IRX14_ARATH
ID IRX14_ARATH Reviewed; 525 AA.
AC Q8L707; O23194;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Beta-1,4-xylosyltransferase IRX14 {ECO:0000305};
DE EC=2.4.2.24 {ECO:0000269|PubMed:22080591};
DE AltName: Full=Protein IRREGULAR XYLEM 14 {ECO:0000303|PubMed:17944810};
DE AltName: Full=Xylan xylosyltransferase IRX14 {ECO:0000305};
GN Name=IRX14 {ECO:0000303|PubMed:17944810};
GN OrderedLocusNames=At4g36890 {ECO:0000312|Araport:AT4G36890};
GN ORFNames=AP22.51 {ECO:0000312|EMBL:CAB16800.1},
GN C7A10.470 {ECO:0000312|EMBL:CAB16800.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17944810; DOI=10.1111/j.1365-313x.2007.03307.x;
RA Brown D.M., Goubet F., Wong V.W., Goodacre R., Stephens E., Dupree P.,
RA Turner S.R.;
RT "Comparison of five xylan synthesis mutants reveals new insight into the
RT mechanisms of xylan synthesis.";
RL Plant J. 52:1154-1168(2007).
RN [7]
RP FUNCTION.
RX PubMed=20595206; DOI=10.1093/mp/ssq028;
RA Keppler B.D., Showalter A.M.;
RT "IRX14 and IRX14-LIKE, two glycosyl transferases involved in glucuronoxylan
RT biosynthesis and drought tolerance in Arabidopsis.";
RL Mol. Plant 3:834-841(2010).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20335400; DOI=10.1104/pp.110.155309;
RA Lee C., Teng Q., Huang W., Zhong R., Ye Z.H.;
RT "The Arabidopsis family GT43 glycosyltransferases form two functionally
RT nonredundant groups essential for the elongation of glucuronoxylan
RT backbone.";
RL Plant Physiol. 153:526-541(2010).
RN [9]
RP FUNCTION.
RX PubMed=20424005; DOI=10.1104/pp.110.154971;
RA Wu A.M., Hoernblad E., Voxeur A., Gerber L., Rihouey C., Lerouge P.,
RA Marchant A.;
RT "Analysis of the Arabidopsis IRX9/IRX9-L and IRX14/IRX14-L pairs of
RT glycosyltransferase genes reveals critical contributions to biosynthesis of
RT the hemicellulose glucuronoxylan.";
RL Plant Physiol. 153:542-554(2010).
RN [10]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=22080591; DOI=10.1093/pcp/pcr158;
RA Lee C., Zhong R., Ye Z.H.;
RT "Arabidopsis family GT43 members are xylan xylosyltransferases required for
RT the elongation of the xylan backbone.";
RL Plant Cell Physiol. 53:135-143(2012).
RN [11]
RP FUNCTION, AND MUTAGENESIS OF 261-ASP-ASP-262; GLN-321 AND CYS-415.
RX PubMed=25118690; DOI=10.1371/journal.pone.0105014;
RA Ren Y., Hansen S.F., Ebert B., Lau J., Scheller H.V.;
RT "Site-directed mutagenesis of IRX9, IRX9L and IRX14 proteins involved in
RT xylan biosynthesis: glycosyltransferase activity is not required for IRX9
RT function in Arabidopsis.";
RL PLoS ONE 9:E105014-E105014(2014).
RN [12]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=26482889; DOI=10.1104/pp.15.01441;
RA Voiniciuc C., Guenl M., Schmidt M.H., Usadel B.;
RT "Highly branched xylan made by IRREGULAR XYLEM14 and MUCILAGE-RELATED21
RT links mucilage to Arabidopsis seeds.";
RL Plant Physiol. 169:2481-2495(2015).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26834178; DOI=10.1093/jxb/erv510;
RA Hu R., Li J., Wang X., Zhao X., Yang X., Tang Q., He G., Zhou G., Kong Y.;
RT "Xylan synthesized by Irregular Xylem 14 (IRX14) maintains the structure of
RT seed coat mucilage in Arabidopsis.";
RL J. Exp. Bot. 67:1243-1257(2016).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30228108; DOI=10.1104/pp.18.00584;
RA Voiniciuc C., Engle K.A., Guenl M., Dieluweit S., Schmidt M.H., Yang J.Y.,
RA Moremen K.W., Mohnen D., Usadel B.;
RT "Identification of key enzymes for pectin synthesis in seed mucilage.";
RL Plant Physiol. 178:1045-1064(2018).
