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P41251 (NRAM1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Natural resistance-associated macrophage protein 1

Short name=NRAMP 1
Alternative name(s):
Solute carrier family 11 member 1
Gene names
Name:Slc11a1
Synonyms:Bcg, Ity, Lsh, Nramp1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length548 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Divalent transition metal (iron and manganese) transporter involved in iron metabolism and host resistance to certain pathogens. Macrophage-specific membrane transport function. Controls natural resistance to infection with intracellular parasites. Pathogen resistance involves sequestration of Fe2+ and Mn2+, cofactors of both prokaryotic and eukaryotic catalases and superoxide dismutases, not only to protect the macrophage against its own generation of reactive oxygen species, but to deny the cations to the pathogen for synthesis of its protective enzymes. HAMAP-Rule MF_00221

Subcellular location

Membrane; Multi-pass membrane protein Probable HAMAP-Rule MF_00221.

Tissue specificity

Macrophages; spleen and liver.

Developmental stage

Expressed in the early stages of infection. HAMAP-Rule MF_00221

Induction

In response to lymphokine or bacterial products. HAMAP-Rule MF_00221

Sequence similarities

Belongs to the NRAMP family.

Ontologies

Keywords
   Biological processIon transport
Iron transport
Transport
   Cellular componentMembrane
   DomainTransmembrane
Transmembrane helix
   LigandIron
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processL-arginine import

Inferred from direct assay PubMed 8529105. Source: MGI

MAPK cascade

Inferred from sequence orthology PubMed 10678911. Source: MGI

MHC class II biosynthetic process

Inferred from mutant phenotype PubMed 8301134. Source: MGI

T cell cytokine production

Inferred from mutant phenotype PubMed 19116231. Source: MGI

T cell proliferation involved in immune response

Inferred from mutant phenotype PubMed 9176118. Source: MGI

activation of protein kinase activity

Inferred from mutant phenotype PubMed 8301134. Source: MGI

antigen processing and presentation of peptide antigen

Inferred from mutant phenotype PubMed 17620357. Source: MGI

cadmium ion transmembrane transport

Inferred from electronic annotation. Source: Ensembl

cellular cadmium ion homeostasis

Inferred from electronic annotation. Source: Ensembl

cellular iron ion homeostasis

Inferred from mutant phenotype PubMed 11903051PubMed 18456389PubMed 19321419. Source: MGI

defense response to Gram-negative bacterium

Inferred from mutant phenotype PubMed 6358358. Source: MGI

defense response to bacterium

Inferred from mutant phenotype PubMed 1541907PubMed 18045875PubMed 18285491PubMed 385184PubMed 7650477. Source: MGI

defense response to protozoan

Inferred from mutant phenotype PubMed 606434PubMed 7561513PubMed 8033407. Source: MGI

