IP6K2_HUMAN
ID IP6K2_HUMAN Reviewed; 426 AA.
AC Q9UHH9; A8K3B1; B4E3G6; G8JLL6; Q6P0N8; Q9BSZ6; Q9BUW3; Q9H4P7; Q9NT63;
AC Q9UFU6;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Inositol hexakisphosphate kinase 2;
DE Short=InsP6 kinase 2 {ECO:0000303|PubMed:10574768};
DE Short=InsP6K2 {ECO:0000303|PubMed:11502751};
DE EC=2.7.4.- {ECO:0000269|PubMed:10574768, ECO:0000269|PubMed:30624931};
DE AltName: Full=P(i)-uptake stimulator;
DE Short=PiUS {ECO:0000303|PubMed:10574768};
GN Name=IP6K2 {ECO:0000303|PubMed:30624931}; Synonyms=IHPK2;
GN ORFNames=TCCCIA00113;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10574768; DOI=10.1016/s0960-9822(00)80055-x;
RA Saiardi A., Erdjument-Bromage H., Snowman A.M., Tempst P., Snyder S.H.;
RT "Synthesis of diphosphoinositol pentakisphosphate by a newly identified
RT family of higher inositol polyphosphate kinases.";
RL Curr. Biol. 9:1323-1326(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Leukemia;
RA Zhou J., Yu W., Tang H., Mei G., Tsang Y.T.M., Bouck J., Gibbs R.A.,
RA Margolin J.F.;
RT "Pediatric leukemia cDNA sequencing project.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
RC TISSUE=Brain, and Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 6).
RC TISSUE=Brain, Lung, and Skin;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 76-426 (ISOFORMS 1 AND 2).
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=11502751; DOI=10.1074/jbc.m106842200;
RA Saiardi A., Nagata E., Luo H.R., Snowman A.M., Snyder S.H.;
RT "Identification and characterization of a novel inositol hexakisphosphate
RT kinase.";
RL J. Biol. Chem. 276:39179-39185(2001).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=30624931; DOI=10.1021/acs.jmedchem.8b01593;
RA Gu C., Stashko M.A., Puhl-Rubio A.C., Chakraborty M., Chakraborty A.,
RA Frye S.V., Pearce K.H., Wang X., Shears S.B., Wang H.;
RT "Inhibition of Inositol Polyphosphate Kinases by Quercetin and Related
RT Flavonoids: A Structure-Activity Analysis.";
RL J. Med. Chem. 62:1443-1454(2019).
CC -!- FUNCTION: Converts inositol hexakisphosphate (InsP6) to
CC diphosphoinositol pentakisphosphate (InsP7/PP-InsP5).
CC {ECO:0000269|PubMed:10574768, ECO:0000269|PubMed:30624931}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol hexakisphosphate + ATP = 5-diphospho-1D-myo-
CC inositol 1,2,3,4,6-pentakisphosphate + ADP; Xref=Rhea:RHEA:12793,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58130, ChEBI:CHEBI:58628,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:10574768,
CC ECO:0000269|PubMed:30624931};
CC -!- ACTIVITY REGULATION: Inhibited by flavonoids, including myricetin,
CC quercetin, luteolin, isorhamnetin, rhamnetin, kaempferol, diosmetin and
CC apigenin. {ECO:0000269|PubMed:30624931}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.0 uM for inositol hexakisphosphate
CC {ECO:0000269|PubMed:10574768};
CC KM=1.0 mM for ATP {ECO:0000269|PubMed:10574768};
CC Vmax=2.0 umol/min/mg enzyme {ECO:0000269|PubMed:10574768};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylinositol metabolism.
CC {ECO:0000269|PubMed:10574768, ECO:0000269|PubMed:30624931}.
