VIP1L_ARATH
ID VIP1L_ARATH Reviewed; 1050 AA.
AC F4J8C6; Q0WSV1; Q9MAD6; Q9SRH8;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase VIP1 {ECO:0000303|PubMed:25231822};
DE EC=2.7.4.24 {ECO:0000269|PubMed:25231822};
DE AltName: Full=Probable protein QUANTITATIVE VITAMIN E-7 {ECO:0000303|PubMed:17077148};
DE AltName: Full=Protein VIP HOMOLOG 2 {ECO:0000303|PubMed:25901085};
DE AltName: Full=VIP1 homolog protein 1 {ECO:0000303|PubMed:25231822};
DE Short=Arabidopsis homolog protein of yeast VIP1 1 {ECO:0000303|PubMed:25231822};
DE Short=AtVIP1 {ECO:0000303|PubMed:25231822};
GN Name=VIP1 {ECO:0000303|PubMed:25231822};
GN Synonyms=QVE7 {ECO:0000303|PubMed:17077148},
GN VIH2 {ECO:0000303|PubMed:25901085};
GN OrderedLocusNames=At3g01310 {ECO:0000312|Araport:AT3G01310};
GN ORFNames=T22N4.6 {ECO:0000312|EMBL:AAF03495.1},
GN T4P13.1 {ECO:0000312|EMBL:AAF26144.1};
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=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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 553-1050.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 296-1050.
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 [5]
RP FUNCTION.
RC STRAIN=cv. Columbia, cv. Cvi-0, and cv. Landsberg erecta;
RX PubMed=17077148; DOI=10.1073/pnas.0606221103;
RA Gilliland L.U., Magallanes-Lundback M., Hemming C., Supplee A.,
RA Koornneef M., Bentsink L., Dellapenna D.;
RT "Genetic basis for natural variation in seed vitamin E levels in
RT Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:18834-18841(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-821, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [8]
RP FUNCTION, MUTAGENESIS OF ASP-292, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=25231822; DOI=10.1111/tpj.12669;
RA Desai M., Rangarajan P., Donahue J.L., Williams S.P., Land E.S.,
RA Mandal M.K., Phillippy B.Q., Perera I.Y., Raboy V., Gillaspy G.E.;
RT "Two inositol hexakisphosphate kinases drive inositol pyrophosphate
RT synthesis in plants.";
RL Plant J. 80:642-653(2014).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF LYS-219 AND ASP-292, AND
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=25901085; DOI=10.1105/tpc.114.135160;
RA Laha D., Johnen P., Azevedo C., Dynowski M., Weiss M., Capolicchio S.,
RA Mao H., Iven T., Steenbergen M., Freyer M., Gaugler P., de Campos M.K.,
RA Zheng N., Feussner I., Jessen H.J., Van Wees S.C., Saiardi A., Schaaf G.;
RT "VIH2 regulates the synthesis of inositol pyrophosphate InsP8 and
RT jasmonate-dependent defenses in Arabidopsis.";
RL Plant Cell 27:1082-1097(2015).
CC -!- FUNCTION: Bifunctional inositol kinase that acts in concert with the
CC IP6K kinases to synthesize the diphosphate group-containing inositol
CC pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-
CC diphosphoinositol tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-
CC InsP4, also respectively called InsP7 and InsP8, may regulate a variety
CC of cellular processes, including apoptosis, vesicle trafficking,
CC cytoskeletal dynamics, and exocytosis. Phosphorylates inositol
CC hexakisphosphate (InsP6) at position 1 to produce PP-InsP5 which is in
CC turn phosphorylated by IP6Ks to produce (PP)2-InsP4. Alternatively,
CC phosphorylates PP-InsP5 at position 1, produced by IP6Ks from InsP6, to
CC produce (PP)2-InsP4 (PubMed:25231822). Probably involved in vitamin E
CC homeostasis via the regulation of gamma-tocopherol biosynthesis
CC (PubMed:17077148). Catalyzes the conversion of InsP7 to InsP8.
CC Regulates jasmonic acid (JA) perception and plant defenses against
CC herbivorous insects (e.g. P.rapae) and necrotrophic fungi (e.g.
CC M.brassicae, B.cinerea and A.brassicicola) by triggering the production
CC of jasmonate-induced pools of InsP8 and subsequent activation of
CC SCF(COI1) E3 ubiquitin ligase complexes with JAZ proteins (e.g.
