ID   VIP1_MOUSE              Reviewed;        1436 AA.
AC   A2ARP1; A2ARP2; A2ARP3; A2ARP4; Q6P1C8; Q7TSP1; Q80U21; Q8BL16; Q8BUN6;
AC   Q8BVG9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   24-JAN-2024, entry version 128.
DE   RecName: Full=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1 {ECO:0000305};
DE            EC=2.7.4.24 {ECO:0000250|UniProtKB:Q6PFW1};
DE   AltName: Full=Diphosphoinositol pentakisphosphate kinase 1;
DE   AltName: Full=Histidine acid phosphatase domain-containing protein 2A;
DE   AltName: Full=InsP6 and PP-IP5 kinase 1;
DE   AltName: Full=VIP1 homolog;
GN   Name=Ppip5k1 {ECO:0000312|MGI:MGI:2443281};
GN   Synonyms=Hisppd2a, Kiaa0377, Vip1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=Swiss Webster; TISSUE=Brain;
RA   Avidan N., Dgany O.D., Cattan D.C., Pariente A., Thulliez M., Borot N.,
RA   Moati L., Alain B., Krasnov T., Olender T., Shalmon L., Ben-Asher E.,
RA   Khen M., Shalev H., Fellous M., Delaunay J., Yaniv I., Zaizov R.,
RA   Beckmann J.S., Lancet D., Tamary H.;
RT   "A 60kb genomic deletion is associated with non-syndromic deafness and
RT   sperm motility disorder but not with congenital dyserythropoietic anemia
RT   type I.";
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT   The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 6).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Adipose tissue, Hippocampus, and Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC   STRAIN=C57BL/6J; TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1140 AND SER-1147, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Kidney, and Lung;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Bifunctional inositol kinase that acts in concert with the
CC       IP6K kinases IP6K1, IP6K2 and IP6K3 to synthesize the diphosphate
CC       group-containing inositol pyrophosphates diphosphoinositol
CC       pentakisphosphate, PP-InsP5, and bis-diphosphoinositol
CC       tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-InsP4, also
CC       respectively called InsP7 and InsP8, regulate a variety of cellular
CC       processes, including apoptosis, vesicle trafficking, cytoskeletal
CC       dynamics, exocytosis, insulin signaling and neutrophil activation.
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. Activated when
CC       cells are exposed to hyperosmotic stress.
CC       {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}. Cell membrane
CC       {ECO:0000250|UniProtKB:Q6PFW1}. Note=Relocalizes to the plasma membrane
CC       upon activation of the PtdIns 3-kinase pathway.
CC       {ECO:0000250|UniProtKB:Q6PFW1}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1;
CC         IsoId=A2ARP1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A2ARP1-2; Sequence=VSP_030631;
CC       Name=3;
CC         IsoId=A2ARP1-3; Sequence=VSP_030634;
CC       Name=4;
CC         IsoId=A2ARP1-5; Sequence=VSP_030625, VSP_030626;
CC       Name=5;
CC         IsoId=A2ARP1-6; Sequence=VSP_030627, VSP_030628;
CC       Name=6;
CC         IsoId=A2ARP1-7; Sequence=VSP_030629, VSP_030630;
CC   -!- DOMAIN: The C-terminal acid phosphatase-like domain binds
CC       PtdIns(3,4,5)P3 and InsP6. Despite its similarity with the phosphatase
CC       domain of histidine acid phosphatases, it has no phosphatase activity.
CC       {ECO:0000250|UniProtKB:Q6PFW1}.
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family. VIP1
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC32838.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC       Sequence=BAC37198.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAC65546.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF502585; AAP46293.1; -; mRNA.
DR   EMBL; AK122264; BAC65546.1; ALT_INIT; mRNA.
DR   EMBL; AK046696; BAC32838.1; ALT_SEQ; mRNA.
DR   EMBL; AK078268; BAC37198.1; ALT_FRAME; mRNA.
DR   EMBL; AK083140; BAC38780.1; -; mRNA.
DR   EMBL; AL845466; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC065138; AAH65138.1; -; mRNA.
DR   CCDS; CCDS16639.1; -. [A2ARP1-1]
DR   RefSeq; NP_848910.3; NM_178795.4. [A2ARP1-1]
DR   RefSeq; XP_006499804.1; XM_006499741.3.
DR   RefSeq; XP_011237919.1; XM_011239617.2.
DR   AlphaFoldDB; A2ARP1; -.
DR   SMR; A2ARP1; -.
DR   BioGRID; 236476; 3.
DR   STRING; 10090.ENSMUSP00000057632; -.
