ID   VIP1_DROME              Reviewed;        1696 AA.
AC   Q9VR59; A2VEZ0; A8JUU5; Q6AWF3; Q8IQ22; Q8IQ23; Q8IQ24;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   24-JAN-2024, entry version 152.
DE   RecName: Full=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase {ECO:0000305};
DE            EC=2.7.4.24 {ECO:0000250|UniProtKB:Q6PFW1};
DE   AltName: Full=InsP6 and PP-IP5 kinase;
GN   Name=l(1)G0196 {ECO:0000312|FlyBase:FBgn0027279}; ORFNames=CG14616;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS G AND H), AND RNA EDITING
RP   OF POSITIONS 1117 AND 1121.
RC   STRAIN=Berkeley; TISSUE=Embryo, and Head;
RA   Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Kapadia B.,
RA   Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   RNA EDITING OF POSITION 1093; 1117 AND 1121.
RX   PubMed=17018572; DOI=10.1261/rna.254306;
RA   Stapleton M., Carlson J.W., Celniker S.E.;
RT   "RNA editing in Drosophila melanogaster: new targets and functional
RT   consequences.";
RL   RNA 12:1922-1932(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1060, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=17372656; DOI=10.1039/b617545g;
RA   Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA   Eng J.K., Aebersold R., Tao W.A.;
RT   "An integrated chemical, mass spectrometric and computational strategy for
RT   (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT   Kc167 cells.";
RL   Mol. Biosyst. 3:275-286(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-974; SER-1001 AND SER-1255,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18327897; DOI=10.1021/pr700696a;
RA   Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT   "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL   J. Proteome Res. 7:1675-1682(2008).
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. {ECO:0000250|UniProtKB:Q6PFW1}.
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:Q6PFW1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37460;
CC         Evidence={ECO:0000250|UniProtKB:Q6PFW1};
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:Q6PFW1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10277;
CC         Evidence={ECO:0000250|UniProtKB:Q6PFW1};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q6PFW1}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=I;
CC         IsoId=Q9VR59-1; Sequence=Displayed;
CC       Name=G;
CC         IsoId=Q9VR59-3; Sequence=VSP_030649, VSP_030650;
CC       Name=H;
CC         IsoId=Q9VR59-6; Sequence=VSP_030640, VSP_030641, VSP_030648,
CC                                  VSP_030651;
CC       Name=J;
CC         IsoId=Q9VR59-5; Sequence=VSP_030643, VSP_030649, VSP_030650;
CC       Name=K;
CC         IsoId=Q9VR59-7; Sequence=VSP_033593, VSP_030649, VSP_030650;
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   -!- RNA EDITING: Modified_positions=1093 {ECO:0000269|PubMed:17018572},
CC       1117 {ECO:0000269|PubMed:17018572, ECO:0000269|Ref.3}, 1121
CC       {ECO:0000269|PubMed:17018572, ECO:0000269|Ref.3}; Note=Partially
CC       edited. Target of Adar.;
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family. VIP1
CC       subfamily. {ECO:0000305}.
CC   -!- CAUTION: Although related to histidine acid phosphatases, it lacks the
CC       conserved active sites, suggesting that it has no phosphatase activity.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABN49448.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AE014298; AAN09569.2; -; Genomic_DNA.
DR   EMBL; AE014298; AAN09570.3; -; Genomic_DNA.
DR   EMBL; AE014298; AAN09571.2; -; Genomic_DNA.
DR   EMBL; AE014298; AAN09573.2; -; Genomic_DNA.
DR   EMBL; AE014298; ABW09458.2; -; Genomic_DNA.
DR   EMBL; BT015295; AAT94524.1; -; mRNA.
DR   EMBL; BT030309; ABN49448.1; ALT_FRAME; mRNA.
