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 24-JAN-2024, entry version 168. DE RecName: Full=Natural resistance-associated macrophage protein 1; DE Short=NRAMP 1 {ECO:0000303|PubMed:11237855}; DE AltName: Full=Solute carrier family 11 member 1; GN Name=Slc11a1; GN Synonyms=Bcg, Ity, Lsh, Nramp1 {ECO:0000303|PubMed:11237855}; 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.A; 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], VARIANT GLY-169, TISSUE SPECIFICITY, AND RP INDUCTION BY LYMPHOKINE. 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 VARIANT GLY-169, FUNCTION, POLYMORPHISM, AND CHARACTERIZATION OF VARIANT. RX PubMed=8757814; DOI=10.1128/iai.64.8.2923-2929.1996; RA Govoni G., Vidal S., Gauthier S., Skamene E., Malo D., Gros P.; RT "The Bcg/Ity/Lsh locus: genetic transfer of resistance to infections in RT C57BL/6J mice transgenic for the Nramp1 Gly169 allele."; RL Infect. Immun. 64:2923-2929(1996). RN [7] RP VARIANT GLY-169, CHARACTERIZATION OF VARIANT GLY-169, AND SUBCELLULAR RP LOCATION. RX PubMed=8871656; RA Vidal S.M., Pinner E., Lepage P., Gauthier S., Gros P.; RT "Natural resistance to intracellular infections: Nramp1 encodes a membrane RT phosphoglycoprotein absent in macrophages from susceptible (Nramp1 D169) RT mouse strains."; RL J. Immunol. 157:3559-3568(1996). RN [8] RP VARIANT GLY-169, CHARACTERIZATION OF VARIANT GLY-169, SUBCELLULAR LOCATION, RP TISSUE SPECIFICITY, INDUCTION BY LPS, AND POLYMORPHISM. RX PubMed=9730978; DOI=10.1242/jcs.111.19.2855; RA Searle S., Bright N.A., Roach T.I., Atkinson P.G., Barton C.H., RA Meloen R.H., Blackwell J.M.; RT "Localisation of Nramp1 in macrophages: modulation with activation and RT infection."; RL J. Cell Sci. 111:2855-2866(1998). RN [9] RP VARIANT GLY-169, CHARACTERIZATION OF VARIANT GLY-169, FUNCTION, AND RP POLYMORPHISM. RX PubMed=11237855; DOI=10.1042/0264-6021:3540511; RA Goswami T., Bhattacharjee A., Babal P., Searle S., Moore E., Li M., RA Blackwell J.M.; RT "Natural-resistance-associated macrophage protein 1 is an H+/bivalent RT cation antiporter."; RL Biochem. J. 354:511-519(2001). RN [10] RP VARIANT GLY-169, CHARACTERIZATION OF VARIANT GLY-169, POLYMORPHISM, RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION. RX PubMed=15202932; DOI=10.1042/bj20040808; RA White J.K., Stewart A., Popoff J.F., Wilson S., Blackwell J.M.; RT "Incomplete glycosylation and defective intracellular targeting of mutant RT solute carrier family 11 member 1 (Slc11a1)."; RL Biochem. J. 382:811-819(2004). RN [11] 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: Macrophage-specific antiporter that fluxes metal ions in CC either direction against a proton gradient. Localized to late endosomal CC lysosomal membranes, delivers bivalent cations from the cytosol into CC these acidic compartments where they may directly affect antimicrobial CC activity. Involved in iron metabolism and host natural resistance to CC infection with intracellular parasites. Pathogen resistance involves CC sequestration of Fe(2+) and Mn(2+), cofactors of both prokaryotic and CC eukaryotic catalases and superoxide dismutases, not only to protect the CC macrophage against its own generation of reactive oxygen species, but CC to deny the cations to the pathogen for synthesis of its protective CC enzymes. {ECO:0000305|PubMed:11237855, ECO:0000305|PubMed:8757814}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+)(out) + Zn(2+)(in) = H(+)(in) + Zn(2+)(out); CC Xref=Rhea:RHEA:28839, ChEBI:CHEBI:15378, ChEBI:CHEBI:29105; CC Evidence={ECO:0000305|PubMed:11237855}; CC -!- CATALYTIC ACTIVITY: CC Reaction=Fe(2+)(in) + H(+)(out) = Fe(2+)(out) + H(+)(in); CC Xref=Rhea:RHEA:29439, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033; CC Evidence={ECO:0000305|PubMed:11237855}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+)(out) + Mn(2+)(in) = H(+)(in) + Mn(2+)(out); CC Xref=Rhea:RHEA:73063, ChEBI:CHEBI:15378, ChEBI:CHEBI:29035; CC Evidence={ECO:0000305|PubMed:11237855}; CC -!- SUBCELLULAR LOCATION: Late endosome membrane CC {ECO:0000269|PubMed:9730978}; Multi-pass membrane protein CC {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:9730978}; Multi- CC pass membrane protein {ECO:0000255}. Note=After onfection, vesicles CC migrate to the site of bacterial phagosomes. CC {ECO:0000269|PubMed:9730978}. CC -!- TISSUE SPECIFICITY: Macrophages; spleen and liver. CC {ECO:0000269|PubMed:15202932, ECO:0000269|PubMed:7665187, CC ECO:0000269|PubMed:9730978}. CC -!- INDUCTION: In response to lymphokine, such as IFNG, or bacterial CC products, such as LPS (PubMed:7665187, PubMed:9730978). Induced in CC macrophages at early stages of infection (PubMed:7665187). CC {ECO:0000269|PubMed:7665187, ECO:0000269|PubMed:9730978}. CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:15202932}. CC -!