CC TIFY10A/JAZ1) (PubMed:25901085). {ECO:0000269|PubMed:17077148,
CC ECO:0000269|PubMed:25231822, ECO:0000269|PubMed:25901085}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol hexakisphosphate + ATP = 1-diphospho-myo-
CC inositol 2,3,4,5,6-pentakisphosphate + ADP; Xref=Rhea:RHEA:37459,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58130, ChEBI:CHEBI:74946,
CC ChEBI:CHEBI:456216; EC=2.7.4.24;
CC Evidence={ECO:0000269|PubMed:25231822};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + ATP
CC + H(+) = 1,5-bis(diphospho)-1D-myo-inositol 2,3,4,6-tetrakisphosphate
CC + ADP; Xref=Rhea:RHEA:10276, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:58628, ChEBI:CHEBI:77983, ChEBI:CHEBI:456216;
CC EC=2.7.4.24; Evidence={ECO:0000269|PubMed:25231822};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:O43314}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=Additional isoforms seem to exist.
CC {ECO:0000312|Araport:AT3G01310};
CC Name=1;
CC IsoId=F4J8C6-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Mostly expressed in vegetative tissues (e.g. leaves
CC and stems), and, to a lower extent, in roots, shoots and reproductive
CC tissues (e.g. flowers and siliques) (PubMed:25231822, PubMed:25901085).
CC Also present in mature pollen (PubMed:25901085).
CC {ECO:0000269|PubMed:25231822, ECO:0000269|PubMed:25901085}.
CC -!- DISRUPTION PHENOTYPE: Abnormal accumulation of InsP7 and reduced levels
CC of InsP8. Increased weight increase of P.rapae and M.brassicae larvae
CC feeded on mutant plants thus leading to a reduced resistance. Increased
CC susceptibility to the necrotrophic fungi B.cinerea and A.brassicicola.
CC Increased levels of jasmonic acid (JA) and bioactive conjugates such as
CC JA-Leu/Ile and JA-Val upon mechanical wounding, but reduced induction
CC of JA-responsive genes in challenged mutant plants.
CC {ECO:0000269|PubMed:25901085}.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family. VIP1
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF03495.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF26144.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC008261; AAF26144.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC010676; AAF03495.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE73636.1; -; Genomic_DNA.
DR EMBL; BT010149; AAQ22618.1; -; mRNA.
DR EMBL; AK227817; BAE99797.1; -; mRNA.
DR RefSeq; NP_001030614.1; NM_001035537.3. [F4J8C6-1]
DR AlphaFoldDB; F4J8C6; -.
DR SMR; F4J8C6; -.
DR STRING; 3702.AT3G01310.1; -.
DR iPTMnet; F4J8C6; -.
DR PRIDE; F4J8C6; -.
DR ProteomicsDB; 242747; -. [F4J8C6-1]
DR EnsemblPlants; AT3G01310.2; AT3G01310.2; AT3G01310. [F4J8C6-1]
DR GeneID; 821297; -.
DR Gramene; AT3G01310.2; AT3G01310.2; AT3G01310. [F4J8C6-1]
DR KEGG; ath:AT3G01310; -.
DR Araport; AT3G01310; -.
DR eggNOG; KOG1057; Eukaryota.
DR HOGENOM; CLU_000914_3_0_1; -.
DR PRO; PR:F4J8C6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4J8C6; baseline and differential.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0102092; F:5-diphosphoinositol pentakisphosphate 3-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0033857; F:diphosphoinositol-pentakisphosphate kinase activity; IMP:UniProtKB.
DR GO; GO:0000829; F:inositol heptakisphosphate kinase activity; IMP:UniProtKB.
DR GO; GO:0052723; F:inositol hexakisphosphate 1-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0052724; F:inositol hexakisphosphate 3-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0000832; F:inositol hexakisphosphate 5-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0000828; F:inositol hexakisphosphate kinase activity; IMP:UniProtKB.
DR GO; GO:0000827; F:inositol-1,3,4,5,6-pentakisphosphate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0006020; P:inositol metabolic process; IMP:UniProtKB.
DR GO; GO:0032958; P:inositol phosphate biosynthetic process; IMP:UniProtKB.
