TRFE_HUMAN
ID TRFE_HUMAN Reviewed; 698 AA.
AC P02787; O43890; Q1HBA5; Q9NQB8; Q9UHV0;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 252.
DE RecName: Full=Serotransferrin;
DE Short=Transferrin;
DE AltName: Full=Beta-1 metal-binding globulin;
DE AltName: Full=Siderophilin;
DE Flags: Precursor;
GN Name=TF; ORFNames=PRO1400;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS TF*B2; TF*CHI; TF*D1 AND VAL-448.
RX PubMed=6585826; DOI=10.1073/pnas.81.9.2752;
RA Yang F., Lum J.B., McGill J.R., Moore C.M., Naylor S.L., van Bragt P.H.,
RA Baldwin W.D., Bowman B.H.;
RT "Human transferrin: cDNA characterization and chromosomal localization.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:2752-2756(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3678832; DOI=10.1016/0378-1119(87)90163-6;
RA Schaeffer E., Lucero M.A., Jeltsch J.-M., Py M.-C., Levin M.J., Chambon P.,
RA Cohen G.N., Zakin M.M.;
RT "Complete structure of the human transferrin gene. Comparison with
RT analogous chicken gene and human pseudogene.";
RL Gene 56:109-116(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-448.
RC TISSUE=Liver;
RX PubMed=1809186; DOI=10.1111/j.1749-6632.1991.tb18573.x;
RA Hershberger C.L., Larson J.L., Arnold B., Rosteck P.R. Jr., Williams P.,
RA Dehoff B., Dunn P., O'Neal K.L., Riemen M.W., Tice P.A.;
RT "A cloned gene for human transferrin.";
RL Ann. N. Y. Acad. Sci. 646:140-154(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-448 AND ATRAF PRO-477.
RX PubMed=11110675;
RA Beutler E., Gelbart T., Lee P.L., Trevino R., Fernandez M.A.,
RA Fairbanks V.F.;
RT "Molecular characterization of a case of atransferrinemia.";
RL Blood 96:4071-4074(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-55; SER-277; GLY-296;
RP VAL-448 AND SER-589.
RG SeattleSNPs variation discovery resource;
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-448.
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-448.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-448.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72 AND 291-300.
RX PubMed=3106157; DOI=10.1016/0378-1119(86)90277-5;
RA Adrian G.S., Korinek B.W., Bowman B.H., Yang F.;
RT "The human transferrin gene: 5' region contains conserved sequences which
RT match the control elements regulated by heavy metals, glucocorticoids and
RT acute phase reaction.";
RL Gene 49:167-175(1986).
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14.
RX PubMed=3786138; DOI=10.1093/nar/14.21.8692;
RA Lucero M.A., Schaeffer E., Cohen G.N., Zakin M.M.;
RT "The 5' region of the human transferrin gene: structure and potential
RT regulatory sites.";
RL Nucleic Acids Res. 14:8692-8692(1986).
RN [12]
RP PROTEIN SEQUENCE OF 20-698, AND VARIANT VAL-448.
RX PubMed=6833213; DOI=10.1016/s0021-9258(18)32696-6;
RA McGillivray R.T.A., Mendez E., Shewale J.G., Sinha S.K., Lineback-Zins J.,
RA Brew K.;
RT "The primary structure of human serum transferrin. The structures of seven
RT cyanogen bromide fragments and the assembly of the complete structure.";
RL J. Biol. Chem. 258:3543-3553(1983).
RN [13]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 45-72.
RX PubMed=10931525;
RX DOI=10.1002/1097-4547(20000815)61:4<388::aid-jnr5>3.0.co;2-q;
RA de Arriba Zerpa G.A., Saleh M.-C., Fernandez P.M., Guillou F.,
RA Espinosa de los Monteros A., de Vellis J., Zakin M.M., Baron B.;
RT "Alternative splicing prevents transferrin secretion during differentiation
RT of a human oligodendrocyte cell line.";
RL J. Neurosci. Res. 61:388-395(2000).
RN [14]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 73-698, AND VARIANT VAL-448.
RX PubMed=3858812; DOI=10.1073/pnas.82.10.3149;
RA Park I., Schaeffer E., Sidoli A., Baralle F.E., Cohen G.N., Zakin M.M.;
RT "Organization of the human transferrin gene: direct evidence that it
RT originated by gene duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:3149-3153(1985).
RN [15]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 99-698, AND VARIANT VAL-448.
RC TISSUE=Fetal liver;
RA Zhang C., Yu Y., Zhang S., Wei H., Zhou G., Bi J., Zhang Y., Liu M., He F.;
RT "Functional prediction of the coding sequences of 33 new genes deduced by
RT analysis of cDNA clones from human fetal liver.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [16]
RP PROTEIN SEQUENCE OF 108-121; 259-273; 332-343; 374-384; 434-452; 454-464;
RP 495-508; 531-541; 577-600 AND 684-696, IDENTIFICATION BY MASS SPECTROMETRY,
RP AND VARIANT VAL-448.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [17]
RP PROTEIN SEQUENCE OF 263-266; 454-458; 531-538 AND 589-595.
RC TISSUE=Heart;
RX PubMed=7498159; DOI=10.1002/elps.11501601192;
RA Kovalyov L.I., Shishkin S.S., Efimochkin A.S., Kovalyova M.A.,
RA Ershova E.S., Egorov T.A., Musalyamov A.K.;
RT "The major protein expression profile and two-dimensional protein database
RT of human heart.";
RL Electrophoresis 16:1160-1169(1995).
RN [18]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 422-698, AND VARIANT VAL-448.
RX PubMed=6322780; DOI=10.1016/0006-291x(84)91648-6;
RA Uzan G., Frain M., Park I., Besmond C., Maessen G., Trepat J.S.,
RA Zakin M.M., Kahn A.;
RT "Molecular cloning and sequence analysis of cDNA for human transferrin.";
RL Biochem. Biophys. Res. Commun. 119:273-281(1984).
RN [19]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 564-624, AND VARIANTS TF*C2 AND SER-589.
RC TISSUE=Brain;
RX PubMed=9272172; DOI=10.1007/s004390050533;
RA Namekata K., Oyama F., Imagawa M., Ihara Y.;
RT "Human transferrin (Tf): a single mutation at codon 570 determines Tf C1 or
RT Tf C2 variant.";
RL Hum. Genet. 100:457-458(1997).
RN [20]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 564-624.
RA Tsuchida S., Ikemoto S., Kajii E.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [21]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 636-696.
