INP5K_MOUSE
ID INP5K_MOUSE Reviewed; 468 AA.
AC Q8C5L6; O09040;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Inositol polyphosphate 5-phosphatase K {ECO:0000305};
DE EC=3.1.3.56 {ECO:0000269|PubMed:22247557, ECO:0000269|PubMed:22751929};
DE AltName: Full=Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase;
DE EC=3.1.3.86 {ECO:0000250|UniProtKB:Q9BT40};
DE AltName: Full=Phosphatidylinositol-4,5-bisphosphate 5-phosphatase;
DE EC=3.1.3.36 {ECO:0000250|UniProtKB:Q9BT40};
DE AltName: Full=Skeletal muscle and kidney-enriched inositol phosphatase {ECO:0000250|UniProtKB:Q9BT40};
GN Name=Inpp5k {ECO:0000312|MGI:MGI:1194899};
GN Synonyms=Pps, Skip {ECO:0000250|UniProtKB:Q9BT40};
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 {ECO:0000312|EMBL:BAC37126.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=9182797; DOI=10.1016/s0896-6273(00)80312-8;
RA Hamilton B.A., Smith D.J., Mueller K.L., Kerrebrock A.W., Bronson R.T.,
RA van Berkel V., Daly M.J., Kruglyak L., Reeve M.P., Nemhauser J.L.,
RA Hawkins T.L., Rubin E.M., Lander E.S.;
RT "The vibrator mutation causes neurodegeneration via reduced expression of
RT PITP alpha: positional complementation cloning and extragenic
RT suppression.";
RL Neuron 18:711-722(1997).
RN [2] {ECO:0000312|EMBL:AAL90796.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ILS {ECO:0000312|EMBL:AAL90796.1}, and
RC ISS {ECO:0000312|EMBL:AAL90797.1};
RA Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata, and Ovary;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=22247557; DOI=10.1074/jbc.m111.335539;
RA Ijuin T., Takenawa T.;
RT "Regulation of insulin signaling and glucose transporter 4 (GLUT4)
RT exocytosis by phosphatidylinositol 3,4,5-trisphosphate (PIP3) phosphatase,
RT skeletal muscle, and kidney enriched inositol polyphosphate phosphatase
RT (SKIP).";
RL J. Biol. Chem. 287:6991-6999(2012).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP PAK1.
RX PubMed=22751929; DOI=10.1128/mcb.00636-12;
RA Ijuin T., Takenawa T.;
RT "Regulation of insulin signaling by the phosphatidylinositol 3,4,5-
RT triphosphate phosphatase SKIP through the scaffolding function of Pak1.";
RL Mol. Cell. Biol. 32:3570-3584(2012).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=28190456; DOI=10.1016/j.ajhg.2017.01.024;
RA Wiessner M., Roos A., Munn C.J., Viswanathan R., Whyte T., Cox D.,
RA Schoser B., Sewry C., Roper H., Phadke R., Marini Bettolo C., Barresi R.,
RA Charlton R., Boennemann C.G., Abath Neto O., Reed U.C., Zanoteli E.,
RA Araujo Martins Moreno C., Ertl-Wagner B., Stucka R., De Goede C.,
RA Borges da Silva T., Hathazi D., Dell'Aica M., Zahedi R.P., Thiele S.,
RA Mueller J., Kingston H., Mueller S., Curtis E., Walter M.C., Strom T.M.,
RA Straub V., Bushby K., Muntoni F., Swan L.E., Lochmueller H., Senderek J.;
RT "Mutations in INPP5K, Encoding a Phosphoinositide 5-Phosphatase, Cause
RT Congenital muscular dystrophy with cataracts and mild cognitive
RT impairment.";
RL Am. J. Hum. Genet. 100:523-536(2017).
