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Transferrin receptor protein 2 (TfR2)

 TFR2_HUMAN              Reviewed;         801 AA.
Q9UP52; A6NGM7; O75422; Q1HE13; Q9HA99; Q9NX67;
11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
12-SEP-2018, entry version 154.
RecName: Full=Transferrin receptor protein 2;
Short=TfR2;
Name=TFR2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA).
TISSUE=Erythroleukemia, and Myeloid leukemia cell;
PubMed=10409623; DOI=10.1074/jbc.274.30.20826;
Kawabata H., Yang R., Hirama T., Vuong P.T., Kawano S., Gombart A.F.,
Koeffler H.P.;
"Molecular cloning of transferrin receptor 2: a new member of the
transferrin receptor-like family.";
J. Biol. Chem. 274:20826-20832(1999).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM GAMMA).
PubMed=9799793;
Gloeckner G., Scherer S., Schattevoy R., Boright A.P., Weber J.,
Tsui L.-C., Rosenthal A.;
"Large-scale sequencing of two regions in human chromosome 7q22:
analysis of 650 kb of genomic sequence around the EPO and CUTL1 loci
reveals 17 genes.";
Genome Res. 8:1060-1073(1998).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [LARGE SCALE MRNA] OF 1-158 AND 370-801.
TISSUE=Carcinoma, and Embryo;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
DISEASE.
PubMed=10802645; DOI=10.1038/75534;
Camaschella C., Roetto A., Cali A., De Gobbi M., Garozzo G.,
Carella M., Majorano N., Totaro A., Gasparini P.;
"The gene TFR2 is mutated in a new type of haemochromatosis mapping to
7q22.";
Nat. Genet. 25:14-15(2000).
[8]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-339 AND ASN-754.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[10]
VARIANT HFE3 LYS-172.
PubMed=11313241; DOI=10.1182/blood.V97.9.2555;
Roetto A., Totaro A., Piperno A., Piga A., Longo F., Garozzo G.,
Cali A., De Gobbi M., Gasparini P., Camaschella C.;
"New mutations inactivating transferrin 2 in hemochromatosis type 3.";
Blood 97:2555-2560(2001).
[11]
VARIANT HFE3 PRO-690.
PubMed=12130528; DOI=10.1182/blood-2002-01-0133;
Mattman A., Huntsman D., Lockitch G., Langlois S., Buskard N.,
Ralston D., Butterfield Y., Rodrigues P., Jones S., Porto G.,
Marra M., De Sousa M., Vatcher G.;
"Transferrin receptor 2 (TfR2) and HFE mutational analysis in non-
C282Y iron overload: identification of a novel TfR2 mutation.";
Blood 100:1075-1077(2002).
[12]
VARIANT GLN-455.
PubMed=12150153; DOI=10.1182/blood-2002-04-1077;
Hofmann W.-K., Tong X.-J., Ajioka R.S., Kushner J.P., Koeffler H.P.;
"Mutation analysis of transferrin-receptor 2 in patients with atypical
hemochromatosis.";
Blood 100:1099-1100(2002).
[13]
VARIANT HFE3 ILE-22.
PubMed=14633868; DOI=10.1373/clinchem.2003.023440;
Biasiotto G., Belloli S., Ruggeri G., Zanella I., Gerardi G.,
Corrado M., Gobbi E., Albertini A., Arosio P.;
"Identification of new mutations of the HFE, hepcidin, and transferrin
receptor 2 genes by denaturing HPLC analysis of individuals with
biochemical indications of iron overload.";
Clin. Chem. 49:1981-1988(2003).
-!- FUNCTION: Mediates cellular uptake of transferrin-bound iron in a
non-iron dependent manner. May be involved in iron metabolism,
hepatocyte function and erythrocyte differentiation.
-!- SUBUNIT: Homodimer.
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane
protein.
-!- SUBCELLULAR LOCATION: Isoform Beta: Cytoplasm {ECO:0000305}.
Note=Lacks the transmembrane domain. Probably intracellular.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=Alpha;
IsoId=Q9UP52-1; Sequence=Displayed;
Name=Beta;
IsoId=Q9UP52-2; Sequence=VSP_005354;
Name=Gamma;
IsoId=Q9UP52-3; Sequence=VSP_005355;
-!- TISSUE SPECIFICITY: Predominantly expressed in liver. While the
alpha form is also expressed in spleen, lung, muscle, prostate and
peripheral blood mononuclear cells, the beta form is expressed in
all tissues tested, albeit weakly.
-!- DISEASE: Hemochromatosis 3 (HFE3) [MIM:604250]: A disorder of iron
metabolism characterized by iron overload. Excess iron is
deposited in a variety of organs leading to their failure, and
resulting in serious illnesses including cirrhosis, hepatomas,
diabetes, cardiomyopathy, arthritis, and hypogonadotropic
hypogonadism. Severe effects of the disease usually do not appear
until after decades of progressive iron loading.
{ECO:0000269|PubMed:11313241, ECO:0000269|PubMed:12130528,
ECO:0000269|PubMed:14633868}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: The variant Lys-172 found in hereditary
hemochromatosis type III affects the putative initiation codon of
the beta isoform thus preventing its translation.