DR   RefSeq; NP_001097041.2; NM_001103571.2. [Q9VR59-7]
DR   RefSeq; NP_788950.2; NM_176777.2. [Q9VR59-1]
DR   RefSeq; NP_788951.2; NM_176778.2. [Q9VR59-3]
DR   RefSeq; NP_788952.2; NM_176779.3. [Q9VR59-6]
DR   RefSeq; NP_788953.2; NM_176780.2. [Q9VR59-5]
DR   AlphaFoldDB; Q9VR59; -.
DR   SMR; Q9VR59; -.
DR   BioGRID; 59411; 4.
DR   DIP; DIP-21851N; -.
DR   IntAct; Q9VR59; 7.
DR   iPTMnet; Q9VR59; -.
DR   EnsemblMetazoa; FBtr0299522; FBpp0288797; FBgn0027279. [Q9VR59-3]
DR   EnsemblMetazoa; FBtr0299523; FBpp0288798; FBgn0027279. [Q9VR59-6]
DR   EnsemblMetazoa; FBtr0299524; FBpp0288799; FBgn0027279. [Q9VR59-1]
DR   EnsemblMetazoa; FBtr0299525; FBpp0288800; FBgn0027279. [Q9VR59-5]
DR   EnsemblMetazoa; FBtr0299526; FBpp0288801; FBgn0027279. [Q9VR59-7]
DR   GeneID; 33137; -.
DR   KEGG; dme:Dmel_CG14616; -.
DR   AGR; FB:FBgn0027279; -.
DR   FlyBase; FBgn0027279; l(1)G0196.
DR   VEuPathDB; VectorBase:FBgn0027279; -.
DR   eggNOG; KOG1057; Eukaryota.
DR   GeneTree; ENSGT00390000009048; -.
DR   InParanoid; Q9VR59; -.
DR   OMA; AQIWACS; -.
DR   OrthoDB; 5476261at2759; -.
DR   PhylomeDB; Q9VR59; -.
DR   Reactome; R-DME-1855167; Synthesis of pyrophosphates in the cytosol.
DR   SignaLink; Q9VR59; -.
DR   BioGRID-ORCS; 33137; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 33137; -.
DR   PRO; PR:Q9VR59; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0027279; Expressed in adult Malpighian tubule (Drosophila) and 36 other cell types or tissues.
DR   ExpressionAtlas; Q9VR59; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0033857; F:diphosphoinositol-pentakisphosphate kinase activity; ISS:UniProtKB.
DR   GO; GO:0000829; F:inositol heptakisphosphate kinase activity; IBA:GO_Central.
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; ISS:UniProtKB.
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; ISS:UniProtKB.
DR   GO; GO:0006020; P:inositol metabolic process; ISS:UniProtKB.
DR   GO; GO:0032958; P:inositol phosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; 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; 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   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR   PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
DR   Genevisible; Q9VR59; DM.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; RNA editing; Transferase.
FT   CHAIN           1..1696
FT                   /note="Inositol hexakisphosphate and diphosphoinositol-
FT                   pentakisphosphate kinase"
FT                   /id="PRO_0000315697"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          43..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          394..465
FT                   /note="Polyphosphoinositide-binding domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q6PFW1"
FT   REGION          503..523
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          942..1001
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1069..1091
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1233..1260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1567..1600
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1676..1696
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        964..992
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1077..1091
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         76..77
