NRAM1_BOVIN
ID NRAM1_BOVIN Reviewed; 548 AA.
AC Q27981;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 103.
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=NRAMP1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8908514; DOI=10.1101/gr.6.10.956;
RA Feng J., Li Y., Hashad M., Schurr E., Gros P., Adams L.G., Templeton J.W.;
RT "Bovine natural resistance associated macrophage protein 1 (Nramp1) gene.";
RL Genome Res. 6:956-964(1996).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the NRAMP family. {ECO:0000305}.
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DR EMBL; U12862; AAA82582.1; -; mRNA.
DR RefSeq; NP_777077.1; NM_174652.2.
DR AlphaFoldDB; Q27981; -.
DR SMR; Q27981; -.
DR STRING; 9913.ENSBTAP00000020627; -.
DR PaxDb; Q27981; -.
DR GeneID; 282470; -.
DR KEGG; bta:282470; -.
DR CTD; 6556; -.
DR eggNOG; KOG1291; Eukaryota.
DR InParanoid; Q27981; -.
DR OrthoDB; 666470at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0051139; F:metal ion:proton antiporter activity; IBA:GO_Central.
DR GO; GO:0006876; P:cellular cadmium ion homeostasis; IBA:GO_Central.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central.
DR GO; GO:0032496; P:response to lipopolysaccharide; IBA:GO_Central.
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 2: Evidence at transcript 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_0000212584"
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..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 548 AA; 59568 MW; FAC8EB2B2B878118 CRC64;
MSGDTGPPKQ GGTRYGSISS PPSPEPQQAP PGGTYLSEKI PIPDTESGTF SLRKLWAFTG
PGFLMSIAFL DPGNIESDLQ AGAVAGFKLL WVLLWATVLG LLCQRLAARL GVVTGKDLGE
VCHLYYPKVP RILLWLTIEL AIVGSDMQEV IGTAIAFSLL SAGRIPLWGG VLITVVDTFF
FLFLDNYGLR KLEAFFGFLI TIMALTFGYE YVVAQPAQGA LLQGLFLPSC PGCGQPELLQ
AVGIIGAIIM PHNIYLHSSL VKSREVDRSR RADIREANMY FLIEATIALS VSFLINLFVM
AVFGQAFYKQ TNQAAFNICA DSSLHDYAPI FPRNNLTVAV DIYQGGVILG CLFGPPALYI
WAVGLLAAGQ SSTMTGTYAG QFVMEGFLKL RWSRFARVLL TRSCAILPTV LLAVFRDLRD
LSGLNDLLNV LQSLLLPFAV LPILTFTSMP ALMQEFANGL VSKVITSSIM VLVCAVNLYF
VISYLPSLPH PAYFSLVALL AAAYLGLTTY LVWTCLITQG ATLLAHSSHQ RFLYGLPEED
QEKGRTSG
