ID   TRFE_MOUSE              Reviewed;         697 AA.
AC   Q921I1; O35421; Q3UBW7; Q58E69; Q61803; Q62357; Q62358; Q62359; Q63915;
AC   Q64515; Q8VII5; Q922C0;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 196.
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; Synonyms=Trf;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/cJ; TISSUE=Liver;
RA   Lai D.-Z.;
RT   "Construction of a robust CHO cell-line for biopharmaceutical production.";
RL   Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Amnion, Bone marrow, Liver, and Mammary gland;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver, and Mammary tumor;
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
RC   STRAIN=BALB/cJ;
RX   PubMed=9621303;
RX   DOI=10.1002/(sici)1098-2795(199807)50:3<273::aid-mrd3>3.0.co;2-g;
RA   Chaudhary J., Skinner M.K.;
RT   "Comparative sequence analysis of the mouse and human transferrin
RT   promoters: hormonal regulation of the transferrin promoter in Sertoli
RT   cells.";
RL   Mol. Reprod. Dev. 50:273-283(1998).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 66-131; 277-337; 462-496 AND 526-575.
RX   PubMed=3693348; DOI=10.1016/s0021-9258(18)45366-5;
RA   Chen L.-H., Bissell M.J.;
RT   "Transferrin mRNA level in the mouse mammary gland is regulated by
RT   pregnancy and extracellular matrix.";
RL   J. Biol. Chem. 262:17247-17250(1987).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 268-307.
RC   TISSUE=Placenta;
RX   PubMed=8248032; DOI=10.1016/s0143-4004(05)80458-8;
RA   Kasik J.W., Rice E.J.;
RT   "Transferrin gene expression in maternal liver, fetal liver and placenta
RT   during pregnancy in the mouse.";
RL   Placenta 14:365-371(1993).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 282-412.
RX   PubMed=3611056; DOI=10.1016/s0021-9258(18)61088-9;
RA   Pentecost B.T., Teng C.T.;
RT   "Lactotransferrin is the major estrogen inducible protein of mouse uterine
RT   secretions.";
RL   J. Biol. Chem. 262:10134-10139(1987).
RN   [8]
RP   PROTEIN SEQUENCE OF 332-343 AND 659-667, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [9]
RP   TISSUE SPECIFICITY.
RX   PubMed=2601714; DOI=10.1128/mcb.9.11.5154-5162.1989;
RA   Idzerda R.L., Behringer R.R., Theisen M., Huggenvik J.I., McKnight G.S.,
RA   Brinster R.L.;
RT   "Expression from the transferrin gene promoter in transgenic mice.";
RL   Mol. Cell. Biol. 9:5154-5162(1989).
RN   [10]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-513.
RC   STRAIN=C57BL/6J; TISSUE=Plasma;
RX   PubMed=17330941; DOI=10.1021/pr0604559;
RA   Bernhard O.K., Kapp E.A., Simpson R.J.;
RT   "Enhanced analysis of the mouse plasma proteome using cysteine-containing
RT   tryptic glycopeptides.";
RL   J. Proteome Res. 6:987-995(2007).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
CC       {ECO:0000269|PubMed:2601714}.
CC   -!- SIMILARITY: Belongs to the transferrin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00741}.
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DR   EMBL; AF440692; AAL34533.1; -; mRNA.
DR   EMBL; AK085754; BAC39532.1; -; mRNA.
DR   EMBL; AK142599; BAE25124.1; -; mRNA.
DR   EMBL; AK146549; BAE27253.1; -; mRNA.
DR   EMBL; AK149559; BAE28960.1; -; mRNA.
DR   EMBL; AK149595; BAE28981.1; -; mRNA.
DR   EMBL; AK150782; BAE29847.1; -; mRNA.
DR   EMBL; AK168419; BAE40332.1; -; mRNA.
DR   EMBL; AK168938; BAE40747.1; -; mRNA.
DR   EMBL; BC008559; AAH08559.1; -; mRNA.
DR   EMBL; BC012313; AAH12313.1; -; mRNA.
DR   EMBL; BC022986; AAH22986.1; -; mRNA.
DR   EMBL; BC092046; AAH92046.1; -; mRNA.
DR   EMBL; AF027336; AAB84034.1; -; Genomic_DNA.
DR   EMBL; M23013; AAA40488.1; -; mRNA.
DR   EMBL; M23014; AAA40489.1; -; mRNA.
DR   EMBL; M23015; AAA40490.1; -; mRNA.
DR   EMBL; M23016; AAA40491.1; -; mRNA.
DR   EMBL; S67217; AAB28966.2; -; mRNA.
DR   EMBL; J03299; AAA39438.1; -; mRNA.
DR   CCDS; CCDS23451.1; -.
DR   PIR; A28446; A28446.
DR   RefSeq; NP_598738.1; NM_133977.2.
DR   AlphaFoldDB; Q921I1; -.
DR   SMR; Q921I1; -.
DR   BioGRID; 204313; 8.
DR   IntAct; Q921I1; 4.
DR   MINT; Q921I1; -.
DR   STRING; 10090.ENSMUSP00000035158; -.
DR   MEROPS; S60.977; -.
DR   MEROPS; S60.978; -.
DR   CarbonylDB; Q921I1; -.
DR   GlyConnect; 556; 20 N-Linked glycans (1 site).
DR   GlyCosmos; Q921I1; 1 site, 26 glycans.
DR   GlyGen; Q921I1; 3 sites, 26 N-linked glycans (2 sites), 1 O-linked glycan (2 sites).
DR   iPTMnet; Q921I1; -.
DR   PhosphoSitePlus; Q921I1; -.
DR   SwissPalm; Q921I1; -.
DR   REPRODUCTION-2DPAGE; IPI00139788; -.
DR   REPRODUCTION-2DPAGE; Q921I1; -.
DR   CPTAC; non-CPTAC-3439; -.
DR   CPTAC; non-CPTAC-5621; -.
DR   jPOST; Q921I1; -.
DR   MaxQB; Q921I1; -.
DR   PaxDb; 10090-ENSMUSP00000035158; -.
DR   PeptideAtlas; Q921I1; -.
DR   ProteomicsDB; 259087; -.
DR   Antibodypedia; 873; 1996 antibodies from 43 providers.
DR   DNASU; 22041; -.
DR   Ensembl; ENSMUST00000035158.16; ENSMUSP00000035158.10; ENSMUSG00000032554.16.
DR   Ensembl; ENSMUST00000112645.8; ENSMUSP00000108264.2; ENSMUSG00000032554.16.
DR   GeneID; 22041; -.
DR   KEGG; mmu:22041; -.
DR   UCSC; uc009rgj.1; mouse.
DR   AGR; MGI:98821; -.
DR   CTD; 22041; -.
DR   MGI; MGI:98821; Trf.
DR   VEuPathDB; HostDB:ENSMUSG00000032554; -.
DR   eggNOG; ENOG502QT0C; Eukaryota.
DR   GeneTree; ENSGT00940000154388; -.
DR   HOGENOM; CLU_011309_1_0_1; -.
DR   InParanoid; Q921I1; -.
DR   OMA; DEWSINS; -.
DR   OrthoDB; 2906687at2759; -.
DR   PhylomeDB; Q921I1; -.
DR   TreeFam; TF324013; -.
DR   Reactome; R-MMU-114608; Platelet degranulation.
DR   Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR   Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR   Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR   Reactome; R-MMU-917937; Iron uptake and transport.
DR   Reactome; R-MMU-917977; Transferrin endocytosis and recycling.
DR   BioGRID-ORCS; 22041; 2 hits in 58 CRISPR screens.
DR   ChiTaRS; Trf; mouse.
DR   PRO; PR:Q921I1; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q921I1; Protein.
DR   Bgee; ENSMUSG00000032554; Expressed in left lobe of liver and 228 other cell types or tissues.
DR   ExpressionAtlas; Q921I1; baseline and differential.
DR   GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR   GO; GO:0045178; C:basal part of cell; ISO:MGI.
DR   GO; GO:0009925; C:basal plasma membrane; ISO:MGI.
DR   GO; GO:0005604; C:basement membrane; ISO:MGI.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0051286; C:cell tip; ISO:MGI.
DR   GO; GO:0005905; C:clathrin-coated pit; IDA:MGI.
DR   GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR   GO; GO:0030425; C:dendrite; ISO:MGI.
DR   GO; GO:0097433; C:dense body; ISO:MGI.
DR   GO; GO:0005769; C:early endosome; IDA:MGI.
DR   GO; GO:0030139; C:endocytic vesicle; IDA:MGI.
DR   GO; GO:0005768; C:endosome; IDA:MGI.
DR   GO; GO:0005576; C:extracellular region; ISO:MGI.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:1990712; C:HFE-transferrin receptor complex; ISO:MGI.
DR   GO; GO:0005770; C:late endosome; ISO:MGI.
DR   GO; GO:0016020; C:membrane; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0055037; C:recycling endosome; IDA:MGI.
DR   GO; GO:0031982; C:vesicle; ISO:MGI.
DR   GO; GO:0030120; C:vesicle coat; ISO:MGI.
DR   GO; GO:0008199; F:ferric iron binding; ISO:MGI.
DR   GO; GO:0008198; F:ferrous iron binding; ISO:MGI.
DR   GO; GO:0034986; F:iron chaperone activity; ISO:MGI.
DR   GO; GO:1990459; F:transferrin receptor binding; ISO:MGI.
DR   GO; GO:0007015; P:actin filament organization; IDA:DFLAT.
DR   GO; GO:0019731; P:antibacterial humoral response; IBA:GO_Central.
DR   GO; GO:0071281; P:cellular response to iron ion; ISO:MGI.
DR   GO; GO:0070371; P:ERK1 and ERK2 cascade; IDA:DFLAT.
DR   GO; GO:0006879; P:intracellular iron ion homeostasis; ISO:MGI.
DR   GO; GO:0006826; P:iron ion transport; IMP:MGI.
DR   GO; GO:0030316; P:osteoclast differentiation; IDA:DFLAT.
DR   GO; GO:0045780; P:positive regulation of bone resorption; IDA:DFLAT.
DR   GO; GO:2000147; P:positive regulation of cell motility; IDA:DFLAT.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:DFLAT.
DR   GO; GO:0031643; P:positive regulation of myelination; ISO:MGI.
DR   GO; GO:0070447; P:positive regulation of oligodendrocyte progenitor proliferation; ISO:MGI.
DR   GO; GO:0042327; P:positive regulation of phosphorylation; IDA:DFLAT.
DR   GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; ISO:MGI.
DR   GO; GO:0034756; P:regulation of iron ion transport; ISO:MGI.
DR   GO; GO:0009617; P:response to bacterium; IEP:MGI.
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; 1.
DR   PROSITE; PS00206; TRANSFERRIN_LIKE_2; 2.
DR   PROSITE; PS00207; TRANSFERRIN_LIKE_3; 2.
DR   PROSITE; PS51408; TRANSFERRIN_LIKE_4; 2.
DR   Genevisible; Q921I1; MM.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Ion transport;
KW   Iron; Iron transport; Metal-binding; Methylation; Phosphoprotein;
KW   Reference proteome; Repeat; Secreted; Signal; Transport.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000250"
FT   CHAIN           20..697
FT                   /note="Serotransferrin"
FT                   /id="PRO_0000035716"
FT   DOMAIN          25..347
FT                   /note="Transferrin-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT   DOMAIN          360..682
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:0000255|PROSITE-ProRule:PRU00741"
FT   BINDING         114
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT   BINDING         139
FT                   /ligand="hydrogencarbonate"
FT                   /ligand_id="ChEBI:CHEBI:17544"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT   BINDING         143
FT                   /ligand="hydrogencarbonate"
FT                   /ligand_id="ChEBI:CHEBI:17544"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT   BINDING         145
FT                   /ligand="hydrogencarbonate"
FT                   /ligand_id="ChEBI:CHEBI:17544"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT   BINDING         146
FT                   /ligand="hydrogencarbonate"
FT                   /ligand_id="ChEBI:CHEBI:17544"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT   BINDING         207
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT   BINDING         268
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT   BINDING         410
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT   BINDING         448
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT   BINDING         474
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         480
FT                   /ligand="hydrogencarbonate"
FT                   /ligand_id="ChEBI:CHEBI:17544"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT   BINDING         481
FT                   /ligand="hydrogencarbonate"
FT                   /ligand_id="ChEBI:CHEBI:17544"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT   BINDING         537
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT   BINDING         605
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT   MOD_RES         42
FT                   /note="Dimethylated arginine"
FT                   /evidence="ECO:0000250|UniProtKB:P12346"
FT   MOD_RES         388
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02787"
FT   MOD_RES         684
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02787"
FT   CARBOHYD        513
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17330941"
FT   DISULFID        28..67
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT   DISULFID        38..58
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT   DISULFID        137..213
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT   DISULFID        156..350
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT   DISULFID        177..193
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT   DISULFID        180..196
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT   DISULFID        190..198
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT   DISULFID        246..260
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT   DISULFID        363..395
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT   DISULFID        373..386
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT   DISULFID        420..692
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT   DISULFID        435..655
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT   DISULFID        472..543
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT   DISULFID        496..683
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT   DISULFID        506..520
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT   DISULFID        517..526
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT   DISULFID        583..597
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT   DISULFID        633..638
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT   CONFLICT        3..4
FT                   /note="LT -> FA (in Ref. 1; AAL34533)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        69
FT                   /note="K -> R (in Ref. 5; AAA40488)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        71..74
FT                   /note="ISAS -> HASG (in Ref. 3; AAH08559)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        72
FT                   /note="S -> A (in Ref. 5; AAA40488)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        85
FT                   /note="W -> L (in Ref. 5; AAA40488)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        104
FT                   /note="Y -> C (in Ref. 5; AAA40488)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        113
FT                   /note="Y -> S (in Ref. 5; AAA40488)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        123..124
FT                   /note="GT -> ER (in Ref. 5; AAA40488)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        135
FT                   /note="K -> E (in Ref. 2; BAE29847)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        283
FT                   /note="W -> L (in Ref. 6; AAB28966)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        307
FT                   /note="P -> L (in Ref. 6; AAB28966)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        350..351
FT                   /note="CP -> SA (in Ref. 7; AAA39438)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        487
FT                   /note="G -> C (in Ref. 5; AAA40490)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        527
FT                   /note="A -> D (in Ref. 5; AAA40491)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        529
FT                   /note="N -> S (in Ref. 2; BAE29847)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        575
FT                   /note="K -> N (in Ref. 5; AAA40491)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        697
FT                   /note="H -> S (in Ref. 1; AAL34533)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   697 AA;  76724 MW;  0996A0C3B64CB1B9 CRC64;
     MRLTVGALLA CAALGLCLAV PDKTVKWCAV SEHENTKCIS FRDHMKTVLP PDGPRLACVK
     KTSYPDCIKA ISASEADAMT LDGGWVYDAG LTPNNLKPVA AEFYGSVEHP QTYYYAVAVV
     KKGTDFQLNQ LEGKKSCHTG LGRSAGWVIP IGLLFCKLSE PRSPLEKAVS SFFSGSCVPC
     ADPVAFPKLC QLCPGCGCSS TQPFFGYVGA FKCLKDGGGD VAFVKHTTIF EVLPEKADRD
     QYELLCLDNT RKPVDQYEDC YLARIPSHAV VARKNNGKED LIWEILKVAQ EHFGKGKSKD
     FQLFSSPLGK DLLFKDSAFG LLRVPPRMDY RLYLGHNYVT AIRNQQEGVC PEGSIDNSPV
     KWCALSHLER TKCDEWSIIS EGKIECESAE TTEDCIEKIV NGEADAMTLD GGHAYIAGQC
     GLVPVMAEYY ESSNCAIPSQ QGIFPKGYYA VAVVKASDTS ITWNNLKGKK SCHTGVDRTA
     GWNIPMGMLY NRINHCKFDE FFSQGCAPGY EKNSTLCDLC IGPLKCAPNN KEEYNGYTGA
     FRCLVEKGDV AFVKHQTVLD NTEGKNPAEW AKNLKQEDFE LLCPDGTRKP VKDFASCHLA
     QAPNHVVVSR KEKAARVKAV LTSQETLFGG SDCTGNFCLF KSTTKDLLFR DDTKCFVKLP
     EGTTPEKYLG AEYMQSVGNM RKCSTSRLLE ACTFHKH
//