ID   VIP1_SCHPO              Reviewed;         920 AA.
AC   O74429;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   24-JAN-2024, entry version 149.
DE   RecName: Full=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase {ECO:0000305};
DE            EC=2.7.4.24 {ECO:0000250|UniProtKB:Q06685};
DE   AltName: Full=Cortical actin cytoskeleton protein asp1;
DE   AltName: Full=InsP6 and PP-IP5 kinase;
GN   Name=asp1 {ECO:0000312|PomBase:SPCC1672.06c}; Synonyms=vip1;
GN   ORFNames=SPCC1672.06c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
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   [3]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19; SER-21; SER-706 AND
RP   SER-720, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
RN   [5]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, DOMAIN, DISRUPTION PHENOTYPE, AND
RP   MUTAGENESIS OF ASP-333 AND HIS-397.
RX   PubMed=25254656; DOI=10.1371/journal.pgen.1004586;
RA   Poehlmann J., Risse C., Seidel C., Pohlmann T., Jakopec V., Walla E.,
RA   Ramrath P., Takeshita N., Baumann S., Feldbruegge M., Fischer R., Fleig U.;
RT   "The Vip1 inositol polyphosphate kinase family regulates polarized growth
RT   and modulates the microtubule cytoskeleton in fungi.";
RL   PLoS Genet. 10:E1004586-E1004586(2014).
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. Phosphorylates
CC       inositol hexakisphosphate (InsP6) at position 1 to produce PP-InsP5
CC       which is in turn phosphorylated by IP6Ks to produce (PP)2-InsP4.
CC       Alternatively, phosphorylates PP-InsP5 at position 1, produced by IP6Ks
CC       from InsP6, to produce (PP)2-InsP4 (By similarity). Required for
CC       maintaining cellular integrity, normal growth and interactions with the
CC       ARP complex (PubMed:10388810). Acts as a regulator of the PHO80-PHO85
CC       cyclin/cyclin-dependent kinase (CDK) complex, thereby regulating
CC       signaling of phosphate availability (By similarity). Required for the
CC       function of the cortical actin cytoskeleton, possibly by participating
CC       in correct F-actin localization and ensuring polarized growth
CC       (PubMed:10388810). Regulates polarized growth and modulates interphase
CC       microtubule cytoskeleton. Regulates microtubule dynamics without the
CC       requirement of microtubule plus-end tracking protein Mal3. Required for
CC       growth zone selection (PubMed:25254656). {ECO:0000250|UniProtKB:O43314,
CC       ECO:0000250|UniProtKB:Q06685, ECO:0000269|PubMed:10388810,
CC       ECO:0000269|PubMed:25254656}.
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:0000250|UniProtKB:Q06685};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37460;
CC         Evidence={ECO:0000250|UniProtKB:Q06685};
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:0000250|UniProtKB:Q06685};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10277;
CC         Evidence={ECO:0000250|UniProtKB:Q06685};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=58.18 uM for inositol hexakisphosphate
CC         {ECO:0000269|PubMed:25254656};
CC         Vmax=450.5 nmol/min/ug enzyme {ECO:0000269|PubMed:25254656};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10388810,
CC       ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
CC       Cytoplasm, cytoskeleton {ECO:0000305|PubMed:10388810}.
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:0000269|PubMed:25254656}.
CC   -!- DISRUPTION PHENOTYPE: Hypersensitive to microtubule poison
CC       thiabendazole (TBZ). Significantly increased number of interphase
CC       microtubules that depolymerize at the lateral cortex/cytoplasm and not
CC       at the cell tip. Microtubules touch the lateral cortex and become
CC       depolymerized instead of being deflected as do the microtubules of
CC       wild-type. {ECO:0000269|PubMed:25254656}.
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; CU329672; CAA20444.1; -; Genomic_DNA.
DR   PIR; T41050; T41050.
DR   RefSeq; NP_587877.1; NM_001022869.2.
DR   PDB; 8E1H; X-ray; 1.90 A; A/B=31-364.
DR   PDB; 8E1I; X-ray; 2.00 A; A/B=31-364.
DR   PDB; 8E1J; X-ray; 1.60 A; A/B=31-364.
DR   PDB; 8E1S; X-ray; 1.72 A; A/B=31-364.
DR   PDB; 8E1T; X-ray; 1.71 A; A/B=31-364.
DR   PDB; 8E1V; X-ray; 1.90 A; A/B=31-364.
DR   PDBsum; 8E1H; -.
DR   PDBsum; 8E1I; -.
DR   PDBsum; 8E1J; -.
DR   PDBsum; 8E1S; -.
