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P49282 (NRAM2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Natural resistance-associated macrophage protein 2

Short name=NRAMP 2
Alternative name(s):
Divalent cation transporter 1
Divalent metal transporter 1
Short name=DMT-1
Solute carrier family 11 member 2
Gene names
Name:Slc11a2
Synonyms:Dct1, Dmt1, Nramp2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length568 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Important in metal transport, in particular iron. 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. Ref.8 Ref.9

Subunit structure

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 By similarity.

Subcellular location

Endosome membrane; Multi-pass membrane protein By similarity HAMAP-Rule MF_00221.

Tissue specificity

Isoform 2 is abundantly expressed in erythroid precursor cells (at protein level). Expressed at low levels in most tissues analyzed. Expressed at low levels in small intestine and at higher levels in kidney. Ref.7 Ref.8

Induction

Isoform 1 is up-regulated under iron-depletion conditions in the proximal portion of the duodenum where it is abundantly expressed in the brush border of absorptive epithelial cells (at protein level). Ref.7

Post-translational modification

Ubiquitinated by WWP2. Ref.11

Involvement in disease

Defects in Slc11a2 are the cause of microcytic anemia (mk). Homozygous mk/mk mice have hypochromic microcytic anemia due to severe defects in intestinal iron absorption and erythroid iron utilization.

Disruption phenotype

Mice display no apparent anatomical abnormalities. They are however anemic, show progressive postnatal growth retardation, and at birth have elevated liver iron stores compared with wild-type littermates. None survive for more than 7 days. Heterozygotes appear normal, showing no significant hematological abnormalities. However, by 8 weeks, their liver iron content is lower than in wild-type littermates. Ref.9

Miscellaneous

Nifedipine induces duodenal iron accumulation and mobilizes iron from the liver of iron-overloaded mice.

Sequence similarities

Belongs to the NRAMP family.

Sequence caution

The sequence CAD38518.1 differs from that shown. Reason: Frameshift at position 69.

Ontologies

Keywords
   Biological processIon transport
Iron transport
Transport
   Cellular componentEndosome
Membrane
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
   DomainTransmembrane
Transmembrane helix
   LigandIron
   PTMGlycoprotein
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from electronic annotation. Source: Ensembl

cellular response to hypoxia

Inferred from electronic annotation. Source: Ensembl

cellular response to iron ion

Inferred from electronic annotation. Source: Ensembl

cellular response to oxidative stress

Inferred from electronic annotation. Source: Ensembl

cellular response to tumor necrosis factor

Inferred from electronic annotation. Source: Ensembl

cobalt ion transport

Inferred from direct assay PubMed 10942769PubMed 12522007PubMed 12724326PubMed 16142913PubMed 16905747. Source: MGI

dendrite morphogenesis

Inferred from mutant phenotype PubMed 19211831. Source: MGI

detection of oxygen

Inferred from electronic annotation. Source: Ensembl

erythrocyte development

Inferred from mutant phenotype Ref.9. Source: MGI

ferrous iron import

Inferred from direct assay PubMed 15024413. Source: MGI

ferrous iron transport

Inferred from direct assay PubMed 10942769. Source: MGI

heme biosynthetic process

Inferred from mutant phenotype Ref.8. Source: MGI

hydrogen ion transmembrane transport

Inferred from direct assay PubMed 15024413. Source: GOC

iron ion transport

Inferred from direct assay PubMed 12522007PubMed 16142913. Source: MGI

learning or memory

Inferred from mutant phenotype PubMed 19211831. Source: MGI

multicellular organismal iron ion homeostasis

Inferred from mutant phenotype PubMed 18076961PubMed 5070129. Source: MGI

porphyrin-containing compound biosynthetic process

Inferred from mutant phenotype PubMed 658175. Source: MGI

porphyrin-containing compound metabolic process

Inferred from mutant phenotype PubMed 4404581. Source: MGI

proton transport

Inferred from direct assay PubMed 15024413. Source: MGI

response to cadmium ion

Inferred from electronic annotation. Source: Ensembl

response to lead ion

Inferred from electronic annotation. Source: Ensembl

response to manganese ion

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentapical plasma membrane

Inferred from electronic annotation. Source: Ensembl

basal part of cell

Inferred from electronic annotation. Source: Ensembl

brush border

Inferred from direct assay PubMed 11090085. Source: MGI

cell surface

Inferred from direct assay PubMed 17097837. Source: MGI

cytoplasmic vesicle

Inferred from electronic annotation. Source: Ensembl

early endosome

Inferred from direct assay PubMed 12724326. Source: MGI

endomembrane system

Inferred from direct assay PubMed 12724326. Source: MGI

endosome

Inferred from direct assay PubMed 16227996. Source: MGI

integral component of plasma membrane

Inferred from direct assay PubMed 10942769. Source: MGI

late endosome membrane

Inferred from electronic annotation. Source: Ensembl

lysosomal membrane

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: Ensembl

paraferritin complex

Inferred from electronic annotation. Source: Ensembl

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay Ref.8PubMed 12724326PubMed 16227996PubMed 16905747. Source: MGI

