TRFL_MOUSE
ID TRFL_MOUSE Reviewed; 707 AA.
AC P08071; P70690; Q61799; Q8CBA0; Q922P2;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Lactotransferrin;
DE Short=Lactoferrin;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=Ltf;
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 TISSUE=Uterus;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Uterus;
RA Moriishi K.;
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone, Bone marrow, and Gall bladder;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [GENOMIC DNA] OF 1-14.
RX PubMed=1939212; DOI=10.1016/s0021-9258(18)54719-0;
RA Liu Y., Teng C.T.;
RT "Characterization of estrogen-responsive mouse lactoferrin promoter.";
RL J. Biol. Chem. 266:21880-21885(1991).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
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.
CC -!- FUNCTION: Lactotransferrin is a major iron-binding and multifunctional
CC protein found in exocrine fluids such as breast milk and mucosal
CC secretions. Has antimicrobial activity. Antimicrobial properties may
CC include bacteriostasis, which is related to its ability to sequester
CC free iron and thus inhibit microbial growth, as well as direct
CC bactericidal properties leading to the release of lipopolysaccharides
CC from the bacterial outer membrane. May have anabolic, differentiating
CC and anti-apoptotic effects on osteoblasts and may also inhibit
CC osteoclastogenesis, possibly playing a role in the regulation of bone
CC growth. May interfere with the lipopolysaccharide (LPS)-stimulated TLR4
CC signaling (By similarity). {ECO:0000250}.
CC -!- FUNCTION: The lactotransferrin transferrin-like domain 1 functions as a
CC serine protease of the peptidase S60 family that cuts arginine rich
CC regions. This function contributes to the antimicrobial activity. Shows
CC a preferential cleavage at -Arg-Ser-Arg-Arg-|- and -Arg-Arg-Ser-Arg-|-,
CC and of Z-Phe-Arg-|-aminomethylcoumarin sites. {ECO:0000250}.
CC -!- SUBUNIT: Monomer. Found in a complex with LTF, CLU, EPPIN and SEMG1 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted. Cytoplasmic granule {ECO:0000250}.
CC Note=Secreted into most exocrine fluids by various endothelial cells.
CC Stored in the secondary granules of neutrophils (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the transferrin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00741}.
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DR EMBL; J03298; AAA40525.1; -; mRNA.
DR EMBL; D88510; BAA13633.1; -; mRNA.
DR EMBL; AK036491; BAC29450.1; -; mRNA.
DR EMBL; AK144556; BAE25936.1; -; mRNA.
DR EMBL; AK151822; BAE30719.1; -; mRNA.
DR EMBL; BC006904; AAH06904.1; -; mRNA.
DR EMBL; M74778; AAA39427.1; -; Genomic_DNA.
DR CCDS; CCDS23581.1; -.
DR PIR; A28438; A28438.
DR RefSeq; NP_032548.2; NM_008522.3.
DR AlphaFoldDB; P08071; -.
DR SMR; P08071; -.
DR BioGRID; 201224; 6.
DR STRING; 10090.ENSMUSP00000035077; -.
DR MEROPS; S60.001; -.
DR MEROPS; S60.970; -.
DR GlyGen; P08071; 2 sites.
DR PhosphoSitePlus; P08071; -.
DR SwissPalm; P08071; -.
DR CPTAC; non-CPTAC-3885; -.
DR jPOST; P08071; -.
DR MaxQB; P08071; -.
DR PaxDb; P08071; -.
DR PeptideAtlas; P08071; -.
DR PRIDE; P08071; -.
DR ProteomicsDB; 259088; -.
DR Antibodypedia; 3271; 1371 antibodies from 44 providers.
DR DNASU; 17002; -.
DR Ensembl; ENSMUST00000035077; ENSMUSP00000035077; ENSMUSG00000032496.
DR GeneID; 17002; -.
DR KEGG; mmu:17002; -.
DR UCSC; uc009rvj.1; mouse.
DR CTD; 4057; -.
DR MGI; MGI:96837; Ltf.
DR VEuPathDB; HostDB:ENSMUSG00000032496; -.
DR eggNOG; ENOG502QSZB; Eukaryota.
DR GeneTree; ENSGT00940000156055; -.
DR HOGENOM; CLU_011309_1_0_1; -.
DR InParanoid; P08071; -.
DR OMA; KSVRWCT; -.
DR OrthoDB; 232859at2759; -.
DR PhylomeDB; P08071; -.
DR TreeFam; TF324013; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-6799990; Metal sequestration by antimicrobial proteins.
DR Reactome; R-MMU-6803157; Antimicrobial peptides.
DR BioGRID-ORCS; 17002; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Ltf; mouse.
DR PRO; PR:P08071; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P08071; protein.
DR Bgee; ENSMUSG00000032496; Expressed in granulocyte and 105 other tissues.
DR ExpressionAtlas; P08071; baseline and differential.
DR Genevisible; P08071; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0055037; C:recycling endosome; IBA:GO_Central.
DR GO; GO:0030141; C:secretory granule; ISO:MGI.
DR GO; GO:0042581; C:specific granule; ISS:UniProtKB.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; ISO:MGI.
DR GO; GO:0008201; F:heparin binding; ISO:MGI.
DR GO; GO:0005506; F:iron ion binding; ISO:MGI.
DR GO; GO:0001530; F:lipopolysaccharide binding; ISO:MGI.
DR GO; GO:0008233; F:peptidase activity; IDA:MGI.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; ISO:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0019731; P:antibacterial humoral response; ISS:UniProtKB.
DR GO; GO:0019732; P:antifungal humoral response; ISS:UniProtKB.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; ISO:MGI.
DR GO; GO:0060349; P:bone morphogenesis; ISS:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; ISO:MGI.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISO:MGI.
