CESA4_ARATH
ID CESA4_ARATH Reviewed; 1049 AA.
AC Q84JA6; Q0WQW9; Q8GZN8; Q9FNC3;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Cellulose synthase A catalytic subunit 4 [UDP-forming];
DE Short=AtCesA4;
DE EC=2.4.1.12;
DE AltName: Full=Protein IRREGULAR XYLEM 5;
DE Short=AtIRX5;
GN Name=CESA4; Synonyms=IRX5; OrderedLocusNames=At5g44030; ORFNames=MRH10.14;
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], FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH
RP CESA7 AND CESA8, AND MUTAGENESIS OF 989-TRP--CYS-1049.
RX PubMed=12538856; DOI=10.1073/pnas.0337628100;
RA Taylor N.G., Howells R.M., Huttly A.K., Vickers K., Turner S.R.;
RT "Interactions among three distinct CesA proteins essential for cellulose
RT synthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1450-1455(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
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 Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11178255; DOI=10.1186/gb-2000-1-4-reviews3001;
RA Richmond T.;
RT "Higher plant cellulose synthases.";
RL Genome Biol. 1:REVIEWS3001.1-REVIEWS3001.6(2000).
RN [7]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=10938350; DOI=10.1104/pp.123.4.1313;
RA Holland N., Holland D., Helentjaris T., Dhugga K.S., Xoconostle-Cazares B.,
RA Delmer D.P.;
RT "A comparative analysis of the plant cellulose synthase (CesA) gene
RT family.";
RL Plant Physiol. 123:1313-1324(2000).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=12481071; DOI=10.1104/pp.102.010603;
RA Beeckman T., Przemeck G.K.H., Stamatiou G., Lau R., Terryn N., De Rycke R.,
RA Inze D., Berleth T.;
RT "Genetic complexity of cellulose synthase A gene function in Arabidopsis
RT embryogenesis.";
RL Plant Physiol. 130:1883-1893(2002).
RN [9]
RP SUBUNIT.
RX PubMed=12897249; DOI=10.1105/tpc.012815;
RA Gardiner J.C., Taylor N.G., Turner S.R.;
RT "Control of cellulose synthase complex localization in developing xylem.";
RL Plant Cell 15:1740-1748(2003).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17351116; DOI=10.1105/tpc.106.048058;
RA Hernandez-Blanco C., Feng D.X., Hu J., Sanchez-Vallet A., Deslandes L.,
RA Llorente F., Berrocal-Lobo M., Keller H., Barlet X., Sanchez-Rodriguez C.,
RA Anderson L.K., Somerville S., Marco Y., Molina A.;
RT "Impairment of cellulose synthases required for Arabidopsis secondary cell
RT wall formation enhances disease resistance.";
RL Plant Cell 19:890-903(2007).
RN [11]
RP PHOSPHORYLATION AT SER-135, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17427041; DOI=10.1007/s11103-007-9142-2;
RA Taylor N.G.;
RT "Identification of cellulose synthase AtCesA7 (IRX3) in vivo
RT phosphorylation sites -- a potential role in regulating protein
RT degradation.";
RL Plant Mol. Biol. 64:161-171(2007).
RN [12]
RP INTERACTION WITH STL1 AND STL2, AND LACK OF INTERACTION WITH GOT1.
RX PubMed=27277162; DOI=10.1038/ncomms11656;
RA Zhang Y., Nikolovski N., Sorieul M., Vellosillo T., McFarlane H.E.,
RA Dupree R., Kesten C., Schneider R., Driemeier C., Lathe R., Lampugnani E.,
RA Yu X., Ivakov A., Doblin M.S., Mortimer J.C., Brown S.P., Persson S.,
RA Dupree P.;
RT "Golgi-localized STELLO proteins regulate the assembly and trafficking of
RT cellulose synthase complexes in Arabidopsis.";
RL Nat. Commun. 7:11656-11656(2016).
RN [13]
RP S-ACYLATION.
RX PubMed=27387950; DOI=10.1126/science.aaf4009;
RA Kumar M., Wightman R., Atanassov I., Gupta A., Hurst C.H., Hemsley P.A.,
RA Turner S.;
RT "S-acylation of the cellulose synthase complex is essential for its plasma
RT membrane localization.";
RL Science 353:166-169(2016).
CC -!- FUNCTION: Catalytic subunit of cellulose synthase terminal complexes
CC ('rosettes'), required for beta-1,4-glucan microfibril crystallization,
CC a major mechanism of the cell wall formation. Involved in the secondary
CC cell wall formation. Required for the xylem cell wall thickening.