RX PubMed=2780570; DOI=10.1073/pnas.86.18.7260;
RA Duguid J.R., Bohmont C.W., Liu N.G., Tourtellotte W.W.;
RT "Changes in brain gene expression shared by scrapie and Alzheimer
RT disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:7260-7264(1989).
RN [22]
RP DISULFIDE BONDS.
RX PubMed=6953407; DOI=10.1073/pnas.79.8.2504;
RA McGillivray R.T.A., Mendez E., Sinha S.K., Sutton M.R., Lineback-Zins J.,
RA Brew K.;
RT "The complete amino acid sequence of human serum transferrin.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:2504-2508(1982).
RN [23]
RP MUTAGENESIS.
RX PubMed=1932003; DOI=10.1021/bi00109a002;
RA Woodworth R.C., Mason A.B., Funk W.D., McGillivray R.T.A.;
RT "Expression and initial characterization of five site-directed mutants of
RT the N-terminal half-molecule of human transferrin.";
RL Biochemistry 30:10824-10829(1991).
RN [24]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-432 AND ASN-630.
RC TISSUE=Bile;
RX PubMed=15084671; DOI=10.1074/mcp.m400015-mcp200;
RA Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., Thuluvath P.J.,
RA Argani P., Goggins M.G., Maitra A., Pandey A.;
RT "A proteomic analysis of human bile.";
RL Mol. Cell. Proteomics 3:715-728(2004).
RN [25]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-432 AND ASN-630.
RC TISSUE=Plasma;
RX PubMed=14760718; DOI=10.1002/pmic.200300556;
RA Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
RT "Screening for N-glycosylated proteins by liquid chromatography mass
RT spectrometry.";
RL Proteomics 4:454-465(2004).
RN [26]
RP GLYCOSYLATION AT ASN-432; ASN-491 AND ASN-630.
RX PubMed=15536627; DOI=10.1002/rcm.1718;
RA Satomi Y., Shimonishi Y., Hase T., Takao T.;
RT "Site-specific carbohydrate profiling of human transferrin by nano-flow
RT liquid chromatography/electrospray ionization mass spectrometry.";
RL Rapid Commun. Mass Spectrom. 18:2983-2988(2004).
RN [27]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-432 AND ASN-630.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [28]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-630.
RC TISSUE=Saliva;
RX PubMed=16740002; DOI=10.1021/pr050492k;
RA Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.;
RT "Identification of N-linked glycoproteins in human saliva by glycoprotein
RT capture and mass spectrometry.";
RL J. Proteome Res. 5:1493-1503(2006).
RN [29]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-432 AND ASN-630.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [30]
RP GLYCOSYLATION AT ASN-630.
RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [31]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-432 AND ASN-630, AND STRUCTURE
RP OF CARBOHYDRATES.
RC TISSUE=Cerebrospinal fluid;
RX PubMed=19838169; DOI=10.1038/nmeth.1392;
RA Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G.,
RA Larson G.;
RT "Enrichment of glycopeptides for glycan structure and attachment site
RT identification.";
RL Nat. Methods 6:809-811(2009).
RN [32]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22905912; DOI=10.1021/pr300539b;
RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P.,
RA Mariman E.C., Renes J.;
RT "Resveratrol-induced changes of the human adipocyte secretion profile.";
RL J. Proteome Res. 11:4733-4743(2012).
RN [33]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [34]
RP PHOSPHORYLATION AT SER-389 AND SER-685.
RX PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT "A single kinase generates the majority of the secreted phosphoproteome.";
RL Cell 161:1619-1632(2015).
RN [35]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 22-350.
RX PubMed=9609685; DOI=10.1021/bi980355j;
RA Macgillivray R.T.A., Moore S.A., Chen J., Anderson B.F., Baker H., Luo Y.,
RA Bewley M.C., Smith C.A., Murphy M.E.P., Wang Y., Mason A.B.,
RA Woodworth R.C., Brayer G.D., Baker E.N.;
RT "Two high-resolution crystal structures of the recombinant N-lobe of human
RT transferrin reveal a structural change implicated in iron release.";
RL Biochemistry 37:7919-7928(1998).
RN [36]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 22-350.
RX PubMed=9760232; DOI=10.1021/bi9812064;
RA Jeffrey P.D., Bewley M.C., Macgillivray R.T.A., Mason A.B., Woodworth R.C.,
RA Baker E.N.;
RT "Ligand-induced conformational change in transferrins: crystal structure of
RT the open form of the N-terminal half-molecule of human transferrin.";
RL Biochemistry 37:13978-13986(1998).
RN [37]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 23-352.
RX PubMed=10029548; DOI=10.1021/bi9824543;
RA Bewley M.C., Tam B.M., Grewal J., He S., Shewry S., Murphy M.E.P.,
RA Mason A.B., Woodworth R.C., Baker E.N., Macgillivray R.T.A.;
RT "X-ray crystallography and mass spectroscopy reveal that the N-lobe of
RT human transferrin expressed in Pichia pastoris is folded correctly but is
RT glycosylated on serine-32.";
RL Biochemistry 38:2535-2541(1999).
RN [38] {ECO:0007744|PDB:3VE1}
RP X-RAY CRYSTALLOGRAPHY (2.96 ANGSTROMS) OF 20-698 IN COMPLEX WITH IRON AND
RP N.MENINGITIDIS TBPB, FUNCTION (MICROBIAL INFECTION), AND SUBUNIT (MICROBIAL
RP INFECTION).
RX PubMed=22343719; DOI=10.1038/nsmb.2251;
RA Calmettes C., Alcantara J., Yu R.H., Schryvers A.B., Moraes T.F.;
RT "The structural basis of transferrin sequestration by transferrin-binding
RT protein B.";
RL Nat. Struct. Mol. Biol. 19:358-360(2012).
RN [39] {ECO:0007744|PDB:3SKP, ECO:0007744|PDB:3V83, ECO:0007744|PDB:3V89, ECO:0007744|PDB:3V8X}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 358-698 IN COMPLEX WITH IRON AND
RP WITH N.MENINGITIDIS TBPA, FUNCTION (MICROBIAL INFECTION), SUBUNIT
RP (MICROBIAL INFECTION), AND GLYCOSYLATION AT ASN-432 AND ASN-630.
RX PubMed=22327295; DOI=10.1038/nature10823;
RA Noinaj N., Easley N.C., Oke M., Mizuno N., Gumbart J., Boura E.,
RA Steere A.N., Zak O., Aisen P., Tajkhorshid E., Evans R.W., Gorringe A.R.,
RA Mason A.B., Steven A.C., Buchanan S.K.;
RT "Structural basis for iron piracy by pathogenic Neisseria.";
RL Nature 483:53-58(2012).
