TRFL_CAMDR
ID TRFL_CAMDR Reviewed; 708 AA.
AC Q9TUM0; Q9MZS5;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Lactotransferrin;
DE Short=Lactoferrin;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=LTF;
OS Camelus dromedarius (Dromedary) (Arabian camel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Camelus.
OX NCBI_TaxID=9838;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Somali; TISSUE=Lactating mammary gland;
RX AGRICOLA=IND22027049; DOI=10.1016/S0958-6946(99)00117-X;
RA Kappeler S.R., Ackermann M., Farah Z., Puhan Z.;
RT "Sequence analysis of camel (Camelus dromedarius) lactoferrin.";
RL Int. Dairy J. 9:481-486(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF
RP 20-708, GLYCOSYLATION, AND DISULFIDE BONDS.
RC TISSUE=Mammary gland;
RX PubMed=11397094; DOI=10.1006/jmbi.2001.4692;
RA Khan J.A., Kumar P., Paramasivam M., Yadav R.S., Sahani M.S., Sharma S.,
RA Srinivasan A., Singh T.P.;
RT "Camel lactoferrin, a transferrin-cum-lactoferrin: crystal structure of
RT camel apolactoferrin at 2.6 A resolution and structural basis of its dual
RT role.";
RL J. Mol. Biol. 309:751-761(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Mammary gland;
RA Paramasivam M., Srinivasan A., Singh R., Sahani M.S., Singh T.P.;
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 20-708 IN COMPLEX WITH IRON AND
RP CARBONATE, AND DISULFIDE BONDS.
RX PubMed=11473113; DOI=10.1074/jbc.m104343200;
RA Khan J.A., Kumar P., Srinivasan A., Singh T.P.;
RT "Protein intermediate trapped by the simultaneous crystallization process.
RT Crystal structure of an iron-saturated intermediate in the Fe3+ binding
RT pathway of camel lactoferrin at 2.7 a resolution.";
RL J. Biol. Chem. 276:36817-36823(2001).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.99 ANGSTROMS) OF 20-64 IN COMPLEX WITH E.COLI
RP OMPC, DISULFIDE BONDS, AND INTERACTION WITH E.COLI OMPC.
RA Baalaji S., Acharya R.K., Singh T.P., Krishnaswamy S.;
RT "Crystal structure of the membrane protein Ompc complex with antibacterial
RT lactoferrin.";
RL Submitted (SEP-2006) to the PDB data bank.
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. {ECO:0000250}.
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 (By similarity). Found in a complex with LTF, CLU,
CC EPPIN and SEMG1 (By similarity). Interacts with E.coli outer membrane
CC protein C (OmpC). {ECO:0000250, ECO:0000269|PubMed:11473113,
CC ECO:0000269|Ref.5}.
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; AJ131674; CAB53387.1; -; mRNA.
DR EMBL; AF165879; AAF82241.1; -; mRNA.
DR RefSeq; NP_001290496.1; NM_001303567.1.
DR PDB; 1DTZ; X-ray; 2.65 A; A=20-708.
DR PDB; 1I6Q; X-ray; 2.70 A; A=20-708.
DR PDB; 2J4U; X-ray; 2.99 A; S/X=20-64.
DR PDBsum; 1DTZ; -.
DR PDBsum; 1I6Q; -.
DR PDBsum; 2J4U; -.
DR AlphaFoldDB; Q9TUM0; -.
DR SMR; Q9TUM0; -.
DR STRING; 9838.ENSCDRP00005008634; -.
DR MEROPS; S60.001; -.
DR MEROPS; S60.970; -.
DR iPTMnet; Q9TUM0; -.
DR PRIDE; Q9TUM0; -.
DR GeneID; 105103507; -.
DR KEGG; cdk:105103507; -.
DR CTD; 4057; -.
DR EvolutionaryTrace; Q9TUM0; -.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0042581; C:specific granule; ISS:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
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:0060349; P:bone morphogenesis; ISS:UniProtKB.
DR GO; GO:0002227; P:innate immune response in mucosa; ISS:UniProtKB.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0031665; P:negative regulation of lipopolysaccharide-mediated signaling pathway; ISS:UniProtKB.
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: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:0045669; P:positive regulation of osteoblast differentiation; ISS:UniProtKB.
DR GO; GO:0033690; P:positive regulation of osteoblast proliferation; ISS:UniProtKB.
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; 2.