- POLYMORPHISM: Variant Asp-169 is displayed in the entry because it is CC the variant found in the inbred strains C57BL/6J and BALB/cJ and even CC if it seems to not be expressed in its mature form. In inbred strains, CC the susceptibility to infection with unrelated intracellular parasites, CC such as Mycobacterium bovis, Salmonella typhimurium and Leishmania CC donovani is associated with the single glycine-to-aspartic acid CC substitution at position 169 (G169D) in the predicted transmembrane CC domain 4. The conserved and resistant Gly-169 variant show the proper CC transporter activity described in the function and is highly induced in CC response to lymphokine, such as IFNG, or bacterial products, such as CC LPS. However the variant Asp-169 shows an altered glycosylated pattern CC and seems to prevent proper maturation of the protein, resulting in its CC rapid degradation. The expression of the mature form of variant Asp-169 CC is strongly decreased in late endosome/lysosome membranes leading to a CC reduced phagosome-lysosome fusion in macrophages after infection. CC {ECO:0000269|PubMed:11237855, ECO:0000269|PubMed:15202932, CC ECO:0000269|PubMed:8757814, ECO:0000269|PubMed:9730978}. CC -!- SIMILARITY: Belongs to the NRAMP family. {ECO:0000305}. CC -!- CAUTION: The variant Asp-169 displayed in the entry is the variant CC found in the inbred strains C57BL/6J and BALB/cJ and may be expressed CC at very low levels in its mature form. In inbred strains, the CC susceptibility to infection with unrelated intracellular parasites, CC such as Mycobacterium bovis, Salmonella typhimurium and Leishmania CC donovani is associated with the single glycine-to-aspartic acid CC substitution at position 169 (G169D) in the predicted transmembrane CC domain 4. The conserved and resistant Gly-169 variant show the proper CC transporter activity described. However the variant Asp-169 shows an CC altered glycosylated pattern and seems to prevent proper maturation of CC the protein, resulting in its rapid degradation. The expression of the CC mature form of variant Asp-169 is strongly decreased in late CC endosome/lysosome membranes leading to a reduced phagosome-lysosome CC fusion in macrophages after infection. {ECO:0000269|PubMed:11237855, CC ECO:0000269|PubMed:15202932, ECO:0000269|PubMed:8757814, CC ECO:0000269|PubMed:9730978}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 GlyCosmos; P41251; 2 sites, No reported glycans. DR GlyGen; P41251; 2 sites. DR iPTMnet; P41251; -. DR PhosphoSitePlus; P41251; -. DR MaxQB; P41251; -. DR PaxDb; 10090-ENSMUSP00000027368; -. DR PeptideAtlas; P41251; -. DR ProteomicsDB; 293890; -. DR Antibodypedia; 3997; 206 antibodies from 27 providers. DR DNASU; 18173; -. DR Ensembl; ENSMUST00000027368.6; ENSMUSP00000027368.6; ENSMUSG00000026177.12. DR GeneID; 18173; -. DR KEGG; mmu:18173; -. DR UCSC; uc007bly.2; mouse. DR AGR; MGI:1345275; -. 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; STYLVWT; -. DR OrthoDB; 1093299at2759; -. 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 81 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 155 other cell types or tissues. DR ExpressionAtlas; P41251; baseline and differential. DR GO; GO:0010008; C:endosome membrane; IDA:MGI. DR GO; GO:0005770; C:late endosome; IDA:MGI. DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. 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; IDA:UniProtKB. DR GO; GO:0005384; F:manganese ion transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0051139; F:metal cation:proton antiporter activity; IDA:UniProtKB. 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: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:0098849; P:cellular detoxification of cadmium ion; ISO: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:0006879; P:intracellular iron ion homeostasis; IMP:MGI. DR GO; GO:0006826; P:iron ion transport; IDA:UniProtKB. 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; IDA:UniProtKB. 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-level 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: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:0032729; P:positive regulation of type II interferon production; IMP:MGI. DR GO; GO:0045730; P:respiratory burst; IDA:MGI. DR GO; GO:0009617; P:response to bacterium; IMP:MGI. DR GO; GO:0032496; P:response to lipopolysaccharide; IDA:MGI. DR GO; GO:0034341; P:response to type II interferon; 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 NCBIfam; TIGR01197; nramp; 1. DR NCBIfam; NF037982; Nramp_1; 1. DR PANTHER; PTHR11706:SF52; NATURAL RESISTANCE-ASSOCIATED MACROPHAGE PROTEIN 1; 1. DR PANTHER; PTHR11706; SOLUTE CARRIER PROTEIN FAMILY 11 MEMBER; 1. DR Pfam; PF01566; Nramp; 1. DR PRINTS; PR00447; NATRESASSCMP. DR Genevisible; P41251; MM. PE 1: Evidence at protein level; KW Endosome; Glycoprotein; Ion transport; Iron; Iron transport; Lysosome; KW Membrane; Reference proteome; Transmembrane; Transmembrane helix; KW 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 (found in strains resistant to unrelated FT intracellular parasites, such as Mycobacterium bovis, FT Salmonella typhimurium and Leishmania donovani; highly FT glycosylated; locates properly to macrophage late FT endosome/lysosome membranes; has divalent transition metal FT transporter activity)" FT /evidence="ECO:0000269|PubMed:11237855, FT ECO:0000269|PubMed:15202932, ECO:0000269|PubMed:7513015, FT ECO:0000269|PubMed:7665187, ECO:0000269|PubMed:8490962, FT ECO:0000269|PubMed:8757814, ECO:0000269|PubMed:8871656, FT ECO:0000269|PubMed:9730978" 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 //