RN [40]
RP VARIANT SER-142.
RX PubMed=9358047; DOI=10.1016/s0378-1119(97)00356-9;
RA Evans P., Kemp J.;
RT "Exon/intron structure of the human transferrin receptor gene.";
RL Gene 199:123-131(1997).
RN [41]
RP VARIANT GLU-646.
RX PubMed=9803271; DOI=10.1046/j.1469-1809.1998.6230271.x;
RA Pang H., Koda Y., Soejima M., Kimura H.;
RT "Identification of a mutation (A1879G) of transferrin from cDNA prepared
RT from peripheral blood cells.";
RL Ann. Hum. Genet. 62:271-274(1998).
RN [42]
RP VARIANTS SER-277; SER-589 AND GLU-671, AND CHARACTERIZATION OF VARIANT
RP SER-277.
RX PubMed=11703331; DOI=10.1046/j.1365-2141.2001.03096.x;
RA Lee P.L., Halloran C., Trevino R., Felitti V., Beutler E.;
RT "Human transferrin G277S mutation: a risk factor for iron deficiency
RT anaemia.";
RL Br. J. Haematol. 115:329-333(2001).
RN [43]
RP VARIANTS SER-277 AND SER-589.
RX PubMed=11702220; DOI=10.1007/s004390100599;
RA Douabin-Gicquel V., Soriano N., Ferran H., Wojcik F., Palierne E.,
RA Tamim S., Jovelin T., McKie A.T., Le Gall J.-Y., David V., Mosser J.;
RT "Identification of 96 single nucleotide polymorphisms in eight genes
RT involved in iron metabolism: efficiency of bioinformatic extraction
RT compared with a systematic sequencing approach.";
RL Hum. Genet. 109:393-401(2001).
RN [44]
RP VARIANT ATRAF ASN-77.
RX PubMed=15466165; DOI=10.1182/blood-2004-05-1751;
RA Knisely A.S., Gelbart T., Beutler E.;
RT "Molecular characterization of a third case of human atransferrinemia.";
RL Blood 104:2607-2607(2004).
RN [45]
RP VARIANT [LARGE SCALE ANALYSIS] VAL-448, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Transferrins are iron binding transport proteins which can
CC bind two Fe(3+) ions in association with the binding of an anion,
CC usually bicarbonate. It is responsible for the transport of iron from
CC sites of absorption and heme degradation to those of storage and
CC utilization. Serum transferrin may also have a further role in
CC stimulating cell proliferation.
CC -!- FUNCTION: (Microbial infection) Serves as an iron source for Neisseria
CC species, which capture the protein and extract its iron for their own
CC use. {ECO:0000269|PubMed:22327295, ECO:0000269|PubMed:22343719}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:22327295,
CC ECO:0000305|PubMed:22343719}.
CC -!- SUBUNIT: (Microbial infection) Binds to Neisseria transferrin-binding
CC protein A (tbpA or tbp1). Forms a large complex with TbpA and TbpB.
CC {ECO:0000269|PubMed:22327295}.
CC -!- SUBUNIT: (Microbial infection) Binds to Neisseria transferrin-binding
CC protein B (tbpb or tbp2). {ECO:0000269|PubMed:22327295,
CC ECO:0000269|PubMed:22343719}.
CC -!- INTERACTION:
CC P02787; O43315: AQP9; NbExp=3; IntAct=EBI-714319, EBI-17444777;
CC P02787; O00501: CLDN5; NbExp=3; IntAct=EBI-714319, EBI-18400628;
CC P02787; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-714319, EBI-18013275;
CC P02787; Q9GZR5: ELOVL4; NbExp=3; IntAct=EBI-714319, EBI-18535450;
CC P02787; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-714319, EBI-781551;
CC P02787; Q96KR6: FAM210B; NbExp=3; IntAct=EBI-714319, EBI-18938272;
CC P02787; P01350: GAST; NbExp=5; IntAct=EBI-714319, EBI-3436637;
CC P02787; P08034: GJB1; NbExp=3; IntAct=EBI-714319, EBI-17565645;
CC P02787; Q8NBJ4: GOLM1; NbExp=3; IntAct=EBI-714319, EBI-712073;
CC P02787; O15529: GPR42; NbExp=3; IntAct=EBI-714319, EBI-18076404;
CC P02787; Q8TED1: GPX8; NbExp=3; IntAct=EBI-714319, EBI-11721746;
CC P02787; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-714319, EBI-18053395;
CC P02787; A8MZ59: LEUTX; NbExp=3; IntAct=EBI-714319, EBI-17490413;
CC P02787; O15173: PGRMC2; NbExp=3; IntAct=EBI-714319, EBI-1050125;
CC P02787; Q96TC7: RMDN3; NbExp=3; IntAct=EBI-714319, EBI-1056589;
CC P02787; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-714319, EBI-18159983;
CC P02787; Q9BXS9-3: SLC26A6; NbExp=3; IntAct=EBI-714319, EBI-12814225;
CC P02787; Q99523: SORT1; NbExp=3; IntAct=EBI-714319, EBI-1057058;
CC P02787; O43278-2: SPINT1; NbExp=3; IntAct=EBI-714319, EBI-12078338;
CC P02787; Q8N9I0: SYT2; NbExp=3; IntAct=EBI-714319, EBI-8032987;
CC P02787; P02786: TFRC; NbExp=11; IntAct=EBI-714319, EBI-355727;
CC P02787; Q4KMG9: TMEM52B; NbExp=3; IntAct=EBI-714319, EBI-18178701;
CC P02787; Q9K0U9: tbp1; Xeno; NbExp=4; IntAct=EBI-714319, EBI-15968954;
CC P02787; Q09057: tbpB; Xeno; NbExp=3; IntAct=EBI-714319, EBI-15970048;
CC P02787; Q9K0V0: tbpB; Xeno; NbExp=2; IntAct=EBI-714319, EBI-15968994;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
CC -!- DOMAIN: Has a bilobed structure, each lobe binds a single Fe(3+) ion.
CC Does not always bind 2 Fe(3+) ions. {ECO:0000269|PubMed:22327295,
CC ECO:0000269|PubMed:22343719}.