divalent metal ion export

Inferred from direct assay PubMed 17932044. Source: BHF-UCL

inflammatory response

Inferred from mutant phenotype PubMed 19116231. Source: MGI

interleukin-2 production

Inferred from mutant phenotype PubMed 9176118. Source: MGI

interleukin-3 production

Inferred from mutant phenotype PubMed 9176118. Source: MGI

iron ion homeostasis

Inferred from mutant phenotype PubMed 9824471. Source: MGI

iron ion transport

Inferred from mutant phenotype PubMed 11903051. Source: MGI

mRNA stabilization

Inferred from mutant phenotype PubMed 9009318. Source: MGI

macrophage activation

Inferred from direct assay PubMed 8529105. Source: MGI

manganese ion transmembrane transport

Inferred from mutant phenotype PubMed 11067873. Source: GOC

manganese ion transport

Inferred from mutant phenotype PubMed 11067873. Source: MGI

multicellular organismal iron ion homeostasis

Inferred from mutant phenotype PubMed 19321419. Source: MGI

negative regulation of cytokine production

Inferred from mutant phenotype PubMed 16470178. Source: MGI

nitrite transport

Inferred from direct assay PubMed 8529105. Source: MGI

phagocytosis

Inferred from mutant phenotype PubMed 18045875. Source: MGI

positive regulation of T-helper 1 type immune response

Inferred from mutant phenotype PubMed 18984740. Source: MGI

positive regulation of cytokine production

Inferred from mutant phenotype PubMed 1541907. Source: MGI

positive regulation of dendritic cell antigen processing and presentation

Inferred from mutant phenotype PubMed 18984740. Source: MGI

positive regulation of gene expression

Inferred from mutant phenotype PubMed 16470178. Source: MGI

positive regulation of interferon-gamma production

Inferred from mutant phenotype PubMed 18984740. Source: MGI

positive regulation of phagocytosis

Inferred from mutant phenotype PubMed 18456389PubMed 18984740. Source: MGI

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 17620357. Source: MGI

protein import into nucleus, translocation

Inferred from mutant phenotype PubMed 10065630. Source: MGI

respiratory burst

Inferred from direct assay PubMed 8529105. Source: MGI

response to bacterium

Inferred from mutant phenotype Ref.5. Source: MGI

response to interferon-gamma

Inferred from direct assay PubMed 9261342. Source: MGI

response to lipopolysaccharide

Inferred from direct assay PubMed 9261342. Source: MGI

vacuolar acidification

Inferred from mutant phenotype PubMed 11067873PubMed 18984740PubMed 9670047. Source: MGI

wound healing

Inferred from mutant phenotype PubMed 16470178. Source: MGI

   Cellular_componentcell outer membrane

Inferred from direct assay PubMed 10065630. Source: MGI

endosome membrane

Inferred from direct assay PubMed 9034150. Source: MGI

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

late endosome

Inferred from direct assay PubMed 16905747PubMed 17620357. Source: MGI

lysosome

Inferred from direct assay PubMed 16905747PubMed 17620357. Source: MGI

phagocytic vesicle membrane

Inferred from direct assay PubMed 11067873PubMed 9034150PubMed 9271100. Source: MGI

plasma membrane

Inferred from electronic annotation. Source: Ensembl

tertiary granule membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionmanganese ion transmembrane transporter activity

Inferred from mutant phenotype PubMed 11067873. Source: MGI

metal ion:proton antiporter activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 548548Natural resistance-associated macrophage protein 1 HAMAP-Rule MF_00221
PRO_0000212589

Regions

Topological domain1 – 5555Cytoplasmic Potential
Transmembrane56 – 7318Helical; Potential
Topological domain74 – 829Extracellular Potential
Transmembrane83 – 10220Helical; Potential
Topological domain103 – 13937Cytoplasmic Potential
Transmembrane140 – 16021Helical; Potential
Topological domain161 – 1644Extracellular Potential
Transmembrane165 – 18420Helical; Potential
Topological domain185 – 1939Cytoplasmic Potential
Transmembrane194 – 21421Helical; Potential
Topological domain215 – 23723Extracellular Potential
Transmembrane238 – 25619Helical; Potential
Topological domain257 – 28428Cytoplasmic Potential
Transmembrane285 – 30420Helical; Potential
Topological domain305 – 34642Extracellular Potential
Transmembrane347 – 36620Helical; Potential
Topological domain367 – 39731Cytoplasmic Potential
Transmembrane398 – 41518Helical; Potential
Topological domain416 – 42611Extracellular Potential
Transmembrane427 – 44721Helical; Potential
Topological domain448 – 46316Cytoplasmic Potential
Transmembrane464 – 48522Helical; Potential
Topological domain486 – 4938Extracellular Potential
Transmembrane494 – 51320Helical; Potential
Topological domain514 – 54835Cytoplasmic Potential
Compositional bias3 – 7775Pro/Ser-rich HAMAP-Rule MF_00221

Amino acid modifications

Glycosylation3211N-linked (GlcNAc...) Potential
Glycosylation3351N-linked (GlcNAc...) Potential

Natural variations

Natural variant1691D → G. Ref.1 Ref.2 Ref.5

Sequences

Sequence LengthMass (Da)Tools
P41251 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: E5F0C1EC9FC0C2FD

FASTA54859,741
        10         20         30         40         50         60 
MISDKSPPRL SRPSYGSISS LPGPAPQPAP CRETYLSEKI PIPSADQGTF SLRKLWAFTG 

        70         80         90        100        110        120 
PGFLMSIAFL DPGNIESDLQ AGAVAGFKLL WVLLWATVLG LLCQRLAARL GVVTGKDLGE 

