SUNN_MEDTR
ID SUNN_MEDTR Reviewed; 974 AA.
AC G7JIK2; A0A396I6W1; Q4QVZ7;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 11-DEC-2019, sequence version 2.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Leucine-rich repeat receptor-like kinase protein SUNN {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=Protein SUPER NUMERIC NODULES {ECO:0000303|PubMed:16240175};
DE Flags: Precursor;
GN Name=SUNN {ECO:0000303|PubMed:16240175};
GN OrderedLocusNames=MTR_4g070970 {ECO:0000312|EMBL:AES89185.1};
GN ORFNames=MtrunA17_Chr4g0035451 {ECO:0000312|EMBL:RHN61330.1};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF SER-575 AND ARG-950.
RX PubMed=16240175; DOI=10.1007/s11103-005-8102-y;
RA Schnabel E., Journet E.P., de Carvalho-Niebel F., Duc G., Frugoli J.;
RT "The Medicago truncatula SUNN gene encodes a CLV1-like leucine-rich repeat
RT receptor kinase that regulates nodule number and root length.";
RL Plant Mol. Biol. 58:809-822(2005).
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jemalong A17;
RX PubMed=30397259; DOI=10.1038/s41477-018-0286-7;
RA Pecrix Y., Staton S.E., Sallet E., Lelandais-Briere C., Moreau S.,
RA Carrere S., Blein T., Jardinaud M.F., Latrasse D., Zouine M., Zahm M.,
RA Kreplak J., Mayjonade B., Satge C., Perez M., Cauet S., Marande W.,
RA Chantry-Darmon C., Lopez-Roques C., Bouchez O., Berard A., Debelle F.,
RA Munos S., Bendahmane A., Berges H., Niebel A., Buitink J., Frugier F.,
RA Benhamed M., Crespi M., Gouzy J., Gamas P.;
RT "Whole-genome landscape of Medicago truncatula symbiotic genes.";
RL Nat. Plants 4:1017-1025(2018).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16941903; DOI=10.1094/mpmi-19-0988;
RA Amiour N., Recorbet G., Robert F., Gianinazzi S., Dumas-Gaudot E.;
RT "Mutations in DMI3 and SUNN modify the appressorium-responsive root
RT proteome in arbuscular mycorrhiza.";
RL Mol. Plant Microbe Interact. 19:988-997(2006).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22168914; DOI=10.1111/j.1365-313x.2011.04881.x;
RA Mortier V., De Wever E., Vuylsteke M., Holsters M., Goormachtig S.;
RT "Nodule numbers are governed by interaction between CLE peptides and
RT cytokinin signaling.";
RL Plant J. 70:367-376(2012).
RN [7]
RP FUNCTION.
RX PubMed=22399647; DOI=10.1104/pp.112.194993;
RA Jin J., Watt M., Mathesius U.;
RT "The autoregulation gene SUNN mediates changes in root organ formation in
RT response to nitrogen through alteration of shoot-to-root auxin transport.";
RL Plant Physiol. 159:489-500(2012).
RN [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=22301956; DOI=10.4161/psb.7.1.18491;
RA Schnabel E., Karve A., Kassaw T., Mukherjee A., Zhou X., Hall T.,
RA Frugoli J.;
RT "The M. truncatula SUNN gene is expressed in vascular tissue, similarly to
RT RDN1, consistent with the role of these nodulation regulation genes in long
RT distance signaling.";
RL Plant Signal. Behav. 7:4-6(2012).
RN [9]
RP FUNCTION.
RX PubMed=27135324; DOI=10.3390/plants4020209;
RA Kassaw T., Bridges W. Jr., Frugoli J.;
RT "Multiple Autoregulation of Nodulation (AON) signals identified through
RT split root analysis of Medicago truncatula sunn and rdn1 mutants.";
RL Plants (Basel) 4:209-224(2015).
RN [10]
RP FUNCTION.
RX PubMed=28592666; DOI=10.1104/pp.17.00278;
RA Kassaw T., Nowak S., Schnabel E., Frugoli J.;
RT "ROOT DETERMINED NODULATION1 is required for M. truncatula CLE12, but not
RT CLE13, peptide signaling through the SUNN receptor kinase.";
RL Plant Physiol. 174:2445-2456(2017).
