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Serotransferrin (Transferrin) (Beta-1 metal-binding globulin) (Siderophilin)

 TRFE_HUMAN              Reviewed;         698 AA.
P02787; O43890; Q1HBA5; Q9NQB8; Q9UHV0;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
30-NOV-2010, sequence version 3.
30-AUG-2017, entry version 216.
RecName: Full=Serotransferrin;
Short=Transferrin;
AltName: Full=Beta-1 metal-binding globulin;
AltName: Full=Siderophilin;
Flags: Precursor;
Name=TF; ORFNames=PRO1400;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS TF*B2; TF*CHI; TF*D1 AND
VAL-448.
PubMed=6585826; DOI=10.1073/pnas.81.9.2752;
Yang F., Lum J.B., McGill J.R., Moore C.M., Naylor S.L.,
van Bragt P.H., Baldwin W.D., Bowman B.H.;
"Human transferrin: cDNA characterization and chromosomal
localization.";
Proc. Natl. Acad. Sci. U.S.A. 81:2752-2756(1984).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3678832; DOI=10.1016/0378-1119(87)90163-6;
Schaeffer E., Lucero M.A., Jeltsch J.-M., Py M.-C., Levin M.J.,
Chambon P., Cohen G.N., Zakin M.M.;
"Complete structure of the human transferrin gene. Comparison with
analogous chicken gene and human pseudogene.";
Gene 56:109-116(1987).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-448.
TISSUE=Liver;
PubMed=1809186; DOI=10.1111/j.1749-6632.1991.tb18573.x;
Hershberger C.L., Larson J.L., Arnold B., Rosteck P.R. Jr.,
Williams P., Dehoff B., Dunn P., O'Neal K.L., Riemen M.W., Tice P.A.;
"A cloned gene for human transferrin.";
Ann. N. Y. Acad. Sci. 646:140-154(1991).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-448 AND ATRAF
PRO-477.
PubMed=11110675;
Beutler E., Gelbart T., Lee P.L., Trevino R., Fernandez M.A.,
Fairbanks V.F.;
"Molecular characterization of a case of atransferrinemia.";
Blood 96:4071-4074(2000).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-55; SER-277;
GLY-296; VAL-448 AND SER-589.
SeattleSNPs variation discovery resource;
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-448.
NHLBI resequencing and genotyping service (RS&G);
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-448.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-448.
TISSUE=Brain;
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).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72 AND 291-300.
PubMed=3106157; DOI=10.1016/0378-1119(86)90277-5;
Adrian G.S., Korinek B.W., Bowman B.H., Yang F.;
"The human transferrin gene: 5' region contains conserved sequences
which match the control elements regulated by heavy metals,
glucocorticoids and acute phase reaction.";
Gene 49:167-175(1986).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14.
PubMed=3786138; DOI=10.1093/nar/14.21.8692;
Lucero M.A., Schaeffer E., Cohen G.N., Zakin M.M.;
"The 5' region of the human transferrin gene: structure and potential
regulatory sites.";
Nucleic Acids Res. 14:8692-8692(1986).
[12]
PROTEIN SEQUENCE OF 20-698, AND VARIANT VAL-448.
PubMed=6833213;
McGillivray R.T.A., Mendez E., Shewale J.G., Sinha S.K.,
Lineback-Zins J., Brew K.;
"The primary structure of human serum transferrin. The structures of
seven cyanogen bromide fragments and the assembly of the complete
structure.";
J. Biol. Chem. 258:3543-3553(1983).
[13]
NUCLEOTIDE SEQUENCE [MRNA] OF 45-72.
PubMed=10931525;
DOI=10.1002/1097-4547(20000815)61:4<388::AID-JNR5>3.0.CO;2-Q;
de Arriba Zerpa G.A., Saleh M.-C., Fernandez P.M., Guillou F.,
Espinosa de los Monteros A., de Vellis J., Zakin M.M., Baron B.;
"Alternative splicing prevents transferrin secretion during
differentiation of a human oligodendrocyte cell line.";
J. Neurosci. Res. 61:388-395(2000).
[14]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 73-698, AND VARIANT VAL-448.
PubMed=3858812; DOI=10.1073/pnas.82.10.3149;
Park I., Schaeffer E., Sidoli A., Baralle F.E., Cohen G.N.,
Zakin M.M.;
"Organization of the human transferrin gene: direct evidence that it
originated by gene duplication.";
Proc. Natl. Acad. Sci. U.S.A. 82:3149-3153(1985).
[15]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 99-698, AND VARIANT VAL-448.
TISSUE=Fetal liver;
Zhang C., Yu Y., Zhang S., Wei H., Zhou G., Bi J., Zhang Y., Liu M.,
He F.;
"Functional prediction of the coding sequences of 33 new genes deduced
by analysis of cDNA clones from human fetal liver.";
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
[16]
PROTEIN SEQUENCE OF 108-121; 259-273; 332-343; 374-384; 434-452;
454-464; 495-508; 531-541; 577-600 AND 684-696, IDENTIFICATION BY MASS
SPECTROMETRY, AND VARIANT VAL-448.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[17]
PROTEIN SEQUENCE OF 263-266; 454-458; 531-538 AND 589-595.
