INV1_ARATH
ID INV1_ARATH Reviewed; 584 AA.
AC Q43866; Q9LIB8;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Beta-fructofuranosidase, insoluble isoenzyme CWINV1;
DE EC=3.2.1.26;
DE AltName: Full=Cell wall beta-fructosidase 1;
DE Short=AtbetaFRUCT1;
DE AltName: Full=Cell wall invertase 1;
DE Short=AtcwINV1;
DE AltName: Full=Sucrose hydrolase 1;
DE Flags: Precursor;
GN Name=CWINV1; Synonyms=BFRUCT1; OrderedLocusNames=At3g13790;
GN ORFNames=MMM17.26;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=8159800; DOI=10.1104/pp.104.2.809;
RA Schwebel-Dugue N., el Mtili N., Krivitzky M., Jean-Jacques I.,
RA Williams J.H., Thomas M., Kreis M., Lecharny A.;
RT "Arabidopsis gene and cDNA encoding cell-wall invertase.";
RL Plant Physiol. 104:809-810(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=9951726; DOI=10.1007/s004250050481;
RA Tymowska-Lalanne Z., Kreis M.;
RT "Expression of the Arabidopsis thaliana invertase gene family.";
RL Planta 207:259-265(1998).
RN [6]
RP TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12508063; DOI=10.1093/jxb/erg055;
RA Sherson S.M., Alford H.L., Forbes S.M., Wallace G., Smith S.M.;
RT "Roles of cell-wall invertases and monosaccharide transporters in the
RT growth and development of Arabidopsis.";
RL J. Exp. Bot. 54:525-531(2003).
RN [7]
RP FUNCTION.
RX DOI=10.1111/j.1365-3040.2004.01281.x;
RA de Coninck B., Le Roy K., Francis I., Clerens S., Vergauwen R.,
RA Halliday A.M., Smith S.M., Van Laere A., Van Den Ende W.;
RT "Arabidopsis AtcwINV3 and 6 are not invertases but are fructan
RT exohydrolases (FEHs) with different substrate specificities.";
RL Plant Cell Environ. 28:432-443(2005).
RN [8]
RP TISSUE SPECIFICITY, AND INDUCTION BY WOUNDING.
RX PubMed=16339783; DOI=10.1093/jxb/erj039;
RA Quilliam R.S., Swarbrick P.J., Scholes J.D., Rolfe S.A.;
RT "Imaging photosynthesis in wounded leaves of Arabidopsis thaliana.";
RL J. Exp. Bot. 57:55-69(2006).
RN [9]
RP FUNCTION, MUTAGENESIS OF TRP-63; ASP-66; TRP-90; TRP-125; GLU-246; ASP-282
RP AND LYS-285, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE BINDING.
RX PubMed=17873089; DOI=10.1104/pp.107.105049;
RA Le Roy K., Lammens W., Verhaest M., De Coninck B., Rabijns A.,
RA Van Laere A., Van den Ende W.;
RT "Unraveling the difference between invertases and fructan exohydrolases: a
RT single amino acid (Asp-239) substitution transforms Arabidopsis cell wall
RT invertase1 into a fructan 1-exohydrolase.";
RL Plant Physiol. 145:616-625(2007).
RN [10]
RP MUTAGENESIS OF ASN-342.
RX PubMed=17888113; DOI=10.1111/j.1469-8137.2007.02174.x;
RA Le Roy K., Verhaest M., Rabijns A., Clerens S., Van Laere A.,
RA Van den Ende W.;
RT "N-glycosylation affects substrate specificity of chicory fructan 1-
RT exohydrolase: evidence for the presence of an inulin binding cleft.";
RL New Phytol. 176:317-324(2007).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 44-584 IN COMPLEX WITH
RP SUBSTRATES, MUTAGENESIS OF ASN-342, AND GLYCOSYLATION.
RX PubMed=17139091; DOI=10.1107/s0907444906044489;
RA Verhaest M., Lammens W., Le Roy K., De Coninck B., De Ranter C.J.,
RA Van Laere A., Van den Ende W., Rabijns A.;
RT "X-ray diffraction structure of a cell-wall invertase from Arabidopsis
RT thaliana.";
RL Acta Crystallogr. D 62:1555-1563(2006).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 48-584 IN COMPLEX WITH SUBSTRATES,
RP MUTAGENESIS OF ASP-66; GLU-246 AND ASP-282, AND GLYCOSYLATION.