CC -!- DOMAIN: (Microbial infection) Binds to Neisseria transferrin-binding
CC proteins A and B via its C-terminal lobe only. The L3 helix finger of
CC TbpA inserts into the C-terminal lobe of TF, altering its conformation
CC and probably disturbing the coordination of iron 2. Electron microscopy
CC suggests that in the TbpA-TbpB-TF complex, TF is captured directly
CC above the loop domain of TbpA in a chamber of about 1000 Angstroms(3)
CC formed by the 3 proteins, where interactions between the proteins serve
CC to abstract iron 2 from TF (PubMed:22343719, PubMed:22327295). Binding
CC to TbpB does not alter the conformation of the C-terminal lobe
CC (PubMed:22343719). {ECO:0000269|PubMed:22327295,
CC ECO:0000269|PubMed:22343719}.
CC -!- POLYMORPHISM: Different polymorphic variants of transferrin are known.
CC The sequence shown is the predominant electrophoretic variant (C1 or
CC TF*C1).
CC -!- DISEASE: Atransferrinemia (ATRAF) [MIM:209300]: A rare autosomal
CC recessive disorder characterized by abnormal synthesis of transferrin
CC leading to iron overload and microcytic hypochromic anemia.
CC {ECO:0000269|PubMed:11110675, ECO:0000269|PubMed:15466165}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the transferrin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00741}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF22007.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Transferrin entry;
CC URL="https://en.wikipedia.org/wiki/Transferrin";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/tf/";
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DR EMBL; M12530; AAA61140.1; -; mRNA.
DR EMBL; M17611; AAA61147.1; -; Genomic_DNA.
DR EMBL; M17610; AAA61147.1; JOINED; Genomic_DNA.
DR EMBL; M17614; AAA61148.1; -; Genomic_DNA.
DR EMBL; M17612; AAA61148.1; JOINED; Genomic_DNA.
DR EMBL; M17613; AAA61148.1; JOINED; Genomic_DNA.
DR EMBL; S95936; AAB22049.1; -; mRNA.
DR EMBL; AF288144; AAK77664.1; -; Genomic_DNA.
DR EMBL; AF294270; AAK77664.1; JOINED; Genomic_DNA.
DR EMBL; AF294271; AAK77664.1; JOINED; Genomic_DNA.
DR EMBL; AF288139; AAK77664.1; JOINED; Genomic_DNA.
DR EMBL; AF288140; AAK77664.1; JOINED; Genomic_DNA.
DR EMBL; AF288141; AAK77664.1; JOINED; Genomic_DNA.
DR EMBL; AF288142; AAK77664.1; JOINED; Genomic_DNA.
DR EMBL; AF288143; AAK77664.1; JOINED; Genomic_DNA.
DR EMBL; AY308797; AAP45055.1; -; Genomic_DNA.
DR EMBL; DQ525716; ABF47110.1; -; Genomic_DNA.
DR EMBL; AC080128; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC083905; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CH471052; EAW79167.1; -; Genomic_DNA.
DR EMBL; BC059367; AAH59367.1; -; mRNA.
DR EMBL; M21569; AAA61143.2; -; Genomic_DNA.
DR EMBL; M15673; AAA61143.2; JOINED; Genomic_DNA.
DR EMBL; M21570; AAA61145.1; -; Genomic_DNA.
DR EMBL; X04600; CAA28265.1; -; Genomic_DNA.
DR EMBL; AJ252279; CAB96907.1; -; mRNA.
DR EMBL; M11372; AAA61141.1; -; Genomic_DNA.
DR EMBL; M11361; AAA61141.1; JOINED; Genomic_DNA.
DR EMBL; M11362; AAA61141.1; JOINED; Genomic_DNA.
DR EMBL; M11363; AAA61141.1; JOINED; Genomic_DNA.
DR EMBL; M11364; AAA61141.1; JOINED; Genomic_DNA.
DR EMBL; M11365; AAA61141.1; JOINED; Genomic_DNA.
DR EMBL; M11366; AAA61141.1; JOINED; Genomic_DNA.
DR EMBL; M11367; AAA61141.1; JOINED; Genomic_DNA.
DR EMBL; M11368; AAA61141.1; JOINED; Genomic_DNA.
DR EMBL; M11369; AAA61141.1; JOINED; Genomic_DNA.
DR EMBL; M11370; AAA61141.1; JOINED; Genomic_DNA.
DR EMBL; M11371; AAA61141.1; JOINED; Genomic_DNA.
DR EMBL; AF118063; AAF22007.1; ALT_INIT; mRNA.
DR EMBL; M12525; AAA61142.1; -; mRNA.
DR EMBL; U88581; AAB97880.1; -; mRNA.
DR EMBL; AF058327; AAC63506.1; -; Genomic_DNA.
DR EMBL; M26641; AAA61233.1; -; mRNA.
DR CCDS; CCDS3080.1; -.
DR PIR; A20981; TFHUP.
DR RefSeq; NP_001054.1; NM_001063.3.
DR RefSeq; XP_016862578.1; XM_017007089.1.
DR RefSeq; XP_016862579.1; XM_017007090.1.
DR PDB; 1A8E; X-ray; 1.60 A; A=22-350.
DR PDB; 1A8F; X-ray; 1.80 A; A=22-350.
DR PDB; 1B3E; X-ray; 2.50 A; A=23-352.
DR PDB; 1BP5; X-ray; 2.20 A; A/B/C/D=20-356.
DR PDB; 1BTJ; X-ray; 3.20 A; A/B=20-356.
DR PDB; 1D3K; X-ray; 1.80 A; A=22-350.
DR PDB; 1D4N; X-ray; 2.00 A; A=22-350.
DR PDB; 1DTG; X-ray; 2.40 A; A=20-353.
DR PDB; 1FQE; X-ray; 1.80 A; A=20-350.
DR PDB; 1FQF; X-ray; 2.10 A; A=20-350.
DR PDB; 1JQF; X-ray; 1.85 A; A=20-353.
DR PDB; 1N7W; X-ray; 2.20 A; A=22-350.
DR PDB; 1N7X; X-ray; 2.10 A; A=20-350.
DR PDB; 1N84; X-ray; 2.05 A; A=20-350.
DR PDB; 1OQG; X-ray; 1.90 A; A=20-354.
DR PDB; 1OQH; X-ray; 2.40 A; A=20-354.
DR PDB; 1RYO; X-ray; 1.20 A; A=20-346.
DR PDB; 1SUV; EM; 7.50 A; C/D=22-350.
DR PDB; 2HAU; X-ray; 2.70 A; A/B=23-698.
DR PDB; 2HAV; X-ray; 2.70 A; A/B=23-698.
DR PDB; 2O7U; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I=20-356.
DR PDB; 2O84; X-ray; 2.60 A; X=20-356.
