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Natural resistance-associated macrophage protein 2 (NRAMP 2) (Divalent cation transporter 1) (Divalent metal transporter 1) (DMT-1) (Solute carrier family 11 member 2)

 NRAM2_MOUSE             Reviewed;         568 AA.
P49282; O54903; Q3UFV5; Q8BJL2; Q8BWV3; Q8CFA0; Q8VCU6;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
22-SEP-2009, sequence version 2.
25-APR-2018, entry version 149.
RecName: Full=Natural resistance-associated macrophage protein 2;
Short=NRAMP 2;
AltName: Full=Divalent cation transporter 1;
AltName: Full=Divalent metal transporter 1;
Short=DMT-1;
AltName: Full=Solute carrier family 11 member 2;
Name=Slc11a2; Synonyms=Dct1, Dmt1, Nramp2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=7789986; DOI=10.1016/0888-7543(95)80053-O;
Gruenheid S., Cellier M., Vidal S., Gros P.;
"Identification and characterization of a second mouse Nramp gene.";
Genomics 25:514-525(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=DBA;
Fleming M.D., Romano M.A., Su M.A., Garrick L.M., Garrick M.D.,
Andrews N.C.;
"Nramp2 is mutated in the anemic Belgrade (b) rat: evidence of a role
for Nramp2 in endosomal iron transport.";
Proc. Natl. Acad. Sci. U.S.A. 95:1148-1153(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Embryo, and Hippocampus;
PubMed=16141072; DOI=10.1126/science.1112014;
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., 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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=FVB/N; TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-80 (ISOFORMS 3/4), AND ALTERNATIVE
SPLICING.
STRAIN=C57BL/6J; TISSUE=Duodenum;
PubMed=12209011; DOI=10.1073/pnas.192423399;
Hubert N., Hentze M.W.;
"Previously uncharacterized isoforms of divalent metal transporter
(DMT)-1: implications for regulation and cellular function.";
Proc. Natl. Acad. Sci. U.S.A. 99:12345-12350(2002).
[7]
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=10361139;
Canonne-Hergaux F., Gruenheid S., Ponka P., Gros P.;
"Cellular and subcellular localization of the Nramp2 iron transporter
in the intestinal brush border and regulation by dietary iron.";
Blood 93:4406-4417(1999).
[8]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=11739192; DOI=10.1182/blood.V98.13.3823;
Canonne-Hergaux F., Zhang A.-S., Ponka P., Gros P.;
"Characterization of the iron transporter DMT1 (NRAMP2/DCT1) in red
blood cells of normal and anemic mk/mk mice.";
Blood 98:3823-3830(2001).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=15849611; DOI=10.1172/JCI24356;
Gunshin H., Fujiwara Y., Custodio A.O., Direnzo C., Robine S.,
Andrews N.C.;
"Slc11a2 is required for intestinal iron absorption and erythropoiesis
but dispensable in placenta and liver.";
J. Clin. Invest. 115:1258-1266(2005).
[10]
NIFEDIPINE TREATMENT.
PubMed=17293870; DOI=10.1038/nm1542;
Ludwiczek S., Theurl I., Muckenthaler M.U., Jakab M., Mair S.M.,
Theurl M., Kiss J., Paulmichl M., Hentze M.W., Ritter M., Weiss G.;
"Ca2+ channel blockers reverse iron overload by a new mechanism via
divalent metal transporter-1.";
Nat. Med. 13:448-454(2007).
[11]
UBIQUITINATION.
PubMed=18776082; DOI=10.1182/blood-2008-04-150953;
Foot N.J., Dalton H.E., Shearwin-Whyatt L.M., Dorstyn L., Tan S.S.,
Yang B., Kumar S.;
"Regulation of the divalent metal ion transporter DMT1 and iron
homeostasis by a ubiquitin-dependent mechanism involving Ndfips and
WWP2.";
Blood 112:4268-4275(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-564 AND SER-567, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-564 AND SER-567,
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-556 (ISOFORM 1),
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-586 (ISOFORM 3), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[14]
INTERACTION WITH ARRDC4, AND SUBCELLULAR LOCATION.
