NRAM1_MOUSE
ID NRAM1_MOUSE Reviewed; 548 AA.
AC P41251; Q3TB84;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Natural resistance-associated macrophage protein 1;
DE Short=NRAMP 1;
DE AltName: Full=Solute carrier family 11 member 1;
GN Name=Slc11a1; Synonyms=Bcg, Ity, Lsh, Nramp1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLY-169.
RC STRAIN=B10.L-LSH; TISSUE=Bone marrow;
RX PubMed=7513015; DOI=10.1084/jem.179.5.1683;
RA Barton C.H., White J.K., Roach T.I.A., Blackwell J.M.;
RT "NH2-terminal sequence of macrophage-expressed natural resistance-
RT associated macrophage protein (Nramp) encodes a proline/serine-rich
RT putative Src homology 3-binding domain.";
RL J. Exp. Med. 179:1683-1687(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLY-169.
RC STRAIN=BALB/cJ;
RX PubMed=7665187; DOI=10.1006/geno.1995.1002;
RA Govoni G., Vidal S., Cellier M., Lepage P., Malo D., Gros P.;
RT "Genomic structure, promoter sequence, and induction of expression of the
RT mouse Nramp1 gene in macrophages.";
RL Genomics 27:9-19(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 65-548, AND VARIANT GLY-169.
RC STRAIN=DBA/2J; TISSUE=Pre-B cell;
RX PubMed=8490962; DOI=10.1016/0092-8674(93)90135-d;
RA Vidal S.M., Malo D., Vogan K., Skamene E., Gros P.;
RT "Natural resistance to infection with intracellular parasites: isolation of
RT a candidate for Bcg.";
RL Cell 73:469-485(1993).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Divalent transition metal (iron and manganese) transporter
CC involved in iron metabolism and host resistance to certain pathogens.
CC Macrophage-specific membrane transport function. Controls natural
CC resistance to infection with intracellular parasites. Pathogen
CC resistance involves sequestration of Fe(2+) and Mn(2+), cofactors of
CC both prokaryotic and eukaryotic catalases and superoxide dismutases,
CC not only to protect the macrophage against its own generation of
CC reactive oxygen species, but to deny the cations to the pathogen for
CC synthesis of its protective enzymes.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Macrophages; spleen and liver.
CC -!- DEVELOPMENTAL STAGE: Expressed in the early stages of infection.
CC -!- INDUCTION: In response to lymphokine or bacterial products.
CC -!- SIMILARITY: Belongs to the NRAMP family. {ECO:0000305}.
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DR EMBL; X75355; CAA53102.1; -; mRNA.
DR EMBL; S79389; AAB35205.2; -; Genomic_DNA.
DR EMBL; S79360; AAB35205.2; JOINED; Genomic_DNA.
DR EMBL; S79361; AAB35205.2; JOINED; Genomic_DNA.
DR EMBL; S79362; AAB35205.2; JOINED; Genomic_DNA.
DR EMBL; S79364; AAB35205.2; JOINED; Genomic_DNA.
DR EMBL; S79365; AAB35205.2; JOINED; Genomic_DNA.
DR EMBL; S79367; AAB35205.2; JOINED; Genomic_DNA.
DR EMBL; S79395; AAB35205.2; JOINED; Genomic_DNA.
DR EMBL; S79396; AAB35205.2; JOINED; Genomic_DNA.
DR EMBL; S79369; AAB35205.2; JOINED; Genomic_DNA.
DR EMBL; S79375; AAB35205.2; JOINED; Genomic_DNA.
DR EMBL; S79380; AAB35205.2; JOINED; Genomic_DNA.
DR EMBL; S79381; AAB35205.2; JOINED; Genomic_DNA.
DR EMBL; S79386; AAB35205.2; JOINED; Genomic_DNA.
DR EMBL; S79387; AAB35205.2; JOINED; Genomic_DNA.
DR EMBL; AK171393; BAE42430.1; -; mRNA.
DR EMBL; BC109137; AAI09138.1; -; mRNA.
DR EMBL; BC109138; AAI09139.1; -; mRNA.
DR EMBL; L13732; AAA39838.1; -; mRNA.
DR CCDS; CCDS15047.1; -.
DR PIR; I48693; I48693.
DR RefSeq; NP_038640.2; NM_013612.2.
DR AlphaFoldDB; P41251; -.
DR SMR; P41251; -.
DR BioGRID; 201840; 5.
DR STRING; 10090.ENSMUSP00000027368; -.
DR GlyGen; P41251; 2 sites.
DR iPTMnet; P41251; -.
DR PhosphoSitePlus; P41251; -.
DR MaxQB; P41251; -.
DR PaxDb; P41251; -.
DR PeptideAtlas; P41251; -.
DR PRIDE; P41251; -.
DR ProteomicsDB; 293890; -.
DR Antibodypedia; 3997; 193 antibodies from 27 providers.
DR DNASU; 18173; -.
DR Ensembl; ENSMUST00000027368; ENSMUSP00000027368; ENSMUSG00000026177.
DR GeneID; 18173; -.
DR KEGG; mmu:18173; -.
DR UCSC; uc007bly.2; mouse.
DR CTD; 6556; -.
DR MGI; MGI:1345275; Slc11a1.
DR VEuPathDB; HostDB:ENSMUSG00000026177; -.
DR eggNOG; KOG1291; Eukaryota.
DR GeneTree; ENSGT00940000160799; -.
DR HOGENOM; CLU_020088_5_2_1; -.
DR InParanoid; P41251; -.
DR OMA; SPKWLRY; -.
DR OrthoDB; 666470at2759; -.