-!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA91153.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF067864; AAD45561.1; -; mRNA.
EMBL; AF053356; AAC78796.1; -; Genomic_DNA.
EMBL; DQ496110; ABF47099.1; -; Genomic_DNA.
EMBL; AC099394; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC142630; AAI42631.1; -; mRNA.
EMBL; AK022002; BAB13951.1; -; mRNA.
EMBL; AK000421; BAA91153.1; ALT_INIT; mRNA.
CCDS; CCDS34707.1; -. [Q9UP52-1]
RefSeq; NP_001193784.1; NM_001206855.1. [Q9UP52-2]
RefSeq; NP_003218.2; NM_003227.3. [Q9UP52-1]
RefSeq; XP_005250610.1; XM_005250553.4. [Q9UP52-1]
RefSeq; XP_016868062.1; XM_017012573.1. [Q9UP52-1]
UniGene; Hs.544932; -.
ProteinModelPortal; Q9UP52; -.
SMR; Q9UP52; -.
BioGrid; 112894; 11.
IntAct; Q9UP52; 3.
STRING; 9606.ENSP00000223051; -.
ChEMBL; CHEMBL3988361; -.
DrugBank; DB09412; Gallium citrate Ga-67.
DrugBank; DB05260; Gallium nitrate.
MEROPS; M28.973; -.
TCDB; 9.B.229.1.2; the transferrin receptor, cd71, (tfr) family.
iPTMnet; Q9UP52; -.
PhosphoSitePlus; Q9UP52; -.
BioMuta; TFR2; -.
DMDM; 20140912; -.
PaxDb; Q9UP52; -.
PeptideAtlas; Q9UP52; -.
PRIDE; Q9UP52; -.
ProteomicsDB; 85352; -.
ProteomicsDB; 85353; -. [Q9UP52-2]
ProteomicsDB; 85354; -. [Q9UP52-3]
Ensembl; ENST00000223051; ENSP00000223051; ENSG00000106327. [Q9UP52-1]
Ensembl; ENST00000462107; ENSP00000420525; ENSG00000106327. [Q9UP52-1]
GeneID; 7036; -.
KEGG; hsa:7036; -.
UCSC; uc003uvv.2; human. [Q9UP52-1]
CTD; 7036; -.
DisGeNET; 7036; -.
EuPathDB; HostDB:ENSG00000106327.12; -.
GeneCards; TFR2; -.
GeneReviews; TFR2; -.
HGNC; HGNC:11762; TFR2.
HPA; CAB016255; -.
HPA; HPA011937; -.
MalaCards; TFR2; -.
MIM; 604250; phenotype.
MIM; 604720; gene.
neXtProt; NX_Q9UP52; -.
OpenTargets; ENSG00000106327; -.
Orphanet; 225123; Hemochromatosis type 3.
PharmGKB; PA36477; -.
eggNOG; KOG2195; Eukaryota.
eggNOG; COG2234; LUCA.
GeneTree; ENSGT00550000074421; -.
HOGENOM; HOG000124067; -.
HOVERGEN; HBG023177; -.
InParanoid; Q9UP52; -.
OMA; LFISWDG; -.
OrthoDB; EOG091G02ZM; -.
PhylomeDB; Q9UP52; -.
TreeFam; TF312981; -.
Reactome; R-HSA-917977; Transferrin endocytosis and recycling.
GeneWiki; TFR2; -.
GenomeRNAi; 7036; -.
PRO; PR:Q9UP52; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000106327; Expressed in 178 organ(s), highest expression level in liver.
CleanEx; HS_TFR2; -.
ExpressionAtlas; Q9UP52; baseline and differential.
Genevisible; Q9UP52; HS.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:BHF-UCL.
GO; GO:0009897; C:external side of plasma membrane; IGI:BHF-UCL.
GO; GO:1990712; C:HFE-transferrin receptor complex; IDA:BHF-UCL.
GO; GO:0005887; C:integral component of plasma membrane; IGI:BHF-UCL.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0039706; F:co-receptor binding; IPI:BHF-UCL.
GO; GO:0004998; F:transferrin receptor activity; IDA:BHF-UCL.
GO; GO:0033570; F:transferrin transmembrane transporter activity; IEA:InterPro.
GO; GO:0006953; P:acute-phase response; IEA:Ensembl.
GO; GO:0006879; P:cellular iron ion homeostasis; TAS:UniProtKB.
GO; GO:0071281; P:cellular response to iron ion; IGI:BHF-UCL.
GO; GO:0033216; P:ferric iron import; IGI:BHF-UCL.
GO; GO:0055072; P:iron ion homeostasis; IMP:BHF-UCL.
GO; GO:0097286; P:iron ion import; IGI:BHF-UCL.
GO; GO:0006826; P:iron ion transport; NAS:UniProtKB.
GO; GO:0045807; P:positive regulation of endocytosis; IGI:BHF-UCL.
GO; GO:0090277; P:positive regulation of peptide hormone secretion; IMP:BHF-UCL.
GO; GO:1903319; P:positive regulation of protein maturation; IGI:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:BHF-UCL.
