SFR2_ARATH
ID SFR2_ARATH Reviewed; 622 AA.
AC Q93Y07; Q8LAN2; Q8LGU4; Q8LGU5; Q8W578; Q9C8Z2; Q9SDL5;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Galactolipid galactosyltransferase SFR2, chloroplastic {ECO:0000305|PubMed:20798281};
DE EC=2.4.1.184 {ECO:0000269|PubMed:20798281, ECO:0000269|PubMed:25100720};
DE AltName: Full=Galactolipid:galactolipid galactosyltransferase {ECO:0000303|PubMed:15590685};
DE Short=GGGT {ECO:0000303|PubMed:15590685};
DE AltName: Full=Protein SENSITIVE TO FREEZING 2 {ECO:0000303|PubMed:15258268};
DE Short=AtSFR2 {ECO:0000303|PubMed:15258268};
GN Name=SFR2 {ECO:0000303|PubMed:15258268};
GN OrderedLocusNames=At3g06510 {ECO:0000312|Araport:AT3G06510};
GN ORFNames=F5E6.16 {ECO:0000312|EMBL:AAG51335.1};
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 [MRNA] (ISOFORM 1), FUNCTION, INDUCTION, TISSUE
RP SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-234.
RX PubMed=15258268; DOI=10.1105/tpc.104.024018;
RA Thorlby G., Fourrier N., Warren G.;
RT "The SENSITIVE TO FREEZING2 gene, required for freezing tolerance in
RT Arabidopsis thaliana, encodes a beta-glucosidase.";
RL Plant Cell 16:2192-2203(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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] (ISOFORMS 1 AND 2).
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] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-622 (ISOFORM 1).
RX PubMed=10954083; DOI=10.1007/pl00008698;
RA Kofler H., Haeusler R.E., Schulz B., Groener F., Fluegge U.-I., Weber A.;
RT "Molecular characterisation of a new mutant allele of the plastid
RT phosphoglucomutase in Arabidopsis, and complementation of the mutant with
RT the wild-type cDNA.";
RL Mol. Gen. Genet. 263:978-986(2000).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14600212; DOI=10.1105/tpc016675;
RA Kelly A.A., Froehlich J.E., Doermann P.;
RT "Disruption of the two digalactosyldiacylglycerol synthase genes DGD1 and
RT DGD2 in Arabidopsis reveals the existence of an additional enzyme of
RT galactolipid synthesis.";
RL Plant Cell 15:2694-2706(2003).
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15604686; DOI=10.1007/s11103-004-0790-1;
RA Xu Z., Escamilla-Trevino L.L., Zeng L., Lalgondar M., Bevan D.R.,
RA Winkel B.S.J., Mohamed A., Cheng C.-L., Shih M.-C., Poulton J.E., Esen A.;
RT "Functional genomic analysis of Arabidopsis thaliana glycoside hydrolase
RT family 1.";
RL Plant Mol. Biol. 55:343-367(2004).
RN [9]
RP REVIEW.
RX PubMed=15590685; DOI=10.1074/jbc.r400032200;
RA Benning C., Ohta H.;
RT "Three enzyme systems for galactoglycerolipid biosynthesis are coordinately
RT regulated in plants.";
RL J. Biol. Chem. 280:2397-2400(2005).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLU-267.
RX PubMed=18466306; DOI=10.1111/j.1365-313x.2008.03549.x;
RA Fourrier N., Bedard J., Lopez-Juez E., Barbrook A., Bowyer J., Jarvis P.,
RA Warren G., Thorlby G.;
RT "A role for SENSITIVE TO FREEZING2 in protecting chloroplasts against
RT freeze-induced damage in Arabidopsis.";
RL Plant J. 55:734-745(2008).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=20798281; DOI=10.1126/science.1191803;
RA Moellering E.R., Muthan B., Benning C.;
RT "Freezing tolerance in plants requires lipid remodeling at the outer
RT chloroplast membrane.";
RL Science 330:226-228(2010).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TOPOLOGY, 3D-STRUCTURE
RP MODELING, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF 1-MET--SER-27;
RP GLU-267; ILE-270; MET-273; LEU-274 AND GLU-429.
RX PubMed=25100720; DOI=10.1074/jbc.m114.576694;
RA Roston R.L., Wang K., Kuhn L.A., Benning C.;
RT "Structural determinants allowing transferase activity in SENSITIVE TO
RT FREEZING 2, classified as a family I glycosyl hydrolase.";
RL J. Biol. Chem. 289:26089-26106(2014).
