6442-6446(2003).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=12785759; DOI=10.1021/ja034507w;
RA Fukui K., Ueki T., Ohya H., Michibata H.;
RT "Vanadium-binding protein in a vanadium-rich ascidian Ascidia sydneiensis
RT samea: CW and pulsed EPR studies.";
RL J. Am. Chem. Soc. 125:6352-6353(2003).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=16631310; DOI=10.1016/j.bbagen.2006.03.013;
RA Kawakami N., Ueki T., Matsuo K., Gekko K., Michibata H.;
RT "Selective metal binding by Vanabin2 from the vanadium-rich ascidian,
RT Ascidia sydneiensis samea.";
RL Biochim. Biophys. Acta 1760:1096-1101(2006).
RN [6] {ECO:0000305}
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=17116994; DOI=10.2108/zsj.23.909;
RA Yamaguchi N., Amakawa Y., Yamada H., Ueki T., Michibata H.;
RT "Localization of vanabins, vanadium-binding proteins, in the blood cells of
RT the vanadium-rich ascidian, Ascidia sydneiensis samea.";
RL Zool. Sci. 23:909-915(2006).
RN [7] {ECO:0000305}
RP INTERACTION WITH VIP1.
RX PubMed=17376595; DOI=10.1016/j.bbagen.2007.02.003;
RA Ueki T., Shintaku K., Yonekawa Y., Takatsu N., Yamada H., Hamada T.,
RA Hirota H., Michibata H.;
RT "Identification of Vanabin-interacting protein 1 (VIP1) from blood cells of
RT the vanadium-rich ascidian Ascidia sydneiensis samea.";
RL Biochim. Biophys. Acta 1770:951-957(2007).
RN [8] {ECO:0000305}
RP MUTAGENESIS OF LYS-35; LYS-49; LYS-63; ARG-66; ARG-67; ARG-85; HIS-89;
RP HIS-104; HIS-106; LYS-107; ARG-112; LYS-116 AND LYS-120.
RX PubMed=19501132; DOI=10.1016/j.bbagen.2009.05.016;
RA Ueki T., Kawakami N., Toshishige M., Matsuo K., Gekko K., Michibata H.;
RT "Characterization of vanadium-binding sites of the vanadium-binding protein
RT Vanabin2 by site-directed mutagenesis.";
RL Biochim. Biophys. Acta 1790:1327-1333(2009).
RN [9] {ECO:0000305}
RP FUNCTION.
RX PubMed=19336037; DOI=10.1016/j.bbapap.2009.01.007;
RA Kawakami N., Ueki T., Amata Y., Kanamori K., Matsuo K., Gekko K.,
RA Michibata H.;
RT "A novel vanadium reductase, Vanabin2, forms a possible cascade involved in
RT electron transfer.";
RL Biochim. Biophys. Acta 1794:674-679(2009).
RN [10] {ECO:0000305, ECO:0000312|PDB:1VFI}
RP STRUCTURE BY NMR OF 30-120, MASS SPECTROMETRY, AND DISULFIDE BONDS.
RX PubMed=15783203; DOI=10.1021/ja042687j;
RA Hamada T., Asanuma M., Ueki T., Hayashi F., Kobayashi N., Yokoyama S.,
RA Michibata H., Hirota H.;
RT "Solution structure of Vanabin2, a vanadium(IV)-binding protein from the
RT vanadium-rich ascidian Ascidia sydneiensis samea.";
RL J. Am. Chem. Soc. 127:4216-4222(2005).
CC -!- FUNCTION: Acts as a vanadium reductase which may form an electron
CC transfer cascade in conjunction with NADPH and glutathione through
CC thiol disulfide exchange reactions. Partial cleavage of its disulfide
CC bonds results in the reduction of V(5+) to V(4+). Binds up to 24 V(4+)
CC ions per protein at pH 7.5. Also binds Fe(3+) and Cu(2+) and, to a
CC lesser extent, Co(2+), Zn(2+) and Ni(2+). {ECO:0000269|PubMed:12697328,
CC ECO:0000269|PubMed:12785759, ECO:0000269|PubMed:14602598,
CC ECO:0000269|PubMed:16631310, ECO:0000269|PubMed:18466774,
CC ECO:0000269|PubMed:19336037}.
CC -!- SUBUNIT: Interacts with VIP1. {ECO:0000269|PubMed:17376595,
CC ECO:0000305}.
CC -!- INTERACTION:
CC Q86BW2; A4F2K9: VIP1; NbExp=3; IntAct=EBI-2892020, EBI-2892029;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17116994}.
CC -!- TISSUE SPECIFICITY: Expressed in vanadocytes.
CC {ECO:0000269|PubMed:17116994}.
CC -!- MASS SPECTROMETRY: Mass=10467; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:15783203};
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DR EMBL; AB088204; BAC76458.1; -; mRNA.
DR PDB; 1VFI; NMR; -; A=30-120.
DR PDBsum; 1VFI; -.
DR AlphaFoldDB; Q86BW2; -.
DR SMR; Q86BW2; -.
DR IntAct; Q86BW2; 2.
DR EvolutionaryTrace; Q86BW2; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.246.100; -; 1.
DR InterPro; IPR021544; Vanabin-2.
