NFP_MEDTR
ID NFP_MEDTR Reviewed; 595 AA.
AC Q0GXS4; A9DLN8; M1G231;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Serine/threonine receptor-like kinase NFP {ECO:0000303|PubMed:16723404};
DE Short=RLK NFP {ECO:0000303|PubMed:16723404};
DE AltName: Full=Nod factor perception protein {ECO:0000303|PubMed:12753588};
DE EC=2.7.10.- {ECO:0000255|PROSITE-ProRule:PRU00159};
DE AltName: Full=Nod-factor receptor 5;
DE Flags: Precursor;
GN Name=NFP {ECO:0000303|PubMed:12753588};
GN OrderedLocusNames=MTR_5g019040 {ECO:0000312|EMBL:AES94847.1};
OS Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3880 {ECO:0000312|EMBL:ABF50224.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE,
RP MUTAGENESIS OF SER-67, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND GENE
RP FAMILY.
RX PubMed=16844829; DOI=10.1104/pp.106.084657;
RA Arrighi J.-F., Barre A., Ben Amor B., Bersoult A., Soriano L.C.,
RA Mirabella R., de Carvalho-Niebel F., Journet E.-P., Gherardi M., Huguet T.,
RA Geurts R., Denarie J., Rouge P., Gough C.;
RT "The Medicago truncatula lysin [corrected] motif-receptor-like kinase gene
RT family includes NFP and new nodule-expressed genes.";
RL Plant Physiol. 142:265-279(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jemalong A17;
RX PubMed=22089132; DOI=10.1038/nature10625;
RA Young N.D., Debelle F., Oldroyd G.E.D., Geurts R., Cannon S.B.,
RA Udvardi M.K., Benedito V.A., Mayer K.F.X., Gouzy J., Schoof H.,
RA Van de Peer Y., Proost S., Cook D.R., Meyers B.C., Spannagl M., Cheung F.,
RA De Mita S., Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K.,
RA Murray J.D., Naoumkina M.A., Rosen B., Silverstein K.A.T., Tang H.,
RA Rombauts S., Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M.,
RA Bellec A., Berger A., Berges H., Bidwell S., Bisseling T., Choisne N.,
RA Couloux A., Denny R., Deshpande S., Dai X., Doyle J.J., Dudez A.-M.,
RA Farmer A.D., Fouteau S., Franken C., Gibelin C., Gish J., Goldstein S.,
RA Gonzalez A.J., Green P.J., Hallab A., Hartog M., Hua A., Humphray S.J.,
RA Jeong D.-H., Jing Y., Jocker A., Kenton S.M., Kim D.-J., Klee K., Lai H.,
RA Lang C., Lin S., Macmil S.L., Magdelenat G., Matthews L., McCorrison J.,
RA Monaghan E.L., Mun J.-H., Najar F.Z., Nicholson C., Noirot C.,
RA O'Bleness M., Paule C.R., Poulain J., Prion F., Qin B., Qu C., Retzel E.F.,
RA Riddle C., Sallet E., Samain S., Samson N., Sanders I., Saurat O.,
RA Scarpelli C., Schiex T., Segurens B., Severin A.J., Sherrier D.J., Shi R.,
RA Sims S., Singer S.R., Sinharoy S., Sterck L., Viollet A., Wang B.-B.,
RA Wang K., Wang M., Wang X., Warfsmann J., Weissenbach J., White D.D.,
RA White J.D., Wiley G.B., Wincker P., Xing Y., Yang L., Yao Z., Ying F.,
RA Zhai J., Zhou L., Zuber A., Denarie J., Dixon R.A., May G.D.,
RA Schwartz D.C., Rogers J., Quetier F., Town C.D., Roe B.A.;
RT "The Medicago genome provides insight into the evolution of rhizobial
RT symbioses.";
RL Nature 480:520-524(2011).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Jemalong A17;
RX PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA Schwartz D.C., Town C.D.;
RT "An improved genome release (version Mt4.0) for the model legume Medicago
RT truncatula.";
RL BMC Genomics 15:312-312(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 42-539.