DR   PDBsum; 8E1T; -.
DR   PDBsum; 8E1V; -.
DR   AlphaFoldDB; O74429; -.
DR   SMR; O74429; -.
DR   BioGRID; 275814; 105.
DR   STRING; 284812.O74429; -.
DR   iPTMnet; O74429; -.
DR   MaxQB; O74429; -.
DR   PaxDb; 4896-SPCC1672-06c-1; -.
DR   EnsemblFungi; SPCC1672.06c.1; SPCC1672.06c.1:pep; SPCC1672.06c.
DR   GeneID; 2539244; -.
DR   KEGG; spo:SPCC1672.06c; -.
DR   PomBase; SPCC1672.06c; asp1.
DR   VEuPathDB; FungiDB:SPCC1672.06c; -.
DR   eggNOG; KOG1057; Eukaryota.
DR   HOGENOM; CLU_000914_3_1_1; -.
DR   InParanoid; O74429; -.
DR   OMA; IQERWCC; -.
DR   PhylomeDB; O74429; -.
DR   BRENDA; 3.6.1.B18; 5613.
DR   Reactome; R-SPO-1855167; Synthesis of pyrophosphates in the cytosol.
DR   PRO; PR:O74429; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IDA:PomBase.
DR   GO; GO:0033857; F:diphosphoinositol-pentakisphosphate kinase activity; IDA:PomBase.
DR   GO; GO:0000829; F:inositol heptakisphosphate kinase activity; IBA:GO_Central.
DR   GO; GO:0052723; F:inositol hexakisphosphate 1-kinase activity; IDA:PomBase.
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; IDA:PomBase.
DR   GO; GO:0000827; F:inositol-1,3,4,5,6-pentakisphosphate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052846; F:inositol-1,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 1-diphosphatase activity; IDA:PomBase.
DR   GO; GO:0052843; F:inositol-1-diphosphate-2,3,4,5,6-pentakisphosphate diphosphatase activity; IDA:PomBase.
DR   GO; GO:0006020; P:inositol metabolic process; IMP:UniProtKB.
DR   GO; GO:0032958; P:inositol phosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0043647; P:inositol phosphate metabolic process; IDA:PomBase.
DR   GO; GO:0090307; P:mitotic spindle assembly; IMP:PomBase.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0051516; P:regulation of bipolar cell growth; IMP:UniProtKB.
DR   GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IMP:UniProtKB.
DR   GO; GO:0110162; P:regulation of mitotic spindle elongation (spindle phase three); IMP:PomBase.
DR   GO; GO:0023052; P:signaling; NAS:PomBase.
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   3D-structure; ATP-binding; Cytoplasm; Cytoskeleton; Kinase;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Transferase.
FT   CHAIN           1..920
FT                   /note="Inositol hexakisphosphate and diphosphoinositol-
FT                   pentakisphosphate kinase"
FT                   /id="PRO_0000270923"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          379..445
FT                   /note="Polyphosphoinositide-binding domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q6PFW1"
FT   REGION          709..732
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        711..732
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         42..43
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         123
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         197
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         204
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         223..224
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         223
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         248..251
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         258..260
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         260
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         274
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         276
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         321
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         333..335
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         338..341
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   MOD_RES         19
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         21
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         706
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         720
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MUTAGEN         333
FT                   /note="D->A: Loss of kinase activity and thus ATP-dependent
FT                   production of inositol pyrophosphates. Altered interphase
FT                   microtubule dynamics. Defective polarized growth."
FT                   /evidence="ECO:0000269|PubMed:25254656"
FT   MUTAGEN         397
FT                   /note="H->A: Increased ATP-dependent production of inositol
FT                   pyrophosphates. Altered interphase microtubule dynamics."