DR InterPro; IPR037242; Vanabin-2_sf.
DR Pfam; PF11437; Vanabin-2; 1.
DR SUPFAM; SSF144129; SSF144129; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Disulfide bond;
KW Metal-binding; Oxidoreductase; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..29
FT /evidence="ECO:0000255, ECO:0000269|PubMed:12697328,
FT ECO:0000269|PubMed:18466774"
FT /id="PRO_0000397931"
FT CHAIN 30..120
FT /note="Vanadium-binding protein 2"
FT /evidence="ECO:0000269|PubMed:12697328"
FT /id="PRO_0000397932"
FT DISULFID 34..88
FT /evidence="ECO:0000269|PubMed:15783203"
FT DISULFID 38..84
FT /evidence="ECO:0000269|PubMed:15783203"
FT DISULFID 42..81
FT /evidence="ECO:0000269|PubMed:15783203"
FT DISULFID 48..74
FT /evidence="ECO:0000269|PubMed:15783203"
FT DISULFID 52..69
FT /evidence="ECO:0000269|PubMed:15783203"
FT DISULFID 56..65
FT /evidence="ECO:0000269|PubMed:15783203"
FT DISULFID 92..119
FT /evidence="ECO:0000269|PubMed:15783203"
FT DISULFID 97..114
FT /evidence="ECO:0000269|PubMed:15783203"
FT DISULFID 101..111
FT /evidence="ECO:0000269|PubMed:15783203"
FT MUTAGEN 35
FT /note="K->A: Loss of VO(2+) binding; when associated with
FT A-85."
FT /evidence="ECO:0000269|PubMed:19501132"
FT MUTAGEN 49
FT /note="K->A: Slightly reduced VO(2+) binding. Reduced
FT VO(2+) binding; when associated with A-63. Loss of VO(2+)
FT binding; when associated with A-63; A-66 and A-67."
FT /evidence="ECO:0000269|PubMed:19501132"
FT MUTAGEN 63
FT /note="K->A: Slightly reduced VO(2+) binding. Reduced
FT VO(2+) binding; when associated with A-49. Loss of VO(2+)
FT binding; when associated with A-49; A-66 and A-67."
FT /evidence="ECO:0000269|PubMed:19501132"
FT MUTAGEN 66
FT /note="R->A: Loss of VO(2+) binding; when associated with
FT A-49; A-63 and A-67."
FT /evidence="ECO:0000269|PubMed:19501132"
FT MUTAGEN 67
FT /note="R->A: Loss of VO(2+) binding; when associated with
FT A-49; A-63 and A-66."
FT /evidence="ECO:0000269|PubMed:19501132"
FT MUTAGEN 85
FT /note="R->A: Loss of VO(2+) binding; when associated with
FT A-35."
FT /evidence="ECO:0000269|PubMed:19501132"
FT MUTAGEN 89
FT /note="H->A: Loss of Co(2+) and Zn(2+) binding and reduced
FT Cu(2+) binding; when associated with A-104 and A-106."
FT /evidence="ECO:0000269|PubMed:19501132"
FT MUTAGEN 104
FT /note="H->A: Loss of Co(2+) and Zn(2+) binding and reduced
FT Cu(2+) binding; when associated with A-89 and A-106."
FT /evidence="ECO:0000269|PubMed:19501132"
FT MUTAGEN 106
FT /note="H->A: Loss of Co(2+) and Zn(2+) binding and reduced
FT Cu(2+) binding; when associated with A-89 and A-104."
FT /evidence="ECO:0000269|PubMed:19501132"
FT MUTAGEN 107
FT /note="K->A: Loss of VO(2+) binding; when associated A-112;
FT A-116 and A-120."
FT /evidence="ECO:0000269|PubMed:19501132"
FT MUTAGEN 112
FT /note="R->A: Loss of VO(2+) binding; when associated A-107;
FT A-116 and A-120."
FT /evidence="ECO:0000269|PubMed:19501132"
FT MUTAGEN 116
FT /note="K->A: Reduced VO(2+) binding; when associated with
FT A-120. Loss of VO(2+) binding; when associated A-107; A-112
FT and A-120."
FT /evidence="ECO:0000269|PubMed:19501132"
FT MUTAGEN 120
FT /note="K->A: Reduced VO(2+) binding; when associated with
FT A-116. Loss of VO(2+) binding; when associated A-107; A-112
FT and A-116."
FT /evidence="ECO:0000269|PubMed:19501132"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:1VFI"
FT HELIX 43..55
FT /evidence="ECO:0007829|PDB:1VFI"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:1VFI"
FT HELIX 62..73
FT /evidence="ECO:0007829|PDB:1VFI"
FT HELIX 75..95
FT /evidence="ECO:0007829|PDB:1VFI"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:1VFI"
FT HELIX 109..117
FT /evidence="ECO:0007829|PDB:1VFI"
SQ SEQUENCE 120 AA; 13225 MW; 97C7A41B100B0051 CRC64;
MSKVIFALVL VVVLVACINA TYVEFEEAYA PVDCKGQCTT PCEPLTACKE KCAESCETSA
DKKTCRRNCK KADCEPQDKV CDACRMKCHK ACRAANCASE CPKHEHKSDT CRACMKTNCK