TISSUE=Heart;
PubMed=7498159; DOI=10.1002/elps.11501601192;
Kovalyov L.I., Shishkin S.S., Efimochkin A.S., Kovalyova M.A.,
Ershova E.S., Egorov T.A., Musalyamov A.K.;
"The major protein expression profile and two-dimensional protein
database of human heart.";
Electrophoresis 16:1160-1169(1995).
[18]
NUCLEOTIDE SEQUENCE [MRNA] OF 422-698, AND VARIANT VAL-448.
PubMed=6322780; DOI=10.1016/0006-291X(84)91648-6;
Uzan G., Frain M., Park I., Besmond C., Maessen G., Trepat J.S.,
Zakin M.M., Kahn A.;
"Molecular cloning and sequence analysis of cDNA for human
transferrin.";
Biochem. Biophys. Res. Commun. 119:273-281(1984).
[19]
NUCLEOTIDE SEQUENCE [MRNA] OF 564-624, AND VARIANTS TF*C2 AND SER-589.
TISSUE=Brain;
PubMed=9272172; DOI=10.1007/s004390050533;
Namekata K., Oyama F., Imagawa M., Ihara Y.;
"Human transferrin (Tf): a single mutation at codon 570 determines Tf
C1 or Tf C2 variant.";
Hum. Genet. 100:457-458(1997).
[20]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 564-624.
Tsuchida S., Ikemoto S., Kajii E.;
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
[21]
NUCLEOTIDE SEQUENCE [MRNA] OF 636-696.
PubMed=2780570; DOI=10.1073/pnas.86.18.7260;
Duguid J.R., Bohmont C.W., Liu N.G., Tourtellotte W.W.;
"Changes in brain gene expression shared by scrapie and Alzheimer
disease.";
Proc. Natl. Acad. Sci. U.S.A. 86:7260-7264(1989).
[22]
DISULFIDE BONDS.
PubMed=6953407; DOI=10.1073/pnas.79.8.2504;
McGillivray R.T.A., Mendez E., Sinha S.K., Sutton M.R.,
Lineback-Zins J., Brew K.;
"The complete amino acid sequence of human serum transferrin.";
Proc. Natl. Acad. Sci. U.S.A. 79:2504-2508(1982).
[23]
MUTAGENESIS.
PubMed=1932003; DOI=10.1021/bi00109a002;
Woodworth R.C., Mason A.B., Funk W.D., McGillivray R.T.A.;
"Expression and initial characterization of five site-directed mutants
of the N-terminal half-molecule of human transferrin.";
Biochemistry 30:10824-10829(1991).
[24]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-432 AND ASN-630.
TISSUE=Bile;
PubMed=15084671; DOI=10.1074/mcp.M400015-MCP200;
Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H.,
Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.;
"A proteomic analysis of human bile.";
Mol. Cell. Proteomics 3:715-728(2004).
[25]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-432 AND ASN-630.
TISSUE=Plasma;
PubMed=14760718; DOI=10.1002/pmic.200300556;
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
"Screening for N-glycosylated proteins by liquid chromatography mass
spectrometry.";
Proteomics 4:454-465(2004).
[26]
GLYCOSYLATION AT ASN-432; ASN-491 AND ASN-630.
PubMed=15536627; DOI=10.1002/rcm.1718;
Satomi Y., Shimonishi Y., Hase T., Takao T.;
"Site-specific carbohydrate profiling of human transferrin by nano-
flow liquid chromatography/electrospray ionization mass
spectrometry.";
Rapid Commun. Mass Spectrom. 18:2983-2988(2004).
[27]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-432 AND ASN-630.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[28]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-630.
TISSUE=Saliva;
PubMed=16740002; DOI=10.1021/pr050492k;
Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T.,
Loo J.A.;
"Identification of N-linked glycoproteins in human saliva by
glycoprotein capture and mass spectrometry.";
J. Proteome Res. 5:1493-1503(2006).
[29]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-432 AND ASN-630.
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).
[30]
GLYCOSYLATION AT ASN-630.
PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
"A strategy for precise and large scale identification of core
fucosylated glycoproteins.";
Mol. Cell. Proteomics 8:913-923(2009).
[31]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-432 AND ASN-630, AND
STRUCTURE OF CARBOHYDRATES.
TISSUE=Cerebrospinal fluid;
PubMed=19838169; DOI=10.1038/nmeth.1392;
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,
Brinkmalm G., Larson G.;
"Enrichment of glycopeptides for glycan structure and attachment site
identification.";
Nat. Methods 6:809-811(2009).
[32]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22905912; DOI=10.1021/pr300539b;
Rosenow A., Noben J.P., Jocken J., Kallendrusch S.,
Fischer-Posovszky P., Mariman E.C., Renes J.;
"Resveratrol-induced changes of the human adipocyte secretion
profile.";
J. Proteome Res. 11:4733-4743(2012).
[33]
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).
[34]
PHOSPHORYLATION AT SER-389 AND SER-685.
PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
Pinna L.A., Pagliarini D.J., Dixon J.E.;
"A single kinase generates the majority of the secreted
phosphoproteome.";
Cell 161:1619-1632(2015).
[35]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 22-350.
PubMed=9609685; DOI=10.1021/bi980355j;
Macgillivray R.T.A., Moore S.A., Chen J., Anderson B.F., Baker H.,
Luo Y., Bewley M.C., Smith C.A., Murphy M.E.P., Wang Y., Mason A.B.,
Woodworth R.C., Brayer G.D., Baker E.N.;
"Two high-resolution crystal structures of the recombinant N-lobe of
human transferrin reveal a structural change implicated in iron
release.";
Biochemistry 37:7919-7928(1998).