CC {ECO:0000269|PubMed:12538856, ECO:0000269|PubMed:17351116}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-
CC beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:19929, Rhea:RHEA-
CC COMP:10033, Rhea:RHEA-COMP:10034, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18246, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.12;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Glycan metabolism; plant cellulose biosynthesis.
CC -!- SUBUNIT: Interacts with CESA7 and CESA8. Assembly with CESA7 and CESA8
CC is required for functional complex and localization in secondary cell
CC wall deposition sites. Interacts with STL1 and STL2, but not with GOT1
CC (PubMed:27277162). {ECO:0000269|PubMed:12538856,
CC ECO:0000269|PubMed:12897249, ECO:0000269|PubMed:27277162}.
CC -!- INTERACTION:
CC Q84JA6; Q84JA6: CESA4; NbExp=3; IntAct=EBI-8579072, EBI-8579072;
CC Q84JA6; Q9SWW6: CESA7; NbExp=7; IntAct=EBI-8579072, EBI-4477361;
CC Q84JA6; Q8LPK5: CESA8; NbExp=4; IntAct=EBI-8579072, EBI-8579199;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Confined to secondary cell wall developing tissues
CC such as xylems and interfascicular regions. Expressed in roots,
CC hypocotyls, leaves, inflorescences and flowers.
CC {ECO:0000269|PubMed:10938350, ECO:0000269|PubMed:12481071,
CC ECO:0000269|PubMed:12538856}.
CC -!- DEVELOPMENTAL STAGE: Not expressed in embryos. In young leaves,
CC localized in transient patches along the vascular system. In young
CC inflorescence stems, observed in vascular bundles of primary xylems. In
CC maturing inflorescence stems, most pronounced in regions of developing
CC interfascicular fibers. {ECO:0000269|PubMed:10938350}.
CC -!- PTM: S-acylated. {ECO:0000269|PubMed:27387950}.
CC -!- DISRUPTION PHENOTYPE: Enhanced resistance to the pathogens Ralstonia
CC solanacearum and Plectosphaerella cucumerina.
CC {ECO:0000269|PubMed:17351116}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. Plant
CC cellulose synthase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09063.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF458083; AAO15532.1; -; mRNA.
DR EMBL; AB006703; BAB09063.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED95050.1; -; Genomic_DNA.
DR EMBL; BT005710; AAO64130.1; -; mRNA.
DR EMBL; BT006111; AAP04096.1; -; mRNA.
DR EMBL; AK228561; BAF00480.1; -; mRNA.
DR RefSeq; NP_199216.2; NM_123770.4.
DR AlphaFoldDB; Q84JA6; -.
DR SMR; Q84JA6; -.
DR BioGRID; 19676; 7.
DR IntAct; Q84JA6; 2.
DR MINT; Q84JA6; -.
DR STRING; 3702.AT5G44030.1; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR TCDB; 4.D.3.1.7; the glycan glucosyl transferase (opgh) family.
DR iPTMnet; Q84JA6; -.
DR SwissPalm; Q84JA6; -.
DR PaxDb; Q84JA6; -.
DR PRIDE; Q84JA6; -.
DR ProteomicsDB; 220473; -.
DR EnsemblPlants; AT5G44030.1; AT5G44030.1; AT5G44030.
DR GeneID; 834426; -.
DR Gramene; AT5G44030.1; AT5G44030.1; AT5G44030.
DR KEGG; ath:AT5G44030; -.
DR Araport; AT5G44030; -.
DR TAIR; locus:2172457; AT5G44030.
DR eggNOG; ENOG502QPUN; Eukaryota.
DR HOGENOM; CLU_001418_0_2_1; -.
DR InParanoid; Q84JA6; -.
DR PhylomeDB; Q84JA6; -.
DR BioCyc; MetaCyc:MON-2364; -.
DR BRENDA; 2.4.1.12; 399.
DR UniPathway; UPA00695; -.
DR PRO; PR:Q84JA6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q84JA6; baseline and differential.
DR Genevisible; Q84JA6; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016760; F:cellulose synthase (UDP-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0016759; F:cellulose synthase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0030244; P:cellulose biosynthetic process; IMP:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0009833; P:plant-type primary cell wall biogenesis; IBA:GO_Central.
DR GO; GO:0009834; P:plant-type secondary cell wall biogenesis; IMP:TAIR.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR005150; Cellulose_synth.
DR InterPro; IPR027934; CES_Znf_RING.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF03552; Cellulose_synt; 1.
DR Pfam; PF14569; zf-UDP; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall biogenesis/degradation; Cellulose biosynthesis;
KW Coiled coil; Glycoprotein; Glycosyltransferase; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Zinc; Zinc-finger.
