ID   VIP1_YEAST              Reviewed;        1146 AA.
AC   Q06685; D6VZ44;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 168.
DE   RecName: Full=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase {ECO:0000305};
DE            EC=2.7.4.24 {ECO:0000269|PubMed:17412958};
DE   AltName: Full=InsP6 and PP-IP5 kinase;
GN   Name=VIP1 {ECO:0000312|SGD:S000004402}; OrderedLocusNames=YLR410W;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   FUNCTION.
RX   PubMed=10388810; DOI=10.1093/genetics/152.3.895;
RA   Feoktistova A., McCollum D., Ohi R., Gould K.L.;
RT   "Identification and characterization of Schizosaccharomyces pombe asp1(+),
RT   a gene that interacts with mutations in the Arp2/3 complex and actin.";
RL   Genetics 152:895-908(1999).
RN   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=YAL6B;
RX   PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA   Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA   Jensen O.N.;
RT   "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT   pathway.";
RL   Mol. Cell. Proteomics 4:310-327(2005).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-487 AND HIS-548.
RX   PubMed=17412958; DOI=10.1126/science.1139099;
RA   Mulugu S., Bai W., Fridy P.C., Bastidas R.J., Otto J.C., Dollins D.E.,
RA   Haystead T.A., Ribeiro A.A., York J.D.;
RT   "A conserved family of enzymes that phosphorylate inositol
RT   hexakisphosphate.";
RL   Science 316:106-109(2007).
RN   [9]
RP   FUNCTION.
RX   PubMed=17412959; DOI=10.1126/science.1139080;
RA   Lee Y.-S., Mulugu S., York J.D., O'Shea E.K.;
RT   "Regulation of a cyclin-CDK-CDK inhibitor complex by inositol
RT   pyrophosphates.";
RL   Science 316:109-112(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31 AND SER-77, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-895 AND SER-1107, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
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 (PubMed:17412958).
CC       Phosphorylates inositol hexakisphosphate (InsP6) at position 1 to
CC       produce PP-InsP5 which is in turn phosphorylated by IP6Ks to produce
CC       (PP)2-InsP4. Alternatively, phosphorylates PP-InsP5 at position 1,
CC       produced by IP6Ks from InsP6, to produce (PP)2-InsP4 (By similarity).
CC       Required for maintaining cellular integrity, normal growth and
CC       interactions with the ARP complex (PubMed:10388810). Acts as a
CC       regulator of the PHO80-PHO85 cyclin/cyclin-dependent kinase (CDK)
CC       complex, thereby regulating signaling of phosphate availability
CC       (PubMed:17412959). Required for the function of the cortical actin
CC       cytoskeleton, possibly by participating in correct F-actin localization
CC       and ensuring polarized growth (PubMed:10388810). Regulates polarized
CC       growth and modulates interphase microtubule cytoskeleton. Regulates
CC       microtubule dynamics without the requirement of microtubule plus-end
CC       tracking protein Mal3. Required for growth zone selection (By
CC       similarity). {ECO:0000250|UniProtKB:O74429,
CC       ECO:0000250|UniProtKB:Q6PFW1, ECO:0000269|PubMed:10388810,
CC       ECO:0000269|PubMed:17412958, ECO:0000269|PubMed:17412959}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol hexakisphosphate + ATP = 1-diphospho-1D-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:17412958};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37460;
CC         Evidence={ECO:0000305|PubMed:17412958};
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:17412958};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10277;
CC         Evidence={ECO:0000305|PubMed:17412958};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC       Cytoplasm, cytoskeleton {ECO:0000269|PubMed:14562095}.
CC   -!- DOMAIN: The N-terminal kinase domain produces inositol polyphosphates.
CC       The C-terminal acid phosphatase-like domain binds inositol
CC       polyphosphates and negatively regulates their accumulation. The C-
CC       terminal domain reduces the amount of inositol pyrophosphates in a
CC       dose-dependent manner in vitro. {ECO:0000250|UniProtKB:O74429}.