FT                   /ligand="substrate"
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         210
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         217
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         236..237
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         236
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         260..263
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         269..271
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         271
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         285
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         287
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         332
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         344..346
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         349..352
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   MOD_RES         974
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         1001
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         1060
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:17372656"
FT   MOD_RES         1255
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   VAR_SEQ         2..40
FT                   /note="SYTELESGYQDISQQHQQQNPHQSQPQQRVGFYLGLQDG -> EWTWFKDWW
FT                   RLKKLRSRHQRHKKKLQATAASAEAAVTASAFLAGSGCAESGGSQDPQTNRLHSLDAVP
FT                   SDGTLARRRHGSRDSLRRNRLLQRQRRSQSAAVRSHRSHDDDDDGEYGPFNVSDYEDYG
FT                   PNHGSDEESDDFCYCEVCM (in isoform H)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_030640"
FT   VAR_SEQ         266
FT                   /note="D -> DVYFS (in isoform H)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_030641"
FT   VAR_SEQ         1090
FT                   /note="P -> PATETAEDTSMDIQPKICIGKCAPGLLTPTVTTTDILKGIRDIAPTA
FT                   TQTSPPTFTPSTTTTTGAAAALFDNTATMSSNRPFTNQFQSIDPTSNDAPHQHHVHQHQ
FT                   YQHHRKTTTTIINNTLNENHTTATITNNTTTTPSCCTKTIAT (in isoform J)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_030643"
FT   VAR_SEQ         1090
FT                   /note="P -> PVSSPDFGDNSRTRSSEFGETCHARVGTASNSDGGGSHPRADHRTAF
FT                   QIRVTNSLSFFKIDSSTNELPLSDIDFSLHPPTPQCGPLSHKRFHILTMRRMESCDDGA
FT                   ELEQVRHLPQISPMATNERPLSSCNCSSSAAQAHSHSKSLMDLAQAVVMTSPQETGPNS
FT                   EQGCDPTTAADVSVSSFDDDFQLSSSAPAILMSAHFGNRPVVASLSSMVHVTTSPSAST
FT                   LQLCRDKDKALASGTSSAHSKATSNSCGQLSMAGSAPVVTENPFRFTVSSLGSAATNTA
FT                   CFVGSFEPIEEQITSIVEVDSKPLQPEPQVVYNLPTVLITGTASSSELSTKLNSNILPT
FT                   VTNAFSAIDTEINDEIGISKEVGIGTIRITNTHTPCNKATVTRPDTKIAITTDPQTVTA
FT                   TETAEDTSMDIQPKICIGKCAPGLLTPTVTTTDILKGIRDIAPTATQTSPPTFTPSTTT
FT                   TTGAAAALFDNTATMSSNRPFTNQFQSIDPTSNDAPHQHHVHQHQYQHHRKTTTTIINN
FT                   TLNENHTTATITNNTTTTPSCCTKTIAT (in isoform K)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_033593"
FT   VAR_SEQ         1293..1305
FT                   /note="LWPQDIVKAAEDE -> RKCRKKSVVEWQC (in isoform H)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_030648"
FT   VAR_SEQ         1293..1300
FT                   /note="LWPQDIVK -> QYPTEPSI (in isoform G, isoform J and
FT                   isoform K)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_030649"
FT   VAR_SEQ         1301..1696