[36]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 22-350.
PubMed=9760232; DOI=10.1021/bi9812064;
Jeffrey P.D., Bewley M.C., Macgillivray R.T.A., Mason A.B.,
Woodworth R.C., Baker E.N.;
"Ligand-induced conformational change in transferrins: crystal
structure of the open form of the N-terminal half-molecule of human
transferrin.";
Biochemistry 37:13978-13986(1998).
[37]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 23-352.
PubMed=10029548; DOI=10.1021/bi9824543;
Bewley M.C., Tam B.M., Grewal J., He S., Shewry S., Murphy M.E.P.,
Mason A.B., Woodworth R.C., Baker E.N., Macgillivray R.T.A.;
"X-ray crystallography and mass spectroscopy reveal that the N-lobe of
human transferrin expressed in Pichia pastoris is folded correctly but
is glycosylated on serine-32.";
Biochemistry 38:2535-2541(1999).
[38]
VARIANT SER-142.
PubMed=9358047; DOI=10.1016/S0378-1119(97)00356-9;
Evans P., Kemp J.;
"Exon/intron structure of the human transferrin receptor gene.";
Gene 199:123-131(1997).
[39]
VARIANT GLU-646.
PubMed=9803271; DOI=10.1046/j.1469-1809.1998.6230271.x;
Pang H., Koda Y., Soejima M., Kimura H.;
"Identification of a mutation (A1879G) of transferrin from cDNA
prepared from peripheral blood cells.";
Ann. Hum. Genet. 62:271-274(1998).
[40]
VARIANTS SER-277; SER-589 AND GLU-671, AND CHARACTERIZATION OF VARIANT
SER-277.
PubMed=11703331; DOI=10.1046/j.1365-2141.2001.03096.x;
Lee P.L., Halloran C., Trevino R., Felitti V., Beutler E.;
"Human transferrin G277S mutation: a risk factor for iron deficiency
anaemia.";
Br. J. Haematol. 115:329-333(2001).
[41]
VARIANTS SER-277 AND SER-589.
PubMed=11702220; DOI=10.1007/s004390100599;
Douabin-Gicquel V., Soriano N., Ferran H., Wojcik F., Palierne E.,
Tamim S., Jovelin T., McKie A.T., Le Gall J.-Y., David V., Mosser J.;
"Identification of 96 single nucleotide polymorphisms in eight genes
involved in iron metabolism: efficiency of bioinformatic extraction
compared with a systematic sequencing approach.";
Hum. Genet. 109:393-401(2001).
[42]
VARIANT ATRAF ASN-77.
PubMed=15466165; DOI=10.1182/blood-2004-05-1751;
Knisely A.S., Gelbart T., Beutler E.;
"Molecular characterization of a third case of human
atransferrinemia.";
Blood 104:2607-2607(2004).
[43]
VARIANT [LARGE SCALE ANALYSIS] VAL-448, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
-!- FUNCTION: Transferrins are iron binding transport proteins which
can bind two Fe(3+) ions in association with the binding of an
anion, usually bicarbonate. It is responsible for the transport of
iron from sites of absorption and heme degradation to those of
storage and utilization. Serum transferrin may also have a further
role in stimulating cell proliferation.
-!- SUBUNIT: Monomer.
-!- INTERACTION:
P01350:GAST; NbExp=5; IntAct=EBI-714319, EBI-3436637;
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
-!- POLYMORPHISM: Different polymorphic variants of transferrin are
known. The sequence shown is the predominant electrophoretic
variant (C1 or TF*C1).
-!- DISEASE: Atransferrinemia (ATRAF) [MIM:209300]: A rare autosomal
recessive disorder characterized by abnormal synthesis of
transferrin leading to iron overload and microcytic hypochromic
anemia. {ECO:0000269|PubMed:11110675,
ECO:0000269|PubMed:15466165}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the transferrin family.
{ECO:0000255|PROSITE-ProRule:PRU00741}.
-!- SEQUENCE CAUTION:
Sequence=AAF22007.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Wikipedia; Note=Transferrin entry;
URL="https://en.wikipedia.org/wiki/Transferrin";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/tf/";
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EMBL; M12530; AAA61140.1; -; mRNA.
EMBL; M17611; AAA61147.1; -; Genomic_DNA.
EMBL; M17610; AAA61147.1; JOINED; Genomic_DNA.
EMBL; M17614; AAA61148.1; -; Genomic_DNA.
EMBL; M17612; AAA61148.1; JOINED; Genomic_DNA.
EMBL; M17613; AAA61148.1; JOINED; Genomic_DNA.
EMBL; S95936; AAB22049.1; -; mRNA.
EMBL; AF288144; AAK77664.1; -; Genomic_DNA.
EMBL; AF294270; AAK77664.1; JOINED; Genomic_DNA.
EMBL; AF294271; AAK77664.1; JOINED; Genomic_DNA.
EMBL; AF288139; AAK77664.1; JOINED; Genomic_DNA.
EMBL; AF288140; AAK77664.1; JOINED; Genomic_DNA.
EMBL; AF288141; AAK77664.1; JOINED; Genomic_DNA.
EMBL; AF288142; AAK77664.1; JOINED; Genomic_DNA.
EMBL; AF288143; AAK77664.1; JOINED; Genomic_DNA.
