GMPP1_ARATH
ID GMPP1_ARATH Reviewed; 361 AA.
AC O22287; Q9C5B8;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Mannose-1-phosphate guanylyltransferase 1 {ECO:0000305|PubMed:10097187};
DE EC=2.7.7.13 {ECO:0000269|PubMed:10097187};
DE AltName: Full=GDP-mannose pyrophosphorylase 1 {ECO:0000303|Ref.1, ECO:0000303|Ref.3};
DE AltName: Full=Protein CYTOKINESIS DEFECTIVE 1 {ECO:0000303|PubMed:11226227, ECO:0000303|PubMed:9750345, ECO:0000303|Ref.2};
DE AltName: Full=Protein EMBRYO DEFECTIVE 101 {ECO:0000303|PubMed:15266054};
DE AltName: Full=Protein HYPERSENSITIVE TO AMMONIUM ION 1 {ECO:0000303|PubMed:19011088};
DE AltName: Full=Protein SENSITIVE TO OZONE 1 {ECO:0000303|PubMed:8790441};
DE AltName: Full=Protein VITAMIN C DEFECTIVE 1 {ECO:0000303|PubMed:10097187, ECO:0000303|PubMed:10655235, ECO:0000303|PubMed:9390448};
GN Name=CYT1 {ECO:0000303|PubMed:11226227, ECO:0000303|PubMed:9750345,
GN ECO:0000303|Ref.2};
GN Synonyms=EMB101 {ECO:0000303|PubMed:15266054}, GMP1 {ECO:0000303|Ref.1,
GN ECO:0000303|Ref.3}, HSN1 {ECO:0000303|PubMed:19011088},
GN SOZ1 {ECO:0000303|PubMed:8790441}, VTC1 {ECO:0000303|PubMed:10097187,
GN ECO:0000303|PubMed:10655235, ECO:0000303|PubMed:12671089,
GN ECO:0000303|PubMed:15064386, ECO:0000303|PubMed:16244149,
GN ECO:0000303|PubMed:16720601, ECO:0000303|PubMed:18849295,
GN ECO:0000303|PubMed:9390448};
GN OrderedLocusNames=At2g39770 {ECO:0000312|Araport:AT2G39770};
GN ORFNames=T5I7.7 {ECO:0000312|EMBL:AAB87126.1};
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].
RC STRAIN=cv. Columbia;
RA Weers B., Thornburg R.;
RT "Characterization of the cDNA and gene for the Arabidopsis thaliana GDP-
RT mannose pyrophosphorylase.";
RL (er) Plant Gene Register PGR98-175(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Lukowitz W., Somerville C.;
RT "Positional cloning of the Arabidopsis cyt1 gene.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Avila C.;
RT "Genes responding to phosphate starvation placed together in Arabidopsis
RT genome.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=8790441; DOI=10.1073/pnas.93.18.9970;
RA Conklin P.L., Williams E.H., Last R.L.;
RT "Environmental stress sensitivity of an ascorbic acid-deficient Arabidopsis
RT mutant.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:9970-9974(1996).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9390448; DOI=10.1104/pp.115.3.1277;
RA Conklin P.L., Pallanca J.E., Last R.L., Smirnoff N.;
RT "L-ascorbic acid metabolism in the ascorbate-deficient arabidopsis mutant
RT vtc1.";
RL Plant Physiol. 115:1277-1285(1997).
RN [10]
RP DISRUPTION PHENOTYPE.
RC STRAIN=cv. Wassilewskija;
RX PubMed=9750345; DOI=10.1046/j.1365-313x.1998.00212.x;
RA Nickle T.C., Meinke D.W.;
RT "A cytokinesis-defective mutant of Arabidopsis (cyt1) characterized by
RT embryonic lethality, incomplete cell walls, and excessive callose
RT accumulation.";
RL Plant J. 15:321-332(1998).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF PRO-22, CATALYTIC ACTIVITY,
RP AND PATHWAY.
RC STRAIN=cv. Columbia;
RX PubMed=10097187; DOI=10.1073/pnas.96.7.4198;
RA Conklin P.L., Norris S.R., Wheeler G.L., Williams E.H., Smirnoff N.,
RA Last R.L.;
RT "Genetic evidence for the role of GDP-mannose in plant ascorbic acid
RT (vitamin C) biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:4198-4203(1999).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=10655235; DOI=10.1093/genetics/154.2.847;
RA Conklin P.L., Saracco S.A., Norris S.R., Last R.L.;
RT "Identification of ascorbic acid-deficient Arabidopsis thaliana mutants.";
RL Genetics 154:847-856(2000).