FT                   /note="Missing (in isoform G, isoform J and isoform K)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_030650"
FT   VAR_SEQ         1306..1696
FT                   /note="Missing (in isoform H)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_030651"
FT   VARIANT         1093
FT                   /note="Q -> R (in RNA edited version)"
FT   VARIANT         1117
FT                   /note="S -> G (in RNA edited version)"
FT   VARIANT         1121
FT                   /note="Q -> R (in RNA edited version)"
FT   CONFLICT        329
FT                   /note="C -> F (in Ref. 3; ABN49448)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        734
FT                   /note="K -> KN (in Ref. 3; ABN49448)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        906
FT                   /note="Y -> H (in Ref. 3; ABN49448)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1092
FT                   /note="S -> G (in Ref. 3; AAT94524)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1116
FT                   /note="H -> R (in Ref. 3; AAT94524)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1124
FT                   /note="Y -> C (in Ref. 3; AAT94524/ABN49448)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1696 AA;  188677 MW;  BB013ECB582C96D3 CRC64;
     MSYTELESGY QDISQQHQQQ NPHQSQPQQR VGFYLGLQDG NGDTDFGDSN DGMDSDTSTS
     SSNSKQVVVG ICAMAKKTQS KPMKEILTRL GEFEFIKLVT FEENVILREP VQNWPTCDCL
     VSFHSKGFPL EKAIEYAQLR NPFVLNNLHM QYDIQDRRRV YAILEKEGIE IPRYAVLDRD
     SPDPKHHELI ESEDHVEVNG ITFNKPFVEK PVSAEDHNIY IYYPTSAGGG SQRLFRKIGS
     RSSVYSPESR VRKTGSFIYE DFMPTDGTDV KVYTVGPDYA HAEARKSPAL DGKVERDSEG
     KEIRYPVILN HSEKLISRKV CLAFKQTVCG FDLLRANGKS YVCDVNGFSF VKNSNKYYDD
     CAKILGNMIL RELTPTLHIP WSVPFQLDDP PIVPTTFGKM MELRCVVAVI RHGDRTPKQK
     MKVEVRHPKF FEIFEKYDGY KLGHVKLKRP KQLQEILDIA RFLLSEIHTK AHAEIEEKES
     KLEQLKNVLE MYGHFSGINR KVQMKYQPKG RPRGSSSDDT NLAADQPVEP SLVLILKWGG
     ELTPAGRIQA EELGRIFRCM YPGGQGRSDY SGTQGLGLLR LHSTFRHDLK IYASDEGRVQ
     MTAAAFAKGL LALEGELTPI LVQMVKSANT NGLLDNDCDS SKYQNLAKGR LHELMQNDRE
     FSKEDRELIN PCNSKSITQA LDFVKNPVDC CHHVHLLIRE LLHIISIKKD DPKTKDAILY
     HGETWDLMRC RWEKIEKDFS TKSKLFDISK IPDIYDCIKY DLQHNQHTLQ YDQAEELYIY
     AKNLADIVIP QEYGLTPQEK LAIGQGICSP LLRKIKGDLQ RNIDEVEDEF MNRLNPHYSH
     GVASPQRHVR TRLYFTSESH VHSLLTVLRY GGLLNVVTDE QWRRAMDYIS MVSELNYMSQ
     IVIMLYEDPT KDPTSEERFH VELHFSPGVN CCVQKNLPPG PGFRPHSHGD NACNVSLQSS
     DESNPARIEE ENDSNSGEER EGKKRGTSGQ RSTDRSAERI SPAFGFNRLE LRSKQFKSKP
     IPIGAHHTVS GHEAMDLAKR LNEELASHQQ QQNQQLRPIS PDIRAVTPDC EPRSRSFEQR
     PTSGVCAKEP DSQVSVSVSA SVSSANASTS SRRQRHSIAG QMSYMKMLGF GGFSKKMATS
     ANSLFSTAVI SGSSSAPNLR DMITVSSSGF GDVPPIRPLE TLHNALSLRK LDSFLQDMIL
     AQIFKTPTGS PPRGFSKNTL PAVSSMTLTA SNQTEVVEHE PISTTVTPTF DRRGSESGST
     ADAHLRLLSE SQCPNLDDSN TELRESLAGK MELWPQDIVK AAEDEELNLS ELETKPSLDL
     TMEIMERGVA GIASIQPMNR DSDETMGGGV FLSVCEEQGS GSTCLTPVSF GMDLDLSMVA
     NKGSITLSME GFDDDEDATL SAATTPSLLA DCEPRLESCY CCPSHAEAPP EVPSDDPRFG
     FALPVRVTQA SPEHARPVRR AHDPVSPRIQ KQISLFEGNA AMATGQEKTE SSGSVGGGAI
     LHASINLPAA GPHHLRQDAR LRKFENLTQS TSNSNFPFES NTLKRVPMQT TKDYDNVSHT
     QSCINLKSGS SGVLGGSPQR QRGSDGGGVG ASGVPAESRE PTRVHYGRMN STCCSASASP
     SPSPGALIVK ERFIEPPKRG VVRGYHGKTQ SMDADFLFNE FLLLPAMAPA KISFDSSDID
     QASDDDSPSS SKQRHA
//