VIP1_MOUSE
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 03-AUG-2022, entry version 121.
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; 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-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. [A2ARP1-1]
DR RefSeq; XP_011237919.1; XM_011239617.2. [A2ARP1-3]
DR AlphaFoldDB; A2ARP1; -.
DR SMR; A2ARP1; -.
DR BioGRID; 236476; 3.
DR STRING; 10090.ENSMUSP00000106256; -.
DR iPTMnet; A2ARP1; -.
DR PhosphoSitePlus; A2ARP1; -.
DR MaxQB; A2ARP1; -.
DR PaxDb; A2ARP1; -.
DR PeptideAtlas; A2ARP1; -.
DR PRIDE; 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 Antibodypedia; 35179; 52 antibodies from 14 providers.
DR DNASU; 327655; -.
DR Ensembl; ENSMUST00000052029; ENSMUSP00000057632; ENSMUSG00000033526. [A2ARP1-1]
DR Ensembl; ENSMUST00000110625; ENSMUSP00000106255; ENSMUSG00000033526. [A2ARP1-3]
DR Ensembl; ENSMUST00000110626; ENSMUSP00000106256; ENSMUSG00000033526. [A2ARP1-1]
DR Ensembl; ENSMUST00000110627; ENSMUSP00000106257; ENSMUSG00000033526. [A2ARP1-3]
DR Ensembl; ENSMUST00000110628; ENSMUSP00000106258; ENSMUSG00000033526. [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 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; IQERWCC; -.
DR OrthoDB; 93740at2759; -.
DR PhylomeDB; A2ARP1; -.
DR TreeFam; TF313594; -.
DR Reactome; R-MMU-1855167; Synthesis of pyrophosphates in the cytosol.
DR BioGRID-ORCS; 327655; 2 hits in 71 CRISPR screens.
DR PRO; PR:A2ARP1; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; A2ARP1; protein.
DR Bgee; ENSMUSG00000033526; Expressed in retinal neural layer and 218 other tissues.
DR ExpressionAtlas; A2ARP1; baseline and differential.
DR Genevisible; A2ARP1; MM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
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; 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; 3.40.50.1240; -; 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; 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