CC -!- FUNCTION: Involved in the synthesis of the hemicellulose
CC glucuronoxylan, a major component of secondary cell walls
CC (PubMed:17944810, PubMed:20595206, PubMed:20335400, PubMed:20424005).
CC Involved in the elongation of glucuronoxylan xylosyl backbone
CC (PubMed:17944810, PubMed:20595206, PubMed:20335400, PubMed:20424005).
CC Xylan xylosyltransferase that acts cooperatively with IRX9 to achieve
CC the successive addition of xylosyl residues during xylan backbone
CC elongation (PubMed:22080591, PubMed:25118690). Required for the proper
CC composition and structural properties of released seed coat mucilage
CC (PubMed:26482889, PubMed:26834178). Required for the production of
CC highly branched xylan polymers in seed coat mucilage (PubMed:26482889,
CC PubMed:26834178). Xylan with xylose side chains seems to be necessary
CC for pectin attachment to the seed surface (PubMed:26482889,
CC PubMed:26834178). Together with MUCI70, required for xylan and pectin
CC synthesis in seed coat epidermal (SCE) cells (PubMed:26482889,
CC PubMed:26834178, PubMed:30228108). {ECO:0000269|PubMed:17944810,
CC ECO:0000269|PubMed:20335400, ECO:0000269|PubMed:20424005,
CC ECO:0000269|PubMed:20595206, ECO:0000269|PubMed:22080591,
CC ECO:0000269|PubMed:25118690, ECO:0000269|PubMed:26482889,
CC ECO:0000269|PubMed:26834178, ECO:0000269|PubMed:30228108}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-beta-D-xylan](n) + UDP-alpha-D-xylose = [(1->4)-beta-
CC D-xylan](n+1) + H(+) + UDP; Xref=Rhea:RHEA:15289, Rhea:RHEA-
CC COMP:9548, Rhea:RHEA-COMP:9549, ChEBI:CHEBI:15378, ChEBI:CHEBI:15447,
CC ChEBI:CHEBI:57632, ChEBI:CHEBI:58223; EC=2.4.2.24;
CC Evidence={ECO:0000269|PubMed:22080591};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15290;
CC Evidence={ECO:0000269|PubMed:22080591};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000305|PubMed:20335400}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:20335400}.
CC -!- TISSUE SPECIFICITY: Expressed in developing interfascicular fibers and
CC xylem cells in stems and developing secondary xylem in roots.
CC {ECO:0000269|PubMed:20335400}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the seed coat at the linear cotyledon
CC and mature green stages, when mucilage synthesis occurs.
CC {ECO:0000269|PubMed:26482889}.
CC -!- DISRUPTION PHENOTYPE: Reduced xylan content in cell wall
CC (PubMed:17944810). Reduced amount and altered composition of seed coat
CC mucilage (PubMed:26482889, PubMed:26834178). Plants missing both MUCI70
CC and IRX14 exhibit a severe reduction in both xylan- and pectin-related
CC sugars in total seed mucilage extracts (PubMed:30228108).
CC {ECO:0000269|PubMed:17944810, ECO:0000269|PubMed:26482889,
CC ECO:0000269|PubMed:26834178, ECO:0000269|PubMed:30228108}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 43 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB16800.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80355.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Z99707; CAB16800.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161590; CAB80355.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86714.1; -; Genomic_DNA.
DR EMBL; AY140036; AAM98177.1; -; mRNA.
DR EMBL; BT014969; AAT47820.1; -; mRNA.
DR PIR; F85435; F85435.
DR RefSeq; NP_195407.2; NM_119853.4.
DR AlphaFoldDB; Q8L707; -.
DR SMR; Q8L707; -.
DR STRING; 3702.AT4G36890.1; -.
DR CAZy; GT43; Glycosyltransferase Family 43.
DR iPTMnet; Q8L707; -.
DR PaxDb; Q8L707; -.
DR PRIDE; Q8L707; -.
DR ProteomicsDB; 247051; -.
DR EnsemblPlants; AT4G36890.1; AT4G36890.1; AT4G36890.
DR GeneID; 829842; -.