EMBL; AY308797; AAP45055.1; -; Genomic_DNA.
EMBL; DQ525716; ABF47110.1; -; Genomic_DNA.
EMBL; AC080128; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AC083905; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; CH471052; EAW79167.1; -; Genomic_DNA.
EMBL; BC059367; AAH59367.1; -; mRNA.
EMBL; M21569; AAA61143.2; -; Genomic_DNA.
EMBL; M15673; AAA61143.2; JOINED; Genomic_DNA.
EMBL; M21570; AAA61145.1; -; Genomic_DNA.
EMBL; X04600; CAA28265.1; -; Genomic_DNA.
EMBL; AJ252279; CAB96907.1; -; mRNA.
EMBL; M11372; AAA61141.1; -; Genomic_DNA.
EMBL; M11361; AAA61141.1; JOINED; Genomic_DNA.
EMBL; M11362; AAA61141.1; JOINED; Genomic_DNA.
EMBL; M11363; AAA61141.1; JOINED; Genomic_DNA.
EMBL; M11364; AAA61141.1; JOINED; Genomic_DNA.
EMBL; M11365; AAA61141.1; JOINED; Genomic_DNA.
EMBL; M11366; AAA61141.1; JOINED; Genomic_DNA.
EMBL; M11367; AAA61141.1; JOINED; Genomic_DNA.
EMBL; M11368; AAA61141.1; JOINED; Genomic_DNA.
EMBL; M11369; AAA61141.1; JOINED; Genomic_DNA.
EMBL; M11370; AAA61141.1; JOINED; Genomic_DNA.
EMBL; M11371; AAA61141.1; JOINED; Genomic_DNA.
EMBL; AF118063; AAF22007.1; ALT_INIT; mRNA.
EMBL; M12525; AAA61142.1; -; mRNA.
EMBL; U88581; AAB97880.1; -; mRNA.
EMBL; AF058327; AAC63506.1; -; Genomic_DNA.
EMBL; M26641; AAA61233.1; -; mRNA.
CCDS; CCDS3080.1; -.
PIR; A20981; TFHUP.
RefSeq; NP_001054.1; NM_001063.3.
RefSeq; XP_016862578.1; XM_017007089.1.
RefSeq; XP_016862579.1; XM_017007090.1.
UniGene; Hs.518267; -.
PDB; 1A8E; X-ray; 1.60 A; A=22-350.
PDB; 1A8F; X-ray; 1.80 A; A=22-350.
PDB; 1B3E; X-ray; 2.50 A; A=23-352.
PDB; 1BP5; X-ray; 2.20 A; A/B/C/D=20-356.
PDB; 1BTJ; X-ray; 3.20 A; A/B=20-356.
PDB; 1D3K; X-ray; 1.80 A; A=22-350.
PDB; 1D4N; X-ray; 2.00 A; A=22-350.
PDB; 1DTG; X-ray; 2.40 A; A=20-353.
PDB; 1FQE; X-ray; 1.80 A; A=20-350.
PDB; 1FQF; X-ray; 2.10 A; A=20-350.
PDB; 1JQF; X-ray; 1.85 A; A=20-353.
PDB; 1N7W; X-ray; 2.20 A; A=22-350.
PDB; 1N7X; X-ray; 2.10 A; A=20-350.
PDB; 1N84; X-ray; 2.05 A; A=20-350.
PDB; 1OQG; X-ray; 1.90 A; A=20-354.
PDB; 1OQH; X-ray; 2.40 A; A=20-354.
PDB; 1RYO; X-ray; 1.20 A; A=20-346.
PDB; 1SUV; EM; 7.50 A; C/D=22-350.
PDB; 2HAU; X-ray; 2.70 A; A/B=23-698.
PDB; 2HAV; X-ray; 2.70 A; A/B=23-698.
PDB; 2O7U; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I=20-356.
PDB; 2O84; X-ray; 2.60 A; X=20-356.
PDB; 3FGS; X-ray; 1.80 A; A=20-356.
PDB; 3QYT; X-ray; 2.80 A; A=20-698.
PDB; 3S9L; X-ray; 3.22 A; C/D=20-698.
PDB; 3S9M; X-ray; 3.32 A; C/D=20-698.
PDB; 3S9N; X-ray; 3.25 A; C/D=20-698.
PDB; 3SKP; X-ray; 1.70 A; A=358-698.
PDB; 3V83; X-ray; 2.10 A; A/B/C/D/E/F=1-698.
PDB; 3V89; X-ray; 3.10 A; B=356-698.
PDB; 3V8X; X-ray; 2.60 A; B=1-698.
PDB; 3VE1; X-ray; 2.96 A; B/D=20-698.
PDB; 4H0W; X-ray; 2.40 A; A=20-698.
PDB; 4X1B; X-ray; 2.45 A; A=20-698.
PDB; 4X1D; X-ray; 2.80 A; A/B=20-698.
PDB; 5DYH; X-ray; 2.68 A; A/B=1-698.
PDBsum; 1A8E; -.
PDBsum; 1A8F; -.
PDBsum; 1B3E; -.
PDBsum; 1BP5; -.
PDBsum; 1BTJ; -.
PDBsum; 1D3K; -.
PDBsum; 1D4N; -.
PDBsum; 1DTG; -.
PDBsum; 1FQE; -.
PDBsum; 1FQF; -.
PDBsum; 1JQF; -.