RX PubMed=18073426; DOI=10.1534/genetics.107.076943;
RA De Mita S., Ronfort J., McKhann H.I., Poncet C., El Malki R., Bataillon T.;
RT "Investigation of the demographic and selective forces shaping the
RT nucleotide diversity of genes involved in Nod factor signaling in Medicago
RT truncatula.";
RL Genetics 177:2123-2133(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 62-281, AND FUNCTION.
RX PubMed=23173081; DOI=10.1534/g3.112.003269;
RA Gorton A.J., Heath K.D., Pilet-Nayel M.-L., Baranger A., Stinchcombe J.R.;
RT "Mapping the genetic basis of symbiotic variation in legume-rhizobium
RT interactions in Medicago truncatula.";
RL G3 (Bethesda) 2:1291-1303(2012).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12753588; DOI=10.1046/j.1365-313x.2003.01743.x;
RA Amor B.B., Shaw S.L., Oldroyd G.E.D., Maillet F., Penmetsa R.V., Cook D.,
RA Long S.R., Denarie J., Gough C.;
RT "The NFP locus of Medicago truncatula controls an early step of Nod factor
RT signal transduction upstream of a rapid calcium flux and root hair
RT deformation.";
RL Plant J. 34:495-506(2003).
RN [7]
RP GLYCOSYLATED, AND DOMAIN.
RX PubMed=16723404; DOI=10.1093/glycob/cwl006;
RA Mulder L., Lefebvre B., Cullimore J., Imberty A.;
RT "LysM domains of Medicago truncatula NFP protein involved in Nod factor
RT perception. Glycosylation state, molecular modeling and docking of
RT chitooligosaccharides and Nod factors.";
RL Glycobiology 16:801-809(2006).
RN [8]
RP FUNCTION, MUTAGENESIS OF LEU-154, AND DOMAIN.
RX PubMed=22087221; DOI=10.1371/journal.pone.0026114;
RA Bensmihen S., de Billy F., Gough C.;
RT "Contribution of NFP LysM domains to the recognition of Nod factors during
RT the Medicago truncatula/Sinorhizobium meliloti symbiosis.";
RL PLoS ONE 6:E26114-E26114(2011).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Jemalong A17;
RX PubMed=22874912; DOI=10.1242/dev.081620;
RA Rival P., de Billy F., Bono J.-J., Gough C., Rosenberg C., Bensmihen S.;
RT "Epidermal and cortical roles of NFP and DMI3 in coordinating early steps
RT of nodulation in Medicago truncatula.";
RL Development 139:3383-3391(2012).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF SER-67.
RX PubMed=23432463; DOI=10.1111/nph.12198;
RA Rey T., Nars A., Bonhomme M., Bottin A., Huguet S., Balzergue S.,
RA Jardinaud M.-F., Bono J.-J., Cullimore J., Dumas B., Gough C., Jacquet C.;
RT "NFP, a LysM protein controlling Nod factor perception, also intervenes in
RT Medicago truncatula resistance to pathogens.";
RL New Phytol. 198:875-886(2013).
RN [11]
RP REVIEW.
RX PubMed=23221781; DOI=10.4161/psb.22999;
RA Rival P., Bono J.-J., Gough C., Bensmihen S., Rosenberg C.;
RT "Cell autonomous and non-cell autonomous control of rhizobial and
RT mycorrhizal infection in Medicago truncatula.";
RL Plant Signal. Behav. 8:E22999-E22999(2013).
RN [12]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Jemalong A17;
RX PubMed=25351493; DOI=10.1105/tpc.114.129502;
RA Moling S., Pietraszewska-Bogiel A., Postma M., Fedorova E., Hink M.A.,
RA Limpens E., Gadella T.W.J., Bisseling T.;
RT "Nod factor receptors form heteromeric complexes and are essential for
RT intracellular infection in medicago nodules.";
RL Plant Cell 26:4188-4199(2014).