RN [13]
RP FUNCTION, AND MUTAGENESIS OF PRO-89.
RX PubMed=11226227; DOI=10.1073/pnas.051625798;
RA Lukowitz W., Nickle T.C., Meinke D.W., Last R.L., Conklin P.L.,
RA Somerville C.R.;
RT "Arabidopsis cyt1 mutants are deficient in a mannose-1-phosphate
RT guanylyltransferase and point to a requirement of N-linked glycosylation
RT for cellulose biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:2262-2267(2001).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12671089; DOI=10.1105/tpc.010538;
RA Pastori G.M., Kiddle G., Antoniw J., Bernard S., Veljovic-Jovanovic S.,
RA Verrier P.J., Noctor G., Foyer C.H.;
RT "Leaf vitamin C contents modulate plant defense transcripts and regulate
RT genes that control development through hormone signaling.";
RL Plant Cell 15:939-951(2003).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15064386; DOI=10.1104/pp.103.032185;
RA Barth C., Moeder W., Klessig D.F., Conklin P.L.;
RT "The timing of senescence and response to pathogens is altered in the
RT ascorbate-deficient Arabidopsis mutant vitamin c-1.";
RL Plant Physiol. 134:1784-1792(2004).
RN [16]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Wassilewskija;
RX PubMed=15266054; DOI=10.1104/pp.104.045179;
RA Tzafrir I., Pena-Muralla R., Dickerman A., Berg M., Rogers R., Hutchens S.,
RA Sweeney T.C., McElver J., Aux G., Patton D., Meinke D.;
RT "Identification of genes required for embryo development in Arabidopsis.";
RL Plant Physiol. 135:1206-1220(2004).
RN [17]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16244149; DOI=10.1104/pp.105.067686;
RA Pavet V., Olmos E., Kiddle G., Mowla S., Kumar S., Antoniw J.,
RA Alvarez M.E., Foyer C.H.;
RT "Ascorbic acid deficiency activates cell death and disease resistance
RT responses in Arabidopsis.";
RL Plant Physiol. 139:1291-1303(2005).
RN [18]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16720601; DOI=10.1093/jxb/erl010;
RA Olmos E., Kiddle G., Pellny T., Kumar S., Foyer C.H.;
RT "Modulation of plant morphology, root architecture, and cell structure by
RT low vitamin C in Arabidopsis thaliana.";
RL J. Exp. Bot. 57:1645-1655(2006).
RN [19]
RP FUNCTION.
RX PubMed=18849295; DOI=10.1093/jxb/ern229;
RA Colville L., Smirnoff N.;
RT "Antioxidant status, peroxidase activity, and PR protein transcript levels
RT in ascorbate-deficient Arabidopsis thaliana vtc mutants.";
RL J. Exp. Bot. 59:3857-3868(2008).
RN [20]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-11.
RX PubMed=19011088; DOI=10.1073/pnas.0806168105;
RA Qin C., Qian W., Wang W., Wu Y., Yu C., Jiang X., Wang D., Wu P.;
RT "GDP-mannose pyrophosphorylase is a genetic determinant of ammonium
RT sensitivity in Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:18308-18313(2008).
RN [21]
RP DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=20007685; DOI=10.1093/jxb/erp310;
RA Barth C., Gouzd Z.A., Steele H.P., Imperio R.M.;
RT "A mutation in GDP-mannose pyrophosphorylase causes conditional
RT hypersensitivity to ammonium, resulting in Arabidopsis root growth
RT inhibition, altered ammonium metabolism, and hormone homeostasis.";
RL J. Exp. Bot. 61:379-394(2010).
RN [22]
RP INTERACTION WITH CSN5A AND CSN5B, DOMAIN, AND SUBCELLULAR LOCATION.
RX PubMed=23424245; DOI=10.1105/tpc.112.106880;
RA Wang J., Yu Y., Zhang Z., Quan R., Zhang H., Ma L., Deng X.W., Huang R.;
RT "Arabidopsis CSN5B interacts with VTC1 and modulates ascorbic acid
RT synthesis.";
RL Plant Cell 25:625-636(2013).
CC -!- FUNCTION: Essential protein during embryogenesis (PubMed:15266054).