DR Gramene; AT4G36890.1; AT4G36890.1; AT4G36890.
DR KEGG; ath:AT4G36890; -.
DR Araport; AT4G36890; -.
DR TAIR; locus:2115090; AT4G36890.
DR eggNOG; KOG1476; Eukaryota.
DR HOGENOM; CLU_042214_1_0_1; -.
DR InParanoid; Q8L707; -.
DR OMA; WTIDPPL; -.
DR OrthoDB; 901158at2759; -.
DR PhylomeDB; Q8L707; -.
DR BioCyc; ARA:AT4G36890-MON; -.
DR BRENDA; 2.4.2.24; 399.
DR PRO; PR:Q8L707; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8L707; baseline and differential.
DR Genevisible; Q8L707; AT.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0000138; C:Golgi trans cisterna; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0047517; F:1,4-beta-D-xylan synthase activity; IMP:TAIR.
DR GO; GO:0015018; F:galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity; IEA:InterPro.
DR GO; GO:0042285; F:xylosyltransferase activity; IMP:TAIR.
DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0010154; P:fruit development; IMP:TAIR.
DR GO; GO:0010417; P:glucuronoxylan biosynthetic process; IMP:TAIR.
DR GO; GO:0048354; P:mucilage biosynthetic process involved in seed coat development; IMP:TAIR.
DR GO; GO:0080001; P:mucilage extrusion from seed coat; IMP:UniProtKB.
DR GO; GO:0048358; P:mucilage pectin biosynthetic process; IMP:UniProtKB.
DR GO; GO:0009834; P:plant-type secondary cell wall biogenesis; IBA:GO_Central.
DR GO; GO:0010246; P:rhamnogalacturonan I biosynthetic process; IGI:TAIR.
DR GO; GO:0048367; P:shoot system development; IMP:TAIR.
DR GO; GO:0045492; P:xylan biosynthetic process; IMP:TAIR.
DR GO; GO:0045491; P:xylan metabolic process; IMP:UniProtKB.
DR GO; GO:0010051; P:xylem and phloem pattern formation; IMP:TAIR.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR005027; Glyco_trans_43.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR10896; PTHR10896; 1.
DR Pfam; PF03360; Glyco_transf_43; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..525
FT /note="Beta-1,4-xylosyltransferase IRX14"
FT /id="PRO_0000407565"
FT TOPO_DOM 1..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..525
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 452..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..502
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 261..262
FT /note="DD->AA: Unable to complement irregular xylem
FT phenotype of irx14 mutant."
FT /evidence="ECO:0000269|PubMed:25118690"
FT MUTAGEN 321
FT /note="Q->A: Complements irregular xylem phenotype of irx14
FT mutant."
FT /evidence="ECO:0000269|PubMed:25118690"
FT MUTAGEN 415
FT /note="C->A: Complements irregular xylem phenotype of irx14
FT mutant."
FT /evidence="ECO:0000269|PubMed:25118690"
SQ SEQUENCE 525 AA; 59099 MW; 025BFCC9A2C1C348 CRC64;
MKLSALHQSY LNRRSNSFRS PTSLDSSVDG SGKSLIAVFW LILHCLCCLI SLVLGFRFSR
LVFFFLFSTS STNLYSLPFR PDLPVKHLDV HTIGRTLDPG ANGTTVVATA TKSSRVVVGR
HGIRIRPWPH PNPVEVMKAH QIIGRVQKEQ KMIFGMKSSK MVIAVTPTYV RTFQALHLTG
VMHSLMLVPY DLVWIVVEAG GATNETGLII AKSGLRTIHV GIDQRMPNTW EDRSKLEVFM
RLQALRVVRE EKLDGIVMFA DDSNMHSMEL FDEIQNVKWF GTVSVGILAH SGNAEEMVLS
MEKRKEMEKE EEEESSSLPV QGPACNSTDQ LIGWHIFNTL PYAGKSAVYI DDVAAVLPQK
LEWSGFVLNS RLLWEEAENK PEWVKDFGSL NENEGVESPL SLLKDPSMVE PLGSCGRQVL
LWWLRVEARA DSKFPPGWII DPPLEITVAA KRTPWPDVPP EPPTKKKDQM PLSQGNTVVV
IPKQQQHPTK IRKPKRKSKK SKHEPRPTDT TTQVYSSSSK HQERN