RX PubMed=18258263; DOI=10.1016/j.jmb.2007.12.074;
RA Lammens W., Le Roy K., Van Laere A., Rabijns A., Van den Ende W.;
RT "Crystal structures of Arabidopsis thaliana cell-wall invertase mutants in
RT complex with sucrose.";
RL J. Mol. Biol. 377:378-385(2008).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 48-584 IN COMPLEX WITH SUBSTRATES,
RP MUTAGENESIS OF GLU-246, AND GLYCOSYLATION.
RX PubMed=17963237; DOI=10.1002/prot.21700;
RA Matrai J., Lammens W., Jonckheer A., Le Roy K., Rabijns A.,
RA Van den Ende W., De Maeyer M.;
RT "An alternate sucrose binding mode in the E203Q Arabidopsis invertase
RT mutant: an X-ray crystallography and docking study.";
RL Proteins 71:552-564(2008).
CC -!- FUNCTION: Beta-fructofuranosidase that can use sucrose and 1-kestose,
CC and, to a lower extent, neokestose and levan, as substrates, but not
CC inuline. {ECO:0000269|PubMed:17873089, ECO:0000269|Ref.7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing beta-D-fructofuranoside
CC residues in beta-D-fructofuranosides.; EC=3.2.1.26;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10067};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.35 mM for sucrose (at pH 5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:17873089};
CC KM=1 mM for 1-kestose (at pH 5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:17873089};
CC -!- INTERACTION:
CC Q43866; O49908: LOC107808322; Xeno; NbExp=3; IntAct=EBI-15879417, EBI-15879452;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000305}. Secreted, cell wall {ECO:0000305}. Note=Associated to
CC the cell wall. {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q43866-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, leaves, flowers, and seeds.
CC {ECO:0000269|PubMed:12508063, ECO:0000269|PubMed:16339783,
CC ECO:0000269|PubMed:9951726}.
CC -!- INDUCTION: By wounding, aeroponic growth condition, darkness, sucrose,
CC glucose and mannitol. {ECO:0000269|PubMed:16339783,
CC ECO:0000269|PubMed:9951726}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB01930.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X74514; CAA52619.1; -; mRNA.
DR EMBL; X74515; CAA52620.1; -; mRNA.
DR EMBL; AP001307; BAB01930.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75414.1; -; Genomic_DNA.
DR EMBL; AY045776; AAK76450.1; -; mRNA.
DR EMBL; AY079422; AAL85153.1; -; mRNA.
DR PIR; S37212; S37212.
DR RefSeq; NP_001189881.1; NM_001202952.1.
DR RefSeq; NP_566464.1; NM_112232.4. [Q43866-1]
DR PDB; 2AC1; X-ray; 2.15 A; A=44-584.
DR PDB; 2OXB; X-ray; 2.60 A; A=48-584.
DR PDB; 2QQU; X-ray; 2.84 A; A=48-582.
DR PDB; 2QQV; X-ray; 3.01 A; A=48-584.
DR PDB; 2QQW; X-ray; 2.80 A; A=48-584.
DR PDB; 2XQR; X-ray; 2.58 A; A/C/E/G/I/K=48-584.
DR PDBsum; 2AC1; -.
DR PDBsum; 2OXB; -.
DR PDBsum; 2QQU; -.
DR PDBsum; 2QQV; -.
DR PDBsum; 2QQW; -.
DR PDBsum; 2XQR; -.
DR AlphaFoldDB; Q43866; -.
DR SMR; Q43866; -.
DR BioGRID; 5925; 1.
DR DIP; DIP-59391N; -.
DR IntAct; Q43866; 1.
DR STRING; 3702.AT3G13790.1; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR PaxDb; Q43866; -.
DR PRIDE; Q43866; -.
DR ProteomicsDB; 247028; -. [Q43866-1]
DR EnsemblPlants; AT3G13790.1; AT3G13790.1; AT3G13790. [Q43866-1]
DR GeneID; 820591; -.
DR Gramene; AT3G13790.1; AT3G13790.1; AT3G13790. [Q43866-1]
DR KEGG; ath:AT3G13790; -.
DR Araport; AT3G13790; -.
DR TAIR; locus:2091606; AT3G13790.
DR eggNOG; KOG0228; Eukaryota.
DR HOGENOM; CLU_001528_6_0_1; -.
DR InParanoid; Q43866; -.
