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NRAMP-like transporter smf-3 (DMT-1) (Divalent metal transporter smf-3)

 NRAMC_CAEEL             Reviewed;         560 AA.
Q95XG8;
05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
25-JAN-2012, sequence version 3.
12-SEP-2018, entry version 107.
RecName: Full=NRAMP-like transporter smf-3 {ECO:0000305};
AltName: Full=DMT-1 {ECO:0000303|PubMed:23106139};
AltName: Full=Divalent metal transporter smf-3 {ECO:0000305};
Name=smf-3 {ECO:0000312|WormBase:Y69A2AR.4};
ORFNames=Y69A2AR.4 {ECO:0000312|EMBL:CCD74141.1};
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
[1] {ECO:0000312|Proteomes:UP000001940}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[2] {ECO:0000305}
FUNCTION, TISSUE SPECIFICITY, INDUCTION BY BACTERIA, AND DISRUPTION
PHENOTYPE.
PubMed=19785996; DOI=10.1016/j.bbrc.2009.09.082;
Bandyopadhyay J., Song H.O., Park B.J., Singaravelu G., Sun J.L.,
Ahnn J., Cho J.H.;
"Functional assessment of Nramp-like metal transporters and manganese
in Caenorhabditis elegans.";
Biochem. Biophys. Res. Commun. 390:136-141(2009).
[3] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY
MANGANESE, AND DISRUPTION PHENOTYPE.
PubMed=19924247; DOI=10.1371/journal.pone.0007792;
Au C., Benedetto A., Anderson J., Labrousse A., Erikson K.,
Ewbank J.J., Aschner M.;
"SMF-1, SMF-2 and SMF-3 DMT1 orthologues regulate and are regulated
differentially by manganese levels in C. elegans.";
PLoS ONE 4:E7792-E7792(2009).
[4] {ECO:0000305}
FUNCTION, INDUCTION BY IRON, AND DISRUPTION PHENOTYPE.
PubMed=22194696; DOI=10.1371/journal.pgen.1002394;
Romney S.J., Newman B.S., Thacker C., Leibold E.A.;
"HIF-1 regulates iron homeostasis in Caenorhabditis elegans by
activation and inhibition of genes involved in iron uptake and
storage.";
PLoS Genet. 7:E1002394-E1002394(2011).
[5] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY
ALUMINUM, AND DISRUPTION PHENOTYPE.
PubMed=23106139; DOI=10.1111/jnc.12072;
VanDuyn N., Settivari R., LeVora J., Zhou S., Unrine J., Nass R.;
"The metal transporter SMF-3/DMT-1 mediates aluminum-induced dopamine
neuron degeneration.";
J. Neurochem. 124:147-157(2013).
-!- FUNCTION: Probable divalent metal ion transporter which regulates
the uptake of several heavy metals such as Mn(2+), Al(3+) and iron
(PubMed:19924247, PubMed:23106139, PubMed:19785996,
PubMed:22194696). Plays a role in modulating Al(3+)-induced
dopamine (DA) neuron degeneration through the intracellular
sequestration of Al(3+) (PubMed:23106139).
{ECO:0000269|PubMed:19785996, ECO:0000269|PubMed:19924247,
ECO:0000269|PubMed:22194696, ECO:0000269|PubMed:23106139}.
-!- SUBCELLULAR LOCATION: Apical cell membrane
{ECO:0000269|PubMed:19924247}; Multi-pass membrane protein
{ECO:0000255}. Cytoplasmic vesicle membrane
{ECO:0000269|PubMed:19924247, ECO:0000269|PubMed:23106139}.
Note=Translocates to apical cytoplasmic vesicles in intestine in
response to high Mn(2+) levels (PubMed:19924247). In dopaminergic
neurons, localizes to cytoplasmic vesicles (PubMed:23106139).
{ECO:0000269|PubMed:19924247, ECO:0000269|PubMed:23106139}.
