SQD1_ARATH
ID SQD1_ARATH Reviewed; 477 AA.
AC O48917;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=UDP-sulfoquinovose synthase, chloroplastic;
DE EC=3.13.1.1;
DE AltName: Full=Sulfite:UDP-glucose sulfotransferase;
DE AltName: Full=Sulfolipid biosynthesis protein;
DE Flags: Precursor;
GN Name=SQD1; OrderedLocusNames=At4g33030; ORFNames=F26P21.150;
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], SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=cv. Col-2;
RX PubMed=9465123; DOI=10.1073/pnas.95.4.1950;
RA Essigmann B., Gueler S., Narang R.A., Linke D., Benning C.;
RT "Phosphate availability affects the thylakoid lipid composition and the
RT expression of SQD1, a gene required for sulfolipid biosynthesis in
RT Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:1950-1955(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 FUNCTION, AND MUTAGENESIS OF THR-228.
RX PubMed=11073956; DOI=10.1074/jbc.m008200200;
RA Sanda S., Leustek T., Theisen M.J., Garavito R.M., Benning C.;
RT "Recombinant Arabidopsis SQD1 converts UDP-glucose and sulfite to the
RT sulfolipid head group precursor UDP-sulfoquinovose in vitro.";
RL J. Biol. Chem. 276:3941-3946(2001).
RN [6]
RP INDUCTION.
RX PubMed=12805589; DOI=10.1104/pp.103.020941;
RA Hammond J.P., Bennett M.J., Bowen H.C., Broadley M.R., Eastwood D.C.,
RA May S.T., Rahn C., Swarup R., Woolaway K.E., White P.J.;
RT "Changes in gene expression in Arabidopsis shoots during phosphate
RT starvation and the potential for developing smart plants.";
RL Plant Physiol. 132:578-596(2003).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH NAD(+) AND
RP UDP-GLUCOSE, AND ACTIVE SITE.
RX PubMed=10557279; DOI=10.1073/pnas.96.23.13097;
RA Mulichak A.M., Theisen M.J., Essigmann B., Benning C., Garavito R.M.;
RT "Crystal structure of SQD1, an enzyme involved in the biosynthesis of the
RT plant sulfolipid headgroup donor UDP-sulfoquinovose.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:13097-13102(1999).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) OF 86-477 IN COMPLEX WITH NAD;
RP UDP-GLUCOSE AND UDP-SULFOQUINOVOSE.
RA Theisen M.J., Sanda S.L., Ginell S.L., Benning C., Garavito R.M.;
RT "Characterization of the active site of UDP-sulfoquinovose synthase:
RT formation of the sulfonic acid product in the crystalline state.";
RL Submitted (FEB-2001) to the PDB data bank.
CC -!- FUNCTION: Involved in the biosynthesis of sulfolipids found in
CC thylakoid membranes. Converts UDP-glucose and sulfite to the sulfolipid
CC head group precursor UDP-sulfoquinovose. {ECO:0000269|PubMed:11073956}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + sulfite + UDP-alpha-D-glucose = H2O + UDP-alpha-D-6-
CC sulfoquinovose; Xref=Rhea:RHEA:13197, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:60009; EC=3.13.1.1;
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC -!- ACTIVITY REGULATION: Concentrations above 100 uM sulfite inhibit the
CC reaction.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=150 uM for UDP-glucose;
CC KM=10 uM for sulfite;
CC pH dependence:
CC Optimum pH is 7.5-9.5.;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10557279}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:9465123}.
CC -!- INDUCTION: Induced in response to altered availability of inorganic
CC phosphate. {ECO:0000269|PubMed:12805589, ECO:0000269|PubMed:9465123}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
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DR EMBL; AF022082; AAB94073.1; -; mRNA.
DR EMBL; AL031804; CAA21212.1; -; Genomic_DNA.
DR EMBL; AL161582; CAB80020.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86162.1; -; Genomic_DNA.
DR EMBL; AF380641; AAK55722.1; -; mRNA.
DR EMBL; AY113071; AAM47379.1; -; mRNA.
DR PIR; T05311; T05311.
DR RefSeq; NP_195029.1; NM_119457.4.
DR PDB; 1I24; X-ray; 1.20 A; A=86-477.
DR PDB; 1I2B; X-ray; 1.75 A; A=86-477.
DR PDB; 1I2C; X-ray; 1.60 A; A=86-477.
DR PDB; 1QRR; X-ray; 1.60 A; A=84-477.
DR PDBsum; 1I24; -.
DR PDBsum; 1I2B; -.
DR PDBsum; 1I2C; -.
DR PDBsum; 1QRR; -.
DR AlphaFoldDB; O48917; -.