DR OrthoDB; 405663at2759; -.
DR PhylomeDB; Q43866; -.
DR BioCyc; ARA:AT3G13790-MON; -.
DR BRENDA; 3.2.1.26; 399.
DR SABIO-RK; Q43866; -.
DR EvolutionaryTrace; Q43866; -.
DR PRO; PR:Q43866; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q43866; baseline and differential.
DR Genevisible; Q43866; AT.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0004564; F:beta-fructofuranosidase activity; IMP:TAIR.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0050832; P:defense response to fungus; IEP:TAIR.
DR GO; GO:0009611; P:response to wounding; IMP:TAIR.
DR Gene3D; 2.115.10.20; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001362; Glyco_hydro_32.
DR InterPro; IPR018053; Glyco_hydro_32_AS.
DR InterPro; IPR013189; Glyco_hydro_32_C.
DR InterPro; IPR013148; Glyco_hydro_32_N.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR Pfam; PF08244; Glyco_hydro_32C; 1.
DR Pfam; PF00251; Glyco_hydro_32N; 1.
DR SMART; SM00640; Glyco_32; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF75005; SSF75005; 1.
DR PROSITE; PS00609; GLYCOSYL_HYDROL_F32; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoplast; Cell wall; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..584
FT /note="Beta-fructofuranosidase, insoluble isoenzyme CWINV1"
FT /id="PRO_0000348347"
FT ACT_SITE 66
FT BINDING 63..66
FT /ligand="substrate"
FT BINDING 82
FT /ligand="substrate"
FT BINDING 90
FT /ligand="substrate"
FT BINDING 125..126
FT /ligand="substrate"
FT BINDING 191..192
FT /ligand="substrate"
FT BINDING 246
FT /ligand="substrate"
FT BINDING 282
FT /ligand="substrate"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 446
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 442..491
FT MUTAGEN 63
FT /note="W->L: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17873089"
FT MUTAGEN 66
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17873089,
FT ECO:0000269|PubMed:18258263"
FT MUTAGEN 90
FT /note="W->L: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17873089"
FT MUTAGEN 125
FT /note="W->L: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17873089"
FT MUTAGEN 246
FT /note="E->A,Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17873089,
FT ECO:0000269|PubMed:17963237, ECO:0000269|PubMed:18258263"
FT MUTAGEN 282
FT /note="D->A: Impaired beta-fructofuranosidase activity but
FT enhanced 1-fructan exohydrolase activity."
FT /evidence="ECO:0000269|PubMed:17873089,
FT ECO:0000269|PubMed:18258263"
FT MUTAGEN 282
FT /note="D->F: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17873089,
FT ECO:0000269|PubMed:18258263"
FT MUTAGEN 282
FT /note="D->N: Normal activity."
FT /evidence="ECO:0000269|PubMed:17873089,
FT ECO:0000269|PubMed:18258263"
FT MUTAGEN 285
FT /note="K->L: Slightly reduced activity."
FT /evidence="ECO:0000269|PubMed:17873089"
FT MUTAGEN 342
FT /note="N->D: Reduced activity and glycosylation."