PDBsum; 1N7W; -.
PDBsum; 1N7X; -.
PDBsum; 1N84; -.
PDBsum; 1OQG; -.
PDBsum; 1OQH; -.
PDBsum; 1RYO; -.
PDBsum; 1SUV; -.
PDBsum; 2HAU; -.
PDBsum; 2HAV; -.
PDBsum; 2O7U; -.
PDBsum; 2O84; -.
PDBsum; 3FGS; -.
PDBsum; 3QYT; -.
PDBsum; 3S9L; -.
PDBsum; 3S9M; -.
PDBsum; 3S9N; -.
PDBsum; 3SKP; -.
PDBsum; 3V83; -.
PDBsum; 3V89; -.
PDBsum; 3V8X; -.
PDBsum; 3VE1; -.
PDBsum; 4H0W; -.
PDBsum; 4X1B; -.
PDBsum; 4X1D; -.
PDBsum; 5DYH; -.
ProteinModelPortal; P02787; -.
SMR; P02787; -.
BioGrid; 112876; 41.
DIP; DIP-2738N; -.
IntAct; P02787; 34.
MINT; MINT-1400694; -.
STRING; 9606.ENSP00000385834; -.
ChEMBL; CHEMBL4865; -.
DrugBank; DB01370; Aluminium.
DrugBank; DB01294; Bismuth Subsalicylate.
DrugBank; DB05260; Gallium nitrate.
DrugBank; DB00893; Iron Dextran.
DrugBank; DB09146; Iron saccharate.
MEROPS; S60.975; -.
iPTMnet; P02787; -.
PhosphoSitePlus; P02787; -.
SwissPalm; P02787; -.
UniCarbKB; P02787; -.
BioMuta; TF; -.
DMDM; 313104271; -.
DOSAC-COBS-2DPAGE; P02787; -.
REPRODUCTION-2DPAGE; IPI00022463; -.
REPRODUCTION-2DPAGE; P02787; -.
SWISS-2DPAGE; P02787; -.
UCD-2DPAGE; P02787; -.
EPD; P02787; -.
MaxQB; P02787; -.
PaxDb; P02787; -.
PeptideAtlas; P02787; -.
PRIDE; P02787; -.
TopDownProteomics; P02787; -.
Ensembl; ENST00000402696; ENSP00000385834; ENSG00000091513.
GeneID; 7018; -.
KEGG; hsa:7018; -.
UCSC; uc003epv.2; human.
CTD; 7018; -.
DisGeNET; 7018; -.
GeneCards; TF; -.
HGNC; HGNC:11740; TF.
HPA; CAB009538; -.
HPA; HPA001527; -.
HPA; HPA005692; -.
MalaCards; TF; -.
MIM; 190000; gene.
MIM; 209300; phenotype.
neXtProt; NX_P02787; -.
OpenTargets; ENSG00000091513; -.
Orphanet; 1195; Congenital atransferrinemia.
PharmGKB; PA36457; -.
eggNOG; ENOG410IEAI; Eukaryota.
eggNOG; ENOG410XQ36; LUCA.
GeneTree; ENSGT00390000001619; -.
HOGENOM; HOG000252723; -.
HOVERGEN; HBG000055; -.
InParanoid; P02787; -.
KO; K14736; -.
OMA; DCIAKIM; -.
OrthoDB; EOG091G0242; -.
PhylomeDB; P02787; -.
TreeFam; TF324013; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
Reactome; R-HSA-917937; Iron uptake and transport.
Reactome; R-HSA-917977; Transferrin endocytosis and recycling.
ChiTaRS; TF; human.
EvolutionaryTrace; P02787; -.
GeneWiki; Transferrin; -.
GenomeRNAi; 7018; -.
PMAP-CutDB; P02787; -.
PRO; PR:P02787; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000091513; -.
CleanEx; HS_TF; -.
ExpressionAtlas; P02787; baseline and differential.
Genevisible; P02787; HS.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0045178; C:basal part of cell; IDA:UniProtKB.
GO; GO:0009925; C:basal plasma membrane; IDA:UniProtKB.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005905; C:clathrin-coated pit; IDA:UniProtKB.
GO; GO:0030665; C:clathrin-coated vesicle membrane; TAS:Reactome.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
GO; GO:0005769; C:early endosome; IDA:UniProtKB.
GO; GO:0030139; C:endocytic vesicle; IDA:MGI.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0010008; C:endosome membrane; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; IDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0031232; C:extrinsic component of external side of plasma membrane; IGI:BHF-UCL.
GO; GO:1990712; C:HFE-transferrin receptor complex; IDA:BHF-UCL.
GO; GO:0005770; C:late endosome; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0031982; C:vesicle; IDA:UniProtKB.
GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
GO; GO:0015091; F:ferric iron transmembrane transporter activity; IEA:InterPro.
GO; GO:0008198; F:ferrous iron binding; IDA:BHF-UCL.
GO; GO:1990459; F:transferrin receptor binding; IPI:BHF-UCL.
GO; GO:0006879; P:cellular iron ion homeostasis; TAS:Reactome.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0071281; P:cellular response to iron ion; IGI:BHF-UCL.
GO; GO:0098707; P:ferrous iron import across plasma membrane; IGI:BHF-UCL.
GO; GO:0055072; P:iron ion homeostasis; IC:BHF-UCL.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; IDA:BHF-UCL.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0031647; P:regulation of protein stability; TAS:BHF-UCL.