CC Catalyzes a reaction of the Smirnoff-Wheeler pathway, the major route
CC to ascorbate biosynthesis in plants. Plays an essential role in plant
CC growth and development and cell-wall architecture. Provides GDP-
CC mannose, used for cell wall carbohydrate biosynthesis, protein N-
CC glycosylation, as well as for the biosynthesis of the antioxidant
CC ascorbate. {ECO:0000269|PubMed:10097187, ECO:0000269|PubMed:10655235,
CC ECO:0000269|PubMed:11226227, ECO:0000269|PubMed:12671089,
CC ECO:0000269|PubMed:15064386, ECO:0000269|PubMed:15266054,
CC ECO:0000269|PubMed:16244149, ECO:0000269|PubMed:16720601,
CC ECO:0000269|PubMed:18849295, ECO:0000269|PubMed:19011088,
CC ECO:0000269|PubMed:8790441, ECO:0000269|PubMed:9390448}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-mannose 1-phosphate + GTP + H(+) = diphosphate + GDP-
CC alpha-D-mannose; Xref=Rhea:RHEA:15229, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57527,
CC ChEBI:CHEBI:58409; EC=2.7.7.13;
CC Evidence={ECO:0000269|PubMed:10097187};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC biosynthesis; GDP-alpha-D-mannose from alpha-D-mannose 1-phosphate (GTP
CC route): step 1/1. {ECO:0000269|PubMed:10097187}.
CC -!- SUBUNIT: Interacts in vitro with CSN5A and CSN5B, but in planta with
CC CSN5B only, targeting CYT1 for degradation in the dark by the 26S
CC proteasome. {ECO:0000269|PubMed:23424245}.
CC -!- INTERACTION:
CC O22287; Q9C9P3: F9E10.24; NbExp=4; IntAct=EBI-4427276, EBI-4427281;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23424245}. Nucleus
CC {ECO:0000269|PubMed:23424245}.
CC -!- DOMAIN: The N-terminus (1-40) is necessary for interaction with CNS5B.
CC {ECO:0000269|PubMed:23424245}.
CC -!- DISRUPTION PHENOTYPE: Embryo defective arrested at the cotyledon stage
CC (PubMed:15266054). Deficient in N-glycosylation, altered in cytokinesis
CC and cell wall architecture during embryogenesis. Mutants vtc1 and hsn1
CC with reduced enzyme activity show reduced root length and leaf cell
CC size, reduced accumulation of ascorbate, increased sensitivity to
CC ozone, UV-B and oxidative stresses, increased levels of abscisic acid
CC (ABA), salicylic acid (SA) and resistance to virulent pathogens and
CC root growth inhibition in the presence of NH(4)(+).
CC {ECO:0000269|PubMed:10097187, ECO:0000269|PubMed:10655235,
CC ECO:0000269|PubMed:12671089, ECO:0000269|PubMed:15064386,
CC ECO:0000269|PubMed:15266054, ECO:0000269|PubMed:16244149,
CC ECO:0000269|PubMed:16720601, ECO:0000269|PubMed:19011088,
CC ECO:0000269|PubMed:20007685, ECO:0000269|PubMed:8790441,
CC ECO:0000269|PubMed:9390448, ECO:0000269|PubMed:9750345}.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Seed defective Arabidopsis mutants;
CC URL="http://seedgenes.org/MutantList";
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DR EMBL; AF076484; AAC78474.1; -; mRNA.
DR EMBL; AF108660; AAD04627.1; -; mRNA.
DR EMBL; AJ275979; CAC35355.1; -; Genomic_DNA.
DR EMBL; AC003000; AAB87126.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09721.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09722.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM63165.1; -; Genomic_DNA.
DR EMBL; AF361812; AAK32825.1; -; mRNA.
DR EMBL; AY057541; AAL09781.1; -; mRNA.
DR EMBL; AF428297; AAL16129.1; -; mRNA.
DR EMBL; AY133643; AAM91473.1; -; mRNA.
DR EMBL; BT000697; AAN31841.1; -; mRNA.
DR EMBL; BT006365; AAP21173.1; -; mRNA.
DR EMBL; AY087698; AAM65235.1; -; mRNA.
DR PIR; T01007; T01007.
DR RefSeq; NP_001189713.1; NM_001202784.1.
DR RefSeq; NP_001325272.1; NM_001336797.1.
DR RefSeq; NP_181507.1; NM_129535.4.
DR AlphaFoldDB; O22287; -.
DR SMR; O22287; -.
