TRFE_RAT
ID TRFE_RAT Reviewed; 698 AA.
AC P12346; Q63602; Q64628; Q64630; Q7TNX0;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Serotransferrin;
DE Short=Transferrin;
DE AltName: Full=Beta-1 metal-binding globulin;
DE AltName: Full=Liver regeneration-related protein LRRG03;
DE AltName: Full=Siderophilin;
DE Flags: Precursor;
GN Name=Tf;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Wistar; TISSUE=Mammary gland;
RX PubMed=7717992; DOI=10.1042/bj3070047;
RA Escriva H., Pierce A., Coddeville B., Gonzalez F., Benaissa M., Leger D.,
RA Wieruszeski J.-M., Spik G., Pamblanco M.;
RT "Rat mammary-gland transferrin: nucleotide sequence, phylogenetic analysis
RT and glycan structure.";
RL Biochem. J. 307:47-55(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=8829802; DOI=10.1016/0305-0491(95)02068-3;
RA Hosino A., Hisayasu S., Shimada T.;
RT "Complete sequence analysis of rat transferrin and expression of
RT transferrin but not lactoferrin in the digestive glands.";
RL Comp. Biochem. Physiol. 113B:491-497(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Xu C.S., Li W.Q., Li Y.C., Han H.P., Wang G.P., Chai L.Q., Yuan J.Y.,
RA Yang K.J., Yan H.M., Chang C.F., Zhao L.F., Ma H., Wang L., Wang S.F.,
RA Shi J.B., Rahman S., Wang Q.N., Zhang J.B.;
RT "Liver regeneration after PH.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-295 (ISOFORM 2).
RX PubMed=6236811; DOI=10.1016/0006-291x(84)91185-9;
RA Aldred A.R., Howlett G.J., Schreiber G.;
RT "Synthesis of rat transferrin in Escherichia coli containing a recombinant
RT bacteriophage.";
RL Biochem. Biophys. Res. Commun. 122:960-965(1984).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 521-698.
RX PubMed=3023031; DOI=10.1210/endo-120-1-332;
RA Huggenvik J.I., Idzerda R.L., Haywood L., Lee D.C., McKnight G.S.,
RA Griswold M.D.;
RT "Transferrin messenger ribonucleic acid: molecular cloning and hormonal
RT regulation in rat Sertoli cells.";
RL Endocrinology 120:332-340(1987).
RN [7]
RP PROTEIN SEQUENCE OF 20-47.
RX PubMed=500689; DOI=10.1016/s0021-9258(19)86420-7;
RA Schreiber G., Dryburgh H., Millership A., Matsuda Y., Inglis A.,
RA Phillips J., Edwards K., Maggs J.;
RT "The synthesis and secretion of rat transferrin.";
RL J. Biol. Chem. 254:12013-12019(1979).
RN [8]
RP PROTEIN SEQUENCE OF 20-30 AND 642-653.
RX PubMed=3046665; DOI=10.1016/0304-4165(88)90081-5;
RA Purves L.R., Purves M., Linton N., Brandt W., Johnson G., Jacobs P.;
RT "Properties of the transferrin associated with rat intestinal mucosa.";
RL Biochim. Biophys. Acta 966:318-327(1988).
RN [9]
RP PROTEIN SEQUENCE OF 89-102; 232-243 AND 404-411.
RX PubMed=1791188; DOI=10.1002/jcb.240470312;
RA Cavanaugh P.G., Nicolson G.L.;
RT "Lung-derived growth factor that stimulates the growth of lung-
RT metastasizing tumor cells: identification as transferrin.";
RL J. Cell. Biochem. 47:261-271(1991).
RN [10]
RP PROTEIN SEQUENCE OF 144-162; 240-251; 332-343; 588-609; 616-624; 630-642
RP AND 660-682, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [11]
RP METHYLATION AT ARG-42, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15047867; DOI=10.1091/mbc.e04-02-0101;
RA Wu C.C., MacCoss M.J., Mardones G., Finnigan C., Mogelsvang S.,
RA Yates J.R. III, Howell K.E.;
RT "Organellar proteomics reveals Golgi arginine dimethylation.";
RL Mol. Biol. Cell 15:2907-2919(2004).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P12346-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P12346-2; Sequence=VSP_011840;
CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
CC -!- SIMILARITY: Belongs to the transferrin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00741}.