CC   -!- MISCELLANEOUS: Present with 8810 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family. VIP1
CC       subfamily. {ECO:0000305}.
CC   -!- CAUTION: Although related to histidine acid phosphatase proteins, it
CC       lacks the conserved active sites, suggesting that it has no phosphatase
CC       activity. {ECO:0000305}.
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DR   EMBL; U20162; AAB67497.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09710.1; -; Genomic_DNA.
DR   PIR; S59376; S59376.
DR   RefSeq; NP_013514.1; NM_001182298.1.
DR   AlphaFoldDB; Q06685; -.
DR   SMR; Q06685; -.
DR   BioGRID; 31667; 560.
DR   IntAct; Q06685; 31.
DR   MINT; Q06685; -.
DR   STRING; 4932.YLR410W; -.
DR   GlyGen; Q06685; 7 sites, 1 O-linked glycan (7 sites).
DR   iPTMnet; Q06685; -.
DR   MaxQB; Q06685; -.
DR   PaxDb; 4932-YLR410W; -.
DR   PeptideAtlas; Q06685; -.
DR   EnsemblFungi; YLR410W_mRNA; YLR410W; YLR410W.
DR   GeneID; 851126; -.
DR   KEGG; sce:YLR410W; -.
DR   AGR; SGD:S000004402; -.
DR   SGD; S000004402; VIP1.
DR   VEuPathDB; FungiDB:YLR410W; -.
DR   eggNOG; KOG1057; Eukaryota.
DR   GeneTree; ENSGT00390000009048; -.
DR   HOGENOM; CLU_000914_3_1_1; -.
DR   InParanoid; Q06685; -.
DR   OMA; IQERWCC; -.
DR   OrthoDB; 5476261at2759; -.
DR   BioCyc; YEAST:MONOMER3O-224; -.
DR   Reactome; R-SCE-1855167; Synthesis of pyrophosphates in the cytosol.
DR   BioGRID-ORCS; 851126; 0 hits in 10 CRISPR screens.
DR   PRO; PR:Q06685; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; Q06685; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0033857; F:diphosphoinositol-pentakisphosphate kinase activity; IBA:GO_Central.
DR   GO; GO:0000829; F:inositol heptakisphosphate kinase activity; IDA:SGD.
DR   GO; GO:0052723; F:inositol hexakisphosphate 1-kinase activity; IDA:SGD.
DR   GO; GO:0052724; F:inositol hexakisphosphate 3-kinase activity; IDA:SGD.
DR   GO; GO:0000830; F:inositol hexakisphosphate 4-kinase activity; IDA:SGD.
DR   GO; GO:0000832; F:inositol hexakisphosphate 5-kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000831; F:inositol hexakisphosphate 6-kinase activity; IDA:SGD.
DR   GO; GO:0000828; F:inositol hexakisphosphate kinase activity; IBA:GO_Central.
DR   GO; GO:0000827; F:inositol-1,3,4,5,6-pentakisphosphate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052843; F:inositol-1-diphosphate-2,3,4,5,6-pentakisphosphate diphosphatase activity; IDA:SGD.
DR   GO; GO:0052845; F:inositol-5-diphosphate-1,2,3,4,6-pentakisphosphate diphosphatase activity; IDA:SGD.
DR   GO; GO:0006020; P:inositol metabolic process; IBA:GO_Central.
DR   GO; GO:0032958; P:inositol phosphate biosynthetic process; IDA:SGD.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0051516; P:regulation of bipolar cell growth; ISS:UniProtKB.
DR   GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; ISS:UniProtKB.
DR   CDD; cd07061; HP_HAP_like; 1.
DR   Gene3D; 3.40.50.11950; -; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR013651; ATP-grasp_RimK-type.
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; DIPHOSPHOINOSITOL PENTAKISPHOSPHATE KINASE; 1.
DR   PANTHER; PTHR12750:SF9; INOSITOL HEXAKISPHOSPHATE AND DIPHOSPHOINOSITOL-PENTAKISPHOSPHATE KINASE; 1.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   Pfam; PF18086; PPIP5K2_N; 1.