DR   iPTMnet; A2ARP1; -.
DR   PhosphoSitePlus; A2ARP1; -.
DR   SwissPalm; A2ARP1; -.
DR   MaxQB; A2ARP1; -.
DR   PaxDb; 10090-ENSMUSP00000106256; -.
DR   PeptideAtlas; A2ARP1; -.
DR   ProteomicsDB; 297913; -. [A2ARP1-1]
DR   ProteomicsDB; 297914; -. [A2ARP1-2]
DR   ProteomicsDB; 297915; -. [A2ARP1-3]
DR   ProteomicsDB; 297916; -. [A2ARP1-5]
DR   ProteomicsDB; 297917; -. [A2ARP1-6]
DR   ProteomicsDB; 297918; -. [A2ARP1-7]
DR   Pumba; A2ARP1; -.
DR   Antibodypedia; 35179; 69 antibodies from 15 providers.
DR   DNASU; 327655; -.
DR   Ensembl; ENSMUST00000052029.10; ENSMUSP00000057632.4; ENSMUSG00000033526.17. [A2ARP1-1]
DR   Ensembl; ENSMUST00000110625.8; ENSMUSP00000106255.2; ENSMUSG00000033526.17. [A2ARP1-3]
DR   Ensembl; ENSMUST00000110626.8; ENSMUSP00000106256.2; ENSMUSG00000033526.17. [A2ARP1-1]
DR   Ensembl; ENSMUST00000110627.8; ENSMUSP00000106257.2; ENSMUSG00000033526.17. [A2ARP1-3]
DR   Ensembl; ENSMUST00000110628.8; ENSMUSP00000106258.2; ENSMUSG00000033526.17. [A2ARP1-2]
DR   GeneID; 327655; -.
DR   KEGG; mmu:327655; -.
DR   UCSC; uc008lyl.1; mouse. [A2ARP1-1]
DR   UCSC; uc008lyq.1; mouse. [A2ARP1-7]
DR   UCSC; uc008lyr.1; mouse. [A2ARP1-5]
DR   UCSC; uc008lys.1; mouse. [A2ARP1-6]
DR   AGR; MGI:2443281; -.
DR   CTD; 9677; -.
DR   MGI; MGI:2443281; Ppip5k1.
DR   VEuPathDB; HostDB:ENSMUSG00000033526; -.
DR   eggNOG; KOG1057; Eukaryota.
DR   GeneTree; ENSGT00390000009048; -.
DR   HOGENOM; CLU_000914_0_0_1; -.
DR   InParanoid; A2ARP1; -.
DR   OMA; AWPRCDA; -.
DR   OrthoDB; 5476261at2759; -.
DR   PhylomeDB; A2ARP1; -.
DR   TreeFam; TF313594; -.
DR   Reactome; R-MMU-1855167; Synthesis of pyrophosphates in the cytosol.
DR   BioGRID-ORCS; 327655; 2 hits in 76 CRISPR screens.
DR   PRO; PR:A2ARP1; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; A2ARP1; Protein.
DR   Bgee; ENSMUSG00000033526; Expressed in retinal neural layer and 221 other cell types or tissues.
DR   ExpressionAtlas; A2ARP1; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
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; ISS:UniProtKB.
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:SF11; INOSITOL HEXAKISPHOSPHATE AND DIPHOSPHOINOSITOL-PENTAKISPHOSPHATE KINASE 1; 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; A2ARP1; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cell membrane; Cytoplasm; Kinase;
KW   Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Transferase.