RN [13]
RP INTERACTION WITH ROP10.
RX PubMed=25794934; DOI=10.1105/tpc.114.135210;
RA Lei M.-J., Wang Q., Li X., Chen A., Luo L., Xie Y., Li G., Luo D.,
RA Mysore K.S., Wen J., Xie Z.-P., Staehelin C., Wang Y.-Z.;
RT "The small GTPase ROP10 of Medicago truncatula is required for both tip
RT growth of root hairs and nod factor-induced root hair deformation.";
RL Plant Cell 27:806-822(2015).
CC -!- FUNCTION: During nodulation, plays a central role in nodule
CC organogenesis (PubMed:22874912). Involved in the perception of Nod
CC factors, the first step of recognition of rhizobia prior to nodulation
CC (PubMed:12753588). Necessary in epidermal cells to induce cortical cell
CC divisions leading to nodule primordia formation (PubMed:22874912).
CC Required during root nodule symbiosis with Sinorhizobium meliloti by
CC triggering infection threads and release of bacteria into the cytoplasm
CC of cells in the infection zone of developing nodules, especially in
CC cells derived from the meristem (PubMed:25351493, PubMed:16844829,
CC PubMed:22087221). Promotes plant fitness (e.g. fruit weight and leaf
CC number) (PubMed:23173081). {ECO:0000269|PubMed:12753588,
CC ECO:0000269|PubMed:16844829, ECO:0000269|PubMed:22087221,
CC ECO:0000269|PubMed:22874912, ECO:0000269|PubMed:23173081,
CC ECO:0000269|PubMed:25351493}.
CC -!- FUNCTION: Involved in resistance to oomycetes (e.g. Aphanomyces
CC euteiches) and to fungi (e.g. Colletotrichum trifolii).
CC {ECO:0000269|PubMed:23432463}.
CC -!- SUBUNIT: Forms heteromeric complexes with LYK3 at the cell periphery in
CC nodules (PubMed:25351493). Interacts with ROP10 (PubMed:25794934).
CC {ECO:0000269|PubMed:25351493, ECO:0000269|PubMed:25794934}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25351493};
CC Single-pass membrane protein {ECO:0000255}. Vacuole lumen
CC {ECO:0000269|PubMed:25351493}. Note=Removed from the plasma membrane
CC upon the release of rhizobia into the host cytoplasm. Vacuolar
CC localization is observed in cells undergoing breakdown of the
CC receptors. {ECO:0000269|PubMed:25351493}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots and nodules and, to a
CC lower extent, in stems (PubMed:16844829, PubMed:22874912). Localized at
CC the cell periphery in a narrow zone of about two cell layers (e.g.
CC L1/L2 zone) at the nodule apex upon infection by rhizobia, from the
CC meristem to the infection zone (at protein level) (PubMed:25351493).
CC {ECO:0000269|PubMed:16844829, ECO:0000269|PubMed:22874912,
CC ECO:0000269|PubMed:25351493}.
CC -!- DEVELOPMENTAL STAGE: In non-inoculated roots, present in root hair
CC cells of lateral roots and fades out in older regions of roots
CC (PubMed:16844829). In young roots, localized at high levels in both
CC epidermis and cortical layers (PubMed:22874912). Associates with
CC primordium formation and with infection throughout the nodulation
CC process. First day after inoculation by S.meliloti, restricted to
CC discrete areas of root epidermis. During the second day, observed in
CC the inner cortex, in regions where cell divisions lead to the formation
CC of nodule primordia and in the middle cortex of regions where root
CC hairs undergo root hair curling (PubMed:16844829). After three to four
CC days, detected in outer cortical cells directly underlying infected
CC root hairs and through which infection threads occur. Weak levels
CC remain in the epidermis (PubMed:16844829, PubMed:22874912). After five
CC days, highly expressed in the central nodule tissue of young, emerging
CC nodules characterized by a highly ramified infection thread network
CC (PubMed:16844829). In mature nodules, restricted to the infection zone,
CC and, at low levels, in interzone II/III, but excluded from the
CC nitrogen-fixing zone (PubMed:16844829, PubMed:22874912). Localized on
CC infection threads before rhizobia are released (PubMed:25351493,
CC PubMed:16844829). {ECO:0000269|PubMed:16844829,
CC ECO:0000269|PubMed:22874912, ECO:0000269|PubMed:25351493}.