DR GO; GO:0009861; P:jasmonic acid and ethylene-dependent systemic resistance; IMP:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:1905036; P:positive regulation of antifungal innate immune response; IMP:UniProtKB.
DR GO; GO:1900367; P:positive regulation of defense response to insect; IMP:UniProtKB.
DR GO; GO:1904966; P:positive regulation of vitamin E biosynthetic process; IMP:UniProtKB.
DR CDD; cd07061; HP_HAP_like; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR InterPro; IPR033379; Acid_Pase_AS.
DR InterPro; IPR000560; His_Pase_clade-2.
DR InterPro; IPR037446; His_Pase_VIP1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR040557; VIP1_N.
DR PANTHER; PTHR12750; PTHR12750; 1.
DR Pfam; PF00328; His_Phos_2; 1.
DR Pfam; PF18086; PPIP5K2_N; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Cytoplasm;
KW Jasmonic acid signaling pathway; Kinase; Nucleotide-binding;
KW Phosphoprotein; Plant defense; Reference proteome; Transferase.
FT CHAIN 1..1050
FT /note="Inositol hexakisphosphate and diphosphoinositol-
FT pentakisphosphate kinase VIP1"
FT /id="PRO_0000439498"
FT REGION 355..429
FT /note="Polyphosphoinositide-binding domain"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT REGION 817..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..834
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..855
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 23..24
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 157
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 183..184
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 183
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 208..211
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 217..219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 233
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 235
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 280
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 292..294
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 297..300
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 821
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MUTAGEN 219
FT /note="K->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:25901085"
FT MUTAGEN 292
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:25231822,
FT ECO:0000269|PubMed:25901085"
FT CONFLICT 505
FT /note="H -> F (in Ref. 4; BAE99797)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1050 AA; 118924 MW; B45949B7E7053BA5 CRC64;
MEMEEGASGV GEKIKIGVCV MEKKVFSAPM GEILDRLQSF GEFEILHFGD KVILEDPIES
WPICDCLIAF HSSGYPLEKA QAYAALRKPF LVNELDPQYL LHDRRKVYEH LEMYGIPVPR
YACVNRKVPN QDLHYFVEEE DFVEVHGERF WKPFVEKPVN GDDHSIMIYY PSSAGGGMKE
LFRKIGNRSS EFHPDVRRVR REGSYIYEEF MATGGTDVKV YTVGPEYAHA EARKSPVVDG
VVMRNTDGKE VRYPVLLTPA EKQMAREVCI AFRQAVCGFD LLRSEGCSYV CDVNGWSFVK
NSYKYYDDAA CVLRKMCLDA KAPHLSSTLP PTLPWKVNEP VQSNEGLTRQ GSGIIGTFGQ
SEELRCVIAV VRHGDRTPKQ KVKLKVTEEK LLNLMLKYNG GKPRAETKLK SAVQLQDLLD
ATRMLVPRTR PGRESDSDAE DLEHAEKLRQ VKAVLEEGGH FSGIYRKVQL KPLKWVKIPK
SDGDGEEERP VEALMVLKYG GVLTHAGRKQ AEELGRYFRN NMYPGEGTGL LRLHSTYRHD
LKIYSSDEGR VQMSAAAFAK GLLDLEGQLT PILVSLVSKD SSMLDGLDNA SIEMEAAKAR
LNEIVTSGTK MIDDDQVSSE DFPWMTDGAG LPPNAHELLR ELVKLTKNVT EQVRLLAMDE
DENLTEPYDI IPPYDQAKAL GKTNIDSDRI ASGLPCGSEG FLLMFARWIK LARDLYNERK
DRFDITQIPD VYDSCKYDLL HNSHLDLKGL DELFKVAQLL ADGVIPNEYG INPQQKLKIG
SKIARRLMGK ILIDLRNTRE EALSVAELKE SQEQVLSLSA SQREDRNSQP KLFINSDELR
RPGTGDKDED DDKETKYRLD PKYANVKTPE RHVRTRLYFT SESHIHSLMN VLRYCNLDES
LLGEESLICQ NALERLCKTK ELDYMSYIVL RLFENTEVSL EDPKRFRIEL TFSRGADLSP
LRNNDDEAET LLREHTLPIM GPERLQEVGS CLSLETMEKM VRPFAMPAED FPPASTPVGF
SGYFSKSAAV LERLVNLFHN YKNSSSNGRS