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 3D-structure; Disulfide bond; Glycoprotein; Hydrolase; Immunity;
KW Ion transport; Iron; Iron transport; Metal-binding; Osteogenesis; Protease;
KW Repeat; Secreted; Serine protease; Signal; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..708
FT /note="Lactotransferrin"
FT /id="PRO_0000035729"
FT DOMAIN 25..352
FT /note="Transferrin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DOMAIN 364..693
FT /note="Transferrin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT REGION 44..51
FT /note="Interaction with E.coli ompC"
FT ACT_SITE 92
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT ACT_SITE 278
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 79
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 111
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:11473113"
FT BINDING 136
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 140
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:11473113"
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 143
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 211
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:11473113"
FT BINDING 272
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 414
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 452
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:11473113"
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 482
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:11473113"
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 485
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 545
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:11473113"
FT BINDING 614
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11397094"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 537
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11397094"
FT CARBOHYD 594
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..64
FT DISULFID 38..55
FT DISULFID 134..217
FT DISULFID 176..192
FT DISULFID 179..202
FT DISULFID 189..200
FT DISULFID 250..264
FT DISULFID 367..399
FT DISULFID 377..390
FT DISULFID 424..703
FT DISULFID 444..666
FT DISULFID 476..551
FT DISULFID 500..694
FT DISULFID 510..524
FT DISULFID 521..534
FT DISULFID 592..606
FT DISULFID 644..649
FT CONFLICT 261
FT /note="F -> S (in Ref. 2; AAF82241)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="G -> A (in Ref. 2; AAF82241)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="S -> P (in Ref. 2; AAF82241)"
FT /evidence="ECO:0000305"
FT CONFLICT 492..494
FT /note="LLS -> PLF (in Ref. 2; AAF82241)"
FT /evidence="ECO:0000305"
FT CONFLICT 506
FT /note="L -> F (in Ref. 2; AAF82241)"
FT /evidence="ECO:0000305"
FT CONFLICT 609
FT /note="A -> P (in Ref. 2; AAF82241)"
FT /evidence="ECO:0000305"
FT CONFLICT 642
FT /note="R -> Q (in Ref. 2; AAF82241)"
FT /evidence="ECO:0000305"
FT STRAND 23..31
FT /evidence="ECO:0007829|PDB:1DTZ"
FT HELIX 32..46
FT /evidence="ECO:0007829|PDB:1DTZ"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:1DTZ"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:1DTZ"
FT HELIX 61..69
FT /evidence="ECO:0007829|PDB:1DTZ"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:1DTZ"
FT HELIX 80..87
FT /evidence="ECO:0007829|PDB:1DTZ"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:1DTZ"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:1DTZ"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:1DTZ"
FT STRAND 108..120
FT /evidence="ECO:0007829|PDB:1DTZ"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:1DTZ"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:1DTZ"
FT TURN 141..144
FT /evidence="ECO:0007829|PDB:1DTZ"
FT HELIX 145..150
FT /evidence="ECO:0007829|PDB:1DTZ"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:1DTZ"
FT HELIX 164..171
