PANK1_MOUSE
ID PANK1_MOUSE Reviewed; 548 AA.
AC Q8K4K6; Q9D3K1; Q9QXM8;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Pantothenate kinase 1;
DE Short=mPank;
DE Short=mPank1;
DE EC=2.7.1.33 {ECO:0000269|PubMed:10625688, ECO:0000269|PubMed:12095677, ECO:0000269|PubMed:16040613, ECO:0000269|PubMed:17379144, ECO:0000269|PubMed:20559429, ECO:0000269|PubMed:22815849};
DE AltName: Full=Pantothenic acid kinase 1;
GN Name=Pank1; Synonyms=Pank;
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 2), FUNCTION (ISOFORM 2), CATALYTIC
RP ACTIVITY (ISOFORM 2), TISSUE SPECIFICITY (ISOFORMS 1 AND 2), AND ACTIVITY
RP REGULATION (ISOFORM 2).
RX PubMed=10625688; DOI=10.1074/jbc.275.2.1377;
RA Rock C.O., Calder R.B., Karim M.A., Jackowski S.;
RT "Pantothenate kinase regulation of the intracellular concentration of
RT coenzyme A.";
RL J. Biol. Chem. 275:1377-1383(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING, FUNCTION
RP (ISOFORMS 1 AND 2), CATALYTIC ACTIVITY (ISOFORMS 1 AND 2), AND ACTIVITY
RP REGULATION (ISOFORMS 1 AND 2).
RX PubMed=12095677; DOI=10.1016/s0378-1119(02)00564-4;
RA Rock C.O., Karim M.A., Zhang Y.M., Jackowski S.;
RT "The murine pantothenate kinase (Pank1) gene encodes two differentially
RT regulated pantothenate kinase isozymes.";
RL Gene 291:35-43(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Head;
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] (ISOFORM 2).
RC TISSUE=Liver, and Skeletal muscle;
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 (ISOFORM 2), CATALYTIC ACTIVITY (ISOFORM 2), ACTIVITY REGULATION
RP (ISOFORM 2), BIOPHYSICOCHEMICAL PROPERTIES (ISOFORM 2), SUBUNIT (ISOFORM
RP 2), SUBCELLULAR LOCATION (ISOFORM 2), AND TISSUE SPECIFICITY (ISOFORMS 1
RP AND 2).
RX PubMed=16040613; DOI=10.1074/jbc.m506275200;
RA Zhang Y.M., Rock C.O., Jackowski S.;
RT "Feedback regulation of murine pantothenate kinase 3 by coenzyme A and
RT coenzyme A thioesters.";
RL J. Biol. Chem. 280:32594-32601(2005).
RN [6]
RP FUNCTION (ISOFORMS 1 AND 2), CATALYTIC ACTIVITY (ISOFORMS 1 AND 2), AND
RP ACTIVITY REGULATION (ISOFORMS 1 AND 2).
RX PubMed=17379144; DOI=10.1016/j.chembiol.2007.01.013;
RA Zhang Y.M., Chohnan S., Virga K.G., Stevens R.D., Ilkayeva O.R.,
RA Wenner B.R., Bain J.R., Newgard C.B., Lee R.E., Rock C.O., Jackowski S.;
RT "Chemical knockout of pantothenate kinase reveals the metabolic and genetic
RT program responsible for hepatic coenzyme A homeostasis.";
RL Chem. Biol. 14:291-302(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30 AND SER-165, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, and Liver;
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, CATALYTIC ACTIVITY, TISSUE SPECIFICITY (ISOFORM 2), AND
RP DISRUPTION PHENOTYPE.
RX PubMed=20559429; DOI=10.1371/journal.pone.0011107;
RA Leonardi R., Rehg J.E., Rock C.O., Jackowski S.;
RT "Pantothenate kinase 1 is required to support the metabolic transition from
RT the fed to the fasted state.";
RL PLoS ONE 5:e11107-e11107(2010).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=22815849; DOI=10.1371/journal.pone.0040871;
RA Garcia M., Leonardi R., Zhang Y.M., Rehg J.E., Jackowski S.;
RT "Germline deletion of pantothenate kinases 1 and 2 reveals the key roles
RT for CoA in postnatal metabolism.";
RL PLoS ONE 7:e40871-e40871(2012).