       130        140        150        160        170        180 
VCHLYYPKVP RILLWLTIEL AIVGSDMQEV IGTAISFNLL SAGRIPLWDG VLITIVDTFF 

       190        200        210        220        230        240 
FLFLDNYGLR KLEAFFGLLI TIMALTFGYE YVVAHPSQGA LLKGLVLPTC PGCGQPELLQ 

       250        260        270        280        290        300 
AVGIVGAIIM PHNIYLHSAL VKSREVDRTR RVDVREANMY FLIEATIALS VSFIINLFVM 

       310        320        330        340        350        360 
AVFGQAFYQQ TNEEAFNICA NSSLQNYAKI FPRDNNTVSV DIYQGGVILG CLFGPAALYI 

       370        380        390        400        410        420 
WAVGLLAAGQ SSTMTGTYAG QFVMEGFLKL RWSRFARVLL TRSCAILPTV LVAVFRDLKD 

       430        440        450        460        470        480 
LSGLNDLLNV LQSLLLPFAV LPILTFTSMP AVMQEFANGR MSKAITSCIM ALVCAINLYF 

       490        500        510        520        530        540 
VISYLPSLPH PAYFGLVALF AIGYLGLTAY LAWTCCIAHG ATFLTHSSHK HFLYGLPNEE 


QGGVQGSG 

« Hide

References

« Hide 'large scale' references
[1]"NH2-terminal sequence of macrophage-expressed natural resistance-associated macrophage protein (Nramp) encodes a proline/serine-rich putative Src homology 3-binding domain."
Barton C.H., White J.K., Roach T.I.A., Blackwell J.M.
J. Exp. Med. 179:1683-1687(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLY-169.
Strain: B10.L-LSH.
Tissue: Bone marrow.
[2]"Genomic structure, promoter sequence, and induction of expression of the mouse Nramp1 gene in macrophages."
Govoni G., Vidal S., Cellier M., Lepage P., Malo D., Gros P.
Genomics 27:9-19(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLY-169.
Strain: BALB/c.
[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].
Strain: C57BL/6J.
[4]"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].
[5]"Natural resistance to infection with intracellular parasites: isolation of a candidate for Bcg."
Vidal S.M., Malo D., Vogan K., Skamene E., Gros P.
Cell 73:469-485(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 65-548, VARIANT GLY-169.
Strain: DBA/2.
Tissue: Pre-B cell.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X75355 mRNA. Translation: CAA53102.1.
S79389 expand/collapse EMBL AC list , S79360, S79361, S79362, S79364, S79365, S79367, S79395, S79396, S79369, S79375, S79380, S79381, S79386, S79387 Genomic DNA. Translation: AAB35205.2.
AK171393 mRNA. Translation: BAE42430.1.
BC109137 mRNA. Translation: AAI09138.1.
BC109138 mRNA. Translation: AAI09139.1.
L13732 mRNA. Translation: AAA39838.1.
CCDSCCDS15047.1.
PIRI48693.
RefSeqNP_038640.2. NM_013612.2.
UniGeneMm.2913.

3D structure databases

ProteinModelPortalP41251.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201840. 5 interactions.
STRING10090.ENSMUSP00000027368.

PTM databases

PhosphoSiteP41251.

Proteomic databases

PaxDbP41251.
PRIDEP41251.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027368; ENSMUSP00000027368; ENSMUSG00000026177.
GeneID18173.
KEGGmmu:18173.
UCSCuc007bly.2. mouse.

Organism-specific databases

CTD6556.
MGIMGI:1345275. Slc11a1.

Phylogenomic databases

eggNOGCOG1914.
GeneTreeENSGT00390000006526.
HOGENOMHOG000152203.
HOVERGENHBG052665.
InParanoidQ3TB84.
KOK12347.
OMASHKHFLY.
OrthoDBEOG77127K.
TreeFamTF315185.

Gene expression databases

BgeeP41251.
GenevestigatorP41251.

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

NextBio293474.
PROP41251.
SOURCESearch...

Entry information

Entry nameNRAM1_MOUSE
AccessionPrimary (citable) accession number: P41251
Secondary accession number(s): Q3TB84
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 110 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