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DR EMBL; X77158; CAA54403.1; -; mRNA.
DR EMBL; D38380; BAA07458.1; -; mRNA.
DR EMBL; AY327504; AAP97736.1; -; mRNA.
DR EMBL; BC087021; AAH87021.1; -; mRNA.
DR EMBL; M26113; AAA42266.1; -; mRNA.
DR EMBL; M27966; AAA42267.1; -; mRNA.
DR PIR; S49163; S49163.
DR RefSeq; NP_001013128.1; NM_001013110.1. [P12346-1]
DR AlphaFoldDB; P12346; -.
DR SMR; P12346; -.
DR BioGRID; 246945; 4.
DR IntAct; P12346; 2.
DR MINT; P12346; -.
DR STRING; 10116.ENSRNOP00000012725; -.
DR Allergome; 1417; Rat n Transferrin.
DR MEROPS; S60.970; -.
DR GlyConnect; 557; 6 N-Linked glycans.
DR GlyGen; P12346; 2 sites, 15 N-linked glycans (2 sites).
DR iPTMnet; P12346; -.
DR PhosphoSitePlus; P12346; -.
DR World-2DPAGE; 0004:P12346; -.
DR PaxDb; P12346; -.
DR PRIDE; P12346; -.
DR Ensembl; ENSRNOT00000045628; ENSRNOP00000045637; ENSRNOG00000030625. [P12346-1]
DR GeneID; 24825; -.
DR KEGG; rno:24825; -.
DR UCSC; RGD:3845; rat. [P12346-1]
DR CTD; 7018; -.
DR RGD; 3845; Tf.
DR eggNOG; KOG0090; Eukaryota.
DR GeneTree; ENSGT00940000154388; -.
DR HOGENOM; CLU_011309_1_0_1; -.
DR InParanoid; P12346; -.
DR OrthoDB; 232859at2759; -.
DR PhylomeDB; P12346; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR Reactome; R-RNO-917937; Iron uptake and transport.
DR Reactome; R-RNO-917977; Transferrin endocytosis and recycling.
DR PRO; PR:P12346; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000030625; Expressed in liver and 19 other tissues.
DR ExpressionAtlas; P12346; baseline and differential.
DR Genevisible; P12346; RN.
DR GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR GO; GO:0045178; C:basal part of cell; ISO:RGD.
DR GO; GO:0009925; C:basal plasma membrane; ISO:RGD.
DR GO; GO:0005604; C:basement membrane; IDA:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0051286; C:cell tip; IDA:RGD.
DR GO; GO:0005905; C:clathrin-coated pit; ISO:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR GO; GO:0097433; C:dense body; ISO:RGD.
DR GO; GO:0005769; C:early endosome; ISO:RGD.
DR GO; GO:0030139; C:endocytic vesicle; ISO:RGD.
DR GO; GO:0005768; C:endosome; ISO:RGD.
DR GO; GO:0005576; C:extracellular region; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0031232; C:extrinsic component of external side of plasma membrane; ISO:RGD.
DR GO; GO:1990712; C:HFE-transferrin receptor complex; ISO:RGD.
DR GO; GO:0005770; C:late endosome; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0055037; C:recycling endosome; ISO:RGD.
DR GO; GO:0031982; C:vesicle; ISO:RGD.
DR GO; GO:0030120; C:vesicle coat; ISO:RGD.
DR GO; GO:0008199; F:ferric iron binding; IDA:RGD.
DR GO; GO:0008198; F:ferrous iron binding; ISO:RGD.
DR GO; GO:0034986; F:iron chaperone activity; ISO:RGD.
DR GO; GO:1990459; F:transferrin receptor binding; ISO:RGD.
DR GO; GO:0007015; P:actin filament organization; ISO:RGD.
DR GO; GO:0006953; P:acute-phase response; IEP:RGD.
DR GO; GO:0019731; P:antibacterial humoral response; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
DR GO; GO:0006879; P:cellular iron ion homeostasis; TAS:RGD.
DR GO; GO:0071320; P:cellular response to cAMP; IEP:UniProtKB.
DR GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; IEP:UniProtKB.
DR GO; GO:0071281; P:cellular response to iron ion; ISO:RGD.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; ISO:RGD.
DR GO; GO:0006826; P:iron ion transport; IDA:RGD.