PubMed=27462458; DOI=10.1038/celldisc.2016.11;
Mackenzie K., Foot N.J., Anand S., Dalton H.E., Chaudhary N.,
Collins B.M., Mathivanan S., Kumar S.;
"Regulation of the divalent metal ion transporter via membrane
budding.";
Cell Discov. 2:16011-16011(2016).
[15]
VARIANT MK ARG-185.
PubMed=9241278;
Fleming M.D., Trenor C.C. III, Su M.A., Foernzler D., Beier D.R.,
Dietrich W.F., Andrews N.C.;
"Microcytic anaemia mice have a mutation in Nramp2, a candidate iron
transporter gene.";
Nat. Genet. 16:383-386(1997).
-!- FUNCTION: May serve to import iron into the mitochondria (By
similarity). Important in metal transport, in particular iron.
Involved in apical iron uptake into duodenal enterocytes. Involved
in iron transport from acidified endosomes into the cytoplasm of
erythroid precursor cells. May play an important role in hepatic
iron accumulation and tissue iron distribution.
{ECO:0000250|UniProtKB:P49281, ECO:0000269|PubMed:11739192,
ECO:0000269|PubMed:15849611}.
-!- SUBUNIT: Forms a complex with NDFIP1 and NEDD4L, in cortical
neurons, in response to iron and colbalt exposure; this
interaction leads to ubiquitination by NEDD4L and proteasome-
dependent degradation. Interacts with NDFIP2. Interacts with COX2
and TOM6 at the outer mitochondrion membrane (By similarity).
Interacts with ARRDC1; controls the incorporation of SLC11A2 into
extracellular vesicles through an ubiquitination-dependent
mechanism (By similarity). Interacts with ARRDC4; controls the
incorporation of SLC11A2 into extracellular vesicles through an
ubiquitination-dependent mechanism (PubMed:27462458).
{ECO:0000250|UniProtKB:P49281, ECO:0000269|PubMed:27462458}.
-!- SUBCELLULAR LOCATION: Endosome membrane
{ECO:0000250|UniProtKB:P49281}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P49281}. Mitochondrion outer membrane
{ECO:0000250|UniProtKB:P49281}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P49281}. Cell membrane
{ECO:0000269|PubMed:27462458}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P49281}. Note=Also found in extracellular
vesicles different from exosomes. {ECO:0000269|PubMed:27462458}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=2; Synonyms=Non-IRE;
IsoId=P49282-1; Sequence=Displayed;
Name=1; Synonyms=IRE;
IsoId=P49282-2; Sequence=VSP_003596;
Note=Contains a phosphoserine at position 556.
{ECO:0000244|PubMed:21183079};
Name=3; Synonyms=1A-IRE;
IsoId=P49282-3; Sequence=VSP_038145, VSP_003596;
Note=No experimental confirmation available. Contains a
phosphoserine at position 586. {ECO:0000244|PubMed:21183079};
Name=4; Synonyms=1A-Non-IRE;
IsoId=P49282-4; Sequence=VSP_038145;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Isoform 2 is abundantly expressed in erythroid
precursor cells (at protein level). Expressed at low levels in
most tissues analyzed. Expressed at low levels in small intestine
and at higher levels in kidney. {ECO:0000269|PubMed:10361139,
ECO:0000269|PubMed:11739192}.
-!- INDUCTION: Isoform 1 is up-regulated under iron-depletion
conditions in the proximal portion of the duodenum where it is
abundantly expressed in the brush border of absorptive epithelial
cells (at protein level). {ECO:0000269|PubMed:10361139}.
-!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P49281}.
-!- PTM: Ubiquitinated by WWP2. {ECO:0000269|PubMed:18776082}.
-!- DISEASE: Note=Defects in Slc11a2 are the cause of microcytic
anemia (mk). Homozygous mk/mk mice have hypochromic microcytic
anemia due to severe defects in intestinal iron absorption and
erythroid iron utilization.