recycling endosome

Inferred from direct assay Ref.8PubMed 16905747. Source: MGI

trans-Golgi network

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncadmium ion binding

Inferred from electronic annotation. Source: Ensembl

cadmium ion transmembrane transporter activity

Inferred from electronic annotation. Source: Ensembl

cobalt ion binding

Inferred from electronic annotation. Source: Ensembl

cobalt ion transmembrane transporter activity

Inferred from direct assay PubMed 10942769PubMed 12522007PubMed 12724326PubMed 16142913PubMed 16905747. Source: MGI

copper ion binding

Inferred from electronic annotation. Source: Ensembl

copper ion transmembrane transporter activity

Inferred from electronic annotation. Source: Ensembl

ferrous iron transmembrane transporter activity

Inferred from direct assay PubMed 10942769PubMed 12522007PubMed 15024413. Source: MGI

hydrogen ion transmembrane transporter activity

Inferred from direct assay PubMed 15024413. Source: MGI

iron ion binding

Inferred from electronic annotation. Source: Ensembl

iron ion transmembrane transporter activity

Inferred from direct assay PubMed 16142913. Source: MGI

lead ion transmembrane transporter activity

Inferred from electronic annotation. Source: Ensembl

manganese ion binding

Inferred from electronic annotation. Source: Ensembl

manganese ion transmembrane transporter activity

Inferred from electronic annotation. Source: Ensembl

nickel cation binding

Inferred from electronic annotation. Source: Ensembl

nickel cation transmembrane transporter activity

Inferred from electronic annotation. Source: Ensembl

solute:hydrogen symporter activity

Inferred from electronic annotation. Source: Ensembl

vanadium ion transmembrane transporter activity

Inferred from electronic annotation. Source: Ensembl

zinc ion binding

Inferred from electronic annotation. Source: Ensembl

zinc ion transmembrane transporter activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 2 (identifier: P49282-1)

Also known as: Non-IRE;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 1 (identifier: P49282-2)

Also known as: IRE;

The sequence of this isoform differs from the canonical sequence as follows:
     544-568: YRLGLTAQPELYLLNTVDADSVVSR → VSISKVLLSEDTSGGNIK
Isoform 3 (identifier: P49282-3)

Also known as: 1A-IRE;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MGKKQPRAAAAAPNCELKSYSKSTDPQVSTM
     544-568: YRLGLTAQPELYLLNTVDADSVVSR → VSISKVLLSEDTSGGNIK
Note: No experimental confirmation available.
Isoform 4 (identifier: P49282-4)

Also known as: 1A-Non-IRE;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MGKKQPRAAAAAPNCELKSYSKSTDPQVSTM
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 568568Natural resistance-associated macrophage protein 2 HAMAP-Rule MF_00221
PRO_0000212595

Regions

Topological domain1 – 6969Cytoplasmic Potential
Transmembrane70 – 9021Helical; Potential
Topological domain91 – 955Extracellular Potential
Transmembrane96 – 11722Helical; Potential
Topological domain118 – 15437Cytoplasmic Potential
Transmembrane155 – 17521Helical; Potential
Topological domain176 – 1794Extracellular Potential
Transmembrane180 – 19415Helical; Potential
Topological domain195 – 20814Cytoplasmic Potential
Transmembrane209 – 22921Helical; Potential
Topological domain230 – 25526Extracellular Potential
Transmembrane256 – 27621Helical; Potential
Topological domain277 – 30125Cytoplasmic Potential
Transmembrane302 – 32221Helical; Potential
Topological domain323 – 36038Extracellular Potential
Transmembrane361 – 38121Helical; Potential
Topological domain382 – 40827Cytoplasmic Potential
Transmembrane409 – 42921Helical; Potential
Topological domain430 – 44011Extracellular Potential
Transmembrane441 – 46121Helical; Potential
Topological domain462 – 48221Cytoplasmic Potential
Transmembrane483 – 50321Helical; Potential
Topological domain504 – 5063Extracellular Potential
Transmembrane507 – 52721Helical; Potential
Topological domain528 – 56841Cytoplasmic Potential