DR BioGRID; 3900; 5.
DR IntAct; O22287; 2.
DR STRING; 3702.AT2G39770.1; -.
DR MetOSite; O22287; -.
DR PaxDb; O22287; -.
DR PRIDE; O22287; -.
DR ProteomicsDB; 247005; -.
DR EnsemblPlants; AT2G39770.1; AT2G39770.1; AT2G39770.
DR EnsemblPlants; AT2G39770.2; AT2G39770.2; AT2G39770.
DR EnsemblPlants; AT2G39770.3; AT2G39770.3; AT2G39770.
DR GeneID; 818562; -.
DR Gramene; AT2G39770.1; AT2G39770.1; AT2G39770.
DR Gramene; AT2G39770.2; AT2G39770.2; AT2G39770.
DR Gramene; AT2G39770.3; AT2G39770.3; AT2G39770.
DR KEGG; ath:AT2G39770; -.
DR Araport; AT2G39770; -.
DR TAIR; locus:2005504; AT2G39770.
DR eggNOG; KOG1322; Eukaryota.
DR HOGENOM; CLU_029499_0_0_1; -.
DR InParanoid; O22287; -.
DR OMA; PFLTHQL; -.
DR OrthoDB; 806744at2759; -.
DR PhylomeDB; O22287; -.
DR BioCyc; MetaCyc:AT2G39770-MON; -.
DR BRENDA; 2.7.7.13; 399.
DR UniPathway; UPA00126; UER00930.
DR PRO; PR:O22287; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22287; baseline and differential.
DR Genevisible; O22287; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004475; F:mannose-1-phosphate guanylyltransferase activity; IMP:TAIR.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0000032; P:cell wall mannoprotein biosynthetic process; IBA:GO_Central.
DR GO; GO:0030244; P:cellulose biosynthetic process; IMP:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0009298; P:GDP-mannose biosynthetic process; IBA:GO_Central.
DR GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IMP:TAIR.
DR GO; GO:0006486; P:protein glycosylation; IBA:GO_Central.
DR GO; GO:0060359; P:response to ammonium ion; IMP:TAIR.
DR GO; GO:0009408; P:response to heat; IMP:TAIR.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:TAIR.
DR GO; GO:0010193; P:response to ozone; IEP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR CDD; cd06425; M1P_guanylylT_B_like_N; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR045233; GMPPB_N.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF00132; Hexapep; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; GTP-binding; Nucleotide-binding; Nucleotidyltransferase;
KW Nucleus; Reference proteome; Transferase.
FT CHAIN 1..361
FT /note="Mannose-1-phosphate guanylyltransferase 1"
FT /id="PRO_0000412464"
FT MUTAGEN 11
FT /note="G->S: In hsn1; reduced enzyme activity, ascorbate
FT concentrations and N-glycosylation, and increased
FT sensitivity to ammonium."
FT /evidence="ECO:0000269|PubMed:19011088"
FT MUTAGEN 22
FT /note="P->S: In vtc1-1 and vtc1-2; reduced enzyme activity
FT and ascorbate concentrations, and ozone-sensitive."
FT /evidence="ECO:0000269|PubMed:10097187"
FT MUTAGEN 89
FT /note="P->L: In cyt1-1; deficient in N-glycosylation and
FT cellulose, and embryo lethal."
FT /evidence="ECO:0000269|PubMed:11226227"
FT CONFLICT 121
FT /note="M -> I (in Ref. 3; CAC35355)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="L -> H (in Ref. 3; CAC35355)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 361 AA; 39577 MW; D282B510E22C2F06 CRC64;
MKALILVGGF GTRLRPLTLS FPKPLVDFAN KPMILHQIEA LKAVGVDEVV LAINYQPEVM
LNFLKDFETK LEIKITCSQE TEPLGTAGPL ALARDKLLDG SGEPFFVLNS DVISEYPLKE
MLEFHKSHGG EASIMVTKVD EPSKYGVVVM EESTGRVEKF VEKPKLYVGN KINAGIYLLN
PSVLDKIELR PTSIEKETFP KIAAAQGLYA MVLPGFWMDI GQPRDYITGL RLYLDSLRKK
SPAKLTSGPH IVGNVLVDET ATIGEGCLIG PDVAIGPGCI VESGVRLSRC TVMRGVRIKK
HACISSSIIG WHSTVGQWAR IENMTILGED VHVSDEIYSN GGVVLPHKEI KSNILKPEIV
M