GO; GO:0001895; P:retina homeostasis; IEP:UniProtKB.
GO; GO:0033572; P:transferrin transport; TAS:Reactome.
InterPro; IPR030685; Serotransferrin_mammal.
InterPro; IPR016357; Transferrin.
InterPro; IPR001156; Transferrin-like_dom.
InterPro; IPR018195; Transferrin_Fe_BS.
Pfam; PF00405; Transferrin; 2.
PIRSF; PIRSF500682; Serotransferrin; 1.
PIRSF; PIRSF002549; Transferrin; 1.
PRINTS; PR00422; TRANSFERRIN.
SMART; SM00094; TR_FER; 2.
PROSITE; PS00205; TRANSFERRIN_LIKE_1; 1.
PROSITE; PS00206; TRANSFERRIN_LIKE_2; 2.
PROSITE; PS00207; TRANSFERRIN_LIKE_3; 2.
PROSITE; PS51408; TRANSFERRIN_LIKE_4; 2.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Disease mutation; Disulfide bond; Glycoprotein; Ion transport; Iron;
Iron transport; Metal-binding; Methylation; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Secreted; Signal; Transport.
SIGNAL 1 19 {ECO:0000269|PubMed:6833213}.
CHAIN 20 698 Serotransferrin.
/FTId=PRO_0000035715.
DOMAIN 25 347 Transferrin-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
DOMAIN 361 683 Transferrin-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
METAL 82 82 Iron 1.
METAL 114 114 Iron 1.
METAL 207 207 Iron 1.
METAL 268 268 Iron 1.
METAL 411 411 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
METAL 445 445 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
METAL 536 536 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
METAL 604 604 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
BINDING 139 139 Carbonate 1.
BINDING 143 143 Carbonate 1.
BINDING 145 145 Carbonate 1; via amide nitrogen.
BINDING 146 146 Carbonate 1; via amide nitrogen.
BINDING 471 471 Carbonate 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
BINDING 475 475 Carbonate 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
BINDING 477 477 Carbonate 2; via amide nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU00741}.
BINDING 478 478 Carbonate 2; via amide nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU00741}.
MOD_RES 42 42 Dimethylated arginine.
{ECO:0000250|UniProtKB:P12346}.
MOD_RES 389 389 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 685 685 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
CARBOHYD 51 51 O-linked (GalNAc...) serine.
/FTId=CAR_000073.
CARBOHYD 432 432 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:15084671,
ECO:0000269|PubMed:15536627,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19838169}.
/FTId=CAR_000074.
CARBOHYD 491 491 N-linked (GlcNAc...) asparagine;
atypical; partial.
{ECO:0000269|PubMed:15536627}.
CARBOHYD 630 630 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:15084671,
ECO:0000269|PubMed:15536627,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:16740002,
ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19838169}.
/FTId=CAR_000075.
DISULFID 28 67 {ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:6953407}.
DISULFID 38 58 {ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:6953407}.
DISULFID 137 213 {ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:6953407}.
DISULFID 156 350 {ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:6953407}.
DISULFID 177 193 {ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:6953407}.
DISULFID 180 196 {ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:6953407}.
DISULFID 190 198 {ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:6953407}.
DISULFID 246 260 {ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:6953407}.
DISULFID 358 615 {ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:6953407}.
DISULFID 364 396 {ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:6953407}.
DISULFID 374 387 {ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:6953407}.
DISULFID 421 693 {ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:6953407}.
DISULFID 437 656 {ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:6953407}.
DISULFID 469 542 {ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:6953407}.
DISULFID 493 684 {ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:6953407}.
DISULFID 503 517 {ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:6953407}.
DISULFID 514 525 {ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:6953407}.
DISULFID 582 596 {ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:6953407}.
DISULFID 634 639 {ECO:0000255|PROSITE-ProRule:PRU00741,
ECO:0000269|PubMed:6953407}.
VARIANT 42 42 R -> L (in dbSNP:rs41298293).
/FTId=VAR_034569.
VARIANT 55 55 S -> R (in dbSNP:rs8177318).
{ECO:0000269|Ref.5}.
/FTId=VAR_029280.
VARIANT 76 76 A -> V (in dbSNP:rs41298977).
/FTId=VAR_034570.
VARIANT 77 77 D -> N (in ATRAF; dbSNP:rs121918681).
{ECO:0000269|PubMed:15466165}.
/FTId=VAR_038810.
VARIANT 142 142 G -> S (in dbSNP:rs1799830).
{ECO:0000269|PubMed:9358047}.
/FTId=VAR_011997.
VARIANT 277 277 G -> S (in allele TF*C3; associated with
a reduction in total iron binding
capacity; risk factor for iron deficiency
anemia in menstruating white women;
dbSNP:rs1799899).
{ECO:0000269|PubMed:11702220,
ECO:0000269|PubMed:11703331,
ECO:0000269|Ref.5}.
/FTId=VAR_011998.
VARIANT 296 296 D -> G (in allele TF*D1;
dbSNP:rs8177238). {ECO:0000269|Ref.5}.
/FTId=VAR_007544.
VARIANT 319 319 H -> R (in allele TF*CHI;
dbSNP:rs41295774).
/FTId=VAR_007545.
VARIANT 377 377 W -> C (in dbSNP:rs1804498).
/FTId=VAR_011999.
VARIANT 448 448 I -> V (in dbSNP:rs2692696).