CC -!- FUNCTION: Glycosyl hydrolase family protein acting primarily as a
CC highly specific galactosyltransferase (PubMed:25100720). Synthesizes
CC digalactosyldiacylglycerol from monogalactosyldiacylglycerol in the
CC absence of UDP-galactose in vitro (PubMed:14600212). Hydrolyzes o- and
CC p-nitrophenyl beta-D-glucoside in vitro (PubMed:15258268). Plays a role
CC in freezing tolerance (PubMed:15258268, PubMed:18466306,
CC PubMed:20798281). May play a role in chloroplast protection
CC (PubMed:18466306). {ECO:0000269|PubMed:14600212,
CC ECO:0000269|PubMed:15258268, ECO:0000269|PubMed:18466306,
CC ECO:0000269|PubMed:20798281, ECO:0000269|PubMed:25100720}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a 1,2-diacyl-3-O-(beta-D-galactosyl)-sn-glycerol = a 1,2-
CC diacyl-3-O-[beta-D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol +
CC a 1,2-diacyl-sn-glycerol; Xref=Rhea:RHEA:15921, ChEBI:CHEBI:17615,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:87082; EC=2.4.1.184;
CC Evidence={ECO:0000269|PubMed:20798281, ECO:0000269|PubMed:25100720};
CC -!- ACTIVITY REGULATION: Induced by MgCl(2). {ECO:0000269|PubMed:20798281}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:25100720};
CC Temperature dependence:
CC Optimum temperature is 24 degrees Celsius.
CC {ECO:0000269|PubMed:25100720};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:14600212}. Plastid, chloroplast outer membrane
CC {ECO:0000269|PubMed:18466306, ECO:0000269|PubMed:25100720}; Single-pass
CC type II membrane protein {ECO:0000269|PubMed:25100720}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q93Y07-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q93Y07-2; Sequence=VSP_038516;
CC -!- TISSUE SPECIFICITY: Expressed in hypocotyls, cotyledons, stems, leaves,
CC pedicels, sepals, anthers and pistils. Limited expression in roots. Not
CC detected in petals or filaments. {ECO:0000269|PubMed:15258268}.
CC -!- INDUCTION: Not induced by cold, dehydration, salt or abscisic acid.
CC {ECO:0000269|PubMed:15258268}.
CC -!- DISRUPTION PHENOTYPE: Sensitive to freezing (PubMed:15258268,
CC PubMed:20798281). Loss of tri- and tetragalactosyldiacylglycerol
CC accumulation during freezing (PubMed:20798281).
CC {ECO:0000269|PubMed:15258268, ECO:0000269|PubMed:20798281}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51335.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ491320; CAD36512.1; -; mRNA.
DR EMBL; AJ491321; CAD36513.1; -; mRNA.
DR EMBL; AJ491322; CAD36514.1; -; mRNA.
DR EMBL; AC020580; AAG51335.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74404.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74405.1; -; Genomic_DNA.
DR EMBL; AF419582; AAL31914.1; -; mRNA.
DR EMBL; AY059889; AAL24371.1; -; mRNA.
DR EMBL; BT002100; AAN72111.1; -; mRNA.
DR EMBL; AY087713; AAM65250.1; -; mRNA.
DR EMBL; AF219380; AAF23823.1; -; mRNA.
DR RefSeq; NP_001118591.1; NM_001125119.2. [Q93Y07-2]
DR RefSeq; NP_566285.1; NM_111527.3. [Q93Y07-1]
DR AlphaFoldDB; Q93Y07; -.
DR SMR; Q93Y07; -.
DR BioGRID; 5164; 1.
DR STRING; 3702.AT3G06510.2; -.
DR SwissLipids; SLP:000001450; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PRIDE; Q93Y07; -.
DR ProteomicsDB; 234557; -. [Q93Y07-1]
DR EnsemblPlants; AT3G06510.1; AT3G06510.1; AT3G06510. [Q93Y07-1]
DR EnsemblPlants; AT3G06510.2; AT3G06510.2; AT3G06510. [Q93Y07-2]
DR GeneID; 819829; -.
DR Gramene; AT3G06510.1; AT3G06510.1; AT3G06510. [Q93Y07-1]
DR Gramene; AT3G06510.2; AT3G06510.2; AT3G06510. [Q93Y07-2]
DR KEGG; ath:AT3G06510; -.
DR Araport; AT3G06510; -.
DR TAIR; locus:2084319; AT3G06510.
DR eggNOG; KOG0626; Eukaryota.
DR InParanoid; Q93Y07; -.
DR OMA; DYIHEKS; -.
DR OrthoDB; 408001at2759; -.
DR PhylomeDB; Q93Y07; -.
DR BioCyc; ARA:AT3G06510-MON; -.
DR BioCyc; MetaCyc:AT3G06510-MON; -.
DR PRO; PR:Q93Y07; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q93Y07; baseline and differential.
DR Genevisible; Q93Y07; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
DR GO; GO:0009707; C:chloroplast outer membrane; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0031359; C:integral component of chloroplast outer membrane; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0102996; F:beta,beta digalactosyldiacylglycerol galactosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008422; F:beta-glucosidase activity; IDA:UniProtKB.
DR GO; GO:0080079; F:cellobiose glucosidase activity; IDA:UniProtKB.
DR GO; GO:0046480; F:galactolipid galactosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008378; F:galactosyltransferase activity; IDA:TAIR.
