VIT1_EUCGR
ID VIT1_EUCGR Reviewed; 249 AA.
AC P0DO17;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-JUN-2019, sequence version 1.
DT 03-AUG-2022, entry version 14.
DE RecName: Full=Vacuolar iron transporter 1 {ECO:0000303|PubMed:30742036};
DE Short=EgVIT1 {ECO:0000303|PubMed:30742036};
GN Name=VIT1 {ECO:0000303|PubMed:30742036};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24919147; DOI=10.1038/nature13308;
RA Myburg A.A., Grattapaglia D., Tuskan G.A., Hellsten U., Hayes R.D.,
RA Grimwood J., Jenkins J., Lindquist E., Tice H., Bauer D., Goodstein D.M.,
RA Dubchak I., Poliakov A., Mizrachi E., Kullan A.R., Hussey S.G., Pinard D.,
RA van der Merwe K., Singh P., van Jaarsveld I., Silva-Junior O.B.,
RA Togawa R.C., Pappas M.R., Faria D.A., Sansaloni C.P., Petroli C.D.,
RA Yang X., Ranjan P., Tschaplinski T.J., Ye C.Y., Li T., Sterck L.,
RA Vanneste K., Murat F., Soler M., Clemente H.S., Saidi N., Cassan-Wang H.,
RA Dunand C., Hefer C.A., Bornberg-Bauer E., Kersting A.R., Vining K.,
RA Amarasinghe V., Ranik M., Naithani S., Elser J., Boyd A.E., Liston A.,
RA Spatafora J.W., Dharmwardhana P., Raja R., Sullivan C., Romanel E.,
RA Alves-Ferreira M., Kuelheim C., Foley W., Carocha V., Paiva J., Kudrna D.,
RA Brommonschenkel S.H., Pasquali G., Byrne M., Rigault P., Tibbits J.,
RA Spokevicius A., Jones R.C., Steane D.A., Vaillancourt R.E., Potts B.M.,
RA Joubert F., Barry K., Pappas G.J., Strauss S.H., Jaiswal P.,
RA Grima-Pettenati J., Salse J., Van de Peer Y., Rokhsar D.S., Schmutz J.;
RT "The genome of Eucalyptus grandis.";
RL Nature 510:356-362(2014).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 23-249 IN COMPLEX WITH IRON IONS;
RP ZINC IONS; COBALT IONS AND NICKEL IONS, FUNCTION, ACTIVITY REGULATION,
RP HOMODIMERIZATION, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF GLU-32;
RP ASP-36; ASP-43; GLY-44; PRO-48; GLY-69; GLU-72; GLY-76; MET-80; GLU-102;
RP GLU-105; GLU-113; GLU-116; 149-MET-MET-150 AND GLU-153.
RX PubMed=30742036; DOI=10.1038/s41477-019-0367-2;
RA Kato T., Kumazaki K., Wada M., Taniguchi R., Nakane T., Yamashita K.,
RA Hirata K., Ishitani R., Ito K., Nishizawa T., Nureki O.;
RT "Crystal structure of plant vacuolar iron transporter VIT1.";
RL Nat. Plants 5:308-315(2019).
CC -!- FUNCTION: Vacuolar iron transporter involved in the transfer of iron
CC ions from the cytosol to the vacuole for intracellular iron storage
CC (PubMed:30742036). Can transport cobalt ions from the cytosol to the
CC vacuole (PubMed:30742036). {ECO:0000269|PubMed:30742036}.
CC -!- ACTIVITY REGULATION: Transport of iron ions is inhibited by zinc ions.
CC {ECO:0000269|PubMed:30742036}.
CC -!- SUBUNIT: Homodimer (PubMed:30742036). The dimeric interaction is
CC mediated by both the transmembrane domains (TMDs) and the cytoplasmic
CC metal binding domain (MBD) (PubMed:30742036).