GO; GO:0006898; P:receptor-mediated endocytosis; IGI:BHF-UCL.
GO; GO:0010039; P:response to iron ion; IMP:BHF-UCL.
GO; GO:0033572; P:transferrin transport; IGI:BHF-UCL.
CDD; cd02128; PA_TfR; 1.
Gene3D; 1.20.930.40; -; 1.
InterPro; IPR003137; PA_domain.
InterPro; IPR007484; Peptidase_M28.
InterPro; IPR039373; Peptidase_M28B.
InterPro; IPR036757; TFR-like_dimer_dom_sf.
InterPro; IPR037324; TfR1/2_PA.
PANTHER; PTHR10404; PTHR10404; 1.
Pfam; PF02225; PA; 1.
Pfam; PF04389; Peptidase_M28; 1.
SUPFAM; SSF47672; SSF47672; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome; Cytoplasm;
Disease mutation; Disulfide bond; Glycoprotein; Membrane;
Polymorphism; Receptor; Reference proteome; Signal-anchor;
Transmembrane; Transmembrane helix.
CHAIN 1 801 Transferrin receptor protein 2.
/FTId=PRO_0000174136.
TOPO_DOM 1 83 Cytoplasmic. {ECO:0000255}.
TRANSMEM 84 104 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 105 801 Extracellular. {ECO:0000255}.
MOTIF 23 26 Endocytosis signal. {ECO:0000255}.
CARBOHYD 240 240 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 339 339 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 540 540 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 754 754 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
DISULFID 108 108 Interchain. {ECO:0000255}.
DISULFID 111 111 Interchain. {ECO:0000255}.
VAR_SEQ 1 171 Missing (in isoform Beta).
{ECO:0000303|PubMed:10409623}.
/FTId=VSP_005354.
VAR_SEQ 343 369 Missing (in isoform Gamma).
{ECO:0000305}.
/FTId=VSP_005355.
VARIANT 22 22 V -> I (in HFE3; dbSNP:rs80338876).
{ECO:0000269|PubMed:14633868}.
/FTId=VAR_042515.
VARIANT 172 172 M -> K (in HFE3; dbSNP:rs80338879).
{ECO:0000269|PubMed:11313241}.
/FTId=VAR_012738.
VARIANT 230 230 D -> E (in dbSNP:rs41303465).
/FTId=VAR_034122.
VARIANT 238 238 I -> M (in dbSNP:rs34242818).
/FTId=VAR_034123.
VARIANT 455 455 R -> Q (hereditary hemochromatosis
modifier; dbSNP:rs41303501).
{ECO:0000269|PubMed:12150153}.
/FTId=VAR_042516.
VARIANT 690 690 Q -> P (in HFE3; dbSNP:rs80338889).
{ECO:0000269|PubMed:12130528}.
/FTId=VAR_042517.
VARIANT 752 752 R -> H (in dbSNP:rs41295942).
/FTId=VAR_034124.
CONFLICT 712 712 R -> RIPLSAQV (in Ref. 2). {ECO:0000305}.
SEQUENCE 801 AA; 88755 MW; D3D3082BA835413A CRC64;
MERLWGLFQR AQQLSPRSSQ TVYQRVEGPR KGHLEEEEED GEEGAETLAH FCPMELRGPE
PLGSRPRQPN LIPWAAAGRR AAPYLVLTAL LIFTGAFLLG YVAFRGSCQA CGDSVLVVSE
DVNYEPDLDF HQGRLYWSDL QAMFLQFLGE GRLEDTIRQT SLRERVAGSA GMAALTQDIR
AALSRQKLDH VWTDTHYVGL QFPDPAHPNT LHWVDEAGKV GEQLPLEDPD VYCPYSAIGN
VTGELVYAHY GRPEDLQDLR ARGVDPVGRL LLVRVGVISF AQKVTNAQDF GAQGVLIYPE
PADFSQDPPK PSLSSQQAVY GHVHLGTGDP YTPGFPSFNQ TQFPPVASSG LPSIPAQPIS
ADIASRLLRK LKGPVAPQEW QGSLLGSPYH LGPGPRLRLV VNNHRTSTPI NNIFGCIEGR
SEPDHYVVIG AQRDAWGPGA AKSAVGTAIL LELVRTFSSM VSNGFRPRRS LLFISWDGGD
FGSVGSTEWL EGYLSVLHLK AVVYVSLDNA VLGDDKFHAK TSPLLTSLIE SVLKQVDSPN
HSGQTLYEQV VFTNPSWDAE VIRPLPMDSS AYSFTAFVGV PAVEFSFMED DQAYPFLHTK
EDTYENLHKV LQGRLPAVAQ AVAQLAGQLL IRLSHDRLLP LDFGRYGDVV LRHIGNLNEF
SGDLKARGLT LQWVYSARGD YIRAAEKLRQ EIYSSEERDE RLTRMYNVRI MRVEFYFLSQ
YVSPADSPFR HIFMGRGDHT LGALLDHLRL LRSNSSGTPG ATSSTGFQES RFRRQLALLT
WTLQGAANAL SGDVWNIDNN F


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San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




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