RN [11]
RP FUNCTION.
RX PubMed=31477892; DOI=10.1038/s41477-019-0501-1;
RA Mueller L.M., Flokova K., Schnabel E., Sun X., Fei Z., Frugoli J.,
RA Bouwmeester H.J., Harrison M.J.;
RT "A CLE-SUNN module regulates strigolactone content and fungal colonization
RT in arbuscular mycorrhiza.";
RL Nat. Plants 5:933-939(2019).
CC -!- FUNCTION: LRR receptor kinase involved in the regulation of root growth
CC and root nodule organogenesis (PubMed:16240175, PubMed:16941903,
CC PubMed:22399647). Involved in long distance nodulation signaling events
CC (PubMed:22399647) (Probable). Involved in the autoregulation of
CC nodulation (AON), a long distance systemic signaling from root to shoot
CC and back again, which allows legumes to limit the number of root
CC nodules formed based on available nitrogen and previous rhizobial
CC colonization (PubMed:27135324) (Probable). Acts from shoot to root to
CC control AON (PubMed:27135324, PubMed:28592666). Interacts with CLE12
CC and CLE13 signaling to control nodule numbers (PubMed:22168914).
CC Required for the modulation of shoot-to-root auxin transport in
CC response to altered nitrogen tissue concentrations and in the absence
CC of rhizobia (PubMed:22399647). Shoot-to-root auxin transport influences
CC lateral root density and length (PubMed:22399647). Involved in the
CC regulation of root colonization by arbuscular mycorrhizal (AM) fungi
CC (PubMed:16941903, PubMed:31477892). Interacts with CLE33 and CL53
CC signaling to repress strigolactone biosynthetic genes and strigolactone
CC content in the roots, and consequently reduces the promotion of further
CC colonization by AM fungi (PubMed:31477892).
CC {ECO:0000269|PubMed:16240175, ECO:0000269|PubMed:16941903,
CC ECO:0000269|PubMed:22168914, ECO:0000269|PubMed:22399647,
CC ECO:0000269|PubMed:27135324, ECO:0000269|PubMed:28592666,
CC ECO:0000269|PubMed:31477892, ECO:0000305|PubMed:22168914,
CC ECO:0000305|PubMed:22301956}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000305};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000305};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and shoots (PubMed:16240175).
CC Expressed in the vasculature of leaves, petioles, stems and roots
CC (PubMed:22301956). {ECO:0000269|PubMed:16240175,
CC ECO:0000269|PubMed:22301956}.
CC -!- DISRUPTION PHENOTYPE: Dramatic increase in root nodule number when
CC inoculated with Sinorhizobium meliloti (PubMed:16240175,
CC PubMed:16941903, PubMed:22168914). Inhibition of root growth in both
CC the presence and absence of rhizobia (PubMed:16240175). Increase in
CC arbuscular mycorrhizal (AM) fungus colonization intensity in roots
CC (hypermycorrhizal phenotype) when inoculated with AM fungi
CC (PubMed:16941903). {ECO:0000269|PubMed:16240175,
CC ECO:0000269|PubMed:16941903, ECO:0000269|PubMed:22168914}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AES89185.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=RHN61330.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY769943; AAW71475.1; -; Genomic_DNA.
DR EMBL; CM001220; AES89185.1; ALT_INIT; Genomic_DNA.
DR EMBL; PSQE01000004; RHN61330.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_003606988.1; XM_003606940.2.
DR AlphaFoldDB; G7JIK2; -.
DR SMR; G7JIK2; -.
DR STRING; 3880.AES89185; -.
DR EnsemblPlants; AES89185; AES89185; MTR_4g070970.
DR GeneID; 11439632; -.
DR Gramene; AES89185; AES89185; MTR_4g070970.
DR KEGG; mtr:MTR_4g070970; -.
DR eggNOG; ENOG502QQ4T; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR OrthoDB; 826997at2759; -.
DR Proteomes; UP000002051; Chromosome 4.
