VIP2_MOUSE
ID VIP2_MOUSE Reviewed; 1129 AA.
AC Q6ZQB6; E9PVE9; Q3TM75; Q3UUA3; Q7TPU4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2 {ECO:0000305};
DE EC=2.7.4.24 {ECO:0000269|PubMed:17690096};
DE AltName: Full=Diphosphoinositol pentakisphosphate kinase 2;
DE AltName: Full=Histidine acid phosphatase domain-containing protein 1;
DE AltName: Full=InsP6 and PP-IP5 kinase 2;
DE AltName: Full=VIP1 homolog 2;
DE Short=mmVIP2;
GN Name=Ppip5k2 {ECO:0000303|PubMed:29590114, ECO:0000312|MGI:MGI:2142810};
GN Synonyms=Hisppd1, Kiaa0433, Vip2;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Lung, and Spinal cord;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Egg;
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 [5]
RP FUNCTION, ENZYME ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17690096; DOI=10.1074/jbc.m704656200;
RA Fridy P.C., Otto J.C., Dollins D.E., York J.D.;
RT "Cloning and characterization of two human VIP1-like inositol
RT hexakisphosphate and diphosphoinositol pentakisphosphate kinases.";
RL J. Biol. Chem. 282:30754-30762(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND SER-1066, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Liver, Lung, Pancreas, Spleen, and
RC Testis;
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).
RN [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=29590114; DOI=10.1371/journal.pgen.1007297;
RA Yousaf R., Gu C., Ahmed Z.M., Khan S.N., Friedman T.B., Riazuddin S.,
RA Shears S.B., Riazuddin S.;
RT "Mutations in Diphosphoinositol-Pentakisphosphate Kinase PPIP5K2 are
RT associated with hearing loss in human and mouse.";
RL PLoS Genet. 14:E1007297-E1007297(2018).
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 (PubMed:17690096). PP-InsP5 and (PP)2-
CC InsP4, also respectively called InsP7 and InsP8, regulate a variety of
CC cellular processes, including apoptosis, vesicle trafficking,
CC cytoskeletal dynamics, exocytosis, insulin signaling and neutrophil
CC activation (PubMed:17690096). Phosphorylates inositol hexakisphosphate
CC (InsP6) at position 1 to produce PP-InsP5 which is in turn
CC phosphorylated by IP6Ks to produce (PP)2-InsP4 (PubMed:17690096).
CC Alternatively, phosphorylates PP-InsP5 at position 1, produced by IP6Ks
CC from InsP6, to produce (PP)2-InsP4 (PubMed:17690096). Required for
CC normal hearing (PubMed:29590114). {ECO:0000269|PubMed:17690096,
CC ECO:0000269|PubMed:29590114}.
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:0000269|PubMed:17690096};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37460;
CC Evidence={ECO:0000305|PubMed:17690096};
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:0000269|PubMed:17690096};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10277;
CC Evidence={ECO:0000305|PubMed:17690096};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.23 uM for InsP6 {ECO:0000269|PubMed:17690096};
CC KM=0.54 uM for InsP7 {ECO:0000269|PubMed:17690096};
CC Vmax=1.70 nmol/min/mg enzyme with InsP6 as substrate
CC {ECO:0000269|PubMed:17690096};
CC Vmax=5.23 nmol/min/mg enzyme with InsP7 as substrate
CC {ECO:0000269|PubMed:17690096};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:O43314}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6ZQB6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZQB6-2; Sequence=VSP_030637, VSP_030638;
CC Name=3;
CC IsoId=Q6ZQB6-3; Sequence=VSP_041618;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed (PubMed:29590114). Expressed
CC in the cochlear and vestibular sensory hair cells, supporting cells and
CC spiral ganglion neurons (PubMed:29590114).
CC {ECO:0000269|PubMed:29590114}.
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:O43314}.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family. VIP1
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC97950.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK129140; BAC97950.1; ALT_INIT; mRNA.
DR EMBL; AK138622; BAE23724.1; -; mRNA.
DR EMBL; AK166095; BAE38567.1; -; mRNA.
DR EMBL; AC099860; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC162298; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC053396; AAH53396.1; -; mRNA.
DR CCDS; CCDS35678.2; -. [Q6ZQB6-1]
DR RefSeq; NP_776121.4; NM_173760.5. [Q6ZQB6-1]
DR AlphaFoldDB; Q6ZQB6; -.
DR SMR; Q6ZQB6; -.
DR STRING; 10090.ENSMUSP00000108466; -.
DR iPTMnet; Q6ZQB6; -.
DR PhosphoSitePlus; Q6ZQB6; -.
DR EPD; Q6ZQB6; -.
DR jPOST; Q6ZQB6; -.
DR MaxQB; Q6ZQB6; -.
DR PaxDb; Q6ZQB6; -.
DR PeptideAtlas; Q6ZQB6; -.
DR PRIDE; Q6ZQB6; -.
DR ProteomicsDB; 297919; -. [Q6ZQB6-1]
DR ProteomicsDB; 297920; -. [Q6ZQB6-2]
DR ProteomicsDB; 297921; -. [Q6ZQB6-3]
DR Antibodypedia; 44750; 78 antibodies from 20 providers.
DR Ensembl; ENSMUST00000042509; ENSMUSP00000043401; ENSMUSG00000040648. [Q6ZQB6-1]
DR Ensembl; ENSMUST00000171129; ENSMUSP00000132889; ENSMUSG00000040648. [Q6ZQB6-3]
DR GeneID; 227399; -.
DR KEGG; mmu:227399; -.
DR UCSC; uc007cfk.4; mouse. [Q6ZQB6-1]
DR UCSC; uc007cfl.1; mouse. [Q6ZQB6-2]
DR CTD; 23262; -.