CC {ECO:0000269|PubMed:30742036}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000305|PubMed:30742036};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- DOMAIN: The cytoplasmic metal binding domain (MBD) is located between
CC transmembrane 2 (TM2) and transmembrane 3 (TM3).
CC {ECO:0000269|PubMed:30742036}.
CC -!- MISCELLANEOUS: Can mediate sequestration of iron ions into vacuoles
CC when expressed in the yeast ccc1 mutant. {ECO:0000269|PubMed:30742036}.
CC -!- SIMILARITY: Belongs to the CCC1 family. {ECO:0000305}.
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DR RefSeq; XP_010066556.1; XM_010068254.2.
DR RefSeq; XP_010066557.1; XM_010068255.2.
DR PDB; 6IU3; X-ray; 2.70 A; A=23-249.
DR PDB; 6IU4; X-ray; 3.50 A; A=23-249.
DR PDB; 6IU5; X-ray; 2.25 A; A/B/C/D/E/F/H/I=90-165.
DR PDB; 6IU6; X-ray; 2.90 A; A/B/C/D/E/F/H/I=90-165.
DR PDB; 6IU8; X-ray; 2.70 A; A/B/C/D/E/F/H/I=90-165.
DR PDB; 6IU9; X-ray; 3.00 A; A/B/C/D/E/F/H/I=90-165.
DR PDBsum; 6IU3; -.
DR PDBsum; 6IU4; -.
DR PDBsum; 6IU5; -.
DR PDBsum; 6IU6; -.
DR PDBsum; 6IU8; -.
DR PDBsum; 6IU9; -.
DR AlphaFoldDB; P0DO17; -.
DR SMR; P0DO17; -.
DR STRING; 71139.XP_010066556.1; -.
DR GeneID; 104453645; -.
DR KEGG; egr:104453645; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005774; C:vacuolar membrane; IDA:UniProtKB.
DR GO; GO:0005384; F:manganese ion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0030026; P:cellular manganese ion homeostasis; IEA:InterPro.
DR GO; GO:0006880; P:intracellular sequestering of iron ion; IDA:UniProtKB.
DR InterPro; IPR008217; Ccc1_fam.
DR PANTHER; PTHR31851; PTHR31851; 1.
DR Pfam; PF01988; VIT1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Ion transport; Iron; Iron transport; Membrane; Metal-binding;
KW Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..249
FT /note="Vacuolar iron transporter 1"
FT /id="PRO_0000447369"
FT TOPO_DOM 1..36
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..63
FT /note="Vacuolar"
FT /evidence="ECO:0000305"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..170
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..194
FT /note="Vacuolar"
FT /evidence="ECO:0000305"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..226
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248..249
FT /note="Vacuolar"
FT /evidence="ECO:0000305"
FT REGION 90..165
FT /note="Cytoplasmic metal binding domain (MBD)"
FT /evidence="ECO:0000269|PubMed:30742036"
FT BINDING 102
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:30742036,
FT ECO:0007744|PDB:6IU3, ECO:0007744|PDB:6IU4"
FT BINDING 102
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:30742036,
FT ECO:0007744|PDB:6IU3, ECO:0007744|PDB:6IU4"
FT BINDING 105
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:30742036,
FT ECO:0007744|PDB:6IU3, ECO:0007744|PDB:6IU4"
FT BINDING 105
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:30742036,
FT ECO:0007744|PDB:6IU3, ECO:0007744|PDB:6IU4"
FT BINDING 113
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:30742036,
FT ECO:0007744|PDB:6IU3, ECO:0007744|PDB:6IU4"
FT BINDING 113
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:30742036,
FT ECO:0007744|PDB:6IU3, ECO:0007744|PDB:6IU4"
FT BINDING 113
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:30742036,
FT ECO:0007744|PDB:6IU3, ECO:0007744|PDB:6IU4"
FT BINDING 116
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:30742036,
FT ECO:0007744|PDB:6IU3, ECO:0007744|PDB:6IU4"
FT BINDING 116
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:30742036,
FT ECO:0007744|PDB:6IU3, ECO:0007744|PDB:6IU4"
FT BINDING 116
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:30742036,
FT ECO:0007744|PDB:6IU3, ECO:0007744|PDB:6IU4"
FT BINDING 149
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:30742036,
FT ECO:0007744|PDB:6IU3, ECO:0007744|PDB:6IU4"
FT BINDING 153
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:30742036,
FT ECO:0007744|PDB:6IU3, ECO:0007744|PDB:6IU4"
FT MUTAGEN 32
FT /note="E->A: Significantly reduces transport of iron ions;
FT when associated with A-36."