DR PDB; 3FGS; X-ray; 1.80 A; A=20-356.
DR PDB; 3QYT; X-ray; 2.80 A; A=20-698.
DR PDB; 3S9L; X-ray; 3.22 A; C/D=20-698.
DR PDB; 3S9M; X-ray; 3.32 A; C/D=20-698.
DR PDB; 3S9N; X-ray; 3.25 A; C/D=20-698.
DR PDB; 3SKP; X-ray; 1.70 A; A=358-698.
DR PDB; 3V83; X-ray; 2.10 A; A/B/C/D/E/F=1-698.
DR PDB; 3V89; X-ray; 3.10 A; B=356-698.
DR PDB; 3V8X; X-ray; 2.60 A; B=1-698.
DR PDB; 3VE1; X-ray; 2.96 A; B/D=20-698.
DR PDB; 4H0W; X-ray; 2.40 A; A=20-698.
DR PDB; 4X1B; X-ray; 2.45 A; A=20-698.
DR PDB; 4X1D; X-ray; 2.80 A; A/B=20-698.
DR PDB; 5DYH; X-ray; 2.68 A; A/B=1-698.
DR PDB; 5H52; X-ray; 3.00 A; A=20-698.
DR PDB; 5WTD; X-ray; 2.50 A; A=20-698.
DR PDB; 5X5P; X-ray; 2.70 A; A=20-698.
DR PDB; 5Y6K; X-ray; 2.86 A; A=20-698.
DR PDB; 6CTC; X-ray; 2.60 A; A=20-698.
DR PDB; 6D03; EM; 3.68 A; C/D=1-698.
DR PDB; 6D04; EM; 3.74 A; C/D=1-698.
DR PDB; 6D05; EM; 3.80 A; C/D=1-698.
DR PDB; 6JAS; X-ray; 2.50 A; A=20-698.
DR PDB; 6SOY; X-ray; 2.75 A; C=22-698.
DR PDB; 6SOZ; X-ray; 3.42 A; C=22-698.
DR PDB; 6UJ6; X-ray; 2.68 A; A=1-698.
DR PDB; 7Q1L; X-ray; 3.00 A; A/B=23-698.
DR PDBsum; 1A8E; -.
DR PDBsum; 1A8F; -.
DR PDBsum; 1B3E; -.
DR PDBsum; 1BP5; -.
DR PDBsum; 1BTJ; -.
DR PDBsum; 1D3K; -.
DR PDBsum; 1D4N; -.
DR PDBsum; 1DTG; -.
DR PDBsum; 1FQE; -.
DR PDBsum; 1FQF; -.
DR PDBsum; 1JQF; -.
DR PDBsum; 1N7W; -.
DR PDBsum; 1N7X; -.
DR PDBsum; 1N84; -.
DR PDBsum; 1OQG; -.
DR PDBsum; 1OQH; -.
DR PDBsum; 1RYO; -.
DR PDBsum; 1SUV; -.
DR PDBsum; 2HAU; -.
DR PDBsum; 2HAV; -.
DR PDBsum; 2O7U; -.
DR PDBsum; 2O84; -.
DR PDBsum; 3FGS; -.
DR PDBsum; 3QYT; -.
DR PDBsum; 3S9L; -.
DR PDBsum; 3S9M; -.
DR PDBsum; 3S9N; -.
DR PDBsum; 3SKP; -.
DR PDBsum; 3V83; -.
DR PDBsum; 3V89; -.
DR PDBsum; 3V8X; -.
DR PDBsum; 3VE1; -.
DR PDBsum; 4H0W; -.
DR PDBsum; 4X1B; -.
DR PDBsum; 4X1D; -.
DR PDBsum; 5DYH; -.
DR PDBsum; 5H52; -.
DR PDBsum; 5WTD; -.
DR PDBsum; 5X5P; -.
DR PDBsum; 5Y6K; -.
DR PDBsum; 6CTC; -.
DR PDBsum; 6D03; -.
DR PDBsum; 6D04; -.
DR PDBsum; 6D05; -.
DR PDBsum; 6JAS; -.
DR PDBsum; 6SOY; -.
DR PDBsum; 6SOZ; -.
DR PDBsum; 6UJ6; -.
DR PDBsum; 7Q1L; -.
DR AlphaFoldDB; P02787; -.
DR SASBDB; P02787; -.
DR SMR; P02787; -.
DR BioGRID; 112876; 197.
DR CORUM; P02787; -.
DR DIP; DIP-2738N; -.
DR IntAct; P02787; 84.
DR MINT; P02787; -.
DR STRING; 9606.ENSP00000385834; -.
DR ChEMBL; CHEMBL4865; -.
DR DrugBank; DB01370; Aluminium.
DR DrugBank; DB14517; Aluminium phosphate.
DR DrugBank; DB14518; Aluminum acetate.
DR DrugBank; DB01294; Bismuth subsalicylate.
DR DrugBank; DB14526; Chromic citrate.
DR DrugBank; DB14527; Chromic nitrate.
DR DrugBank; DB11136; Chromium.
DR DrugBank; DB14528; Chromium gluconate.
DR DrugBank; DB14529; Chromium nicotinate.
DR DrugBank; DB14530; Chromous sulfate.
DR DrugBank; DB00515; Cisplatin.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB11397; Dichlorvos.
DR DrugBank; DB13949; Ferric cation.
DR DrugBank; DB14490; Ferrous ascorbate.
DR DrugBank; DB14491; Ferrous fumarate.
DR DrugBank; DB14488; Ferrous gluconate.
DR DrugBank; DB14501; Ferrous glycine sulfate.
DR DrugBank; DB14489; Ferrous succinate.
DR DrugBank; DB13257; Ferrous sulfate anhydrous.
DR DrugBank; DB06215; Ferumoxytol.
DR DrugBank; DB06784; Gallium citrate Ga-67.
DR DrugBank; DB05260; Gallium nitrate.
DR DrugBank; DB01592; Iron.
DR DrugBank; DB00893; Iron Dextran.
DR DrugBank; DB00677; Isoflurophate.
DR DrugBank; DB06757; Manganese.
DR DrugBank; DB11182; Rose bengal.
DR DrugBank; DB14520; Tetraferric tricitrate decahydrate.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR MEROPS; S60.972; -.
DR MEROPS; S60.975; -.
DR CarbonylDB; P02787; -.
DR GlyConnect; 558; 125 N-Linked glycans (3 sites), 3 O-Linked glycans (1 site).
DR GlyGen; P02787; 8 sites, 145 N-linked glycans (6 sites), 6 O-linked glycans (2 sites).