{ECO:0000244|PubMed:21269460,
ECO:0000269|PubMed:11110675,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:1809186,
ECO:0000269|PubMed:3858812,
ECO:0000269|PubMed:6322780,
ECO:0000269|PubMed:6585826,
ECO:0000269|PubMed:6833213,
ECO:0000269|Ref.15, ECO:0000269|Ref.16,
ECO:0000269|Ref.5, ECO:0000269|Ref.6,
ECO:0000269|Ref.8}.
/FTId=VAR_058199.
VARIANT 477 477 A -> P (in ATRAF; dbSNP:rs121918679).
{ECO:0000269|PubMed:11110675}.
/FTId=VAR_012997.
VARIANT 562 562 G -> V (in dbSNP:rs41296590).
/FTId=VAR_034571.
VARIANT 589 589 P -> S (in allele TF*C2;
dbSNP:rs1049296).
{ECO:0000269|PubMed:11702220,
ECO:0000269|PubMed:11703331,
ECO:0000269|PubMed:9272172,
ECO:0000269|Ref.5}.
/FTId=VAR_012000.
VARIANT 645 645 T -> P (in dbSNP:rs1130537).
/FTId=VAR_012001.
VARIANT 646 646 K -> E (in allele TF*BV;
dbSNP:rs121918678).
{ECO:0000269|PubMed:9803271}.
/FTId=VAR_012998.
VARIANT 671 671 G -> E (in allele TF*B2;
dbSNP:rs121918677).
{ECO:0000269|PubMed:11703331}.
/FTId=VAR_012999.
CONFLICT 216 216 D -> N (in Ref. 9; AAH59367).
{ECO:0000305}.
CONFLICT 264 264 Q -> E (in Ref. 12; AA sequence).
{ECO:0000305}.
CONFLICT 329 329 D -> N (in Ref. 12; AA sequence and 14;
AAA61141). {ECO:0000305}.
CONFLICT 351 351 P -> Q (in Ref. 9; AAH59367).
{ECO:0000305}.
CONFLICT 380 381 NS -> SD (in Ref. 12; AA sequence).
{ECO:0000305}.
CONFLICT 436 436 N -> D (in Ref. 12; AA sequence).
{ECO:0000305}.
CONFLICT 558 561 PQNT -> TQNP (in Ref. 12; AA sequence).
{ECO:0000305}.
CONFLICT 591 591 E -> Q (in Ref. 12; AA sequence).
{ECO:0000305}.
CONFLICT 672 672 E -> Q (in Ref. 12; AA sequence).
{ECO:0000305}.
CONFLICT 691 691 E -> G (in Ref. 18; AAA61142).
{ECO:0000305}.
STRAND 24 30 {ECO:0000244|PDB:1RYO}.
HELIX 31 48 {ECO:0000244|PDB:1RYO}.
STRAND 51 54 {ECO:0000244|PDB:3V8X}.
STRAND 55 63 {ECO:0000244|PDB:1RYO}.
HELIX 64 72 {ECO:0000244|PDB:1RYO}.
STRAND 78 81 {ECO:0000244|PDB:1RYO}.
HELIX 83 90 {ECO:0000244|PDB:1RYO}.
TURN 92 94 {ECO:0000244|PDB:1RYO}.
STRAND 97 105 {ECO:0000244|PDB:1RYO}.
STRAND 107 121 {ECO:0000244|PDB:1RYO}.
HELIX 128 130 {ECO:0000244|PDB:1RYO}.
STRAND 136 139 {ECO:0000244|PDB:1RYO}.
TURN 144 147 {ECO:0000244|PDB:1RYO}.
HELIX 148 154 {ECO:0000244|PDB:1RYO}.
HELIX 155 157 {ECO:0000244|PDB:1RYO}.
STRAND 158 160 {ECO:0000244|PDB:1A8F}.
HELIX 165 172 {ECO:0000244|PDB:1RYO}.
STRAND 173 177 {ECO:0000244|PDB:1RYO}.
TURN 183 185 {ECO:0000244|PDB:1RYO}.
HELIX 187 190 {ECO:0000244|PDB:1RYO}.
STRAND 191 193 {ECO:0000244|PDB:1A8E}.
HELIX 194 196 {ECO:0000244|PDB:2HAU}.
STRAND 198 202 {ECO:0000244|PDB:3QYT}.
HELIX 206 215 {ECO:0000244|PDB:1RYO}.
STRAND 220 225 {ECO:0000244|PDB:1RYO}.
HELIX 228 232 {ECO:0000244|PDB:1RYO}.
HELIX 236 239 {ECO:0000244|PDB:1RYO}.
STRAND 242 245 {ECO:0000244|PDB:1RYO}.
TURN 247 249 {ECO:0000244|PDB:1A8E}.
STRAND 251 253 {ECO:0000244|PDB:1RYO}.
HELIX 254 259 {ECO:0000244|PDB:1RYO}.
STRAND 262 266 {ECO:0000244|PDB:1RYO}.
STRAND 269 272 {ECO:0000244|PDB:1RYO}.
STRAND 274 276 {ECO:0000244|PDB:1RYO}.
HELIX 279 293 {ECO:0000244|PDB:1RYO}.
TURN 295 297 {ECO:0000244|PDB:1RYO}.
STRAND 298 300 {ECO:0000244|PDB:3V8X}.
STRAND 310 314 {ECO:0000244|PDB:1RYO}.