CC -!- DOMAIN: LysM domains are involved in Nod factors perception, especially
CC in chitooligosaccharide-binding. {ECO:0000303|PubMed:16723404,
CC ECO:0000305|PubMed:22087221}.
CC -!- PTM: Highly N-glycosylated. {ECO:0000269|PubMed:16723404}.
CC -!- DISRUPTION PHENOTYPE: Nod(-) phenotype characterized by absence of
CC response to Nod factors (e.g. no rapid calcium flux, no calcium
CC spiking, absence of early nodulin gene expression, and no root hair
CC deformation) (PubMed:12753588). In the nfp-1 mutant, there is impaired
CC nodulation response to S.meliloti, with no root hair curling or
CC infection thread formation and no Nod factor-induced root hair
CC deformation (PubMed:16844829). There are smaller nodules with an
CC aberrant infection zone that contains more cell layers with smaller
CC cells in the central tissue. Infection threads enter the cells, but the
CC release of the bacteria is hampered, and the few released bacteria fail
CC to develop into mature symbiosomes (PubMed:25351493). Increased
CC susceptibility to the root oomycete A.euteiches and to the fungus
CC C.trifolii (PubMed:23432463). {ECO:0000269|PubMed:12753588,
CC ECO:0000269|PubMed:16844829, ECO:0000269|PubMed:23432463,
CC ECO:0000269|PubMed:25351493}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; DQ496250; ABF50224.1; -; Genomic_DNA.
DR EMBL; CM001221; AES94847.1; -; Genomic_DNA.
DR EMBL; AM501337; CAO02956.1; -; Genomic_DNA.
DR EMBL; JX468459; AFX97031.1; -; Genomic_DNA.
DR EMBL; JX468461; AFX97033.1; -; Genomic_DNA.
DR EMBL; JX468518; AFX97090.1; -; Genomic_DNA.
DR RefSeq; XP_003611889.1; XM_003611841.2.
DR PDB; 7AU7; X-ray; 2.55 A; A=27-246.
DR PDBsum; 7AU7; -.
DR AlphaFoldDB; Q0GXS4; -.
DR SMR; Q0GXS4; -.
DR STRING; 3880.AES94847; -.
DR EnsemblPlants; AES94847; AES94847; MTR_5g019040.
DR GeneID; 11410973; -.
DR Gramene; AES94847; AES94847; MTR_5g019040.
DR KEGG; mtr:MTR_5g019040; -.
DR eggNOG; ENOG502QQTK; Eukaryota.
DR HOGENOM; CLU_000288_99_1_1; -.
DR OMA; VHMDIRT; -.
DR OrthoDB; 340934at2759; -.
DR Proteomes; UP000002051; Chromosome 5.
DR ExpressionAtlas; Q0GXS4; differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005775; C:vacuolar lumen; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009877; P:nodulation; IMP:UniProtKB.
DR GO; GO:1902290; P:positive regulation of defense response to oomycetes; IMP:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IDA:UniProtKB.
DR GO; GO:1900150; P:regulation of defense response to fungus; IMP:UniProtKB.
DR GO; GO:0002237; P:response to molecule of bacterial origin; IMP:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Glycoprotein; Kinase; Membrane;
KW Nodulation; Nucleotide-binding; Plant defense; Receptor;
KW Reference proteome; Repeat; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Tyrosine-protein kinase; Vacuole.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..595
FT /note="Serine/threonine receptor-like kinase NFP"
FT /evidence="ECO:0000255"
FT /id="PRO_5006740226"
FT TOPO_DOM 28..246
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..595
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 51..98
FT /note="LysM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 113..160
FT /note="LysM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 284..573
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 435
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 290..298
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 339
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 154
FT /note="Required for nodulation"
FT /evidence="ECO:0000269|PubMed:22087221"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 67
FT /note="S->F: In nfp-2; impaired nodulation response to
FT S.meliloti, with no root hair curling or infection thread
FT formation and no Nod factor-induced root hair deformation.