DR SMR; O48917; -.
DR BioGRID; 14725; 8.
DR IntAct; O48917; 1.
DR STRING; 3702.AT4G33030.1; -.
DR iPTMnet; O48917; -.
DR PaxDb; O48917; -.
DR PRIDE; O48917; -.
DR ProteomicsDB; 226854; -.
DR EnsemblPlants; AT4G33030.1; AT4G33030.1; AT4G33030.
DR GeneID; 829440; -.
DR Gramene; AT4G33030.1; AT4G33030.1; AT4G33030.
DR KEGG; ath:AT4G33030; -.
DR Araport; AT4G33030; -.
DR TAIR; locus:2123797; AT4G33030.
DR eggNOG; KOG1371; Eukaryota.
DR HOGENOM; CLU_040971_1_0_1; -.
DR InParanoid; O48917; -.
DR OMA; IHFAEQR; -.
DR OrthoDB; 848823at2759; -.
DR PhylomeDB; O48917; -.
DR BioCyc; MetaCyc:MON-1201; -.
DR BRENDA; 3.13.1.1; 399.
DR EvolutionaryTrace; O48917; -.
DR PRO; PR:O48917; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O48917; baseline and differential.
DR Genevisible; O48917; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0008146; F:sulfotransferase activity; IDA:TAIR.
DR GO; GO:0046507; F:UDPsulfoquinovose synthase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; HDA:TAIR.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IEP:TAIR.
DR GO; GO:0009247; P:glycolipid biosynthetic process; IDA:TAIR.
DR GO; GO:0046506; P:sulfolipid biosynthetic process; IBA:GO_Central.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Hydrolase; NAD; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..86
FT /note="Chloroplast"
FT /evidence="ECO:0000305"
FT CHAIN 87..477
FT /note="UDP-sulfoquinovose synthase, chloroplastic"
FT /id="PRO_0000010469"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 228
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:1QRR"
FT ACT_SITE 265
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:1QRR"
FT ACT_SITE 269
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:1QRR"
FT BINDING 95..96
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:10557279, ECO:0000269|Ref.8,
FT ECO:0007744|PDB:1I24, ECO:0007744|PDB:1I2B,
FT ECO:0007744|PDB:1I2C, ECO:0007744|PDB:1QRR"
FT BINDING 115..119
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:10557279, ECO:0000269|Ref.8,
FT ECO:0007744|PDB:1I24, ECO:0007744|PDB:1I2B,
FT ECO:0007744|PDB:1I2C, ECO:0007744|PDB:1QRR"
FT BINDING 158..159
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:10557279, ECO:0000269|Ref.8,
FT ECO:0007744|PDB:1I24, ECO:0007744|PDB:1I2B,
FT ECO:0007744|PDB:1I2C, ECO:0007744|PDB:1QRR"
FT BINDING 184
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:10557279, ECO:0000269|Ref.8,
FT ECO:0007744|PDB:1I24, ECO:0007744|PDB:1I2B,
FT ECO:0007744|PDB:1I2C, ECO:0007744|PDB:1QRR"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10557279, ECO:0000269|Ref.8,
FT ECO:0007744|PDB:1I24, ECO:0007744|PDB:1I2B,
FT ECO:0007744|PDB:1I2C, ECO:0007744|PDB:1QRR"
FT BINDING 202
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:10557279, ECO:0000269|Ref.8,
FT ECO:0007744|PDB:1I24, ECO:0007744|PDB:1I2B,
FT ECO:0007744|PDB:1I2C, ECO:0007744|PDB:1QRR"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:1QRR"
FT BINDING 265
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:10557279, ECO:0000269|Ref.8,
FT ECO:0007744|PDB:1I24, ECO:0007744|PDB:1I2B,
FT ECO:0007744|PDB:1I2C, ECO:0007744|PDB:1QRR"
FT BINDING 265
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10557279, ECO:0000269|Ref.8,
FT ECO:0007744|PDB:1I24, ECO:0007744|PDB:1I2B,
FT ECO:0007744|PDB:1I2C, ECO:0007744|PDB:1QRR"
FT BINDING 269
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:10557279, ECO:0000269|Ref.8,
FT ECO:0007744|PDB:1I24, ECO:0007744|PDB:1I2B,
FT ECO:0007744|PDB:1I2C, ECO:0007744|PDB:1QRR"
FT BINDING 292