FT   CHAIN           1..1436
FT                   /note="Inositol hexakisphosphate and diphosphoinositol-
FT                   pentakisphosphate kinase 1"
FT                   /id="PRO_0000315689"
FT   REGION          382..453
FT                   /note="Polyphosphoinositide-binding domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q6PFW1"
FT   REGION          915..998
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1131..1191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1389..1436
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        983..998
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1161..1191
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1411..1428
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         64..65
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         145
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         198
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         205
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         224..225
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         224
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         257..259
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         259
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         273
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         275
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         320
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         332..334
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   BINDING         337..340
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O43314"
FT   MOD_RES         939
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6PFW1"
FT   MOD_RES         982
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6PFW1"
FT   MOD_RES         1032
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6PFW1"
FT   MOD_RES         1068
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6PFW1"
FT   MOD_RES         1140
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1147
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         261..266
FT                   /note="YTVGPD -> MVDAEI (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_030625"
FT   VAR_SEQ         267..1436
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_030626"
FT   VAR_SEQ         403..439
FT                   /note="RTPKQKMKMEVTHPRFFALFEKHGGYKTGKLKLKRPE -> HPSFVIEKLVP
FT                   WRCCLKLHLQDLVATVCFHLHGHQQR (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_030627"
FT   VAR_SEQ         440..1436
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_030628"
FT   VAR_SEQ         653..671
FT                   /note="LAPTGSTSLLNSMSVIQNP -> VTLFSSPCSNYIATQFLKF (in
FT                   isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_030629"
FT   VAR_SEQ         672..1436
FT                   /note="Missing (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_030630"
FT   VAR_SEQ         818..837
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_030631"
FT   VAR_SEQ         1057..1077
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_030634"
FT   CONFLICT        441
FT                   /note="L -> I (in Ref. 3; BAC38780)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        831
FT                   /note="T -> A (in Ref. 3; BAC32838)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1049
FT                   /note="P -> S (in Ref. 2; BAC65546)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1180
FT                   /note="T -> A (in Ref. 1; AAP46293 and 2; BAC65546)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1436 AA;  159923 MW;  D160DDDA7F34B4F2 CRC64;
     MWSLTANEDE STTAHFFLGA GDEGLGTCGI GMRTEESDSE LLEDEEDEVP PEPQIIVGIC
     AMTKKSKSKP MTQILERLCR FDYLTVVILG EDVILNEPVE NWPSCHCLIS FHSKGFPLDK
     AVAYSKLRNP FLINDLAMQY YIQDRREVYR ILQEEGIDLP RYAVLNRDPA CPEECSLIEG
     EDQVEVNGAV FPKPFVEKPV SAEDHNVYIY YPSSAGGGSQ RLFRKIGSRS SVYSPESSVR
     KTGSYIYEEF MPTDGTDVKV YTVGPDYAHA EARKSPALDG KVERDSEGKE VRYPVMLTAM
     EKLVARKVCV AFKQTVCGFD LLRANGHSFV CDVNGFSFVK NSMKYYDDCA KILGNTIMRE
     LAPQFQIPWS IPTEAEDIPI VPTTSGTMME LRCVIAIIRH GDRTPKQKMK MEVTHPRFFA
     LFEKHGGYKT GKLKLKRPEQ LQEVLDITRL LLAELEKEPE AEIEEKTGKL EQLKSVLEMY
     GHFSGINRKV QLTYYPHGVK ASNEGQDLQR EPLAPSLLLV LKWGGELTPD GRVQAEELGR
     AFRCMYPGGQ GDYAGFPGCG LLRLHSTFRH DLKIYASDEG RVQMTAAAFA KGLLALEGEL
     TPILVQMVKS ANMNGLLDSD SDSLSSCQHR VKARLHHILQ QDAPFGPEDY DQLAPTGSTS
     LLNSMSVIQN PVKVCDQVFA LIENLTHQIR ERMQDPSSVD LQLYHSETLE LMLQRWSKLE
     RDFRQKSGRY DISKIPDIYD CVKYDVQHNG SLGLQGTAEL LRLSKALADV VIPQEYGISR
     EEKVEIAVGF CLPLLRKILL DLQRTHEDES VNKLHPLYSR GVLSPGRHVR TRLYFTSESH
     VHSLLSVFRY GGLLDETQDA QWQRALAYLS AISELNYMTQ IVIMLYEDNT RDPLSEERFH
     VELHFSPGVK GVEEGSAPAG CGFRPASSEN EEMKTDPGSI ENLCPGKASD EPDRALQTSP
     QPVEGTGLPR RSPLIRNRKA GSMEVLSETS SSRPGGYRLF SSSRPPTEMK QSGLGSQCTG
     LFSTTVLGGS SSAPNLQDYA RTHGKKLPPA SLKHRDELLF VPAVKRFSVS FAKHPTNGFE
     GCSMVPTIYP LETLHNALSL RQVSEFLTKV CQRHTDAHAQ ASAALFDSMH NHQASDSPFS
     PPRTLHSPPL QLRHRSEKPP WYSSGPSSTV SSAGPSSPTT VDGNSHFGFS DQSSVNIHMT
     EEKQGFGLLQ ETPGDGTREL HIERQQELVE PAQSPQELPV EICPSGSQGV TKVSQTCQEV
     PDIVQPCHNI HEEIGQPQQE VPDISQLLLK DHDTTTNTCH LCQASQLSQK VCEEICQLCQ
     DNHEESNQLC QEVSVKLGRM VHGFPVNVDS TAQETLMEIG RPTQEIPEDP YQEFSVKVGV
     LAQKAPAISE LSQDIPEADK PSQELSEETE LQAQEVSEEI DQESEVVDEL PPEAIS
//