DR GO; GO:0030316; P:osteoclast differentiation; ISO:RGD.
DR GO; GO:0045780; P:positive regulation of bone resorption; ISO:RGD.
DR GO; GO:2000147; P:positive regulation of cell motility; ISO:RGD.
DR GO; GO:0031643; P:positive regulation of myelination; IDA:RGD.
DR GO; GO:0070447; P:positive regulation of oligodendrocyte progenitor proliferation; IDA:RGD.
DR GO; GO:0042327; P:positive regulation of phosphorylation; ISO:RGD.
DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0034756; P:regulation of iron ion transport; ISO:RGD.
DR GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0010288; P:response to lead ion; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0060395; P:SMAD protein signal transduction; ISO:RGD.
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 Alternative splicing; Direct protein sequencing; 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:3046665,
FT ECO:0000269|PubMed:500689"
FT CHAIN 20..698
FT /note="Serotransferrin"
FT /id="PRO_0000035718"
FT DOMAIN 25..347
FT /note="Transferrin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DOMAIN 360..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: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 447
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 473
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 479
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 536
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
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 MOD_RES 42
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000269|PubMed:15047867"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02787"
FT MOD_RES 685
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02787"
FT CARBOHYD 512
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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..693
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 435..656
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 471..542
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 495..684
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 505..519
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 516..525
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 582..596
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 634..639
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT VAR_SEQ 65..266
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:6236811"
FT /id="VSP_011840"
FT CONFLICT 57
FT /note="A -> P (in Ref. 1; CAA54403)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="P -> R (in Ref. 1; CAA54403)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="A -> R (in Ref. 1; CAA54403)"
FT /evidence="ECO:0000305"
FT CONFLICT 321..323
FT /note="LLR -> CYG (in Ref. 2; BAA07458)"
FT /evidence="ECO:0000305"
FT CONFLICT 324..354
FT /note="VPPRMDYRLYLGHSYVTAIRNQREGVCPEGS -> APKDGLQAVPRPQLCHC
FT HSKSAGSCPDA (in Ref. 1; CAA54403)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="G -> A (in Ref. 2; BAA07458)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="S -> T (in Ref. 1; CAA54403 and 2; BAA07458)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="S -> G (in Ref. 1; CAA54403)"
FT /evidence="ECO:0000305"
FT CONFLICT 691
FT /note="E -> D (in Ref. 6; AAA42267)"
FT /evidence="ECO:0000305"
FT CONFLICT 696..697
FT /note="HK -> TA (in Ref. 6; AAA42267)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 698 AA; 76395 MW; B91ABB41CA447194 CRC64;
MRFAVGALLA CAALGLCLAV PDKTVKWCAV SEHENTKCIS FRDHMKTVLP ADGPRLACVK
KTSYQDCIKA ISGGEADAIT LDGGWVYDAG LTPNNLKPVA AEFYGSLEHP QTHYLAVAVV
KKGTDFQLNQ LQGKKSCHTG LGRSAGWIIP IGLLFCNLPE PRKPLEKAVA SFFSGSCVPC
ADPVAFPQLC QLCPGCGCSP TQPFFGYVGA FKCLRDGGGD VAFVKHTTIF EVLPQKADRD
QYELLCLDNT RKPVDQYEDC YLARIPSHAV VARNGDGKED LIWEILKVAQ EHFGKGKSKD
FQLFGSPLGK DLLFKDSAFG LLRVPPRMDY RLYLGHSYVT AIRNQREGVC PEGSIDSAPV
KWCALSHQER AKCDEWSVSS NGQIECESAE STEDCIDKIV NGEADAMSLD GGHAYIAGQC
GLVPVMAENY DISSCTNPQS DVFPKGYYAV AVVKASDSSI NWNNLKGKKS CHTGVDRTAG
WNIPMGLLFS RINHCKFDEF FSQGCAPGYK KNSTLCDLCI GPAKCAPNNR EGYNGYTGAF
QCLVEKGDVA FVKHQTVLEN TNGKNTAAWA KDLKQEDFQL LCPDGTKKPV TEFATCHLAQ
APNHVVVSRK EKAARVSTVL TAQKDLFWKG DKDCTGNFCL FRSSTKDLLF RDDTKCLTKL
PEGTTYEEYL GAEYLQAVGN IRKCSTSRLL EACTFHKS