CC -!- FUNCTION: Inositol 5-phosphatase which acts on inositol 1,4,5-
CC trisphosphate, inositol 1,3,4,5-tetrakisphosphate, phosphatidylinositol
CC 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate. Has 6-
CC fold higher affinity for phosphatidylinositol 4,5-bisphosphate than for
CC inositol 1,4,5-trisphosphate (By similarity). Negatively regulates
CC assembly of the actin cytoskeleton. Controls insulin-dependent glucose
CC uptake among inositol 3,4,5-trisphosphate phosphatases; therefore, is
CC the specific regulator for insulin signaling in skeletal muscle
CC (PubMed:22247557, PubMed:22751929). {ECO:0000250|UniProtKB:Q9BT40,
CC ECO:0000269|PubMed:22247557, ECO:0000269|PubMed:22751929}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,4,5-trisphosphate + H2O = 1D-myo-inositol
CC 1,4-bisphosphate + phosphate; Xref=Rhea:RHEA:19797,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58282,
CC ChEBI:CHEBI:203600; EC=3.1.3.56;
CC Evidence={ECO:0000250|UniProtKB:Q9BT40, ECO:0000269|PubMed:22247557,
CC ECO:0000269|PubMed:22751929};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-
CC trisphosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-3,4-bisphosphate) + phosphate; Xref=Rhea:RHEA:43548,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:83416,
CC ChEBI:CHEBI:83417; Evidence={ECO:0000250|UniProtKB:Q9BT40};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-
CC inositol 1,3,4-trisphosphate + phosphate; Xref=Rhea:RHEA:11392,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57895,
CC ChEBI:CHEBI:58414; EC=3.1.3.56;
CC Evidence={ECO:0000250|UniProtKB:Q9BT40};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol 4-phosphate) + phosphate; Xref=Rhea:RHEA:22764,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58178,
CC ChEBI:CHEBI:58456; EC=3.1.3.36;
CC Evidence={ECO:0000250|UniProtKB:Q9BT40};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-
CC trisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-3,4-bisphosphate) + phosphate; Xref=Rhea:RHEA:25528,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57658,
CC ChEBI:CHEBI:57836; EC=3.1.3.86;
CC Evidence={ECO:0000250|UniProtKB:Q9BT40};
CC -!- SUBUNIT: Interacts with GPR78; necessary for INPP5K localization at the
CC endoplasmic reticulum. Interacts with PAK1; competes with GPR78.
CC {ECO:0000250|UniProtKB:Q9BT40}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:22247557, ECO:0000269|PubMed:22751929}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9BT40}. Note=Following stimulation with EGF,
CC translocates to membrane ruffles. {ECO:0000250|UniProtKB:Q9BT40}.
CC -!- TISSUE SPECIFICITY: Expressed in the skeletal muscle and the eye.
CC {ECO:0000269|PubMed:28190456}.
CC -!- SIMILARITY: Belongs to the inositol 1,4,5-trisphosphate 5-phosphatase
CC type II family. {ECO:0000305}.
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DR EMBL; U96724; AAC53265.1; -; mRNA.
DR EMBL; U96726; AAC60757.1; -; Genomic_DNA.
DR EMBL; AF483522; AAL90796.1; -; mRNA.
DR EMBL; AF483523; AAL90797.1; -; mRNA.
DR EMBL; AK054436; BAC35778.1; -; mRNA.
DR EMBL; AK078104; BAC37126.1; -; mRNA.
DR EMBL; BC066112; AAH66112.1; -; mRNA.
DR CCDS; CCDS25053.1; -.
DR RefSeq; NP_032942.1; NM_008916.2.
DR AlphaFoldDB; Q8C5L6; -.
DR SMR; Q8C5L6; -.
DR STRING; 10090.ENSMUSP00000006286; -.
DR iPTMnet; Q8C5L6; -.
DR PhosphoSitePlus; Q8C5L6; -.
DR EPD; Q8C5L6; -.
DR jPOST; Q8C5L6; -.
DR MaxQB; Q8C5L6; -.
DR PaxDb; Q8C5L6; -.
DR PRIDE; Q8C5L6; -.
DR ProteomicsDB; 269227; -.
DR Antibodypedia; 22714; 146 antibodies from 25 providers.
DR DNASU; 19062; -.
DR Ensembl; ENSMUST00000006286; ENSMUSP00000006286; ENSMUSG00000006127.
DR GeneID; 19062; -.
DR KEGG; mmu:19062; -.
DR UCSC; uc007kek.1; mouse.
DR CTD; 51763; -.
DR MGI; MGI:1194899; Inpp5k.
DR VEuPathDB; HostDB:ENSMUSG00000006127; -.
DR eggNOG; KOG0565; Eukaryota.
DR GeneTree; ENSGT00940000156538; -.
DR HOGENOM; CLU_011711_3_2_1; -.
DR InParanoid; Q8C5L6; -.
DR OMA; FEHILEM; -.
DR OrthoDB; 772410at2759; -.
DR PhylomeDB; Q8C5L6; -.
DR TreeFam; TF317034; -.
DR Reactome; R-MMU-1660499; Synthesis of PIPs at the plasma membrane.
DR BioGRID-ORCS; 19062; 20 hits in 75 CRISPR screens.
DR ChiTaRS; Inpp5k; mouse.
DR PRO; PR:Q8C5L6; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8C5L6; protein.
DR Bgee; ENSMUSG00000006127; Expressed in pigmented layer of retina and 253 other tissues.
DR ExpressionAtlas; Q8C5L6; baseline and differential.