DR GO; GO:0016757; F:glycosyltransferase activity; IDA:TAIR.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0009409; P:response to cold; IMP:UniProtKB.
DR GO; GO:0050826; P:response to freezing; IMP:TAIR.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR018120; Glyco_hydro_1_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10353; PTHR10353; 1.
DR Pfam; PF00232; Glyco_hydro_1; 2.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Glycosidase; Hydrolase; Membrane;
KW Plastid; Plastid outer membrane; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..622
FT /note="Galactolipid galactosyltransferase SFR2,
FT chloroplastic"
FT /id="PRO_0000390354"
FT TOPO_DOM 1..3
FT /note="Stromal"
FT TRANSMEM 4..24
FT /note="Helical; Signal-anchor"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..622
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:25100720"
FT ACT_SITE 267
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q7XKV4"
FT ACT_SITE 429
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q7XKV4"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P49235"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P49235"
FT BINDING 377
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P49235"
FT BINDING 467
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P49235"
FT BINDING 474..475
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P49235"
FT VAR_SEQ 379
FT /note="Q -> QVRELQVKIAIRSQILINNIAFSRISMLESDSRNQ (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_038516"
FT MUTAGEN 1..27
FT /note="Missing: No effect on transferase activity."
FT /evidence="ECO:0000269|PubMed:25100720"
FT MUTAGEN 234
FT /note="G->D: In sfr2-1; no effect on glucosidase activity,
FT but loss of freezing tolerance."
FT /evidence="ECO:0000269|PubMed:15258268"
FT MUTAGEN 267
FT /note="E->A: Loss of transferase activity."
FT /evidence="ECO:0000269|PubMed:25100720"
FT MUTAGEN 267
FT /note="E->G: Loss of catalytic activity and freezing
FT tolerance."
FT /evidence="ECO:0000269|PubMed:18466306"
FT MUTAGEN 270
FT /note="I->A: Decreased transferase activity. Total loss of
FT transferase activity; when associated with A-273 and A-
FT 274."
FT /evidence="ECO:0000269|PubMed:25100720"
FT MUTAGEN 273
FT /note="M->A: No effect on transferase activity. Total loss
FT of transferase activity; when associated with A-270 and A-
FT 274."
FT /evidence="ECO:0000269|PubMed:25100720"
FT MUTAGEN 274
FT /note="L->A: Decreased transferase activity. Total loss of
FT transferase activity; when associated with A-270 and A-
FT 273."
FT /evidence="ECO:0000269|PubMed:25100720"
FT MUTAGEN 429
FT /note="E->A: Loss of transferase activity."
FT /evidence="ECO:0000269|PubMed:25100720"
FT CONFLICT 7
FT /note="L -> I (in Ref. 6; AAF23823)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="P -> H (in Ref. 4; AAL31914)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="C -> W (in Ref. 6; AAF23823)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="A -> S (in Ref. 6; AAF23823)"
FT /evidence="ECO:0000305"
FT CONFLICT 182..183
FT /note="MP -> KH (in Ref. 1; CAD36514)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="W -> C (in Ref. 5; AAM65250)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="G -> D (in Ref. 5; AAM65250)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="G -> D (in Ref. 1; CAD36513)"
FT /evidence="ECO:0000305"
FT CONFLICT 564..571
FT /note="RDWRFGHY -> TRLAVGPLN (in Ref. 6; AAF23823)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 622 AA; 70779 MW; 3680EFBCC112DEE1 CRC64;
MELFALLIKV AGLLATVTVG ANVVSYSRFR RQNLAKFRSP IDESKEVLAD FNSIEHEEGK
FFFGLATAPA HAEDDLDDAW LQFAKETPCS AEEAEAADKK ARRKKVKLAV GAITKGLAKN
THGKEDKNAA DKPPSKNVAA WHNAPHAEDR LKFWSDPDKE VKLAKDTGVT VFRMGVDWSR
IMPVEPTKGI KEAVNYEAVE HYKWILKKVR SNGMKVMLTL FHHSLPPWAA DYGGWKMEKT
VDYFMDFTRI VVDSMYDLVD SWVTFNEPHI FTMLTYMCGS WPGNNPDFLE IATSTLPMGV
FHRALHWMAV AHSKAYDYIH GKISLKKPLV GVAHHVSFMR PYGLFDIGAV TISNSLTIFP
YIDSICEKLD FIGINYYGQE AVCGAGLKLV ETDEYSESGR GVYPDGLYRV LLMFHERYKH
LKVPFIVTEN GVSDETDVIR RPYLIEHLLA LYAAMLKGVP VLGYIFWTIS DNWEWADGYG
PKFGLVAVDR SHDLARTLRQ SYHLFSKIVK SGKVTRKDRS LAWNELQKAA KAGKLRPFYR
GVDNHNLMYA DGLDKPQWRP FVDRDWRFGH YQMDGLQDPL SRVARTLLIW PLIMKKRIRK
VKIKHTDDAG LVLHPALASP FD