FT /ligand="substrate"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:1QRR"
FT BINDING 295
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:10557279, ECO:0000269|Ref.8,
FT ECO:0007744|PDB:1I24, ECO:0007744|PDB:1I2B,
FT ECO:0007744|PDB:1I2C, ECO:0007744|PDB:1QRR"
FT BINDING 322..325
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10557279, ECO:0000269|Ref.8,
FT ECO:0007744|PDB:1I24, ECO:0007744|PDB:1I2B,
FT ECO:0007744|PDB:1I2C, ECO:0007744|PDB:1QRR"
FT BINDING 337..339
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10557279, ECO:0000269|Ref.8,
FT ECO:0007744|PDB:1I24, ECO:0007744|PDB:1I2B,
FT ECO:0007744|PDB:1I2C, ECO:0007744|PDB:1QRR"
FT BINDING 410..412
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10557279, ECO:0000269|Ref.8,
FT ECO:0007744|PDB:1I24, ECO:0007744|PDB:1I2B,
FT ECO:0007744|PDB:1I2C, ECO:0007744|PDB:1QRR"
FT MUTAGEN 228
FT /note="T->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11073956"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:1I24"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:1I24"
FT HELIX 95..106
FT /evidence="ECO:0007829|PDB:1I24"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:1I24"
FT HELIX 118..126
FT /evidence="ECO:0007829|PDB:1I24"
FT HELIX 137..148
FT /evidence="ECO:0007829|PDB:1I24"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:1I24"
FT HELIX 162..172
FT /evidence="ECO:0007829|PDB:1I24"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:1I24"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:1I24"
FT HELIX 193..217
FT /evidence="ECO:0007829|PDB:1I24"
FT STRAND 222..226
FT /evidence="ECO:0007829|PDB:1I24"
FT HELIX 229..232
FT /evidence="ECO:0007829|PDB:1I24"
FT STRAND 241..248
FT /evidence="ECO:0007829|PDB:1I24"
FT STRAND 251..256
FT /evidence="ECO:0007829|PDB:1I24"
FT HELIX 264..283
FT /evidence="ECO:0007829|PDB:1I24"
FT STRAND 286..292
FT /evidence="ECO:0007829|PDB:1I24"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:1I24"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:1I24"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:1I24"
FT TURN 317..319
FT /evidence="ECO:0007829|PDB:1I24"
FT HELIX 322..332
FT /evidence="ECO:0007829|PDB:1I24"
FT STRAND 336..339
FT /evidence="ECO:0007829|PDB:1I24"
FT STRAND 345..350
FT /evidence="ECO:0007829|PDB:1I24"
FT HELIX 351..363
FT /evidence="ECO:0007829|PDB:1I24"
FT STRAND 371..376
FT /evidence="ECO:0007829|PDB:1I24"
FT STRAND 378..382
FT /evidence="ECO:0007829|PDB:1I24"
FT HELIX 383..395
FT /evidence="ECO:0007829|PDB:1I24"
FT TURN 396..398
FT /evidence="ECO:0007829|PDB:1I24"
FT STRAND 403..406
FT /evidence="ECO:0007829|PDB:1I24"
FT HELIX 424..427
FT /evidence="ECO:0007829|PDB:1I24"
FT HELIX 437..449
FT /evidence="ECO:0007829|PDB:1I24"
FT HELIX 451..453
FT /evidence="ECO:0007829|PDB:1I24"
FT HELIX 456..458
FT /evidence="ECO:0007829|PDB:1I24"
FT TURN 465..467
FT /evidence="ECO:0007829|PDB:1I24"
FT STRAND 469..471
FT /evidence="ECO:0007829|PDB:1I2C"
SQ SEQUENCE 477 AA; 53114 MW; 25F7304C10B025A9 CRC64;
MAHLLSASCP SVISLSSSSS KNSVKPFVSG QTFFNAQLLS RSSLKGLLFQ EKKPRKSCVF
RATAVPITQQ APPETSTNNS SSKPKRVMVI GGDGYCGWAT ALHLSKKNYE VCIVDNLVRR
LFDHQLGLES LTPIASIHDR ISRWKALTGK SIELYVGDIC DFEFLAESFK SFEPDSVVHF
GEQRSAPYSM IDRSRAVYTQ HNNVIGTLNV LFAIKEFGEE CHLVKLGTMG EYGTPNIDIE
EGYITITHNG RTDTLPYPKQ ASSFYHLSKV HDSHNIAFTC KAWGIRATDL NQGVVYGVKT
DETEMHEELR NRLDYDAVFG TALNRFCVQA AVGHPLTVYG KGGQTRGYLD IRDTVQCVEI
AIANPAKAGE FRVFNQFTEQ FSVNELASLV TKAGSKLGLD VKKMTVPNPR VEAEEHYYNA
KHTKLMELGL EPHYLSDSLL DSLLNFAVQF KDRVDTKQIM PSVSWKKIGV KTKSMTT