FT                   /evidence="ECO:0000269|PubMed:25254656"
FT   STRAND          34..39
FT                   /evidence="ECO:0007829|PDB:8E1J"
FT   HELIX           41..44
FT                   /evidence="ECO:0007829|PDB:8E1J"
FT   HELIX           47..57
FT                   /evidence="ECO:0007829|PDB:8E1J"
FT   STRAND          63..66
FT                   /evidence="ECO:0007829|PDB:8E1J"
FT   HELIX           69..74
FT                   /evidence="ECO:0007829|PDB:8E1J"
FT   HELIX           77..79
FT                   /evidence="ECO:0007829|PDB:8E1J"
FT   STRAND          84..88
FT                   /evidence="ECO:0007829|PDB:8E1J"
FT   HELIX           96..106
FT                   /evidence="ECO:0007829|PDB:8E1J"
FT   STRAND          109..112
FT                   /evidence="ECO:0007829|PDB:8E1J"
FT   HELIX           115..121
FT                   /evidence="ECO:0007829|PDB:8E1J"
FT   HELIX           123..132
FT                   /evidence="ECO:0007829|PDB:8E1J"
FT   STRAND          140..143
FT                   /evidence="ECO:0007829|PDB:8E1J"
FT   STRAND          145..148
FT                   /evidence="ECO:0007829|PDB:8E1J"
FT   HELIX           153..163
FT                   /evidence="ECO:0007829|PDB:8E1J"
FT   STRAND          175..179
FT                   /evidence="ECO:0007829|PDB:8E1J"
FT   STRAND          182..185
FT                   /evidence="ECO:0007829|PDB:8E1J"
FT   STRAND          188..200
FT                   /evidence="ECO:0007829|PDB:8E1J"
FT   STRAND          207..209
FT                   /evidence="ECO:0007829|PDB:8E1J"
FT   HELIX           212..214
FT                   /evidence="ECO:0007829|PDB:8E1J"
FT   STRAND          218..225
FT                   /evidence="ECO:0007829|PDB:8E1J"
FT   STRAND          228..233
FT                   /evidence="ECO:0007829|PDB:8E1J"
FT   STRAND          245..249
FT                   /evidence="ECO:0007829|PDB:8E1J"
FT   HELIX           254..256
FT                   /evidence="ECO:0007829|PDB:8E1T"
FT   STRAND          259..265
FT                   /evidence="ECO:0007829|PDB:8E1J"
FT   STRAND          269..273
FT                   /evidence="ECO:0007829|PDB:8E1J"
FT   TURN            277..280
FT                   /evidence="ECO:0007829|PDB:8E1J"
FT   STRAND          294..296
FT                   /evidence="ECO:0007829|PDB:8E1J"
FT   HELIX           300..312
FT                   /evidence="ECO:0007829|PDB:8E1J"
FT   STRAND          316..325
FT                   /evidence="ECO:0007829|PDB:8E1J"
FT   STRAND          328..337
FT                   /evidence="ECO:0007829|PDB:8E1J"
FT   HELIX           344..361
FT                   /evidence="ECO:0007829|PDB:8E1J"
SQ   SEQUENCE   920 AA;  105680 MW;  507872D240110C0A CRC64;
     MIQNASHLTS IDTESSTRTA SPVSSIVTPT KRNVVGICAM DAKARSKPCR NILNRIIAEG
     EFEAIVFGDN MILDEAVENW PACDYLICFY SSGFPLKKAE KYVELRKPFC VNDVVFQELL
     WDRRLVLNIL DAIRVSTPQR LICSRDGGPK INKVLEEKLR RKFGIEITEV PTPEVKMLDE
     DTLSVDGKII KKPYVEKPVY GEDHNIYIYF PKSVGGGGRK LFRKVANKSS DYDPDLCAPR
     TEGSFIYEEF MNVDNAEDVK VYTVGPHYSH AETRKSPVVD GIVRRNPHGK EIRFITNLSE
     EEKNMASKIS IAFEQPVCGF DLLRVSGQSY VIDVNGWSFV KDNNDYYDNA ARILKQMFHV
     AERHRRNRVP SVQEVLNPPP RESEAWRLKS LVGVLRHADR TPKQKFKFSF TSDPFVKLLQ
     GHTEEVILRN EQLNSVLAAT NLATELKCED INKLKQLRLA LETKKDLPGT KVQLKPAYSP
     EGKLLKLQLI IKWGGEFTHS ARYQSKDLGE QFHKDLYIMN RDCLKDVEIY TSSERRVSAS
     AEIFAMAFLE QETIPSDLLK VRKDLLDDSN AAKDTMDKVK KHLKSLLRVG DTARKEFTWP
     ENMPKPCEVM QQVVQLMKYH RAVMRENFII LGPEVEQVQS RWCCNENPAL FRERWEKLFS
     EFCDSEKADP SKVSELYDTL KYDALHNRQF LERIFTPYQY LKLPQSPSLI AKEPPQRTDS
     NGNLVGMTGA NTNHTERPLE KLYELYDLAK VLFDFVSPQE YGIEPKEKLE IGLLTSVPLL
     RQIIHDIKEA RDSDHASTRM YFTKESHIYT LLNCILESGL PMKLPRNQIP ELDYLTQICF
     ELFERTNPSG NKEFSVRITL SPGCYAQCPL DMNLDAKHCI SVSPRRSLTR HLDLQQFITK
     TEDLCNSVHL PKRFIPVNIN
//