FT Increased susceptibility to the root oomycete A.euteiches
FT and to the fungus C.trifolii."
FT /evidence="ECO:0000269|PubMed:16844829,
FT ECO:0000269|PubMed:23432463"
FT MUTAGEN 154
FT /note="L->P: Impaired nodulation upon S. meliloti
FT infection."
FT /evidence="ECO:0000269|PubMed:22087221"
FT CONFLICT 314
FT /note="T -> M (in Ref. 4; CAO02956)"
FT /evidence="ECO:0000305"
FT CONFLICT 536..539
FT /note="LASL -> MASW (in Ref. 4; CAO02956)"
FT /evidence="ECO:0000305"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:7AU7"
FT STRAND 45..54
FT /evidence="ECO:0007829|PDB:7AU7"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:7AU7"
FT HELIX 63..67
FT /evidence="ECO:0007829|PDB:7AU7"
FT TURN 68..71
FT /evidence="ECO:0007829|PDB:7AU7"
FT HELIX 74..81
FT /evidence="ECO:0007829|PDB:7AU7"
FT STRAND 95..105
FT /evidence="ECO:0007829|PDB:7AU7"
FT STRAND 108..116
FT /evidence="ECO:0007829|PDB:7AU7"
FT HELIX 123..128
FT /evidence="ECO:0007829|PDB:7AU7"
FT TURN 129..133
FT /evidence="ECO:0007829|PDB:7AU7"
FT HELIX 137..143
FT /evidence="ECO:0007829|PDB:7AU7"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:7AU7"
FT HELIX 169..173
FT /evidence="ECO:0007829|PDB:7AU7"
FT STRAND 178..184
FT /evidence="ECO:0007829|PDB:7AU7"
FT HELIX 190..197
FT /evidence="ECO:0007829|PDB:7AU7"
FT HELIX 201..208
FT /evidence="ECO:0007829|PDB:7AU7"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:7AU7"
FT STRAND 218..226
FT /evidence="ECO:0007829|PDB:7AU7"
SQ SEQUENCE 595 AA; 66014 MW; 5E52FF7A8AA1F0EA CRC64;
MSAFFLPSSS HALFLVLMLF FLTNISAQPL YISETNFTCP VDSPPSCETY VAYRAQSPNF
LSLSNISDIF NLSPLRIAKA SNIEAEDKKL IPDQLLLVPV TCGCTKNHSF ANITYSIKQG
DNFFILSITS YQNLTNYLEF KNFNPNLSPT LLPLDTKVSV PLFCKCPSKN QLNKGIKYLI
TYVWQDNDNV TLVSSKFGAS QVEMLAENNH NFTASTNRSV LIPVTSLPKL DQPSSNGRKS
SSQNLALIIG ISLGSAFFIL VLTLSLVYVY CLKMKRLNRS TSSSETADKL LSGVSGYVSK
PTMYEIDAIM EGTTNLSDNC KIGESVYKAN IDGRVLAVKK IKKDASEELK ILQKVNHGNL
VKLMGVSSDN DGNCFLVYEY AENGSLEEWL FSESSKTSNS VVSLTWSQRI TIAMDVAIGL
QYMHEHTYPR IIHRDITTSN ILLGSNFKAK IANFGMARTS TNSMMPKIDV FAFGVVLIEL
LTGKKAMTTK ENGEVVILWK DFWKIFDLEG NREERLRKWM DPKLESFYPI DNALSLASLA
VNCTADKSLS RPTIAEIVLC LSLLNQPSSE PMLERSLTSG LDAEATHVVT SVIAR