-!- DISRUPTION PHENOTYPE: Mice display no apparent anatomical
abnormalities. They are however anemic, show progressive postnatal
growth retardation, and at birth have elevated liver iron stores
compared with wild-type littermates. None survive for more than 7
days. Heterozygotes appear normal, showing no significant
hematological abnormalities. However, by 8 weeks, their liver iron
content is lower than in wild-type littermates.
{ECO:0000269|PubMed:15849611}.
-!- MISCELLANEOUS: Nifedipine induces duodenal iron accumulation and
mobilizes iron from the liver of iron-overloaded mice.
-!- SIMILARITY: Belongs to the NRAMP family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAD38518.1; Type=Frameshift; Positions=69; Evidence={ECO:0000305};
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EMBL; L33415; AAC42051.1; -; mRNA.
EMBL; AF029758; AAC24496.1; -; mRNA.
EMBL; AK049856; BAC33960.1; -; mRNA.
EMBL; AK083478; BAC38930.1; -; mRNA.
EMBL; AK148276; BAE28454.1; -; mRNA.
EMBL; CH466550; EDL04090.1; -; Genomic_DNA.
EMBL; BC019137; AAH19137.1; -; mRNA.
EMBL; AJ493663; CAD38518.1; ALT_FRAME; mRNA.
CCDS; CCDS37211.1; -. [P49282-1]
CCDS; CCDS49733.1; -. [P49282-2]
PIR; A56852; A56852.
RefSeq; NP_001139633.1; NM_001146161.1. [P49282-2]
RefSeq; NP_032758.2; NM_008732.2. [P49282-1]
RefSeq; XP_006520640.1; XM_006520577.3. [P49282-1]
RefSeq; XP_006520641.1; XM_006520578.3. [P49282-1]
RefSeq; XP_011243789.1; XM_011245487.2. [P49282-4]
UniGene; Mm.234608; -.
ProteinModelPortal; P49282; -.
STRING; 10090.ENSMUSP00000023774; -.
iPTMnet; P49282; -.
PhosphoSitePlus; P49282; -.
EPD; P49282; -.
MaxQB; P49282; -.
PaxDb; P49282; -.
PeptideAtlas; P49282; -.
PRIDE; P49282; -.
Ensembl; ENSMUST00000023774; ENSMUSP00000023774; ENSMUSG00000023030. [P49282-1]
Ensembl; ENSMUST00000138843; ENSMUSP00000116463; ENSMUSG00000023030. [P49282-2]
GeneID; 18174; -.
KEGG; mmu:18174; -.
UCSC; uc007xrc.2; mouse. [P49282-1]
UCSC; uc007xrd.2; mouse. [P49282-2]
CTD; 4891; -.
MGI; MGI:1345279; Slc11a2.
eggNOG; KOG1291; Eukaryota.
eggNOG; COG1914; LUCA.
GeneTree; ENSGT00390000006526; -.
HOVERGEN; HBG052665; -.
InParanoid; P49282; -.
KO; K21398; -.
OMA; SLRPVMN; -.
OrthoDB; EOG091G05M9; -.
PhylomeDB; P49282; -.
TreeFam; TF315185; -.
Reactome; R-MMU-425410; Metal ion SLC transporters.
Reactome; R-MMU-917937; Iron uptake and transport.
ChiTaRS; Slc11a2; mouse.
PRO; PR:P49282; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000023030; -.
ExpressionAtlas; P49282; baseline and differential.
Genevisible; P49282; MM.
GO; GO:0045177; C:apical part of cell; ISO:MGI.
GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
GO; GO:0045178; C:basal part of cell; ISO:MGI.
GO; GO:0005903; C:brush border; IDA:MGI.
GO; GO:0031526; C:brush border membrane; IGI:BHF-UCL.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
GO; GO:0005769; C:early endosome; IDA:MGI.
GO; GO:0012505; C:endomembrane system; IDA:MGI.
GO; GO:0005768; C:endosome; IDA:MGI.
GO; GO:1903561; C:extracellular vesicle; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
GO; GO:0005770; C:late endosome; ISO:MGI.
GO; GO:0031902; C:late endosome membrane; ISO:MGI.
GO; GO:0005765; C:lysosomal membrane; ISO:MGI.
GO; GO:0005764; C:lysosome; ISO:MGI.
GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0070826; C:paraferritin complex; ISO:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0055037; C:recycling endosome; IDA:MGI.
GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
GO; GO:0005773; C:vacuole; ISO:MGI.
GO; GO:0046870; F:cadmium ion binding; ISS:UniProtKB.
GO; GO:0015086; F:cadmium ion transmembrane transporter activity; ISO:MGI.
GO; GO:0015087; F:cobalt ion transmembrane transporter activity; IDA:MGI.
GO; GO:0005375; F:copper ion transmembrane transporter activity; ISO:MGI.
GO; GO:0015093; F:ferrous iron transmembrane transporter activity; IDA:MGI.
GO; GO:0022890; F:inorganic cation transmembrane transporter activity; ISO:MGI.
GO; GO:0005381; F:iron ion transmembrane transporter activity; IDA:MGI.
GO; GO:0015094; F:lead ion transmembrane transporter activity; ISO:MGI.
GO; GO:0005384; F:manganese ion transmembrane transporter activity; ISO:MGI.
GO; GO:0015099; F:nickel cation transmembrane transporter activity; ISO:MGI.
GO; GO:0015078; F:proton transmembrane transporter activity; IDA:MGI.
GO; GO:0015295; F:solute:proton symporter activity; ISO:MGI.
GO; GO:0046915; F:transition metal ion transmembrane transporter activity; ISO:MGI.
GO; GO:0015100; F:vanadium ion transmembrane transporter activity; ISO:MGI.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
GO; GO:0070574; P:cadmium ion transmembrane transport; ISS:UniProtKB.
GO; GO:0034599; P:cellular response to oxidative stress; ISO:MGI.
GO; GO:0006824; P:cobalt ion transport; IDA:MGI.
GO; GO:0006825; P:copper ion transport; ISO:MGI.
GO; GO:0048813; P:dendrite morphogenesis; IMP:MGI.
GO; GO:0048821; P:erythrocyte development; IMP:MGI.
GO; GO:0070627; P:ferrous iron import; IDA:MGI.
GO; GO:0015684; P:ferrous iron transport; IDA:MGI.
GO; GO:0006783; P:heme biosynthetic process; IMP:MGI.
GO; GO:0006826; P:iron ion transport; IDA:MGI.
GO; GO:0015692; P:lead ion transport; ISO:MGI.
GO; GO:0007611; P:learning or memory; IMP:MGI.
GO; GO:0006828; P:manganese ion transport; ISO:MGI.
GO; GO:0060586; P:multicellular organismal iron ion homeostasis; IMP:MGI.
GO; GO:0015675; P:nickel cation transport; ISO:MGI.
GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IMP:MGI.
GO; GO:0006778; P:porphyrin-containing compound metabolic process; IMP:MGI.
GO; GO:0010039; P:response to iron ion; IEA:Ensembl.
GO; GO:0015676; P:vanadium ion transport; ISO:MGI.
HAMAP; MF_00221; NRAMP; 1.
InterPro; IPR001046; NRAMP_fam.
PANTHER; PTHR11706; PTHR11706; 1.
Pfam; PF01566; Nramp; 1.
PRINTS; PR00447; NATRESASSCMP.
TIGRFAMs; TIGR01197; nramp; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome;
Disease mutation; Endosome; Glycoprotein; Ion transport; Iron;
Iron transport; Membrane; Mitochondrion; Mitochondrion outer membrane;
Phosphoprotein; Reference proteome; Transmembrane;
Transmembrane helix; Transport; Ubl conjugation.
CHAIN 1 568 Natural resistance-associated macrophage
protein 2.
/FTId=PRO_0000212595.
TOPO_DOM 1 69 Cytoplasmic. {ECO:0000255}.
TRANSMEM 70 90 Helical. {ECO:0000255}.
TOPO_DOM 91 95 Extracellular. {ECO:0000255}.
TRANSMEM 96 117 Helical. {ECO:0000255}.
TOPO_DOM 118 154 Cytoplasmic. {ECO:0000255}.
TRANSMEM 155 175 Helical. {ECO:0000255}.
TOPO_DOM 176 179 Extracellular. {ECO:0000255}.