DR GO; GO:0045087; P:innate immune response; ISO:MGI.
DR GO; GO:0002227; P:innate immune response in mucosa; ISS:UniProtKB.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR GO; GO:0006826; P:iron ion transport; IBA:GO_Central.
DR GO; GO:0031640; P:killing of cells of another organism; ISO:MGI.
DR GO; GO:0051673; P:membrane disruption in another organism; ISO:MGI.
DR GO; GO:0044793; P:negative regulation by host of viral process; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0032780; P:negative regulation of ATP-dependent activity; ISO:MGI.
DR GO; GO:2000117; P:negative regulation of cysteine-type endopeptidase activity; ISO:MGI.
DR GO; GO:0031665; P:negative regulation of lipopolysaccharide-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0045837; P:negative regulation of membrane potential; ISO:MGI.
DR GO; GO:2001205; P:negative regulation of osteoclast development; ISS:UniProtKB.
DR GO; GO:1900229; P:negative regulation of single-species biofilm formation in or on host organism; ISS:UniProtKB.
DR GO; GO:2000308; P:negative regulation of tumor necrosis factor (ligand) superfamily member 11 production; ISS:UniProtKB.
DR GO; GO:0045071; P:negative regulation of viral genome replication; ISO:MGI.
DR GO; GO:0048525; P:negative regulation of viral process; ISO:MGI.
DR GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
DR GO; GO:1900159; P:positive regulation of bone mineralization involved in bone maturation; ISS:UniProtKB.
DR GO; GO:1902732; P:positive regulation of chondrocyte proliferation; ISS:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISS:UniProtKB.
DR GO; GO:0033690; P:positive regulation of osteoblast proliferation; ISS:UniProtKB.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0034145; P:positive regulation of toll-like receptor 4 signaling pathway; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0001817; P:regulation of cytokine production; ISS:UniProtKB.
DR GO; GO:0032680; P:regulation of tumor necrosis factor production; ISS:UniProtKB.
DR InterPro; IPR030684; Lactotransferrin.
DR InterPro; IPR016357; Transferrin.
DR InterPro; IPR001156; Transferrin-like_dom.
DR InterPro; IPR018195; Transferrin_Fe_BS.
DR Pfam; PF00405; Transferrin; 2.
DR PIRSF; PIRSF500683; Lactotransferrin; 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 Disulfide bond; Glycoprotein; Hydrolase; Immunity; Ion transport; Iron;
KW Iron transport; Metal-binding; Osteogenesis; Protease; Reference proteome;
KW Repeat; Secreted; Serine protease; Signal; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..707
FT /note="Lactotransferrin"
FT /id="PRO_0000035737"
FT DOMAIN 24..351
FT /note="Transferrin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DOMAIN 363..692
FT /note="Transferrin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT ACT_SITE 91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT ACT_SITE 277
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 78
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 110
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 135
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
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 141
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 142
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 210
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 271
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 413
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 451
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
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 481
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 483
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 484
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 544
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 613
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 494
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 27..63
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 37..54
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 133..216
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 175..191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 188..199
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 249..263
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 366..398
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 376..389
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 423..702
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 443..665
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 475..550
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 499..693
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 509..523
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 520..533
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 591..605
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 643..648
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT CONFLICT 1..2
FT /note="MR -> IQG (in Ref. 1; AAA40525)"
FT /evidence="ECO:0000305"
FT CONFLICT 25
FT /note="Q -> R (in Ref. 1; AAA40525 and 4; AAH06904)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="M -> L (in Ref. 2; BAA13633)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="S -> T (in Ref. 2; BAA13633)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="A -> D (in Ref. 1; AAA40525)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="E -> G (in Ref. 2; BAA13633)"
FT /evidence="ECO:0000305"
FT CONFLICT 629
FT /note="L -> V (in Ref. 1; AAA40525)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 707 AA; 77838 MW; E1B32F5FD8748A0F CRC64;
MRLLIPSLIF LEALGLCLAK ATTVQWCAVS NSEEEKCLRW QNEMRKVGGP PLSCVKKSST
RQCIQAIVTN RADAMTLDGG TMFDAGKPPY KLRPVAAEVY GTKEQPRTHY YAVAVVKNSS
NFHLNQLQGL RSCHTGIGRS AGWKIPIGTL RPYLNWNGPP ASLEEAVSKF FSKSCVPGAQ
KDRFPNLCSS CAGTGANKCA SSPEEPYSGY AGALRCLRDN AGDVAFTRGS TVFEELPNKA
ERDQYKLLCP DNTWKPVTEY KECHLAQVPS HAVVSRSTND KEEAIWELLR QSQEKFGKKQ
ASGFQLFASP SGQKDLLFKE SAIGFVRVPQ KVDVGLYLTF SYTTSIQNLN KKQQDVIASK
ARVTWCAVGS EEKRKCDQWN RASRGRVTCI SFPTTEDCIV AIMKGDADAM SLDGGYIYTA
GKCGLVPVLA ENQKSSKSNG LDCVNRPVEG YLAVAAVRRE DAGFTWSSLR GKKSCHTAVD
RTAGWNIPMG LLANQTRSCK FNEFFSQSCA PGADPKSNLC ALCIGDEKGE NKCAPNSKER
YQGYTGALRC LAEKAGNVAF LKDSTVLQNT DGKNTEEWAR NLKLKDFELL CLDDTRKPVT
EAKNCHLAIA PNHAVVSRTD KVEVLQQVLL DQQVQFGRNG QRCPGEFCLF QSKTKNLLFN
DNTECLAKIP GKTTSEKYLG KEYVIATERL KQCSSSPLLE ACAFLTQ
