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Natural resistance-associated macrophage protein 2 (NRAMP 2) (Divalent cation transporter 1) (Divalent metal transporter 1) (DMT-1) (Solute carrier family 11 member 2)

 NRAM2_RAT               Reviewed;         568 AA.
O54902; O35172;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
22-NOV-2017, entry version 143.
RecName: Full=Natural resistance-associated macrophage protein 2;
Short=NRAMP 2;
AltName: Full=Divalent cation transporter 1;
AltName: Full=Divalent metal transporter 1;
Short=DMT-1;
AltName: Full=Solute carrier family 11 member 2;
Name=Slc11a2; Synonyms=Dct1, Dmt1, Nramp2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
STRAIN=Sprague-Dawley;
PubMed=9242408; DOI=10.1038/41343;
Gunshin H., Mackenzie B., Berger U.V., Gunshin Y., Romero M.F.,
Boron W.F., Nussberger S., Gollan J.L., Hediger M.A.;
"Cloning and characterization of a mammalian proton-coupled metal-ion
transporter.";
Nature 388:482-488(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Cerebellum;
Fleming M.D., Romano M.A., Su M.A., Garrick L.M., Garrick M.D.,
Andrews N.C.;
"Rat natural resistance associated macrophage protein-2 (Nramp2), C-
terminal exon alternative splice variant.";
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-556 (ISOFORM 1), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[4]
VARIANT B ARG-185.
PubMed=9448300; DOI=10.1073/pnas.95.3.1148;
Fleming M.D., Romano M.A., Su M.A., Garrick L.M., Garrick M.D.,
Andrews N.C.;
"Nramp2 is mutated in the anemic Belgrade (b) rat: evidence of a role
for Nramp2 in endosomal iron transport.";
Proc. Natl. Acad. Sci. U.S.A. 95:1148-1153(1998).
-!- FUNCTION: May serve to import iron into the mitochondria (By
similarity). Important in metal transport, in particular iron. Can
also transport zinc, manganese, cobalt, cadmium, copper, nickel
and lead. Involved in apical iron uptake into duodenal
enterocytes. Involved in iron transport from acidified endosomes
into the cytoplasm of erythroid precursor cells. May play an
important role in hepatic iron accumulation and tissue iron
distribution. {ECO:0000250|UniProtKB:P49281,
ECO:0000269|PubMed:9242408}.
-!- SUBUNIT: Forms a complex with NDFIP1 and NEDD4L, in cortical
neurons, in response to iron and colbalt exposure; this
interaction leads to ubiquitination by NEDD4L and proteasome-
dependent degradation. Interacts with NDFIP2. Interacts with COX2
and TOM6 at the outer mitochondrion membrane. Interacts with
ARRDC1; controls the incorporation of SLC11A2 into extracellular
vesicles through an ubiquitination-dependent mechanism. Interacts
with ARRDC4; controls the incorporation of SLC11A2 into
extracellular vesicles through an ubiquitination-dependent
mechanism. {ECO:0000250|UniProtKB:P49281,
ECO:0000250|UniProtKB:P49282}.
-!- SUBCELLULAR LOCATION: Endosome membrane
{ECO:0000250|UniProtKB:P49281}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P49281}. Mitochondrion outer membrane
{ECO:0000250|UniProtKB:P49281}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P49281}. Cell membrane
{ECO:0000250|UniProtKB:P49281}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P49281}. Note=Also found in extracellular
vesicles different from exosomes. {ECO:0000250|UniProtKB:P49281}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=2; Synonyms=Non-IRE;
IsoId=O54902-1; Sequence=Displayed;
Name=1; Synonyms=IRE;
IsoId=O54902-2; Sequence=VSP_003597;
Note=Contains a phosphoserine at position 556.
{ECO:0000244|PubMed:22673903};
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- PTM: Ubiquitinated by WWP2. {ECO:0000250}.
-!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P49281}.
-!- DISEASE: Note=Defects in Slc11a2 are the cause of microcytic
anemia (Belgrade or b). Homozygous b/b rats have hypochromic
microcytic anemia due to severe defects in intestinal iron
absorption and erythroid iron utilization.
-!- SIMILARITY: Belongs to the NRAMP family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF008439; AAC53319.1; -; mRNA.
EMBL; AF029757; AAC24495.1; -; mRNA.
RefSeq; NP_037305.2; NM_013173.2.
UniGene; Rn.11418; -.
ProteinModelPortal; O54902; -.
BioGrid; 247744; 1.
STRING; 10116.ENSRNOP00000026531; -.
TCDB; 2.A.55.2.2; the metal ion (mn(2+)-iron) transporter (nramp) family.
iPTMnet; O54902; -.
PhosphoSitePlus; O54902; -.
PaxDb; O54902; -.
GeneID; 25715; -.
KEGG; rno:25715; -.
UCSC; RGD:3684; rat. [O54902-1]
CTD; 4891; -.
RGD; 3684; Slc11a2.
eggNOG; KOG1291; Eukaryota.
eggNOG; COG1914; LUCA.
HOGENOM; HOG000152203; -.