TRANSMEM 180 194 Helical. {ECO:0000255}.
TOPO_DOM 195 208 Cytoplasmic. {ECO:0000255}.
TRANSMEM 209 229 Helical. {ECO:0000255}.
TOPO_DOM 230 255 Extracellular. {ECO:0000255}.
TRANSMEM 256 276 Helical. {ECO:0000255}.
TOPO_DOM 277 301 Cytoplasmic. {ECO:0000255}.
TRANSMEM 302 322 Helical. {ECO:0000255}.
TOPO_DOM 323 360 Extracellular. {ECO:0000255}.
TRANSMEM 361 381 Helical. {ECO:0000255}.
TOPO_DOM 382 408 Cytoplasmic. {ECO:0000255}.
TRANSMEM 409 429 Helical. {ECO:0000255}.
TOPO_DOM 430 440 Extracellular. {ECO:0000255}.
TRANSMEM 441 461 Helical. {ECO:0000255}.
TOPO_DOM 462 482 Cytoplasmic. {ECO:0000255}.
TRANSMEM 483 503 Helical. {ECO:0000255}.
TOPO_DOM 504 506 Extracellular. {ECO:0000255}.
TRANSMEM 507 527 Helical. {ECO:0000255}.
TOPO_DOM 528 568 Cytoplasmic. {ECO:0000255}.
MOD_RES 564 564 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 567 567 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
CARBOHYD 336 336 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 349 349 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 1 M -> MGKKQPRAAAAAPNCELKSYSKSTDPQVSTM (in
isoform 3 and isoform 4). {ECO:0000305}.
/FTId=VSP_038145.
VAR_SEQ 544 568 YRLGLTAQPELYLLNTVDADSVVSR -> VSISKVLLSEDT
SGGNIK (in isoform 1 and isoform 3).
{ECO:0000303|PubMed:16141072,
ECO:0000303|Ref.2}.
/FTId=VSP_003596.
VARIANT 185 185 G -> R (in microcytic anemia).
{ECO:0000269|PubMed:9241278}.
CONFLICT 6 6 K -> E (in Ref. 3; BAE28454 and 6;
CAD38518). {ECO:0000305}.
CONFLICT 68 68 R -> S (in Ref. 2; AAC24496).
{ECO:0000305}.
CONFLICT 69 70 Missing (in Ref. 6; CAD38518).
{ECO:0000305}.
CONFLICT 142 142 P -> R (in Ref. 3; BAC38930).
{ECO:0000305}.
CONFLICT 182 182 L -> V (in Ref. 1; AAC42051).
{ECO:0000305}.
SEQUENCE 568 AA; 62368 MW; 603AAF697AAD3C74 CRC64;
MVLDPKEKMP DDGASGDHGD SASLGAINPA YSNSSLPHST GDSEEPFTTY FDEKIPIPEE
EYSCFSFRKL WAFTGPGFLM SIAYLDPGNI ESDLQSGAVA GFKLLWVLLL ATIVGLLLQR
LAARLGVVTG LHLAEVCHRQ YPKVPRIILW LMVELAIIGS DMQEVIGSAI AINLLSAGRV
PLWGGVLITI ADTFVFLFLD KYGLRKLEAF FGFLITIMAL TFGYEYITVK PSQSQVLRGM
FVPSCPGCRT PQVEQAVGIV GAVIMPHNMY LHSALVKSRQ VNRANKQEVR EANKYFFIES
CIALFVSFII NVFVVSVFAE AFFEKTNKQV VEVCKNNSSP HADLFPSDNS TLAVDIYKGG
VVLGCYFGPA ALYIWAVGIL AAGQSSTMTG TYSGQFVMEG FLNLKWSRFA RVILTRSIAI
IPTLLVAVFQ DVEHLTGMND FLNVLQSLQL PFALIPILTF TSLRPVMSEF SNGIGWRIAG
GILVLIVCSI NMYFVVVYVQ ELGHVALYVV AAVVSVAYLT FVFYLGWQCL IALGLSFLDC
GRSYRLGLTA QPELYLLNTV DADSVVSR


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