CC -!- INTERACTION:
CC Q9UHH9; P07900: HSP90AA1; NbExp=2; IntAct=EBI-747509, EBI-296047;
CC Q9UHH9; Q8N448: LNX2; NbExp=3; IntAct=EBI-747509, EBI-2340947;
CC Q9UHH9; P50222: MEOX2; NbExp=3; IntAct=EBI-747509, EBI-748397;
CC Q9UHH9; O60568: PLOD3; NbExp=3; IntAct=EBI-747509, EBI-741582;
CC Q9UHH9; Q93062: RBPMS; NbExp=3; IntAct=EBI-747509, EBI-740322;
CC Q9UHH9; P04637: TP53; NbExp=4; IntAct=EBI-747509, EBI-366083;
CC Q9UHH9; Q8N680: ZBTB2; NbExp=3; IntAct=EBI-747509, EBI-2515601;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11502751}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q9UHH9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UHH9-2; Sequence=VSP_010925, VSP_010928;
CC Name=3;
CC IsoId=Q9UHH9-3; Sequence=VSP_010926, VSP_010927;
CC Name=4;
CC IsoId=Q9UHH9-4; Sequence=VSP_042698, VSP_042699, VSP_042700;
CC Name=5;
CC IsoId=Q9UHH9-5; Sequence=VSP_042845, VSP_042699, VSP_042700;
CC Name=6;
CC IsoId=Q9UHH9-6; Sequence=VSP_045416, VSP_045417;
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the inositol phosphokinase (IPK) family.
CC {ECO:0000305}.
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DR EMBL; AF177145; AAF15057.1; -; mRNA.
DR EMBL; AY007091; AAG01984.1; -; mRNA.
DR EMBL; AK290526; BAF83215.1; -; mRNA.
DR EMBL; AK304714; BAG65478.1; -; mRNA.
DR EMBL; AC141002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001864; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC004469; AAH04469.2; -; mRNA.
DR EMBL; BC019694; AAH19694.1; -; mRNA.
DR EMBL; BC065533; AAH65533.1; -; mRNA.
DR EMBL; CA488567; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL117458; CAB55936.1; -; mRNA.
DR EMBL; AL137514; CAB70780.1; -; mRNA.
DR CCDS; CCDS2777.1; -. [Q9UHH9-1]
DR CCDS; CCDS33752.1; -. [Q9UHH9-2]
DR CCDS; CCDS54579.1; -. [Q9UHH9-6]
DR CCDS; CCDS54580.1; -. [Q9UHH9-4]
DR CCDS; CCDS54581.1; -. [Q9UHH9-5]
DR PIR; T17246; T17246.
DR PIR; T46275; T46275.
DR RefSeq; NP_001005909.1; NM_001005909.2. [Q9UHH9-1]
DR RefSeq; NP_001005910.1; NM_001005910.2. [Q9UHH9-2]
DR RefSeq; NP_001005911.1; NM_001005911.2. [Q9UHH9-2]
DR RefSeq; NP_001139650.1; NM_001146178.2. [Q9UHH9-6]
DR RefSeq; NP_001139651.1; NM_001146179.2. [Q9UHH9-6]
DR RefSeq; NP_001177245.1; NM_001190316.1. [Q9UHH9-4]
DR RefSeq; NP_001177246.1; NM_001190317.1. [Q9UHH9-5]
DR RefSeq; NP_057375.2; NM_016291.3. [Q9UHH9-1]
DR RefSeq; XP_011532124.1; XM_011533822.1. [Q9UHH9-6]
DR RefSeq; XP_011532125.1; XM_011533823.1. [Q9UHH9-6]
DR RefSeq; XP_016862072.1; XM_017006583.1. [Q9UHH9-1]
DR RefSeq; XP_016862073.1; XM_017006584.1. [Q9UHH9-1]
DR RefSeq; XP_016862074.1; XM_017006585.1. [Q9UHH9-1]
DR AlphaFoldDB; Q9UHH9; -.
DR BioGRID; 119546; 24.
DR DIP; DIP-29676N; -.
DR IntAct; Q9UHH9; 12.
DR MINT; Q9UHH9; -.
DR STRING; 9606.ENSP00000331103; -.
DR BindingDB; Q9UHH9; -.
DR ChEMBL; CHEMBL4523488; -.
DR iPTMnet; Q9UHH9; -.
DR PhosphoSitePlus; Q9UHH9; -.
DR BioMuta; IP6K2; -.
DR DMDM; 50400688; -.
DR EPD; Q9UHH9; -.
DR MassIVE; Q9UHH9; -.
DR MaxQB; Q9UHH9; -.
DR PaxDb; Q9UHH9; -.
DR PeptideAtlas; Q9UHH9; -.
