ID TRFE_HUMAN Reviewed; 698 AA. AC P02787; O43890; Q1HBA5; Q9NQB8; Q9UHV0; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 14-DEC-2022, sequence version 4. DT 27-MAR-2024, entry version 261. DE RecName: Full=Serotransferrin {ECO:0000305}; DE Short=Transferrin; DE AltName: Full=Beta-1 metal-binding globulin; DE AltName: Full=Siderophilin; DE Flags: Precursor; GN Name=TF {ECO:0000312|HGNC:HGNC:11740}; 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 AND TF*D1. 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]. 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 VARIANT 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 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]. 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]. 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]. 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. 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. 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. 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, AND IDENTIFICATION BY MASS RP SPECTROMETRY. 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. 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 VARIANT 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] {ECO:0007744|PDB:6SOY, ECO:0007744|PDB:6SOZ} RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 22-698 IN COMPLEX WITH IRON; RP ESAG6 AND ESAG7, FUNCTION, GLYCOSYLATION AT ASN-432, AND DISULFIDE BONDS. RX PubMed=31636418; DOI=10.1038/s41564-019-0589-0; RA Trevor C.E., Gonzalez-Munoz A.L., Macleod O.J.S., Woodcock P.G., Rust S., RA Vaughan T.J., Garman E.F., Minter R., Carrington M., Higgins M.K.; RT "Structure of the trypanosome transferrin receptor reveals mechanisms of RT ligand recognition and immune evasion."; RL Nat. Microbiol. 4:2074-2081(2019). RN [41] 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 [42] 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 [43] 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 [44] 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 [45] 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 [46] RP VARIANT [LARGE SCALE ANALYSIS] ILE-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 -!- FUNCTION: (Microbial infection) Serves as an iron source for parasite CC T.brucei (strain 427), which capture TF via its own transferrin CC receptor ESAG6:ESAG7 and extract its iron for its own use. CC {ECO:0000269|PubMed:31636418}. 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=7; 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 PRO_0000035715; P02786: TFRC; NbExp=4; IntAct=EBI-40201768, EBI-355727; 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/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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; 7FFM; X-ray; 3.06 A; A=20-698. DR PDB; 7FFU; X-ray; 2.60 A; A=20-698. DR PDB; 7Q1L; X-ray; 3.00 A; A/B=23-698. DR PDB; 8BRC; X-ray; 3.17 A; A=20-698. 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; 7FFM; -. DR PDBsum; 7FFU; -. DR PDBsum; 7Q1L; -. DR PDBsum; 8BRC; -. DR AlphaFoldDB; P02787; -. DR EMDB; EMD-7783; -. DR EMDB; EMD-7784; -. DR EMDB; EMD-7785; -. DR SASBDB; P02787; -. DR SMR; P02787; -. DR BioGRID; 112876; 207. DR CORUM; P02787; -. DR DIP; DIP-2738N; -. DR IntAct; P02787; 88. 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 GlyCosmos; P02787; 7 sites, 144 glycans. DR GlyGen; P02787; 8 sites, 152 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 CPTAC; non-CPTAC-1157; -. DR CPTAC; non-CPTAC-1159; -. DR EPD; P02787; -. DR jPOST; P02787; -. DR MassIVE; P02787; -. DR MaxQB; P02787; -. DR PaxDb; 9606-ENSP00000385834; -. DR PeptideAtlas; P02787; -. DR PRIDE; P02787; -. DR ProteomicsDB; 51596; -. DR TopDownProteomics; P02787; -. DR ABCD; P02787; 1 sequenced antibody. DR Antibodypedia; 873; 1996 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 AGR; HGNC:11740; -. DR CTD; 7018; -. DR DisGeNET; 7018; -. DR GeneCards; TF; -. DR HGNC; HGNC:11740; TF. DR HPA; ENSG00000091513; Tissue enhanced (brain, liver, retina). DR MalaCards; TF; -. DR MIM; 190000; gene. DR MIM; 209300; phenotype. DR neXtProt; NX_P02787; -. DR Orphanet; 1195; Congenital atransferrinemia. DR PharmGKB; PA36457; -. DR VEuPathDB; HostDB:ENSG00000091513; -. DR eggNOG; ENOG502QT0C; Eukaryota. DR HOGENOM; CLU_011309_1_0_1; -. DR InParanoid; P02787; -. DR OrthoDB; 2906687at2759; -. 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; 18 hits in 1166 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 177 other cell types or tissues. DR ExpressionAtlas; P02787; baseline and differential. 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: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:0071281; P:cellular response to iron ion; IGI:BHF-UCL. DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IEA:Ensembl. DR GO; GO:0006879; P:intracellular iron ion homeostasis; IGI: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:0045893; P:positive regulation of DNA-templated transcription; 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:0034756; P:regulation of iron ion transport; IGI:BHF-UCL. DR GO; GO:0031647; P:regulation of protein stability; TAS:BHF-UCL. DR CDD; cd13617; PBP2_transferrin_C; 1. DR CDD; cd13618; PBP2_transferrin_N; 1. DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 4. DR InterPro; IPR030685; Serotransferrin_mammal. DR InterPro; IPR016357; Transferrin. DR InterPro; IPR001156; Transferrin-like_dom. DR InterPro; IPR018195; Transferrin_Fe_BS. DR PANTHER; PTHR11485:SF31; SEROTRANSFERRIN; 1. DR PANTHER; PTHR11485; TRANSFERRIN; 1. 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 SUPFAM; SSF53850; Periplasmic binding protein-like II; 2. DR PROSITE; PS00205; TRANSFERRIN_LIKE_1; 2. DR PROSITE; PS00206; TRANSFERRIN_LIKE_2; 2. DR PROSITE; PS00207; TRANSFERRIN_LIKE_3; 2. DR PROSITE; PS51408; TRANSFERRIN_LIKE_4; 2. DR SWISS-2DPAGE; P02787; -. DR UCD-2DPAGE; P02787; -. DR Genevisible; P02787; HS. 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:0000269|PubMed:31636418, ECO:0007744|PDB:3V83, FT ECO:0007744|PDB:3VE1, ECO:0007744|PDB:6SOY, FT ECO:0007744|PDB:6SOZ" 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:0000269|PubMed:31636418, ECO:0007744|PDB:3V83, FT ECO:0007744|PDB:3VE1, ECO:0007744|PDB:6SOY, FT ECO:0007744|PDB:6SOZ" 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:0000269|PubMed:31636418, ECO:0007744|PDB:3V83, FT ECO:0007744|PDB:3VE1, ECO:0007744|PDB:6SOY, FT ECO:0007744|PDB:6SOZ" 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:0000269|PubMed:31636418, ECO:0007744|PDB:3V83, FT ECO:0007744|PDB:3VE1, ECO:0007744|PDB:6SOY, FT ECO:0007744|PDB:6SOZ" 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 ECO:0000269|PubMed:31636418, ECO:0007744|PDB:6SOY, FT ECO:0007744|PDB:6SOZ" 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:31636418, ECO:0000269|PubMed:6953407, FT ECO:0007744|PDB:6SOY, ECO:0007744|PDB:6SOZ" FT DISULFID 38..58 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741, FT ECO:0000269|PubMed:31636418, ECO:0000269|PubMed:6953407, FT ECO:0007744|PDB:6SOY, ECO:0007744|PDB:6SOZ" FT DISULFID 137..213 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741, FT ECO:0000269|PubMed:31636418, ECO:0000269|PubMed:6953407, FT ECO:0007744|PDB:6SOY, ECO:0007744|PDB:6SOZ" FT DISULFID 156..350 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741, FT ECO:0000269|PubMed:31636418, ECO:0000269|PubMed:6953407, FT ECO:0007744|PDB:6SOY, ECO:0007744|PDB:6SOZ" FT DISULFID 177..193 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741, FT ECO:0000269|PubMed:31636418, ECO:0000269|PubMed:6953407, FT ECO:0007744|PDB:6SOY, ECO:0007744|PDB:6SOZ" FT DISULFID 180..198 FT /evidence="ECO:0000269|PubMed:31636418, FT ECO:0007744|PDB:6SOY, ECO:0007744|PDB:6SOZ" FT DISULFID 190..196 FT /evidence="ECO:0000269|PubMed:31636418, FT ECO:0007744|PDB:6SOY, ECO:0007744|PDB:6SOZ" FT DISULFID 246..260 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741, FT ECO:0000269|PubMed:31636418, ECO:0000269|PubMed:6953407, FT ECO:0007744|PDB:6SOY, ECO:0007744|PDB:6SOZ" 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:31636418, ECO:0000269|PubMed:6953407, FT ECO:0007744|PDB:6SOY, ECO:0007744|PDB:6SOZ" FT DISULFID 374..387 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741, FT ECO:0000269|PubMed:31636418, ECO:0000269|PubMed:6953407, FT ECO:0007744|PDB:6SOY, ECO:0007744|PDB:6SOZ" FT DISULFID 421..693 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741, FT ECO:0000269|PubMed:31636418, ECO:0000269|PubMed:6953407, FT ECO:0007744|PDB:6SOY, ECO:0007744|PDB:6SOZ" FT DISULFID 437..656 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741, FT ECO:0000269|PubMed:31636418, ECO:0000269|PubMed:6953407, FT ECO:0007744|PDB:6SOY, ECO:0007744|PDB:6SOZ" FT DISULFID 469..542 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741, FT ECO:0000269|PubMed:31636418, ECO:0000269|PubMed:6953407, FT ECO:0007744|PDB:6SOY, ECO:0007744|PDB:6SOZ" FT DISULFID 493..684 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741, FT ECO:0000269|PubMed:31636418, ECO:0000269|PubMed:6953407, FT ECO:0007744|PDB:6SOY, ECO:0007744|PDB:6SOZ" FT DISULFID 503..517 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741, FT ECO:0000269|PubMed:31636418, ECO:0000269|PubMed:6953407, FT ECO:0007744|PDB:6SOY, ECO:0007744|PDB:6SOZ" FT DISULFID 514..525 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741, FT ECO:0000269|PubMed:31636418, ECO:0000269|PubMed:6953407, FT ECO:0007744|PDB:6SOY, ECO:0007744|PDB:6SOZ" FT DISULFID 582..596 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741, FT ECO:0000269|PubMed:31636418, ECO:0000269|PubMed:6953407, FT ECO:0007744|PDB:6SOY, ECO:0007744|PDB:6SOZ" 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="V -> I (in dbSNP:rs2692696)" FT /evidence="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; 77050 MW; 9A73BEAE8C567C79 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 PEAGYFAVAV 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 //