DR MGI; MGI:2142810; Ppip5k2.
DR VEuPathDB; HostDB:ENSMUSG00000040648; -.
DR eggNOG; KOG1057; Eukaryota.
DR GeneTree; ENSGT00390000009048; -.
DR HOGENOM; CLU_000914_0_0_1; -.
DR InParanoid; Q6ZQB6; -.
DR OMA; YLAHIVI; -.
DR OrthoDB; 93740at2759; -.
DR BRENDA; 2.7.4.21; 3474.
DR BRENDA; 2.7.4.24; 3474.
DR Reactome; R-MMU-1855167; Synthesis of pyrophosphates in the cytosol.
DR SABIO-RK; Q6ZQB6; -.
DR BioGRID-ORCS; 227399; 5 hits in 56 CRISPR screens.
DR PRO; PR:Q6ZQB6; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q6ZQB6; protein.
DR Bgee; ENSMUSG00000040648; Expressed in manus and 256 other tissues.
DR ExpressionAtlas; Q6ZQB6; baseline and differential.
DR Genevisible; Q6ZQB6; MM.
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; IDA:MGI.
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; IDA:MGI.
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 GO; GO:0007605; P:sensory perception of sound; 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; 2.
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; Hearing; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..1129
FT /note="Inositol hexakisphosphate and diphosphoinositol-
FT pentakisphosphate kinase 2"
FT /id="PRO_0000315693"
FT REGION 377..448
FT /note="Polyphosphoinositide-binding domain"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT REGION 904..945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1070..1129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..945
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 59..60
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 140
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 193
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 200
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 219..220
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 243..246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 252..254
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 254
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 268
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 270
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 315
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 327..329
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT BINDING 332..335
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT MOD_RES 1051
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT MOD_RES 1058
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT MOD_RES 1066
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1106
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT MOD_RES 1107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43314"
FT VAR_SEQ 1..6
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_041618"
FT VAR_SEQ 545
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030637"
FT VAR_SEQ 1051..1129
FT /note="SSMATRSSPGMRRKISLNTYTPTKILPTPPAALKSSKASSKAAAGGPSQAMA
FT PHTSSRKKSINSKTEGHEPKKSTGKKR -> CMEFTFIVT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030638"
FT CONFLICT 197
FT /note="A -> V (in Ref. 1; BAE38567)"
FT /evidence="ECO:0000305"
FT CONFLICT 582
FT /note="A -> T (in Ref. 4; AAH53396)"
FT /evidence="ECO:0000305"
FT CONFLICT 729
FT /note="I -> V (in Ref. 4; AAH53396)"
FT /evidence="ECO:0000305"
FT CONFLICT 1035
FT /note="S -> P (in Ref. 4; AAH53396)"
FT /evidence="ECO:0000305"
FT CONFLICT 1109
FT /note="K -> M (in Ref. 1; BAC97950)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1129 AA; 128427 MW; A563826CC0085E3C CRC64;
MSNSRKMSEP PRFFVGPEDA EINPGNYRRF FHHAEEEEEE EDESPPERQI VVGICSMAKK
SKSKPMKEIL ERISLFKYIT VVVFEEEIIL NEPVENWPLC DCLISFHSKG FPLDKAVAYA
KLRNPFVIND LNMQYLIQDR RDVYSILQAE GILLPRYAIL NRDPNNPKEC NLIEGEDHVE
VNGEVFQKPF VEKPVSAEDH NVYIYYPTSA GGGSQRLFRK IGSRSSVYSP ESNVRKTGSY
IYEEFMPTDG TDVKVYTVGP DYAHAEARKS PALDGKVERD SEGKEVRYPV ILNAREKLIA
WKVCLAFKQT VCGFDLLRAN GQSYVCDVNG FSFVKNSMKY YDDCAKILGN IVMRELAPQF
HIPWSIPLEA EDIPIVPTTS GTMMELRCVI AVIRHGDRTP KQKMKMEVRH QKFFDLFEKC
DGYKSGKLKL KKPKQLQEVL DIARQLLMEL GQNNDSEIEE NKSKLEQLKT VLEMYGHFSG
INRKVQLTYL PHGCPKTSSE EEDNRREEPS LLLVLKWGGE LTPAGRVQAE ELGRAFRCMY
PGGQGDYAGF PGCGLLRLHS TYRHDLKIYA SDEGRVQMTA AAFAKGLLAL EGELTPILVQ
MVKSANMNGL LDSDSDSLSS CQQRVKARLH EILQKDRDFT AEDYEKLTPS GSISVIKSMH
LIKNPVKTCD KVYSLIQSLT SQIRYRMEDP KSADIQLYHS ETLELMLRRW SKLEKDFKTK
NGRYDISKIP DIYDCIKYDV QHNGSLKLEN TMELYRLSKA LADIVIPQEY GITKAEKLEI
AKGYCTPLVR KIRSDLQRTQ DDDTVNKLHP VYSRGVLSPE RHVRTRLYFT SESHVHSLLS
ILRYGALCDD SKDEQWKRAM DYLNVVNELN YMTQIVIMLY EDPNKDLSSE ERFHVELHFS
PGAKGCEEDK NLPSGYGYRP ASRENEGRRS LKTDDDEPHT SKRDEVDRAV MLFKPLVSEP
IHIHRKSPLP RSRKITANEV VSENANYLRT PRNLVEQKQN PTVGFELYSM VPSICPLETL
HNALFLKQVD DFLASIASPS TEVLRKVPEM SSMATRSSPG MRRKISLNTY TPTKILPTPP
AALKSSKASS KAAAGGPSQA MAPHTSSRKK SINSKTEGHE PKKSTGKKR