DR iPTMnet; P02787; -.
DR PhosphoSitePlus; P02787; -.
DR SwissPalm; P02787; -.
DR BioMuta; TF; -.
DR DMDM; 313104271; -.
DR DOSAC-COBS-2DPAGE; P02787; -.
DR REPRODUCTION-2DPAGE; IPI00022463; -.
DR REPRODUCTION-2DPAGE; P02787; -.
DR SWISS-2DPAGE; P02787; -.
DR UCD-2DPAGE; P02787; -.
DR CPTAC; non-CPTAC-1157; -.
DR CPTAC; non-CPTAC-1159; -.
DR EPD; P02787; -.
DR jPOST; P02787; -.
DR MassIVE; P02787; -.
DR MaxQB; P02787; -.
DR PaxDb; P02787; -.
DR PeptideAtlas; P02787; -.
DR PRIDE; P02787; -.
DR ProteomicsDB; 51596; -.
DR TopDownProteomics; P02787; -.
DR ABCD; P02787; 1 sequenced antibody.
DR Antibodypedia; 873; 1706 antibodies from 43 providers.
DR DNASU; 7018; -.
DR Ensembl; ENST00000402696.9; ENSP00000385834.3; ENSG00000091513.16.
DR GeneID; 7018; -.
DR KEGG; hsa:7018; -.
DR MANE-Select; ENST00000402696.9; ENSP00000385834.3; NM_001063.4; NP_001054.2.
DR UCSC; uc003epv.2; human.
DR CTD; 7018; -.
DR DisGeNET; 7018; -.
DR GeneCards; TF; -.
DR HGNC; HGNC:11740; TF.
DR HPA; ENSG00000091513; Group enriched (liver, retina).
DR MalaCards; TF; -.
DR MIM; 190000; gene.
DR MIM; 209300; phenotype.
DR neXtProt; NX_P02787; -.
DR OpenTargets; ENSG00000091513; -.
DR Orphanet; 1195; Congenital atransferrinemia.
DR PharmGKB; PA36457; -.
DR VEuPathDB; HostDB:ENSG00000091513; -.
DR eggNOG; ENOG502QT0C; Eukaryota.
DR GeneTree; ENSGT00940000154388; -.
DR HOGENOM; CLU_011309_1_0_1; -.
DR InParanoid; P02787; -.
DR OMA; SGNFCLF; -.
DR OrthoDB; 232859at2759; -.
DR PhylomeDB; P02787; -.
DR TreeFam; TF324013; -.
DR PathwayCommons; P02787; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR Reactome; R-HSA-917937; Iron uptake and transport.
DR Reactome; R-HSA-917977; Transferrin endocytosis and recycling.
DR SignaLink; P02787; -.
DR SIGNOR; P02787; -.
DR BioGRID-ORCS; 7018; 17 hits in 1083 CRISPR screens.
DR ChiTaRS; TF; human.
DR EvolutionaryTrace; P02787; -.
DR GeneWiki; Transferrin; -.
DR GenomeRNAi; 7018; -.
DR Pharos; P02787; Tbio.
DR PRO; PR:P02787; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P02787; protein.
DR Bgee; ENSG00000091513; Expressed in inferior vagus X ganglion and 175 other tissues.
DR ExpressionAtlas; P02787; baseline and differential.
DR Genevisible; P02787; HS.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0045178; C:basal part of cell; IDA:UniProtKB.
DR GO; GO:0009925; C:basal plasma membrane; IDA:UniProtKB.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005905; C:clathrin-coated pit; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0030139; C:endocytic vesicle; IDA:MGI.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0031232; C:extrinsic component of external side of plasma membrane; IGI:BHF-UCL.
DR GO; GO:1990712; C:HFE-transferrin receptor complex; IDA:BHF-UCL.
DR GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:0031982; C:vesicle; IDA:UniProtKB.
DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR GO; GO:0008198; F:ferrous iron binding; IDA:BHF-UCL.
DR GO; GO:0034986; F:iron chaperone activity; IDA:BHF-UCL.
DR GO; GO:1990459; F:transferrin receptor binding; IPI:BHF-UCL.
DR GO; GO:0007015; P:actin filament organization; IEA:Ensembl.
DR GO; GO:0019731; P:antibacterial humoral response; IBA:GO_Central.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IEA:InterPro.
DR GO; GO:0071281; P:cellular response to iron ion; IGI:BHF-UCL.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0055072; P:iron ion homeostasis; IC:BHF-UCL.
DR GO; GO:0006826; P:iron ion transport; IBA:GO_Central.
DR GO; GO:0030316; P:osteoclast differentiation; IEA:Ensembl.
DR GO; GO:0045780; P:positive regulation of bone resorption; IEA:Ensembl.
DR GO; GO:2000147; P:positive regulation of cell motility; IEA:Ensembl.
DR GO; GO:0042327; P:positive regulation of phosphorylation; IEA:Ensembl.
DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; IDA:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0034756; P:regulation of iron ion transport; IGI:BHF-UCL.
DR GO; GO:0031647; P:regulation of protein stability; TAS:BHF-UCL.
DR GO; GO:0001895; P:retina homeostasis; HEP:UniProtKB.
DR GO; GO:0060395; P:SMAD protein signal transduction; IEA:Ensembl.
DR InterPro; IPR030685; Serotransferrin_mammal.
DR InterPro; IPR016357; Transferrin.
DR InterPro; IPR001156; Transferrin-like_dom.
DR InterPro; IPR018195; Transferrin_Fe_BS.
DR Pfam; PF00405; Transferrin; 2.
DR PIRSF; PIRSF500682; Serotransferrin; 1.
DR PIRSF; PIRSF002549; Transferrin; 1.
DR PRINTS; PR00422; TRANSFERRIN.
DR SMART; SM00094; TR_FER; 2.
DR PROSITE; PS00205; TRANSFERRIN_LIKE_1; 1.
DR PROSITE; PS00206; TRANSFERRIN_LIKE_2; 2.
DR PROSITE; PS00207; TRANSFERRIN_LIKE_3; 2.