DR Proteomes; UP000265566; Chromosome 4.
DR ExpressionAtlas; G7JIK2; differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0033612; F:receptor serine/threonine kinase binding; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR Gene3D; 3.80.10.10; -; 4.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13516; LRR_6; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00369; LRR_TYP; 7.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Differentiation; Glycoprotein;
KW Growth regulation; Kinase; Leucine-rich repeat; Membrane;
KW Nucleotide-binding; Receptor; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..974
FT /note="Leucine-rich repeat receptor-like kinase protein
FT SUNN"
FT /evidence="ECO:0000255"
FT /id="PRO_0000448628"
FT TRANSMEM 635..655
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 92..116
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 117..141
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 143..165
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 166..188
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 189..213
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 238..262
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 263..286
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 288..309
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 310..334
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 335..358
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 360..382
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 383..406
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 407..430
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 431..454
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 456..477
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 478..501
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 503..525
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 527..549
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 550..573
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 574..598
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT DOMAIN 685..972
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 810
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 691..699
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 713
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 508
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 513
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 556
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 585
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 575
FT /note="S->R: In sunn-2; dramatic increase in root nodule
FT number when infected by Sinorhizobium meliloti, and
FT inhibition of root growth in both the presence and absence
FT of rhizobia."
FT /evidence="ECO:0000269|PubMed:16240175"
FT MUTAGEN 950
FT /note="R->K: In sunn-1; dramatic increase in root nodule
FT number when infected by Sinorhizobium meliloti, and
FT inhibition of root growth in both the presence and absence
FT of rhizobia."
FT /evidence="ECO:0000269|PubMed:16240175"
SQ SEQUENCE 974 AA; 107808 MW; 315BF83DFB7AE2A7 CRC64;
MKNITCYLLL LCMLFTTCYS LNNDLDALLK LKKSMKGEKA KDDALKDWKF STSASAHCSF
SGVKCDEDQR VIALNVTQVP LFGHLSKEIG ELNMLESLTI TMDNLTGELP TELSKLTSLR
ILNISHNLFS GNFPGNITFG MKKLEALDAY DNNFEGPLPE EIVSLMKLKY LSFAGNFFSG
TIPESYSEFQ KLEILRLNYN SLTGKIPKSL SKLKMLKELQ LGYENAYSGG IPPELGSIKS
LRYLEISNAN LTGEIPPSLG NLENLDSLFL QMNNLTGTIP PELSSMRSLM SLDLSINGLS
GEIPETFSKL KNLTLINFFQ NKLRGSIPAF IGDLPNLETL QVWENNFSFV LPQNLGSNGK
FIYFDVTKNH LTGLIPPELC KSKKLKTFIV TDNFFRGPIP NGIGPCKSLE KIRVANNYLD
GPVPPGIFQL PSVQIIELGN NRFNGQLPTE ISGNSLGNLA LSNNLFTGRI PASMKNLRSL
QTLLLDANQF LGEIPAEVFA LPVLTRINIS GNNLTGGIPK TVTQCSSLTA VDFSRNMLTG
EVPKGMKNLK VLSIFNVSHN SISGKIPDEI RFMTSLTTLD LSYNNFTGIV PTGGQFLVFN
DRSFAGNPSL CFPHQTTCSS LLYRSRKSHA KEKAVVIAIV FATAVLMVIV TLHMMRKRKR
HMAKAWKLTA FQKLEFRAEE VVECLKEENI IGKGGAGIVY RGSMANGTDV AIKRLVGQGS
GRNDYGFKAE IETLGRIRHR NIMRLLGYVS NKDTNLLLYE YMPNGSLGEW LHGAKGCHLS
WEMRYKIAVE AAKGLCYLHH DCSPLIIHRD VKSNNILLDA DFEAHVADFG LAKFLYDPGA
SQSMSSIAGS YGYIAPEYAY TLKVDEKSDV YSFGVVLLEL IIGRKPVGEF GDGVDIVGWI
NKTELELYQP SDKALVSAVV DPRLNGYPLT SVIYMFNIAM MCVKEMGPAR PTMREVVHML
TNPPHSTSHN LINL