FT /evidence="ECO:0000269|PubMed:17139091,
FT ECO:0000269|PubMed:17888113"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:2QQU"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:2AC1"
FT STRAND 60..73
FT /evidence="ECO:0007829|PDB:2AC1"
FT STRAND 76..83
FT /evidence="ECO:0007829|PDB:2AC1"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:2AC1"
FT STRAND 94..113
FT /evidence="ECO:0007829|PDB:2AC1"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:2AC1"
FT STRAND 124..131
FT /evidence="ECO:0007829|PDB:2AC1"
FT STRAND 137..144
FT /evidence="ECO:0007829|PDB:2AC1"
FT STRAND 150..158
FT /evidence="ECO:0007829|PDB:2AC1"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:2AC1"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:2AC1"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:2AC1"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:2OXB"
FT STRAND 204..212
FT /evidence="ECO:0007829|PDB:2AC1"
FT STRAND 215..228
FT /evidence="ECO:0007829|PDB:2AC1"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:2AC1"
FT STRAND 245..256
FT /evidence="ECO:0007829|PDB:2AC1"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:2QQW"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:2OXB"
FT STRAND 273..281
FT /evidence="ECO:0007829|PDB:2AC1"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:2AC1"
FT STRAND 287..295
FT /evidence="ECO:0007829|PDB:2AC1"
FT TURN 296..299
FT /evidence="ECO:0007829|PDB:2AC1"
FT STRAND 300..303
FT /evidence="ECO:0007829|PDB:2AC1"
FT STRAND 309..312
FT /evidence="ECO:0007829|PDB:2OXB"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:2AC1"
FT STRAND 322..329
FT /evidence="ECO:0007829|PDB:2AC1"
FT TURN 330..333
FT /evidence="ECO:0007829|PDB:2AC1"
FT STRAND 334..341
FT /evidence="ECO:0007829|PDB:2AC1"
FT HELIX 347..353
FT /evidence="ECO:0007829|PDB:2AC1"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:2OXB"
FT STRAND 363..367
FT /evidence="ECO:0007829|PDB:2AC1"
FT STRAND 371..378
FT /evidence="ECO:0007829|PDB:2AC1"
FT HELIX 380..385
FT /evidence="ECO:0007829|PDB:2AC1"
FT STRAND 391..398
FT /evidence="ECO:0007829|PDB:2AC1"
FT STRAND 402..405
FT /evidence="ECO:0007829|PDB:2AC1"
FT STRAND 413..421
FT /evidence="ECO:0007829|PDB:2AC1"
FT HELIX 425..427
FT /evidence="ECO:0007829|PDB:2AC1"
FT STRAND 428..430
FT /evidence="ECO:0007829|PDB:2AC1"
FT HELIX 438..444
FT /evidence="ECO:0007829|PDB:2AC1"
FT STRAND 452..462
FT /evidence="ECO:0007829|PDB:2AC1"
FT STRAND 466..468
FT /evidence="ECO:0007829|PDB:2AC1"
FT STRAND 470..480
FT /evidence="ECO:0007829|PDB:2AC1"
FT STRAND 486..493
FT /evidence="ECO:0007829|PDB:2AC1"
FT STRAND 501..503
FT /evidence="ECO:0007829|PDB:2OXB"
FT STRAND 508..512
FT /evidence="ECO:0007829|PDB:2AC1"
FT STRAND 520..527
FT /evidence="ECO:0007829|PDB:2AC1"
FT STRAND 530..535
FT /evidence="ECO:0007829|PDB:2AC1"
FT TURN 536..539
FT /evidence="ECO:0007829|PDB:2AC1"
FT STRAND 540..545
FT /evidence="ECO:0007829|PDB:2AC1"
FT STRAND 549..551
FT /evidence="ECO:0007829|PDB:2AC1"
FT HELIX 553..555
FT /evidence="ECO:0007829|PDB:2AC1"
FT STRAND 557..562
FT /evidence="ECO:0007829|PDB:2AC1"
FT STRAND 564..566
FT /evidence="ECO:0007829|PDB:2AC1"
FT STRAND 568..578
FT /evidence="ECO:0007829|PDB:2AC1"
SQ SEQUENCE 584 AA; 66280 MW; C571359FB1825E36 CRC64;
MTKEVCSNIG LWLLLTLLIG NYVVNLEASH HVYKRLTQST NTKSPSVNQP YRTGFHFQPP
KNWMNDPNGP MIYKGIYHLF YQWNPKGAVW GNIVWAHSTS TDLINWDPHP PAIFPSAPFD
INGCWSGSAT ILPNGKPVIL YTGIDPKNQQ VQNIAEPKNL SDPYLREWKK SPLNPLMAPD
AVNGINASSF RDPTTAWLGQ DKKWRVIIGS KIHRRGLAIT YTSKDFLKWE KSPEPLHYDD
GSGMWECPDF FPVTRFGSNG VETSSFGEPN EILKHVLKIS LDDTKHDYYT IGTYDRVKDK
FVPDNGFKMD GTAPRYDYGK YYASKTFFDS AKNRRILWGW TNESSSVEDD VEKGWSGIQT
IPRKIWLDRS GKQLIQWPVR EVERLRTKQV KNLRNKVLKS GSRLEVYGVT AAQADVEVLF
KVRDLEKADV IEPSWTDPQL ICSKMNVSVK SGLGPFGLMV LASKNLEEYT SVYFRIFKAR
QNSNKYVVLM CSDQSRSSLK EDNDKTTYGA FVDINPHQPL SLRALIDHSV VESFGGKGRA
CITSRVYPKL AIGKSSHLFA FNYGYQSVDV LNLNAWSMNS AQIS