Amino acid modifications

Modified residue5641Phosphoserine Ref.12
Modified residue5671Phosphoserine Ref.12
Glycosylation3361N-linked (GlcNAc...) Potential
Glycosylation3491N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence11M → MGKKQPRAAAAAPNCELKSY SKSTDPQVSTM in isoform 3 and isoform 4.
VSP_038145
Alternative sequence544 – 56825YRLGL…SVVSR → VSISKVLLSEDTSGGNIK in isoform 1 and isoform 3.
VSP_003596
Natural variant1851G → R in microcytic anemia. Ref.13

Experimental info

Sequence conflict61K → E in BAE28454. Ref.3
Sequence conflict61K → E in CAD38518. Ref.6
Sequence conflict681R → S in AAC24496. Ref.2
Sequence conflict69 – 702Missing in CAD38518. Ref.6
Sequence conflict1421P → R in BAC38930. Ref.3
Sequence conflict1821L → V in AAC42051. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 2 (Non-IRE) [UniParc].

Last modified September 22, 2009. Version 2.
Checksum: 603AAF697AAD3C74

FASTA56862,368
        10         20         30         40         50         60 
MVLDPKEKMP DDGASGDHGD SASLGAINPA YSNSSLPHST GDSEEPFTTY FDEKIPIPEE 

        70         80         90        100        110        120 
EYSCFSFRKL WAFTGPGFLM SIAYLDPGNI ESDLQSGAVA GFKLLWVLLL ATIVGLLLQR 

       130        140        150        160        170        180 
LAARLGVVTG LHLAEVCHRQ YPKVPRIILW LMVELAIIGS DMQEVIGSAI AINLLSAGRV 

       190        200        210        220        230        240 
PLWGGVLITI ADTFVFLFLD KYGLRKLEAF FGFLITIMAL TFGYEYITVK PSQSQVLRGM 

       250        260        270        280        290        300 
FVPSCPGCRT PQVEQAVGIV GAVIMPHNMY LHSALVKSRQ VNRANKQEVR EANKYFFIES 

       310        320        330        340        350        360 
CIALFVSFII NVFVVSVFAE AFFEKTNKQV VEVCKNNSSP HADLFPSDNS TLAVDIYKGG 

       370        380        390        400        410        420 
VVLGCYFGPA ALYIWAVGIL AAGQSSTMTG TYSGQFVMEG FLNLKWSRFA RVILTRSIAI 

       430        440        450        460        470        480 
IPTLLVAVFQ DVEHLTGMND FLNVLQSLQL PFALIPILTF TSLRPVMSEF SNGIGWRIAG 

       490        500        510        520        530        540 
GILVLIVCSI NMYFVVVYVQ ELGHVALYVV AAVVSVAYLT FVFYLGWQCL IALGLSFLDC 

       550        560 
GRSYRLGLTA QPELYLLNTV DADSVVSR 

« Hide

Isoform 1 (IRE) [UniParc].

Checksum: D2FAA52B8F73FFBC
Show »

FASTA56161,421
Isoform 3 (1A-IRE) [UniParc].

Checksum: F8119C955315B2F6
Show »

FASTA59164,568
Isoform 4 (1A-Non-IRE) [UniParc].

Checksum: ED4B62ED656BAEBE
Show »