HOVERGEN; HBG052665; -.
InParanoid; O54902; -.
KO; K21398; -.
OrthoDB; EOG091G05M9; -.
PhylomeDB; O54902; -.
PRO; PR:O54902; -.
Proteomes; UP000002494; Unplaced.
Genevisible; O54902; RN.
GO; GO:0045177; C:apical part of cell; IDA:RGD.
GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
GO; GO:0045178; C:basal part of cell; ISO:RGD.
GO; GO:0005903; C:brush border; ISO:RGD.
GO; GO:0031526; C:brush border membrane; ISO:RGD.
GO; GO:0009986; C:cell surface; ISO:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
GO; GO:0005769; C:early endosome; ISS:UniProtKB.
GO; GO:0012505; C:endomembrane system; ISO:RGD.
GO; GO:0005768; C:endosome; ISO:RGD.
GO; GO:0016021; C:integral component of membrane; IDA:RGD.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0005770; C:late endosome; ISO:RGD.
GO; GO:0031902; C:late endosome membrane; IDA:RGD.
GO; GO:0005765; C:lysosomal membrane; IDA:RGD.
GO; GO:0005764; C:lysosome; ISO:RGD.
GO; GO:0016020; C:membrane; ISO:RGD.
GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; ISO:RGD.
GO; GO:0070826; C:paraferritin complex; ISO:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
GO; GO:0005886; C:plasma membrane; ISO:RGD.
GO; GO:0055037; C:recycling endosome; ISO:RGD.
GO; GO:0005802; C:trans-Golgi network; ISO:RGD.
GO; GO:0005773; C:vacuole; ISO:RGD.
GO; GO:0046870; F:cadmium ion binding; IDA:RGD.
GO; GO:0015086; F:cadmium ion transmembrane transporter activity; IDA:RGD.
GO; GO:0050897; F:cobalt ion binding; IDA:RGD.
GO; GO:0015087; F:cobalt ion transmembrane transporter activity; IDA:RGD.
GO; GO:0005507; F:copper ion binding; IDA:RGD.
GO; GO:0005375; F:copper ion transmembrane transporter activity; IDA:RGD.
GO; GO:0015093; F:ferrous iron transmembrane transporter activity; IMP:RGD.
GO; GO:0015639; F:ferrous iron uptake transmembrane transporter activity; ISS:UniProtKB.
GO; GO:0015078; F:hydrogen ion transmembrane transporter activity; ISO:RGD.
GO; GO:0022890; F:inorganic cation transmembrane transporter activity; ISO:RGD.
GO; GO:0005506; F:iron ion binding; IDA:RGD.
GO; GO:0005381; F:iron ion transmembrane transporter activity; IDA:RGD.
GO; GO:0015094; F:lead ion transmembrane transporter activity; IDA:RGD.
GO; GO:0030145; F:manganese ion binding; IDA:RGD.
GO; GO:0005384; F:manganese ion transmembrane transporter activity; IDA:RGD.
GO; GO:0016151; F:nickel cation binding; IDA:RGD.
GO; GO:0015099; F:nickel cation transmembrane transporter activity; IDA:RGD.
GO; GO:0015295; F:solute:proton symporter activity; ISO:RGD.
GO; GO:0046915; F:transition metal ion transmembrane transporter activity; ISO:RGD.
GO; GO:0015100; F:vanadium ion transmembrane transporter activity; ISO:RGD.
GO; GO:0008270; F:zinc ion binding; IDA:RGD.
GO; GO:0005385; F:zinc ion transmembrane transporter activity; ISO:RGD.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:RGD.
GO; GO:0070574; P:cadmium ion transmembrane transport; ISO:RGD.
GO; GO:0006878; P:cellular copper ion homeostasis; IMP:RGD.
GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
GO; GO:0071281; P:cellular response to iron ion; IEP:RGD.
GO; GO:0034599; P:cellular response to oxidative stress; ISO:RGD.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
GO; GO:0006824; P:cobalt ion transport; ISO:RGD.
GO; GO:0098705; P:copper ion import across plasma membrane; IMP:RGD.
GO; GO:0006825; P:copper ion transport; ISO:RGD.
GO; GO:0048813; P:dendrite morphogenesis; ISO:RGD.
GO; GO:0003032; P:detection of oxygen; ISO:RGD.
GO; GO:0048821; P:erythrocyte development; ISO:RGD.
GO; GO:0070627; P:ferrous iron import; ISO:RGD.
GO; GO:0015684; P:ferrous iron transport; IMP:RGD.
GO; GO:0006783; P:heme biosynthetic process; ISO:RGD.
GO; GO:0006826; P:iron ion transport; ISO:RGD.
GO; GO:0015692; P:lead ion transport; ISO:RGD.
GO; GO:0007611; P:learning or memory; ISO:RGD.
GO; GO:0006828; P:manganese ion transport; ISO:RGD.
GO; GO:0060586; P:multicellular organismal iron ion homeostasis; ISO:RGD.
GO; GO:0015675; P:nickel cation transport; ISO:RGD.
GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; ISO:RGD.
