VIP1_DROME
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 03-AUG-2022, entry version 146.
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-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 PaxDb; Q9VR59; -.
DR PRIDE; 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 FlyBase; FBgn0027279; l(1)G0196.
DR VEuPathDB; VectorBase:FBgn0027279; -.
DR eggNOG; KOG1057; Eukaryota.
DR GeneTree; ENSGT00390000009048; -.
DR InParanoid; Q9VR59; -.
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 tissues.
DR ExpressionAtlas; Q9VR59; baseline and differential.
DR Genevisible; Q9VR59; DM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0102092; F:5-diphosphoinositol pentakisphosphate 3-kinase activity; IEA:UniProtKB-EC.
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; 3.40.50.1240; -; 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 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