DR Genevisible; Q8C5L6; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0001726; C:ruffle; ISS:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; ISS:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR GO; GO:0016312; F:inositol bisphosphate phosphatase activity; IMP:UniProtKB.
DR GO; GO:0046030; F:inositol trisphosphate phosphatase activity; ISS:UniProtKB.
DR GO; GO:0052659; F:inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052658; F:inositol-1,4,5-trisphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004445; F:inositol-polyphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0034595; F:phosphatidylinositol phosphate 5-phosphatase activity; ISS:UniProtKB.
DR GO; GO:0034594; F:phosphatidylinositol trisphosphate phosphatase activity; ISS:UniProtKB.
DR GO; GO:0034485; F:phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity; IDA:UniProtKB.
DR GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; ISS:UniProtKB.
DR GO; GO:0005000; F:vasopressin receptor activity; IDA:UniProtKB.
DR GO; GO:0071320; P:cellular response to cAMP; IDA:UniProtKB.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0032870; P:cellular response to hormone stimulus; IDA:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISS:UniProtKB.
DR GO; GO:0016311; P:dephosphorylation; IDA:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0042593; P:glucose homeostasis; IMP:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; ISO:MGI.
DR GO; GO:0043922; P:negative regulation by host of viral transcription; ISS:UniProtKB.
DR GO; GO:0051926; P:negative regulation of calcium ion transport; ISS:UniProtKB.
DR GO; GO:0035305; P:negative regulation of dephosphorylation; IMP:UniProtKB.
DR GO; GO:0010829; P:negative regulation of glucose transmembrane transport; ISS:UniProtKB.
DR GO; GO:2000466; P:negative regulation of glycogen (starch) synthase activity; IMP:UniProtKB.
DR GO; GO:0045719; P:negative regulation of glycogen biosynthetic process; IMP:UniProtKB.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; ISS:UniProtKB.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IMP:UniProtKB.
DR GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; ISS:UniProtKB.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:UniProtKB.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; IMP:UniProtKB.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0090315; P:negative regulation of protein targeting to membrane; ISS:UniProtKB.
DR GO; GO:0045869; P:negative regulation of single stranded viral RNA replication via double stranded DNA intermediate; ISS:UniProtKB.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; ISS:UniProtKB.
DR GO; GO:2001153; P:positive regulation of renal water transport; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0035810; P:positive regulation of urine volume; IDA:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IDA:UniProtKB.
DR GO; GO:0005979; P:regulation of glycogen biosynthetic process; IMP:UniProtKB.
DR GO; GO:0032868; P:response to insulin; IMP:MGI.
DR GO; GO:0097178; P:ruffle assembly; ISS:UniProtKB.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR000300; IPPc.
DR InterPro; IPR041611; SKICH.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR Pfam; PF17751; SKICH; 1.
DR SMART; SM00128; IPPc; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Endoplasmic reticulum; Hydrolase; Lipid metabolism;
KW Reference proteome.
FT CHAIN 1..468
FT /note="Inositol polyphosphate 5-phosphatase K"
FT /id="PRO_0000209728"
FT REGION 34..337
FT /note="Catalytic"
FT /evidence="ECO:0000255"
FT REGION 318..448
FT /note="Required for interaction with GPR78 and PAK1"
FT /evidence="ECO:0000250|UniProtKB:Q9BT40"
FT REGION 340..468
FT /note="Required for ruffle localization"
FT CONFLICT 329
FT /note="D -> E (in Ref. 3; BAC37126)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 468 AA; 54159 MW; F2E1CA370B97A8A1 CRC64;
MQHGDRNTPG YREGIMSAVS LRRPSAPKGF ALSVHVVTWN VASAAPTVDL SDLLQLNNQD
LNLDIYIIGL QEMNFGIISL LSDAAFEDPW SSLFMDMLSP LNFVKISQVR MQGLLLLVFA
KYQHLPYIQI ISTKSTPTGL YGYWGNKGGV NVCLKLYGYY VSIINCHLPP HMYNNDQRLE
HFDRILESLT FEGYDVPNIL DHDLILWFGD MNFRIEDFGL LFVQESITRK YYKELWEKDQ
LFIAKKNDQL LREFQEGPLL FPPTYKFDRH SNNYDTSEKK RKPAWTDRIL WRLKRQPSQA
SPLASSVPTS YFLLTLKNYV SHMAYSISDH KPVTGTFDLE LNPLMSVPLI TMMPEHLWTM
ENDMLISYTS TPEFLSSSWD WIGLYKVGMR HINDYVAYVW VGDNQVSYGN NPNQVYINIS
AIPDTEDQFL LCYYSNNLHS VVGISQPFKI PIRSFLREDT LYEPEPQI