FT CHAIN 1..1049
FT /note="Cellulose synthase A catalytic subunit 4 [UDP-
FT forming]"
FT /id="PRO_0000166370"
FT TOPO_DOM 1..215
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 237..239
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..831
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 832..852
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 853..857
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 858..878
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 879..895
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 896..916
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 917..945
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 946..966
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 967..977
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 978..998
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 999..1007
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1008..1028
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1029..1049
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ZN_FING 23..69
FT /note="RING-type; degenerate"
FT REGION 76..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 389..416
FT /evidence="ECO:0000255"
FT COMPBIAS 77..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 335
FT /evidence="ECO:0000255"
FT ACT_SITE 748
FT /evidence="ECO:0000255"
FT BINDING 23
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 26
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 45
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 50
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SWW6"
FT BINDING 501
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 503
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17427041"
FT CARBOHYD 921
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 989..1049
FT /note="Missing: In irx5-2; reduced levels of crystalline
FT cellulose in secondary cell wall, dwarf and dark green,
FT with irregular xylems and thinner cell walls in xylem and
FT interfascicular tissues."
FT /evidence="ECO:0000269|PubMed:12538856"
FT CONFLICT 127
FT /note="W -> C (in Ref. 1; AAO15532)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="Y -> EL (in Ref. 1; AAO15532)"
FT /evidence="ECO:0000305"
FT CONFLICT 542
FT /note="L -> H (in Ref. 1; AAO15532)"
FT /evidence="ECO:0000305"
FT CONFLICT 616..618
FT /note="KSD -> HKSKSSDS (in Ref. 1; AAO15532)"
FT /evidence="ECO:0000305"
FT CONFLICT 630
FT /note="F -> L (in Ref. 1; AAO15532)"
FT /evidence="ECO:0000305"
FT CONFLICT 637
FT /note="T -> N (in Ref. 1; AAO15532)"
FT /evidence="ECO:0000305"
FT CONFLICT 655
FT /note="S -> A (in Ref. 1; AAO15532)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1049 AA; 119599 MW; D6D2B1B73BBC3E41 CRC64;
MEPNTMASFD DEHRHSSFSA KICKVCGDEV KDDDNGQTFV ACHVCVYPVC KPCYEYERSN
GNKCCPQCNT LYKRHKGSPK IAGDEENNGP DDSDDELNIK YRQDGSSIHQ NFAYGSENGD
YNSKQQWRPN GRAFSSTGSV LGKDFEAERD GYTDAEWKER VDKWKARQEK RGLVTKGEQT
NEDKEDDEEE YLDAEARQPL WRKVPISSSK ISPYRIVIVL RLVILVFFFR FRILTPAKDA
YPLWLISVIC EIWFALSWIL DQFPKWFPIN RETYLDRLSM RFERDGEKNK LAPVDVFVST
VDPLKEPPII TANTILSILA VDYPVNKVSC YVSDDGASML LFDTLSETSE FARRWVPFCK
KYNVEPRAPE FYFSEKIDYL KDKVQTTFVK DRRAMKREYE EFKVRINALV AKAQKKPEEG
WVMQDGTPWP GNNTRDHPGM IQVYLGKEGA FDIDGNELPR LVYVSREKRP GYAHHKKAGA
MNAMVRVSAV LTNAPFMLNL DCDHYINNSK AIRESMCFLM DPQLGKKLCY VQFPQRFDGI
DLNDRYANRN IVFFDINMRG LDGIQGPVYV GTGCVFNRPA LYGYEPPVSE KRKKMTCDCW
PSWICCCCGG GNRNHKSDSS KKKSGIKSLF SKLKKKTKKK SDDKTMSSYS RKRSSTEAIF
DLEDIEEGLE GYDELEKSSL MSQKNFEKRF GMSPVFIAST LMENGGLPEA TNTSSLIKEA
IHVISCGYEE KTEWGKEIGW IYGSVTEDIL TGFRMHCRGW KSVYCMPKRP AFKGSAPINL
SDRLHQVLRW ALGSVEIFFS RHCPLWYAWG GKLKILERLA YINTIVYPFT SIPLLAYCTI
PAVCLLTGKF IIPTINNFAS IWFLALFLSI IATAILELRW SGVSINDLWR NEQFWVIGGV
SAHLFAVFQG LLKVLFGVDT NFTVTSKGAS DEADEFGDLY LFKWTTLLIP PTTLIILNMV
GVVAGVSDAI NNGYGSWGPL FGKLFFAFWV IVHLYPFLKG LMGRQNRTPT IVVLWSILLA
SIFSLVWVRI DPFLPKQTGP LLKQCGVDC