DR PRIDE; Q9UHH9; -.
DR ProteomicsDB; 34267; -.
DR ProteomicsDB; 84351; -. [Q9UHH9-1]
DR ProteomicsDB; 84352; -. [Q9UHH9-2]
DR ProteomicsDB; 84353; -. [Q9UHH9-3]
DR ProteomicsDB; 84354; -. [Q9UHH9-4]
DR ProteomicsDB; 84355; -. [Q9UHH9-5]
DR Antibodypedia; 1556; 217 antibodies from 31 providers.
DR DNASU; 51447; -.
DR Ensembl; ENST00000328631.10; ENSP00000331103.5; ENSG00000068745.15. [Q9UHH9-1]
DR Ensembl; ENST00000340879.8; ENSP00000341925.4; ENSG00000068745.15. [Q9UHH9-2]
DR Ensembl; ENST00000413298.5; ENSP00000396203.1; ENSG00000068745.15. [Q9UHH9-2]
DR Ensembl; ENST00000416707.1; ENSP00000387759.1; ENSG00000068745.15. [Q9UHH9-3]
DR Ensembl; ENST00000431721.6; ENSP00000414139.2; ENSG00000068745.15. [Q9UHH9-4]
DR Ensembl; ENST00000432678.6; ENSP00000400812.2; ENSG00000068745.15. [Q9UHH9-6]
DR Ensembl; ENST00000446860.5; ENSP00000399052.1; ENSG00000068745.15. [Q9UHH9-5]
DR GeneID; 51447; -.
DR KEGG; hsa:51447; -.
DR MANE-Select; ENST00000328631.10; ENSP00000331103.5; NM_016291.4; NP_057375.2.
DR UCSC; uc003cuq.4; human. [Q9UHH9-1]
DR CTD; 51447; -.
DR DisGeNET; 51447; -.
DR GeneCards; IP6K2; -.
DR HGNC; HGNC:17313; IP6K2.
DR HPA; ENSG00000068745; Low tissue specificity.
DR MIM; 606992; gene.
DR neXtProt; NX_Q9UHH9; -.
DR OpenTargets; ENSG00000068745; -.
DR PharmGKB; PA164720999; -.
DR VEuPathDB; HostDB:ENSG00000068745; -.
DR eggNOG; KOG1620; Eukaryota.
DR GeneTree; ENSGT00940000156310; -.
DR HOGENOM; CLU_014862_0_0_1; -.
DR InParanoid; Q9UHH9; -.
DR OMA; CEPKSKV; -.
DR OrthoDB; 902814at2759; -.
DR PhylomeDB; Q9UHH9; -.
DR TreeFam; TF314066; -.
DR BioCyc; MetaCyc:HS00942-MON; -.
DR BRENDA; 2.7.4.21; 2681.
DR PathwayCommons; Q9UHH9; -.
DR Reactome; R-HSA-1855191; Synthesis of IPs in the nucleus.
DR Reactome; R-HSA-909733; Interferon alpha/beta signaling.
DR SABIO-RK; Q9UHH9; -.
DR SignaLink; Q9UHH9; -.
DR UniPathway; UPA00949; -.
DR BioGRID-ORCS; 51447; 8 hits in 1085 CRISPR screens.
DR ChiTaRS; IP6K2; human.
DR GeneWiki; IHPK2; -.
DR GenomeRNAi; 51447; -.
DR Pharos; Q9UHH9; Tbio.
DR PRO; PR:Q9UHH9; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9UHH9; protein.
DR Bgee; ENSG00000068745; Expressed in right hemisphere of cerebellum and 187 other tissues.
DR ExpressionAtlas; Q9UHH9; baseline and differential.
DR Genevisible; Q9UHH9; HS.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0097243; F:flavonoid binding; IDA:UniProtKB.
DR GO; GO:0052836; F:inositol 5-diphosphate pentakisphosphate 5-kinase activity; TAS:Reactome.
DR GO; GO:0052839; F:inositol diphosphate tetrakisphosphate kinase activity; TAS:Reactome.
DR GO; GO:0000829; F:inositol heptakisphosphate kinase activity; TAS:Reactome.
DR GO; GO:0000832; F:inositol hexakisphosphate 5-kinase activity; IDA:UniProtKB.