GO; GO:0006778; P:porphyrin-containing compound metabolic process; ISO:RGD.
GO; GO:0015992; P:proton transport; ISO:RGD.
GO; GO:0046686; P:response to cadmium ion; IEP:RGD.
GO; GO:0001666; P:response to hypoxia; IEP:RGD.
GO; GO:0010039; P:response to iron ion; IEP:RGD.
GO; GO:0010288; P:response to lead ion; IEP:RGD.
GO; GO:0010042; P:response to manganese ion; IMP:RGD.
GO; GO:0000041; P:transition metal ion transport; IDA:RGD.
GO; GO:0015676; P:vanadium ion transport; ISO:RGD.
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;
Alternative splicing; Cell membrane; Complete proteome;
Disease mutation; Endosome; Glycoprotein; Ion transport; Iron;
Iron transport; Membrane; Mitochondrion; Mitochondrion outer membrane;
Phosphoprotein; Reference proteome; Transmembrane;
Transmembrane helix; Transport; Ubl conjugation.
CHAIN 1 568 Natural resistance-associated macrophage
protein 2.
/FTId=PRO_0000212596.
TOPO_DOM 1 69 Cytoplasmic. {ECO:0000255}.
TRANSMEM 70 90 Helical. {ECO:0000255}.
TOPO_DOM 91 95 Extracellular. {ECO:0000255}.
TRANSMEM 96 117 Helical. {ECO:0000255}.
TOPO_DOM 118 154 Cytoplasmic. {ECO:0000255}.
TRANSMEM 155 175 Helical. {ECO:0000255}.
TOPO_DOM 176 179 Extracellular. {ECO:0000255}.
TRANSMEM 180 194 Helical. {ECO:0000255}.
TOPO_DOM 195 208 Cytoplasmic. {ECO:0000255}.
TRANSMEM 209 229 Helical. {ECO:0000255}.
TOPO_DOM 230 255 Extracellular. {ECO:0000255}.
TRANSMEM 256 276 Helical. {ECO:0000255}.
TOPO_DOM 277 301 Cytoplasmic. {ECO:0000255}.
TRANSMEM 302 322 Helical. {ECO:0000255}.
TOPO_DOM 323 360 Extracellular. {ECO:0000255}.
TRANSMEM 361 381 Helical. {ECO:0000255}.
TOPO_DOM 382 408 Cytoplasmic. {ECO:0000255}.
TRANSMEM 409 429 Helical. {ECO:0000255}.
TOPO_DOM 430 440 Extracellular. {ECO:0000255}.
TRANSMEM 441 461 Helical. {ECO:0000255}.
TOPO_DOM 462 482 Cytoplasmic. {ECO:0000255}.
TRANSMEM 483 503 Helical. {ECO:0000255}.
TOPO_DOM 504 506 Extracellular. {ECO:0000255}.
TRANSMEM 507 527 Helical. {ECO:0000255}.
TOPO_DOM 528 568 Cytoplasmic. {ECO:0000255}.
MOD_RES 564 564 Phosphoserine.
{ECO:0000250|UniProtKB:P49282}.
MOD_RES 567 567 Phosphoserine.
{ECO:0000250|UniProtKB:P49282}.
CARBOHYD 336 336 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 349 349 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 544 568 YHLGLTARPEIYLLNTVDAVSLVSR -> VSISKVLLSEDT
SGGNTK (in isoform 1).
{ECO:0000303|PubMed:9242408}.
/FTId=VSP_003597.
VARIANT 185 185 G -> R (in microcytic anemia).
{ECO:0000269|PubMed:9448300}.
SEQUENCE 568 AA; 62277 MW; C7B77E964E741F4D CRC64;
MVLDPEEKIP DDGASGDHGD SASLGAINPA YSNSSLPHST GDSEEPFTTY FDEKIPIPEE
EYSCFSFRKL WAFTGPGFLM SIAYLDPGNI ESDLQSGAVA GFKLLWVLLL ATIVGLLLQR
LAARLGVVTG LHLAEVCHRQ YPKVPRIILW LMVELAIIGS DMQEVIGSAI AINLLSAGRV
PLYGGVLITI ADTFVFLFLD KYGLRKLEAF FGFLITIMAL TFGYEYVTVK PSQSQVLRGM
FVPSCSGCHT PQVEQAVGIV GAVIMPHNMY LHSALVKSRQ VNRANKQEVR EANKYFFIES
CIALFVSFII NVFVVSVFAE AFFEKTNEQV VEVCRNSSSP HADLFPNDNS TLAVDIYKGG
VVLGCYFGPA ALYIWAVGIL AAGQSSTMTG TYSGQFVMEG FLNLKWSRFA RVILTRSIAI
IPTLLVAVFQ DVEHLTGMND FLNVLQSLQL PFALIPILTF TSLRPVMSEF SNGIGWRIAG
GILVLLVCSI NMYFVVVYVQ ELGHVALYVV AAVVSVAYLG FVFYLGWQCL IALGLSFLDC
GRSYHLGLTA RPEIYLLNTV DAVSLVSR


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