NRAMB_CAEEL
ID NRAMB_CAEEL Reviewed; 546 AA.
AC Q21433;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=NRAMP-like transporter smf-2 {ECO:0000305};
DE AltName: Full=Divalent metal transporter smf-2 {ECO:0000305};
GN Name=smf-2 {ECO:0000312|WormBase:K11G12.3};
GN ORFNames=K11G12.3 {ECO:0000312|WormBase:K11G12.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
RX PubMed=19785996; DOI=10.1016/j.bbrc.2009.09.082;
RA Bandyopadhyay J., Song H.O., Park B.J., Singaravelu G., Sun J.L., Ahnn J.,
RA Cho J.H.;
RT "Functional assessment of Nramp-like metal transporters and manganese in
RT Caenorhabditis elegans.";
RL Biochem. Biophys. Res. Commun. 390:136-141(2009).
RN [3] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION BY MANGANESE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19801673; DOI=10.1074/jbc.m109.051409;
RA Settivari R., Levora J., Nass R.;
RT "The divalent metal transporter homologues SMF-1/2 mediate dopamine neuron
RT sensitivity in caenorhabditis elegans models of manganism and parkinson
RT disease.";
RL J. Biol. Chem. 284:35758-35768(2009).
RN [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY MANGANESE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=19924247; DOI=10.1371/journal.pone.0007792;
RA Au C., Benedetto A., Anderson J., Labrousse A., Erikson K., Ewbank J.J.,
RA Aschner M.;
RT "SMF-1, SMF-2 and SMF-3 DMT1 orthologues regulate and are regulated
RT differentially by manganese levels in C. elegans.";
RL PLoS ONE 4:E7792-E7792(2009).
CC -!- FUNCTION: Probable divalent metal ion transporter which regulates
CC Mn(2+) uptake. {ECO:0000269|PubMed:19801673,
CC ECO:0000269|PubMed:19924247}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:19924247}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:19924247}. Note=Predominantly localizes in
CC cytoplasmic vesicles in epithelial cells.
CC {ECO:0000269|PubMed:19924247}.
CC -!- TISSUE SPECIFICITY: Expressed in dopaminergic neurons (at protein
CC level) (PubMed:19801673). Primarily expressed in mc1, mc2 and mc3
CC epithelial cells of the pharynx and vpil-6 pharyngeal-intestinal valve
CC cells displaying an anterior-posterior expression gradient
CC (PubMed:19924247). Expressed in gonad sheath cells (PubMed:19924247).
CC {ECO:0000269|PubMed:19801673, ECO:0000269|PubMed:19924247}.
CC -!- INDUCTION: Slightly repressed by high levels of Mn(2+)
CC (PubMed:19801673, PubMed:19924247). {ECO:0000269|PubMed:19801673,
CC ECO:0000269|PubMed:19924247}.
CC -!- DISRUPTION PHENOTYPE: Increased mortality rate and increased body
CC levels of Mn(2+) when Mn(2+) levels are high in the environment
CC (PubMed:19924247, PubMed:19785996). Reduced survival rate in response
CC to infection mediated by pathogenic bacterium S.aureus
CC (PubMed:19785996). Iron levels are low, independently of Mn(2+) levels
CC (PubMed:19924247). RNAi-mediated knockdown partially prevents CEP
CC neuron death mediated by the neurotoxin 6-hydroxy dopamine (6-OHDA) but
CC not when mediated by high levels of Mn(2+) (PubMed:19801673).
CC {ECO:0000269|PubMed:19785996, ECO:0000269|PubMed:19801673,
CC ECO:0000269|PubMed:19924247}.
CC -!- SIMILARITY: Belongs to the NRAMP family. {ECO:0000305}.
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DR EMBL; BX284606; CCD70795.2; -; Genomic_DNA.
DR RefSeq; NP_509131.2; NM_076730.2.
DR AlphaFoldDB; Q21433; -.
DR SMR; Q21433; -.