DR PROSITE; PS51408; TRANSFERRIN_LIKE_4; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disease variant; Disulfide bond;
KW Glycoprotein; Ion transport; Iron; Iron transport; Metal-binding;
KW Methylation; Phosphoprotein; Reference proteome; Repeat; Secreted; Signal;
KW Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:6833213"
FT CHAIN 20..698
FT /note="Serotransferrin"
FT /id="PRO_0000035715"
FT DOMAIN 25..347
FT /note="Transferrin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DOMAIN 361..683
FT /note="Transferrin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 82
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:22327295,
FT ECO:0007744|PDB:3V83"
FT BINDING 114
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:22327295,
FT ECO:0007744|PDB:3V83"
FT BINDING 139
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT BINDING 143
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT BINDING 145
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT BINDING 146
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT BINDING 207
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:22327295,
FT ECO:0007744|PDB:3V83"
FT BINDING 268
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:22327295,
FT ECO:0007744|PDB:3V83"
FT BINDING 411
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:22327295, ECO:0000269|PubMed:22343719,
FT ECO:0007744|PDB:3V83, ECO:0007744|PDB:3VE1"
FT BINDING 445
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:22327295, ECO:0000269|PubMed:22343719,
FT ECO:0007744|PDB:3V83, ECO:0007744|PDB:3VE1"
FT BINDING 471
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 475
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 477
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 478
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 536
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:22327295, ECO:0000269|PubMed:22343719,
FT ECO:0007744|PDB:3V83, ECO:0007744|PDB:3VE1"
FT BINDING 604
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:22327295, ECO:0000269|PubMed:22343719,
FT ECO:0007744|PDB:3V83, ECO:0007744|PDB:3VE1"
FT MOD_RES 42
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000250|UniProtKB:P12346"
FT MOD_RES 389
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT MOD_RES 685
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT CARBOHYD 51
FT /note="O-linked (GalNAc...) serine"
FT /id="CAR_000073"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:14760718,
FT ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:15536627,
FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22327295"
FT /id="CAR_000074"
FT CARBOHYD 491
FT /note="N-linked (GlcNAc...) asparagine; atypical; partial"
FT /evidence="ECO:0000269|PubMed:15536627"
FT CARBOHYD 630
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:14760718,
FT ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:15536627,
FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002,
FT ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22327295"
FT /id="CAR_000075"
FT DISULFID 28..67
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:6953407"
FT DISULFID 38..58
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:6953407"
FT DISULFID 137..213
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:6953407"
FT DISULFID 156..350
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:6953407"
FT DISULFID 177..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:6953407"
FT DISULFID 180..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:6953407"
FT DISULFID 190..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:6953407"
FT DISULFID 246..260
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:6953407"
FT DISULFID 358..615
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:6953407"
FT DISULFID 364..396
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:6953407"
FT DISULFID 374..387
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:6953407"
FT DISULFID 421..693
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:6953407"
FT DISULFID 437..656
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:6953407"
FT DISULFID 469..542
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:6953407"
FT DISULFID 493..684
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:6953407"
FT DISULFID 503..517
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:6953407"
FT DISULFID 514..525
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:6953407"
FT DISULFID 582..596
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:6953407"
FT DISULFID 634..639
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:6953407"
FT VARIANT 42
FT /note="R -> L (in dbSNP:rs41298293)"
FT /id="VAR_034569"
FT VARIANT 55
FT /note="S -> R (in dbSNP:rs8177318)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_029280"
FT VARIANT 76
FT /note="A -> V (in dbSNP:rs41298977)"
FT /id="VAR_034570"
FT VARIANT 77
FT /note="D -> N (in ATRAF; dbSNP:rs121918681)"
FT /evidence="ECO:0000269|PubMed:15466165"
FT /id="VAR_038810"
FT VARIANT 142
FT /note="G -> S (in dbSNP:rs1799830)"
FT /evidence="ECO:0000269|PubMed:9358047"
FT /id="VAR_011997"
FT VARIANT 277
FT /note="G -> S (in allele TF*C3; associated with a reduction
FT in total iron binding capacity; risk factor for iron
FT deficiency anemia in menstruating white women;
FT dbSNP:rs1799899)"
FT /evidence="ECO:0000269|PubMed:11702220,
FT ECO:0000269|PubMed:11703331, ECO:0000269|Ref.5"
FT /id="VAR_011998"
FT VARIANT 296
FT /note="D -> G (in allele TF*D1; dbSNP:rs8177238)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_007544"
FT VARIANT 319
FT /note="H -> R (in allele TF*CHI; dbSNP:rs41295774)"
FT /id="VAR_007545"
FT VARIANT 377
FT /note="W -> C (in dbSNP:rs1804498)"
FT /id="VAR_011999"
FT VARIANT 448
FT /note="I -> V (in dbSNP:rs2692696)"
FT /evidence="ECO:0000269|PubMed:11110675,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:1809186,
FT ECO:0000269|PubMed:3858812, ECO:0000269|PubMed:6322780,
FT ECO:0000269|PubMed:6585826, ECO:0000269|PubMed:6833213,
FT ECO:0000269|Ref.15, ECO:0000269|Ref.16, ECO:0000269|Ref.5,
FT ECO:0000269|Ref.6, ECO:0000269|Ref.8,
FT ECO:0007744|PubMed:21269460"
FT /id="VAR_058199"
FT VARIANT 477
FT /note="A -> P (in ATRAF; dbSNP:rs121918679)"
FT /evidence="ECO:0000269|PubMed:11110675"
FT /id="VAR_012997"
FT VARIANT 562
FT /note="G -> V (in dbSNP:rs41296590)"
FT /id="VAR_034571"
FT VARIANT 589