STRAND 318 323 {ECO:0000244|PDB:1RYO}.
HELIX 330 334 {ECO:0000244|PDB:1RYO}.
HELIX 336 345 {ECO:0000244|PDB:1RYO}.
TURN 346 348 {ECO:0000244|PDB:1B3E}.
HELIX 354 357 {ECO:0000244|PDB:3V83}.
STRAND 360 365 {ECO:0000244|PDB:3SKP}.
HELIX 368 380 {ECO:0000244|PDB:3SKP}.
TURN 381 383 {ECO:0000244|PDB:3SKP}.
STRAND 384 389 {ECO:0000244|PDB:3SKP}.
HELIX 393 401 {ECO:0000244|PDB:3SKP}.
STRAND 407 410 {ECO:0000244|PDB:3SKP}.
HELIX 412 420 {ECO:0000244|PDB:3SKP}.
STRAND 424 430 {ECO:0000244|PDB:3SKP}.
HELIX 437 439 {ECO:0000244|PDB:3SKP}.
STRAND 445 452 {ECO:0000244|PDB:3SKP}.
STRAND 455 457 {ECO:0000244|PDB:2HAV}.
HELIX 460 462 {ECO:0000244|PDB:3SKP}.
STRAND 466 471 {ECO:0000244|PDB:3SKP}.
TURN 476 479 {ECO:0000244|PDB:3SKP}.
HELIX 480 485 {ECO:0000244|PDB:3SKP}.
HELIX 487 489 {ECO:0000244|PDB:3SKP}.
HELIX 495 497 {ECO:0000244|PDB:3SKP}.
STRAND 498 503 {ECO:0000244|PDB:3SKP}.
STRAND 509 511 {ECO:0000244|PDB:5DYH}.
HELIX 512 514 {ECO:0000244|PDB:3SKP}.
HELIX 521 523 {ECO:0000244|PDB:3SKP}.
STRAND 531 533 {ECO:0000244|PDB:2HAU}.
HELIX 535 545 {ECO:0000244|PDB:3SKP}.
STRAND 548 553 {ECO:0000244|PDB:3SKP}.
HELIX 556 559 {ECO:0000244|PDB:3SKP}.
TURN 568 572 {ECO:0000244|PDB:3SKP}.
HELIX 575 577 {ECO:0000244|PDB:3SKP}.
STRAND 578 581 {ECO:0000244|PDB:3SKP}.
STRAND 583 585 {ECO:0000244|PDB:4X1D}.
STRAND 587 589 {ECO:0000244|PDB:3SKP}.
HELIX 590 595 {ECO:0000244|PDB:3SKP}.
STRAND 598 601 {ECO:0000244|PDB:3SKP}.
STRAND 605 608 {ECO:0000244|PDB:3SKP}.
HELIX 610 612 {ECO:0000244|PDB:3SKP}.
HELIX 613 627 {ECO:0000244|PDB:3SKP}.
STRAND 628 630 {ECO:0000244|PDB:4H0W}.
STRAND 635 637 {ECO:0000244|PDB:3SKP}.
STRAND 644 646 {ECO:0000244|PDB:3SKP}.
STRAND 648 650 {ECO:0000244|PDB:3SKP}.
STRAND 656 659 {ECO:0000244|PDB:3SKP}.
HELIX 661 663 {ECO:0000244|PDB:3VE1}.
HELIX 666 669 {ECO:0000244|PDB:3SKP}.
HELIX 672 684 {ECO:0000244|PDB:3SKP}.
HELIX 688 694 {ECO:0000244|PDB:3SKP}.
SEQUENCE 698 AA; 77064 MW; 9A73B90D8C5671E9 CRC64;
MRLAVGALLV CAVLGLCLAV PDKTVRWCAV SEHEATKCQS FRDHMKSVIP SDGPSVACVK
KASYLDCIRA IAANEADAVT LDAGLVYDAY LAPNNLKPVV AEFYGSKEDP QTFYYAVAVV
KKDSGFQMNQ LRGKKSCHTG LGRSAGWNIP IGLLYCDLPE PRKPLEKAVA NFFSGSCAPC
ADGTDFPQLC QLCPGCGCST LNQYFGYSGA FKCLKDGAGD VAFVKHSTIF ENLANKADRD
QYELLCLDNT RKPVDEYKDC HLAQVPSHTV VARSMGGKED LIWELLNQAQ EHFGKDKSKE
FQLFSSPHGK DLLFKDSAHG FLKVPPRMDA KMYLGYEYVT AIRNLREGTC PEAPTDECKP
VKWCALSHHE RLKCDEWSVN SVGKIECVSA ETTEDCIAKI MNGEADAMSL DGGFVYIAGK
CGLVPVLAEN YNKSDNCEDT PEAGYFAIAV VKKSASDLTW DNLKGKKSCH TAVGRTAGWN
IPMGLLYNKI NHCRFDEFFS EGCAPGSKKD SSLCKLCMGS GLNLCEPNNK EGYYGYTGAF
RCLVEKGDVA FVKHQTVPQN TGGKNPDPWA KNLNEKDYEL LCLDGTRKPV EEYANCHLAR
APNHAVVTRK DKEACVHKIL RQQQHLFGSN VTDCSGNFCL FRSETKDLLF RDDTVCLAKL
HDRNTYEKYL GEEYVKAVGN LRKCSTSSLL EACTFRRP


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