DR GO; GO:0000828; F:inositol hexakisphosphate kinase activity; IDA:UniProtKB.
DR GO; GO:0000827; F:inositol-1,3,4,5,6-pentakisphosphate kinase activity; TAS:Reactome.
DR GO; GO:0016301; F:kinase activity; IBA:GO_Central.
DR GO; GO:1905396; P:cellular response to flavonoid; IMP:UniProtKB.
DR GO; GO:0032958; P:inositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0043647; P:inositol phosphate metabolic process; IDA:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; IMP:UniProtKB.
DR GO; GO:0006817; P:phosphate ion transport; IEA:Ensembl.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
DR Gene3D; 3.30.470.160; -; 1.
DR InterPro; IPR005522; IPK.
DR InterPro; IPR038286; IPK_sf.
DR PANTHER; PTHR12400; PTHR12400; 1.
DR Pfam; PF03770; IPK; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Kinase; Lipid metabolism;
KW Nucleotide-binding; Nucleus; Phospholipid metabolism; Reference proteome;
KW Transferase.
FT CHAIN 1..426
FT /note="Inositol hexakisphosphate kinase 2"
FT /id="PRO_0000066877"
FT BINDING 207..209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8NFU5"
FT BINDING 220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8NFU5"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NFU5"
FT BINDING 236..243
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NFU5"
FT BINDING 383
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8NFU5"
FT BINDING 386
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8NFU5"
FT VAR_SEQ 1
FT /note="M -> MSLNLPEASLLSRASWPEQAKEPRREGHTDKQQTEDVLAAGLRCLPH
FT LPAICARRM (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042698"
FT VAR_SEQ 1
FT /note="M -> MNLCQSPFQEGCQSLLASWPEQAKEPRREGHTDKQQTEDVLAAGLRC
FT LPHLPAICARRM (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042845"
FT VAR_SEQ 69..130
FT /note="VVSVRFEEDEDRNLCLIAYPLKGDHGIVDIVDNSDCEPKSKLLRWTTNKKHH
FT VLETEKTPKD -> KSQLLEGLPHWRGDVRDRGHGRPWQPSLEPSLPPTLCFPSLSSFS
FT SSWPSAQHLTPSVFNPW (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042699"
FT VAR_SEQ 69..97
FT /note="VVSVRFEEDEDRNLCLIAYPLKGDHGIVD -> QSQRPLVSWPSLPHFFPWS
FT FPLWPQGSVA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_010925"
FT VAR_SEQ 69..87
FT /note="VVSVRFEEDEDRNLCLIAY -> DISSHQHGGVFVGEWGSLL (in
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045416"
FT VAR_SEQ 70
FT /note="V -> S (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010926"
FT VAR_SEQ 71..426
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010927"
FT VAR_SEQ 88..426
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045417"
FT VAR_SEQ 98..426
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_010928"
FT VAR_SEQ 131..426
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042700"
FT CONFLICT 99..100
FT /note="VD -> AH (in Ref. 1; AAF15057)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="G -> W (in Ref. 5; AAH65533)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 426 AA; 49186 MW; 11BDFF12C22EECFB CRC64;
MSPAFRAMDV EPRAKGVLLE PFVHQVGGHS CVLRFNETTL CKPLVPREHQ FYETLPAEMR
KFTPQYKGVV SVRFEEDEDR NLCLIAYPLK GDHGIVDIVD NSDCEPKSKL LRWTTNKKHH
VLETEKTPKD WVRQHRKEEK MKSHKLEEEF EWLKKSEVLY YTVEKKGNIS SQLKHYNPWS
MKCHQQQLQR MKENAKHRNQ YKFILLENLT SRYEVPCVLD LKMGTRQHGD DASEEKAANQ
IRKCQQSTSA VIGVRVCGMQ VYQAGSGQLM FMNKYHGRKL SVQGFKEALF QFFHNGRYLR
RELLGPVLKK LTELKAVLER QESYRFYSSS LLVIYDGKER PEVVLDSDAE DLEDLSEESA
DESAGAYAYK PIGASSVDVR MIDFAHTTCR LYGEDTVVHE GQDAGYIFGL QSLIDIVTEI
SEESGE