DR STRING; 6239.K11G12.3; -.
DR PeptideAtlas; Q21433; -.
DR EnsemblMetazoa; K11G12.3.1; K11G12.3.1; WBGene00004877.
DR GeneID; 191766; -.
DR KEGG; cel:CELE_K11G12.3; -.
DR UCSC; K11G12.3; c. elegans.
DR CTD; 191766; -.
DR WormBase; K11G12.3; CE47234; WBGene00004877; smf-2.
DR eggNOG; KOG1291; Eukaryota.
DR HOGENOM; CLU_020088_5_2_1; -.
DR InParanoid; Q21433; -.
DR OMA; PHTIYLG; -.
DR OrthoDB; 666470at2759; -.
DR PhylomeDB; Q21433; -.
DR Reactome; R-CEL-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-CEL-425410; Metal ion SLC transporters.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-6803544; Ion influx/efflux at host-pathogen interface.
DR PRO; PR:Q21433; -.
DR Proteomes; UP000001940; Chromosome X.
DR GO; GO:0016324; C:apical plasma membrane; IDA:WormBase.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043229; C:intracellular organelle; IDA:WormBase.
DR GO; GO:0015086; F:cadmium ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005381; F:iron ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005384; F:manganese ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0046915; F:transition metal ion transmembrane transporter activity; ISS:WormBase.
DR GO; GO:0055072; P:iron ion homeostasis; IMP:WormBase.
DR GO; GO:0055071; P:manganese ion homeostasis; IMP:WormBase.
DR GO; GO:0010042; P:response to manganese ion; IMP:WormBase.
DR GO; GO:0010038; P:response to metal ion; IGI:WormBase.
DR GO; GO:0000041; P:transition metal ion transport; ISS:WormBase.
DR HAMAP; MF_00221; NRAMP; 1.
DR InterPro; IPR001046; NRAMP_fam.
DR PANTHER; PTHR11706; PTHR11706; 1.
DR Pfam; PF01566; Nramp; 1.
DR PRINTS; PR00447; NATRESASSCMP.
DR TIGRFAMs; TIGR01197; nramp; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasmic vesicle; Glycoprotein; Ion transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..546
FT /note="NRAMP-like transporter smf-2"
FT /evidence="ECO:0000305"
FT /id="PRO_0000437465"
FT TOPO_DOM 1..42
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..70
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..119
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..152
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..181
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 203..228
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 250..270
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..334
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..386
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 387..407
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 408..415
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 437..453
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 454..474
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 475..483
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 484..504
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 505..546
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 546 AA; 61238 MW; 00BF38D18242C63D CRC64;
MPGFQNANIS DLAPPAREKT FDDTIAVKIP EDEKNTWFSW RKLWAFTGPG FLMSIAYLDP
GNIESDLQAG AQAEYKLLWV LLVSHIVGML LQRMSARLGV VSGKHMAEIA YDYYPLVPRI
ILWLMIEIAI VCSDMQEVIG TAIAIYLLSS GKIPLLVGVL ITILDTFTFL FIDRYGIRKL
EFIFVALIST MAISFGYEFV VMKPVLTKVL TGTVVPWCSG CGKEEIITAI SIFGAVIMPH
NFYLHSALVK SRKVDRSSKT RIAEANKYFS IESAFALSVS FFINLFVLSV FARGLYQKTN
GDVNSMCLSH NDIPDSNVFP NNTSSVTVDL FQGGIYLGCQ FGLFAMIIWA IGIFAAGQSS
TMTGTYTGQF VMEGFVRISW PKWKRVLITR AVAITPTLIL CIKAHGIKNL TGMNDFLNCV
QMVQLPFALI PMITFTSSKR IMHNFRTSKP LQYFSIICGI ITIGINVYFI FQYVTENFGT
GWLIFVIIGP FTLLYIAFIL YLAIYCLVAC ELMNDTVNLP GFDFHRTLEL DAPWITETFV
VNDVYF