-!- TISSUE SPECIFICITY: Expressed in dopaminergic neurons (at protein
level) (PubMed:23106139). Expressed in intestine with a weaker
expression in the most proximal and distal regions
(PubMed:19785996, PubMed:19924247). Weakly expressed in the hyp1-
6, hyp7 and hyp8-12 hypodermis and in head and tail neurons
(PubMed:19924247). {ECO:0000269|PubMed:19785996,
ECO:0000269|PubMed:19924247, ECO:0000269|PubMed:23106139}.
-!- INDUCTION: Induced by pathogenic bacterium S.aureus
(PubMed:19785996). Repressed by high levels of Mn(2+)
(PubMed:19924247). Repressed by high levels of Al(3+)
(PubMed:23106139). Induced by low iron levels (PubMed:22194696).
{ECO:0000269|PubMed:19785996, ECO:0000269|PubMed:19924247,
ECO:0000269|PubMed:22194696, ECO:0000269|PubMed:23106139}.
-!- DISRUPTION PHENOTYPE: Increased survival rate and reduced body
levels of iron in response to increasing Mn(2+) levels
(PubMed:19924247). Reduced survival rate in response to high
Mn(2+) levels or to infection mediated by pathogenic bacterium
S.aureus (PubMed:19785996). Reduced CEP neuron death and higher
Al(3+) accumulation in the body in response to high Al(3+) levels
(PubMed:23106139). Reduced ferritin ftn-1 mRNA levels and Mn(2+)
and iron body levels (PubMed:22194696). Increased sfm-1, sfm-2 and
sfm-3 mRNA levels (PubMed:19924247). {ECO:0000269|PubMed:19785996,
ECO:0000269|PubMed:19924247, ECO:0000269|PubMed:22194696,
ECO:0000269|PubMed:23106139}.
-!- SIMILARITY: Belongs to the NRAMP family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; BX284604; CCD74141.1; -; Genomic_DNA.
RefSeq; NP_500235.4; NM_067834.4.
UniGene; Cel.30494; -.
ProteinModelPortal; Q95XG8; -.
SMR; Q95XG8; -.
STRING; 6239.Y69A2AR.4; -.
TCDB; 2.A.55.2.15; the metal ion (mn(2+)-iron) transporter (nramp) family.
PaxDb; Q95XG8; -.
EnsemblMetazoa; Y69A2AR.4; Y69A2AR.4; WBGene00004878.
GeneID; 177044; -.
KEGG; cel:CELE_Y69A2AR.4; -.
UCSC; Y69A2AR.4; c. elegans.
CTD; 177044; -.
WormBase; Y69A2AR.4; CE46127; WBGene00004878; smf-3.
eggNOG; KOG1291; Eukaryota.
eggNOG; KOG3923; Eukaryota.
eggNOG; COG1914; LUCA.
GeneTree; ENSGT00390000006526; -.
HOGENOM; HOG000152203; -.
InParanoid; Q95XG8; -.
KO; K21398; -.
OMA; FMWLQQY; -.
OrthoDB; EOG091G05M9; -.
Reactome; R-CEL-1222556; ROS, RNS production in phagocytes.
Reactome; R-CEL-425410; Metal ion SLC transporters.
Reactome; R-CEL-6798695; Neutrophil degranulation.
Reactome; R-CEL-6803544; Ion influx/efflux at host-pathogen interface.
Reactome; R-CEL-917937; Iron uptake and transport.
PRO; PR:Q95XG8; -.
Proteomes; UP000001940; Chromosome IV.
Bgee; WBGene00004878; Expressed in 3 organ(s), highest expression level in multi-cellular organism.
GO; GO:0016324; C:apical plasma membrane; IDA:WormBase.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005622; C:intracellular; IDA:WormBase.
GO; GO:0046915; F:transition metal ion transmembrane transporter activity; ISS:WormBase.
GO; GO:0055072; P:iron ion homeostasis; IMP:WormBase.
GO; GO:0055071; P:manganese ion homeostasis; IMP:WormBase.
GO; GO:0010042; P:response to manganese ion; IMP:WormBase.
GO; GO:0010038; P:response to metal ion; IGI:WormBase.
GO; GO:0006979; P:response to oxidative stress; IMP:WormBase.