FT /evidence="ECO:0000269|PubMed:30742036"
FT MUTAGEN 36
FT /note="D->A: Significantly reduces transport of iron ions;
FT when associated with A-32."
FT /evidence="ECO:0000269|PubMed:30742036"
FT MUTAGEN 43
FT /note="D->A: Strongly reduces transport of iron ions."
FT /evidence="ECO:0000269|PubMed:30742036"
FT MUTAGEN 44
FT /note="G->A: Strongly reduces transport of iron ions."
FT /evidence="ECO:0000269|PubMed:30742036"
FT MUTAGEN 48
FT /note="P->A: Strongly reduces transport of iron ions."
FT /evidence="ECO:0000269|PubMed:30742036"
FT MUTAGEN 69
FT /note="G->A: Reduces transport of iron ions 2-fold."
FT /evidence="ECO:0000269|PubMed:30742036"
FT MUTAGEN 72
FT /note="E->A: Strongly reduces transport of iron ions."
FT /evidence="ECO:0000269|PubMed:30742036"
FT MUTAGEN 76
FT /note="G->A: Strongly reduces transport of iron ions."
FT /evidence="ECO:0000269|PubMed:30742036"
FT MUTAGEN 80
FT /note="M->A: Strongly reduces transport of iron ions."
FT /evidence="ECO:0000269|PubMed:30742036"
FT MUTAGEN 102
FT /note="E->Q: Strongly reduces transport of iron ions; when
FT associated with Q-105; Q-113; Q-116 and Q-153."
FT /evidence="ECO:0000269|PubMed:30742036"
FT MUTAGEN 105
FT /note="E->Q: Strongly reduces transport of iron ions; when
FT associated with Q-102; Q-113; Q-116 and Q-153."
FT /evidence="ECO:0000269|PubMed:30742036"
FT MUTAGEN 113
FT /note="E->Q: Strongly reduces transport of iron ions; when
FT associated with Q-102; Q-105; Q-116 and Q-153."
FT /evidence="ECO:0000269|PubMed:30742036"
FT MUTAGEN 116
FT /note="E->Q: Strongly reduces transport of iron ions; when
FT associated with Q-102; Q-105; Q-113 and Q-153."
FT /evidence="ECO:0000269|PubMed:30742036"
FT MUTAGEN 149..150
FT /note="MM->LL: Strongly reduces transport of iron ions."
FT /evidence="ECO:0000269|PubMed:30742036"
FT MUTAGEN 153
FT /note="E->Q: Strongly reduces transport of iron ions; when
FT associated with Q-102; Q-105; Q-113 and Q-116."
FT /evidence="ECO:0000269|PubMed:30742036"
SQ SEQUENCE 249 AA; 26278 MW; F6138534EDC8E2C5 CRC64;
MADGANDGGN PGAEEQQRLL DQHKEAHFTA GEIVRDIIIG VSDGLTVPFA LAAGLSGANA
SSSIVLTAGI AEVAAGAISM GLGGYLAAKS EADNYARELK REQEEIIRVP DTEAAEVAEI
LARYGIEPHE YGPVVNALRK KPQAWLDFMM KFELGLEKPD PKRALQSAFT IAIAYVLGGL
VPLIPYMFIP VARKAVVASV ILTLMALLIF GYAKGYFTDN KPFKSALQTA LIGAIASAAA
FGMAKAVQS