FASTA59865,515

References

« Hide 'large scale' references
[1]"Identification and characterization of a second mouse Nramp gene."
Gruenheid S., Cellier M., Vidal S., Gros P.
Genomics 25:514-525(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]"Nramp2 is mutated in the anemic Belgrade (b) rat: evidence of a role for Nramp2 in endosomal iron transport."
Fleming M.D., Romano M.A., Su M.A., Garrick L.M., Garrick M.D., Andrews N.C.
Proc. Natl. Acad. Sci. U.S.A. 95:1148-1153(1998)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: DBA.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Embryo and Hippocampus.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: FVB/N.
Tissue: Kidney.
[6]"Previously uncharacterized isoforms of divalent metal transporter (DMT)-1: implications for regulation and cellular function."
Hubert N., Hentze M.W.
Proc. Natl. Acad. Sci. U.S.A. 99:12345-12350(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-80 (ISOFORMS 3/4), ALTERNATIVE SPLICING.
Strain: C57BL/6.
Tissue: Duodenum.
[7]"Cellular and subcellular localization of the Nramp2 iron transporter in the intestinal brush border and regulation by dietary iron."
Canonne-Hergaux F., Gruenheid S., Ponka P., Gros P.
Blood 93:4406-4417(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INDUCTION.
[8]"Characterization of the iron transporter DMT1 (NRAMP2/DCT1) in red blood cells of normal and anemic mk/mk mice."
Canonne-Hergaux F., Zhang A.-S., Ponka P., Gros P.
Blood 98:3823-3830(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[9]"Slc11a2 is required for intestinal iron absorption and erythropoiesis but dispensable in placenta and liver."
Gunshin H., Fujiwara Y., Custodio A.O., Direnzo C., Robine S., Andrews N.C.
J. Clin. Invest. 115:1258-1266(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[10]"Ca2+ channel blockers reverse iron overload by a new mechanism via divalent metal transporter-1."
Ludwiczek S., Theurl I., Muckenthaler M.U., Jakab M., Mair S.M., Theurl M., Kiss J., Paulmichl M., Hentze M.W., Ritter M., Weiss G.
Nat. Med. 13:448-454(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NIFEDIPINE TREATMENT.
[11]"Regulation of the divalent metal ion transporter DMT1 and iron homeostasis by a ubiquitin-dependent mechanism involving Ndfips and WWP2."
Foot N.J., Dalton H.E., Shearwin-Whyatt L.M., Dorstyn L., Tan S.S., Yang B., Kumar S.
Blood 112:4268-4275(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION.
[12]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-564 AND SER-567, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Microcytic anaemia mice have a mutation in Nramp2, a candidate iron transporter gene."
Fleming M.D., Trenor C.C. III, Su M.A., Foernzler D., Beier D.R., Dietrich W.F., Andrews N.C.
Nat. Genet. 16:383-386(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MK ARG-185.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L33415 mRNA. Translation: AAC42051.1.
AF029758 mRNA. Translation: AAC24496.1.
AK049856 mRNA. Translation: BAC33960.1.
AK083478 mRNA. Translation: BAC38930.1.
AK148276 mRNA. Translation: BAE28454.1.
CH466550 Genomic DNA. Translation: EDL04090.1.
BC019137 mRNA. Translation: AAH19137.1.
AJ493663 mRNA. Translation: CAD38518.1. Frameshift.
PIRA56852.
RefSeqNP_001139633.1. NM_001146161.1.
NP_032758.2. NM_008732.2.
XP_006520639.1. XM_006520576.1.
XP_006520640.1. XM_006520577.1.
XP_006520641.1. XM_006520578.1.
UniGeneMm.234608.

3D structure databases

ProteinModelPortalP49282.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteP49282.

Proteomic databases

PaxDbP49282.
PRIDEP49282.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000023774; ENSMUSP00000023774; ENSMUSG00000023030. [P49282-1]
ENSMUST00000138843; ENSMUSP00000116463; ENSMUSG00000023030. [P49282-2]
GeneID18174.
KEGGmmu:18174.
UCSCuc007xrc.2. mouse. [P49282-1]
uc007xrd.2. mouse. [P49282-2]

Organism-specific databases

CTD4891.
MGIMGI:1345279. Slc11a2.

Phylogenomic databases

eggNOGCOG1914.
GeneTreeENSGT00390000006526.
HOVERGENHBG052665.
InParanoidQ8BWV3.
KOK12347.
OMACYFGPAT.
OrthoDBEOG77127K.
PhylomeDBP49282.
TreeFamTF315185.

Gene expression databases

ArrayExpressP49282.
BgeeP49282.
GenevestigatorP49282.

Family and domain databases

HAMAPMF_00221. NRAMP.
InterProIPR001046. NRAMP-like.
[Graphical view]
PANTHERPTHR11706. PTHR11706. 1 hit.
PfamPF01566. Nramp. 1 hit.
[Graphical view]
PRINTSPR00447. NATRESASSCMP.
TIGRFAMsTIGR01197. nramp. 1 hit.
ProtoNetSearch...

Other

ChiTaRSSLC11A2. mouse.
NextBio293478.
PROP49282.
SOURCESearch...

Entry information

Entry nameNRAM2_MOUSE
AccessionPrimary (citable) accession number: P49282
Secondary accession number(s): O54903 expand/collapse secondary AC list , Q3UFV5, Q8BJL2, Q8BWV3, Q8CFA0, Q8VCU6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: September 22, 2009
Last modified: April 16, 2014
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot