TRFE_MOUSE
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 03-AUG-2022, entry version 187.
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, Pancreas,
RC 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; 7.
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 GlyGen; Q921I1; 2 sites, 26 N-linked glycans (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; Q921I1; -.
DR PeptideAtlas; Q921I1; -.
DR PRIDE; Q921I1; -.
DR ProteomicsDB; 259087; -.
DR Antibodypedia; 873; 1706 antibodies from 43 providers.
DR DNASU; 22041; -.
DR Ensembl; ENSMUST00000035158; ENSMUSP00000035158; ENSMUSG00000032554.
DR Ensembl; ENSMUST00000112645; ENSMUSP00000108264; ENSMUSG00000032554.
DR GeneID; 22041; -.
DR KEGG; mmu:22041; -.
DR UCSC; uc009rgj.1; mouse.
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; SGNFCLF; -.
DR OrthoDB; 232859at2759; -.
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 53 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 226 other tissues.
DR ExpressionAtlas; Q921I1; baseline and differential.
DR Genevisible; Q921I1; MM.
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: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:0031232; C:extrinsic component of external side of plasma membrane; 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:0006879; P:cellular iron ion homeostasis; IEA:InterPro.
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: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: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:0045893; P:positive regulation of transcription, DNA-templated; IDA:DFLAT.
DR GO; GO:0034756; P:regulation of iron ion transport; ISO:MGI.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR GO; GO:0060395; P:SMAD protein signal transduction; IDA:MGI.
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 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
