ID F1LSN8_RAT Unreviewed; 507 AA. AC F1LSN8; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 02-SEP-2026, entry version 86. DE RecName: Full=Natural resistance-associated macrophage protein 1 {ECO:0000256|ARBA:ARBA00015099}; DE AltName: Full=Solute carrier family 11 member 1 {ECO:0000256|ARBA:ARBA00032337}; GN Name=Slc11a1 {ECO:0000313|Ensembl:ENSRNOP00000054282.2, GN ECO:0000313|RGD:1601463}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000054282.2, ECO:0000313|Proteomes:UP000002494}; RN [1] {ECO:0000313|Ensembl:ENSRNOP00000054282.2} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000054282.2}; RA Doris P.A., Kalbfleisch T., Li K., Howe K., Wood J.; RT "GRCr8: a new rat reference genome assembly contstructed from accurate long RT reads and long range scaffolding."; RL Submitted (JAN-2024) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSRNOP00000054282.2} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000054282.2}; RG Ensembl; RL Submitted (JAN-2026) to UniProtKB. 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:0000256|ARBA:ARBA00035618}. 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:0000256|ARBA:ARBA00035584}; CC -!- CATALYTIC ACTIVITY: CC Reaction=Mn(2+)(in) + H(+)(out) = Mn(2+)(out) + H(+)(in); CC Xref=Rhea:RHEA:73063, ChEBI:CHEBI:15378, ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|ARBA:ARBA00048522}; CC -!- CATALYTIC ACTIVITY: CC Reaction=Zn(2+)(in) + H(+)(out) = Zn(2+)(out) + H(+)(in); CC Xref=Rhea:RHEA:28839, ChEBI:CHEBI:15378, ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|ARBA:ARBA00047695}; CC -!- SUBCELLULAR LOCATION: Late endosome membrane CC {ECO:0000256|ARBA:ARBA00004107}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004107}. Lysosome membrane CC {ECO:0000256|ARBA:ARBA00004155}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004155}. CC -!- SIMILARITY: Belongs to the NRAMP (TC 2.A.55) family. CC {ECO:0000256|ARBA:ARBA00009965}. 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 RefSeq; NP_001026828.2; NM_001031658.2. DR AlphaFoldDB; F1LSN8; -. DR SMR; F1LSN8; -. DR Ensembl; ENSRNOT00000057472.5; ENSRNOP00000054282.2; ENSRNOG00000014956.9. DR GeneID; 316519; -. DR KEGG; rno:316519; -. DR CTD; 6556; -. DR RGD; 1601463; Slc11a1. DR GeneTree; ENSGT00940000160799; -. DR Proteomes; UP000002494; Chromosome 9. DR Bgee; ENSRNOG00000014956; Expressed in spleen and 18 other cell types or tissues. DR ExpressionAtlas; F1LSN8; baseline and differential. DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005381; F:iron ion transmembrane transporter activity; IEA:UniProtKB-ARBA. 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. PE 1: Evidence at protein level; KW Endosome {ECO:0000256|ARBA:ARBA00022753}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Ion transport {ECO:0000256|ARBA:ARBA00023065}; KW Iron {ECO:0000256|ARBA:ARBA00023004}; KW Iron transport {ECO:0000256|ARBA:ARBA00022496}; KW Lysosome {ECO:0000256|ARBA:ARBA00023228}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Proteomics identification {ECO:0007829|PeptideAtlas:F1LSN8}; KW Reference proteome {ECO:0000313|Proteomes:UP000002494}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}. FT TRANSMEM 48..67 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 124..143 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 155..173 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 197..215 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 236..262 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 301..327 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 354..373 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 393..411 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 423..445 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 451..472 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT REGION 1..36 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 8..22 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 507 AA; 55936 MW; 66AA452FBBEA12BE CRC64; MIRDKNPQRV NRPSYGSISS LPSPAPQPEP SRNTYLSEKI PIPSTEQLLW VLLWATVLGL LCQRLAARLG VVTGKDLGEI CHLYYPKVPR ILLWLTIELA IVGSDMQEVI GTAISFNLLS AGRIPLWGGV LITIVDTFFF LFLDNYGLRK LEAFFGFLIT IMALTFGYEY VVARPSQGAL LKGLFLPSCP GCGQPELLQA VGIVGAIIMP HNIYLHSALV KSREVDRTRR GDVREANMYF LTEATIALFV SFIINLFVMA VFGQAFYQQT NEEAFNICAN SSLHNYAKIF PRDNNTVSVD IYQGGVILGC LFGPAALYIW AVGLLAAGQS STMTGTYAGQ FVMEGFLKLR WSRFARVLLT RSCAILPTVL VAVFRDLRDL SGLNDLLNVL QSLLLPFAVL PILTFTSMPA VMQEFANGWL SKVITSCIMA LVCAINLYFV ISYLPSLPHP AYFGLVALLA IGYLGLTAYL AWTCCIAHGA KFLTHSSHQR FLYGLPIEEQ EGREGSG //