FT /note="P -> S (in allele TF*C2; dbSNP:rs1049296)"
FT /evidence="ECO:0000269|PubMed:11702220,
FT ECO:0000269|PubMed:11703331, ECO:0000269|PubMed:9272172,
FT ECO:0000269|Ref.5"
FT /id="VAR_012000"
FT VARIANT 645
FT /note="T -> P (in dbSNP:rs1130537)"
FT /id="VAR_012001"
FT VARIANT 646
FT /note="K -> E (in allele TF*BV; dbSNP:rs121918678)"
FT /evidence="ECO:0000269|PubMed:9803271"
FT /id="VAR_012998"
FT VARIANT 671
FT /note="G -> E (in allele TF*B2; dbSNP:rs121918677)"
FT /evidence="ECO:0000269|PubMed:11703331"
FT /id="VAR_012999"
FT CONFLICT 216
FT /note="D -> N (in Ref. 9; AAH59367)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="Q -> E (in Ref. 12; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="D -> N (in Ref. 12; AA sequence and 14; AAA61141)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="P -> Q (in Ref. 9; AAH59367)"
FT /evidence="ECO:0000305"
FT CONFLICT 380..381
FT /note="NS -> SD (in Ref. 12; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 436
FT /note="N -> D (in Ref. 12; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 558..561
FT /note="PQNT -> TQNP (in Ref. 12; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 591
FT /note="E -> Q (in Ref. 12; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 672
FT /note="E -> Q (in Ref. 12; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 691
FT /note="E -> G (in Ref. 18; AAA61142)"
FT /evidence="ECO:0000305"
FT STRAND 24..30
FT /evidence="ECO:0007829|PDB:1RYO"
FT HELIX 31..48
FT /evidence="ECO:0007829|PDB:1RYO"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 55..63
FT /evidence="ECO:0007829|PDB:1RYO"
FT HELIX 64..72
FT /evidence="ECO:0007829|PDB:1RYO"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:1RYO"
FT HELIX 83..90
FT /evidence="ECO:0007829|PDB:1RYO"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:1RYO"
FT STRAND 97..105
FT /evidence="ECO:0007829|PDB:1RYO"
FT STRAND 107..121
FT /evidence="ECO:0007829|PDB:1RYO"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:1RYO"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:1RYO"
FT TURN 144..147
FT /evidence="ECO:0007829|PDB:1RYO"
FT HELIX 148..154
FT /evidence="ECO:0007829|PDB:1RYO"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:1RYO"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:1A8F"
FT HELIX 165..172
FT /evidence="ECO:0007829|PDB:1RYO"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:1RYO"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:1RYO"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:1RYO"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:1A8E"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:2HAU"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:3QYT"
FT HELIX 206..215
FT /evidence="ECO:0007829|PDB:1RYO"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:1RYO"
FT HELIX 228..232
FT /evidence="ECO:0007829|PDB:1RYO"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:1RYO"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:1RYO"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:1A8E"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:1RYO"
FT HELIX 254..259
FT /evidence="ECO:0007829|PDB:1RYO"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:1RYO"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:1RYO"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:1RYO"
FT HELIX 279..293
FT /evidence="ECO:0007829|PDB:1RYO"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:1RYO"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:3V8X"
FT STRAND 310..314
FT /evidence="ECO:0007829|PDB:1RYO"
FT STRAND 318..323
FT /evidence="ECO:0007829|PDB:1RYO"
FT HELIX 330..334
FT /evidence="ECO:0007829|PDB:1RYO"
FT HELIX 336..345
FT /evidence="ECO:0007829|PDB:1RYO"
FT TURN 346..348
FT /evidence="ECO:0007829|PDB:1B3E"
FT HELIX 354..357
FT /evidence="ECO:0007829|PDB:3V83"
FT STRAND 360..365
FT /evidence="ECO:0007829|PDB:3SKP"
FT HELIX 368..380
FT /evidence="ECO:0007829|PDB:3SKP"
FT TURN 381..383
FT /evidence="ECO:0007829|PDB:3SKP"
FT STRAND 384..389
FT /evidence="ECO:0007829|PDB:3SKP"
FT HELIX 393..401
FT /evidence="ECO:0007829|PDB:3SKP"
FT STRAND 407..410
FT /evidence="ECO:0007829|PDB:3SKP"
FT HELIX 412..420
FT /evidence="ECO:0007829|PDB:3SKP"
FT STRAND 424..430
FT /evidence="ECO:0007829|PDB:3SKP"
FT HELIX 437..439
FT /evidence="ECO:0007829|PDB:3SKP"
FT STRAND 445..452
FT /evidence="ECO:0007829|PDB:3SKP"
FT STRAND 455..457
FT /evidence="ECO:0007829|PDB:2HAV"
FT HELIX 460..462
FT /evidence="ECO:0007829|PDB:3SKP"
FT STRAND 466..471
FT /evidence="ECO:0007829|PDB:3SKP"
FT TURN 476..479
FT /evidence="ECO:0007829|PDB:3SKP"
FT HELIX 480..485
FT /evidence="ECO:0007829|PDB:3SKP"
FT HELIX 487..489
FT /evidence="ECO:0007829|PDB:3SKP"
FT STRAND 491..493
FT /evidence="ECO:0007829|PDB:6JAS"
FT HELIX 495..497
FT /evidence="ECO:0007829|PDB:3SKP"
FT STRAND 498..503
FT /evidence="ECO:0007829|PDB:3SKP"
FT STRAND 509..511
FT /evidence="ECO:0007829|PDB:5DYH"
FT HELIX 512..514
FT /evidence="ECO:0007829|PDB:3SKP"
FT HELIX 521..523
FT /evidence="ECO:0007829|PDB:3SKP"
FT STRAND 531..533
FT /evidence="ECO:0007829|PDB:2HAU"
FT HELIX 535..545
FT /evidence="ECO:0007829|PDB:3SKP"
FT STRAND 548..553
FT /evidence="ECO:0007829|PDB:3SKP"
FT HELIX 556..559
FT /evidence="ECO:0007829|PDB:3SKP"
FT TURN 561..564
FT /evidence="ECO:0007829|PDB:6SOY"
FT TURN 568..572
FT /evidence="ECO:0007829|PDB:3SKP"
FT HELIX 575..577
FT /evidence="ECO:0007829|PDB:3SKP"
FT STRAND 578..581
FT /evidence="ECO:0007829|PDB:3SKP"
FT STRAND 583..585
FT /evidence="ECO:0007829|PDB:4X1D"
FT STRAND 587..589
FT /evidence="ECO:0007829|PDB:3SKP"
FT HELIX 590..595
FT /evidence="ECO:0007829|PDB:3SKP"
FT STRAND 598..601
FT /evidence="ECO:0007829|PDB:3SKP"
FT STRAND 605..608
FT /evidence="ECO:0007829|PDB:3SKP"
FT HELIX 610..612
FT /evidence="ECO:0007829|PDB:3SKP"
FT HELIX 613..627
FT /evidence="ECO:0007829|PDB:3SKP"
FT STRAND 628..630
FT /evidence="ECO:0007829|PDB:4H0W"
FT STRAND 635..637
FT /evidence="ECO:0007829|PDB:3SKP"
FT STRAND 644..646
FT /evidence="ECO:0007829|PDB:3SKP"
FT STRAND 648..650
FT /evidence="ECO:0007829|PDB:3SKP"
FT STRAND 656..659
FT /evidence="ECO:0007829|PDB:3SKP"
FT HELIX 661..663
FT /evidence="ECO:0007829|PDB:3VE1"
FT HELIX 666..669
FT /evidence="ECO:0007829|PDB:3SKP"
FT HELIX 672..684
FT /evidence="ECO:0007829|PDB:3SKP"
FT HELIX 688..694
FT /evidence="ECO:0007829|PDB:3SKP"
SQ 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