DR   Pfam; PF08443; RimK; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Cytoskeleton; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN           1..1146
FT                   /note="Inositol hexakisphosphate and diphosphoinositol-
FT                   pentakisphosphate kinase"
FT                   /id="PRO_0000270924"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          93..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          530..597
FT                   /note="Polyphosphoinositide-binding domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q6PFW1"
FT   REGION          1106..1146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..33
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..111
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..178
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1128..1146
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         197..198
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         278
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         351
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         358
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         377..378
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         377
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         402..405
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         412..414
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         414
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         428
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         430
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         475
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         487..489
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         492..495
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   MOD_RES         31
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         54
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
FT   MOD_RES         77
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         895
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         1107
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MUTAGEN         487
FT                   /note="D->A: Abolishes enzyme activity."
FT                   /evidence="ECO:0000269|PubMed:17412958"
FT   MUTAGEN         548
FT                   /note="H->A: Does not affect enzyme activity."
FT                   /evidence="ECO:0000269|PubMed:17412958"
SQ   SEQUENCE   1146 AA;  129755 MW;  D69E44EAD16490F9 CRC64;
     MSGIKKEPIE SDEVPQQETK NNLPSAPSEM SPLFLNKNTQ KAMQSIAPIL EGFSPKTSAS
     ENMSLKLPPP GIQDDHSEEN LTVHDTLQRT ISTALGNGNN TNTVTTSGLK KADSESKSEA
     DPEGLSNSNI VNDADNINSI SKTGSPHLPQ GTMDAEQTNM GTNSVPTSSA SSRKSSTSHP
     KPRLPKVGKI GVCAMDAKVL SKPMRHILNR LIEHGEFETV IFGDKVILDE RIENWPTCDF
     LISFFSSGFP LDKAIKYVKL RKPFIINDLI MQKILWDRRL CLQVLEAYNV PTPPRLEISR
     DGGPRANEEL RAKLREHGVE VKPVEEPEWK MVDDDTLEVD GKTMTKPFVE KPVDGEDHNI
     YIYYHSKNGG GGRRLFRKVG NKSSEFDPTL VHPRTEGSYI YEQFMDTDNF EDVKAYTIGE
     NFCHAETRKS PVVDGIVRRN THGKEVRYIT ELSDEEKTIA GKVSKAFSQM ICGFDLLRVS
     GKSYVIDVNG FSFVKDNKAY YDSCANILRS TFIEAKKKMD MEKKNLPIIR EEKEQKWVFK
     GLAIIIRHAD RTPKQKFKHS FTSPIFISLL KGHKEEVVIR NVNDLKIVLQ ALRIALDEKA
     GNPAKIKVLA NALEKKLNFP GTKIQLKPVL NKENEVEKVQ FILKWGGEPT HSAKYQATEL
     GEQMRQDFDL LNKSILQNIK IFSSSERRVL HTAQYWTRAL FGADELGSDE ISIRKDLLDD
     SNAAKDLMDK VKKKLKPLLR EGKEAPPQFA WPSKMPEPYL VIKRVVELMN YHKKIMDNNF
     AKKDVNSMQT RWCTSEDPSL FKERWDKLFK EFNNAEKVDP SKISELYDTM KYDALHNRQF
     LENIFDPGLP NEAIADELGS HSLVDRYPIN VLAKNNFKII DSHSMNNSGK NSSNSVGSLG
     WVLESGKTST ARNPKSSSQF DEPRFMQLRE LYKLAKVLFD FICPKEYGIS DAEKLDIGLL
     TSLPLAKQIL NDIGDMKNRE TPACVAYFTK ESHIYTLLNI IYESGIPMRI ARNALPELDY
     LSQITFELYE STDASGQKSH SIRLKMSPGC HTQDPLDVQL DDRHYISCIP KISLTKHLDM
     DYVQQKLRNK FTRVIMPPKF TPVNITSPNL SFQKRKTRRK SVSVEKLKRP ASSGSSSSTS
     VNKTLD
//