FT /evidence="ECO:0007829|PDB:1DTZ"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:1DTZ"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:1I6Q"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:1DTZ"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:1DTZ"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:1DTZ"
FT HELIX 210..219
FT /evidence="ECO:0007829|PDB:1DTZ"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:1DTZ"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:1DTZ"
FT HELIX 232..236
FT /evidence="ECO:0007829|PDB:1DTZ"
FT HELIX 240..243
FT /evidence="ECO:0007829|PDB:1DTZ"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:1DTZ"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:1DTZ"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:1DTZ"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:1DTZ"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:1DTZ"
FT STRAND 266..270
FT /evidence="ECO:0007829|PDB:1DTZ"
FT STRAND 273..278
FT /evidence="ECO:0007829|PDB:1DTZ"
FT HELIX 283..297
FT /evidence="ECO:0007829|PDB:1DTZ"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:1DTZ"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:1DTZ"
FT HELIX 335..339
FT /evidence="ECO:0007829|PDB:1DTZ"
FT HELIX 341..348
FT /evidence="ECO:0007829|PDB:1DTZ"
FT TURN 349..351
FT /evidence="ECO:0007829|PDB:1DTZ"
FT HELIX 354..362
FT /evidence="ECO:0007829|PDB:1DTZ"
FT STRAND 363..370
FT /evidence="ECO:0007829|PDB:1DTZ"
FT HELIX 371..384
FT /evidence="ECO:0007829|PDB:1DTZ"
FT STRAND 387..395
FT /evidence="ECO:0007829|PDB:1DTZ"
FT HELIX 396..404
FT /evidence="ECO:0007829|PDB:1DTZ"
FT STRAND 410..413
FT /evidence="ECO:0007829|PDB:1DTZ"
FT HELIX 415..422
FT /evidence="ECO:0007829|PDB:1DTZ"
FT TURN 423..425
FT /evidence="ECO:0007829|PDB:1DTZ"
FT STRAND 427..434
FT /evidence="ECO:0007829|PDB:1DTZ"
FT TURN 444..446
FT /evidence="ECO:0007829|PDB:1DTZ"
FT STRAND 453..461
FT /evidence="ECO:0007829|PDB:1DTZ"
FT TURN 467..472
FT /evidence="ECO:0007829|PDB:1DTZ"
FT STRAND 473..478
FT /evidence="ECO:0007829|PDB:1DTZ"
FT TURN 483..493
FT /evidence="ECO:0007829|PDB:1DTZ"
FT STRAND 494..497
FT /evidence="ECO:0007829|PDB:1DTZ"
FT STRAND 504..510
FT /evidence="ECO:0007829|PDB:1DTZ"
FT STRAND 521..523
FT /evidence="ECO:0007829|PDB:1DTZ"
FT TURN 528..530
FT /evidence="ECO:0007829|PDB:1DTZ"
FT HELIX 544..553
FT /evidence="ECO:0007829|PDB:1DTZ"
FT STRAND 558..563
FT /evidence="ECO:0007829|PDB:1DTZ"
FT HELIX 564..567
FT /evidence="ECO:0007829|PDB:1DTZ"
FT TURN 569..574
FT /evidence="ECO:0007829|PDB:1I6Q"
FT STRAND 575..578
FT /evidence="ECO:0007829|PDB:1DTZ"
FT STRAND 580..582
FT /evidence="ECO:0007829|PDB:1I6Q"
FT STRAND 588..591
FT /evidence="ECO:0007829|PDB:1I6Q"
FT HELIX 600..605
FT /evidence="ECO:0007829|PDB:1DTZ"
FT STRAND 615..618
FT /evidence="ECO:0007829|PDB:1DTZ"
FT TURN 620..622
FT /evidence="ECO:0007829|PDB:1DTZ"
FT HELIX 623..637
FT /evidence="ECO:0007829|PDB:1DTZ"
FT TURN 642..646
FT /evidence="ECO:0007829|PDB:1DTZ"
FT STRAND 654..656
FT /evidence="ECO:0007829|PDB:1DTZ"
FT STRAND 664..669
FT /evidence="ECO:0007829|PDB:1DTZ"
FT HELIX 676..680
FT /evidence="ECO:0007829|PDB:1DTZ"
FT HELIX 682..692
FT /evidence="ECO:0007829|PDB:1DTZ"
FT HELIX 698..705
FT /evidence="ECO:0007829|PDB:1DTZ"
SQ SEQUENCE 708 AA; 77211 MW; 0B0C175A0B69D430 CRC64;
MKLFFPALLS LGALGLCLAA SKKSVRWCTT SPAESSKCAQ WQRRMKKVRG PSVTCVKKTS
RFECIQAIST EKADAVTLDG GLVYDAGLDP YKLRPIAAEV YGTENNPQTH YYAVAIAKKG
TNFQLNQLQG LKSCHTGLGR SAGWNIPMGL LRPFLDWTGP PEPLQKAVAK FFSASCVPCV
DGKEYPNLCQ LCAGTGENKC ACSSQEPYFG YSGAFKCLQD GAGDVAFVKD STVFESLPAK
ADRDQYELLC PNNTRKPVDA FQECHLARVP SHAVVARSVN GKEDLIWKLL VKAQEKFGRG
KPSGFQLFGS PAGQKDLLFK DSALGLLRIS SKIDSGLYLG SNYITAIRGL RETAAEVELR
RAQVVWCAVG SDEQLKCQEW SRQSNQSVVC ATASTTEDCI ALVLKGEADA LSLDGGYIYI
AGKCGLVPVL AESQQSPESS GLDCVHRPVK GYLAVAVVRK ANDKITWNSL RGKKSCHTAV
DRTAGWNIPM GLLSKNTDSC RFDEFLSQSC APGSDPRSKL CALCAGNEEG QNKCVPNSSE
RYYGYTGAFR CLAENVGDVA FVKDVTVLDN TDGKNTEQWA KDLKLGDFEL LCLNGTRKPV
TEAESCHLAV APNHAVVSRI DKVAHLEQVL LRQQAHFGRN GRDCPGKFCL FQSKTKNLLF
NDNTECLAKL QGKTTYEEYL GPQYVTAIAK LRRCSTSPLL EACAFLMR