GO; GO:0000041; P:transition metal ion transport; ISS:WormBase.
HAMAP; MF_00221; NRAMP; 1.
InterPro; IPR001046; NRAMP_fam.
PANTHER; PTHR11706; PTHR11706; 1.
Pfam; PF01566; Nramp; 1.
PRINTS; PR00447; NATRESASSCMP.
TIGRFAMs; TIGR01197; nramp; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Cytoplasmic vesicle; Glycoprotein;
Ion transport; Iron; Iron transport; Membrane; Reference proteome;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 560 NRAMP-like transporter smf-3.
{ECO:0000305}.
/FTId=PRO_0000437466.
TOPO_DOM 1 43 Cytoplasmic. {ECO:0000305}.
TRANSMEM 44 64 Helical. {ECO:0000255}.
TOPO_DOM 65 71 Extracellular. {ECO:0000305}.
TRANSMEM 72 92 Helical. {ECO:0000255}.
TOPO_DOM 93 120 Cytoplasmic. {ECO:0000305}.
TRANSMEM 121 141 Helical. {ECO:0000255}.
TOPO_DOM 142 152 Extracellular. {ECO:0000305}.
TRANSMEM 153 173 Helical. {ECO:0000255}.
TOPO_DOM 174 182 Cytoplasmic. {ECO:0000305}.
TRANSMEM 183 203 Helical. {ECO:0000255}.
TOPO_DOM 204 229 Extracellular. {ECO:0000305}.
TRANSMEM 230 250 Helical. {ECO:0000255}.
TOPO_DOM 251 268 Cytoplasmic. {ECO:0000305}.
TRANSMEM 269 289 Helical. {ECO:0000255}.
TOPO_DOM 290 339 Extracellular. {ECO:0000305}.
TRANSMEM 340 360 Helical. {ECO:0000255}.
TOPO_DOM 361 390 Cytoplasmic. {ECO:0000305}.
TRANSMEM 391 411 Helical. {ECO:0000255}.
TOPO_DOM 412 420 Extracellular. {ECO:0000305}.
TRANSMEM 421 441 Helical. {ECO:0000255}.
TOPO_DOM 442 458 Cytoplasmic. {ECO:0000305}.
TRANSMEM 459 479 Helical. {ECO:0000255}.
TOPO_DOM 480 486 Extracellular. {ECO:0000305}.
TRANSMEM 487 507 Helical. {ECO:0000255}.
TOPO_DOM 508 560 Cytoplasmic. {ECO:0000305}.
CARBOHYD 310 310 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 414 414 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
SEQUENCE 560 AA; 63186 MW; BCFF0BC8B3055ABC CRC64;
MEGEMKCPIE EIREKPEMRK AQQTYEVQVE VEDTPDTTFS WRKLWAFTGP GFLMSIAYLD
PGNIESDLQA GAISYFKLIW VLLVAHIMGL LLQRLAARLG VVSGKHMAEI AFSYYPKIPR
LVLWMLVESA IVGSDMQEVI GTAISFYLLS NGVIPLWAGV LITICDTFTF LFLEKYGVRK
FEAFFCFLIT CMAITFGYEF GVSAPDAGKM FSGMFVPWCN GCDNNMVMQG VAIIGAVIMP
HNFYLHSALV KSRRVDRRRA EKVTEANKYF FIESAFALFV SFIINTLVIS VFAQGMYGKT
NQDIRDTCYN NTHNGMPDFY KVEFPANNDA AQSDIYHAGI FLGCTFGIFA LYVWAVGILA
AGQSSTMTGT YAGQFAMEGF IQIKLPQWKR ILITRSLAIL PTLAVVIFSG GIDNISSLND
FLNCLQLIQL PFALIPVLTF VSDRNIMHEY KLASVSKVVS IVISLIILFI NFYFLYSWIG
STFGYNAVSI PITIFCAIFY IIFIAYLTYY CLVAMEFISP IQTKWLAEPI YHDFDAPWLE
DSENPSTKNT ISDDELSMRY


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