DR PhylomeDB; P41251; -.
DR TreeFam; TF315185; -.
DR Reactome; R-MMU-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-MMU-425410; Metal ion SLC transporters.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-6803544; Ion influx/efflux at host-pathogen interface.
DR BioGRID-ORCS; 18173; 2 hits in 76 CRISPR screens.
DR ChiTaRS; Slc11a1; mouse.
DR PRO; PR:P41251; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P41251; protein.
DR Bgee; ENSMUSG00000026177; Expressed in granulocyte and 152 other tissues.
DR ExpressionAtlas; P41251; baseline and differential.
DR Genevisible; P41251; MM.
DR GO; GO:0010008; C:endosome membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005770; C:late endosome; IDA:MGI.
DR GO; GO:0005764; C:lysosome; IDA:MGI.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0070821; C:tertiary granule membrane; ISO:MGI.
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; IMP:MGI.
DR GO; GO:0051139; F:metal ion:proton antiporter activity; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0046915; F:transition metal ion transmembrane transporter activity; ISO:MGI.
DR GO; GO:0032147; P:activation of protein kinase activity; IMP:MGI.
DR GO; GO:0048002; P:antigen processing and presentation of peptide antigen; IMP:MGI.
DR GO; GO:0070574; P:cadmium ion transmembrane transport; ISO:MGI.
DR GO; GO:0006876; P:cellular cadmium ion homeostasis; ISO:MGI.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IMP:MGI.
DR GO; GO:0042742; P:defense response to bacterium; IMP:MGI.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:MGI.
DR GO; GO:0042832; P:defense response to protozoan; IMP:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0006954; P:inflammatory response; IMP:MGI.
DR GO; GO:0055072; P:iron ion homeostasis; IMP:MGI.
DR GO; GO:0006826; P:iron ion transport; IMP:MGI.
DR GO; GO:1903826; P:L-arginine transmembrane transport; IDA:MGI.
DR GO; GO:0042116; P:macrophage activation; IDA:MGI.
DR GO; GO:0006828; P:manganese ion transport; IMP:MGI.
DR GO; GO:0000165; P:MAPK cascade; ISO:MGI.
DR GO; GO:0030001; P:metal ion transport; IDA:BHF-UCL.
DR GO; GO:0045342; P:MHC class II biosynthetic process; IMP:MGI.
DR GO; GO:0048255; P:mRNA stabilization; IMP:MGI.
DR GO; GO:0060586; P:multicellular organismal iron ion homeostasis; IMP:MGI.
DR GO; GO:0001818; P:negative regulation of cytokine production; IMP:MGI.
DR GO; GO:0015707; P:nitrite transport; IDA:MGI.
DR GO; GO:0006909; P:phagocytosis; IMP:MGI.
DR GO; GO:0001819; P:positive regulation of cytokine production; IMP:MGI.
DR GO; GO:0002606; P:positive regulation of dendritic cell antigen processing and presentation; IMP:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IMP:MGI.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IMP:MGI.
DR GO; GO:0002827; P:positive regulation of T-helper 1 type immune response; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0045730; P:respiratory burst; IDA:MGI.
DR GO; GO:0009617; P:response to bacterium; IMP:MGI.
DR GO; GO:0034341; P:response to interferon-gamma; IDA:MGI.
DR GO; GO:0032496; P:response to lipopolysaccharide; IDA:MGI.
DR GO; GO:0002309; P:T cell proliferation involved in immune response; IMP:MGI.
DR GO; GO:0007035; P:vacuolar acidification; IMP:MGI.
DR GO; GO:0042060; P:wound healing; IMP:MGI.
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 Glycoprotein; Ion transport; Iron; Iron transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..548
FT /note="Natural resistance-associated macrophage protein 1"
FT /id="PRO_0000212589"
FT TOPO_DOM 1..55
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..82
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..139
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..164
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..193
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..237
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..284
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 305..346
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 367..397
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 416..426
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 448..463
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 464..485
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 486..493
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 494..513
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 514..548
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 169
FT /note="D -> G"
FT /evidence="ECO:0000269|PubMed:7513015,
FT ECO:0000269|PubMed:7665187, ECO:0000269|PubMed:8490962"
SQ SEQUENCE 548 AA; 59741 MW; E5F0C1EC9FC0C2FD CRC64;
MISDKSPPRL SRPSYGSISS LPGPAPQPAP CRETYLSEKI PIPSADQGTF SLRKLWAFTG
PGFLMSIAFL DPGNIESDLQ AGAVAGFKLL WVLLWATVLG LLCQRLAARL GVVTGKDLGE
VCHLYYPKVP RILLWLTIEL AIVGSDMQEV IGTAISFNLL SAGRIPLWDG VLITIVDTFF
FLFLDNYGLR KLEAFFGLLI TIMALTFGYE YVVAHPSQGA LLKGLVLPTC PGCGQPELLQ
AVGIVGAIIM PHNIYLHSAL VKSREVDRTR RVDVREANMY FLIEATIALS VSFIINLFVM
AVFGQAFYQQ TNEEAFNICA NSSLQNYAKI FPRDNNTVSV DIYQGGVILG CLFGPAALYI
WAVGLLAAGQ SSTMTGTYAG QFVMEGFLKL RWSRFARVLL TRSCAILPTV LVAVFRDLKD
LSGLNDLLNV LQSLLLPFAV LPILTFTSMP AVMQEFANGR MSKAITSCIM ALVCAINLYF
VISYLPSLPH PAYFGLVALF AIGYLGLTAY LAWTCCIAHG ATFLTHSSHK HFLYGLPNEE
QGGVQGSG