RN [10]
RP SUBCELLULAR LOCATION (ISOFORMS 1 AND 2), NUCLEAR LOCALIZATION SIGNAL, AND
RP MUTAGENESIS OF 4-ARG-ARG-5 AND 168-LYS--ARG-183.
RX PubMed=23152917; DOI=10.1371/journal.pone.0049509;
RA Alfonso-Pecchio A., Garcia M., Leonardi R., Jackowski S.;
RT "Compartmentalization of mammalian pantothenate kinases.";
RL PLoS ONE 7:e49509-e49509(2012).
CC -!- FUNCTION: Catalyzes the phosphorylation of pantothenate to generate 4'-
CC phosphopantothenate in the first and rate-determining step of coenzyme
CC A (CoA) synthesis (PubMed:20559429, PubMed:22815849). Required for the
CC hepatic CoA increase during the switch from glucose to fatty acid
CC oxidation that occurs in the fasting state (PubMed:20559429).
CC {ECO:0000269|PubMed:20559429, ECO:0000269|PubMed:22815849}.
CC -!- FUNCTION: [Isoform 1]: Catalyzes the phosphorylation of pantothenate to
CC generate 4'-phosphopantothenate in the first and rate-determining step
CC of coenzyme A (CoA) synthesis. {ECO:0000269|PubMed:12095677,
CC ECO:0000269|PubMed:17379144}.
CC -!- FUNCTION: [Isoform 2]: Catalyzes the phosphorylation of pantothenate to
CC generate 4'-phosphopantothenate in the first and rate-determining step
CC of coenzyme A (CoA) synthesis. {ECO:0000269|PubMed:10625688,
CC ECO:0000269|PubMed:12095677, ECO:0000269|PubMed:16040613,
CC ECO:0000269|PubMed:17379144}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP +
CC H(+); Xref=Rhea:RHEA:16373, ChEBI:CHEBI:10986, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216;
CC EC=2.7.1.33; Evidence={ECO:0000269|PubMed:10625688,
CC ECO:0000269|PubMed:12095677, ECO:0000269|PubMed:16040613,
CC ECO:0000269|PubMed:17379144, ECO:0000269|PubMed:20559429,
CC ECO:0000269|PubMed:22815849};
CC -!- ACTIVITY REGULATION: [Isoform 1]: Strongly inhibited by non-esterified
CC CoA (CoASH), acetyl-CoA and malonyl-CoA (PubMed:12095677). Also
CC inhibited by palmitoyl CoA (PubMed:12095677). Inhibited by calcium
CC hopantenate (PubMed:17379144). {ECO:0000269|PubMed:12095677,
CC ECO:0000269|PubMed:17379144}.
CC -!- ACTIVITY REGULATION: [Isoform 2]: Strongly inhibited by acetyl-CoA and
CC modestly by malonyl-CoA (PubMed:16040613, PubMed:10625688,
CC PubMed:12095677). Refractory to inhibition by both CoA and palmitoyl-
CC CoA (PubMed:16040613). Inhibited by calcium hopantenate
CC (PubMed:17379144). {ECO:0000269|PubMed:10625688,
CC ECO:0000269|PubMed:12095677, ECO:0000269|PubMed:16040613,
CC ECO:0000269|PubMed:17379144}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES: [Isoform 2]:
CC Kinetic parameters:
CC KM=5.7 uM for pantothenate {ECO:0000269|PubMed:16040613};
CC KM=87.0 uM for ATP {ECO:0000269|PubMed:16040613};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 1/5. {ECO:0000269|PubMed:10625688,
CC ECO:0000269|PubMed:12095677, ECO:0000269|PubMed:17379144,
CC ECO:0000269|PubMed:20559429, ECO:0000269|PubMed:22815849}.
CC -!- SUBUNIT: [Isoform 2]: Homodimer. {ECO:0000269|PubMed:16040613}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus
CC {ECO:0000269|PubMed:23152917}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:23152917}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:16040613, ECO:0000269|PubMed:23152917}. Cytoplasmic
CC vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:23152917}.
CC Recycling endosome {ECO:0000269|PubMed:23152917}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=PanK1-alpha;
CC IsoId=Q8K4K6-1; Sequence=Displayed;
CC Name=2; Synonyms=PanK1-beta;
CC IsoId=Q8K4K6-2; Sequence=VSP_004522, VSP_004523;
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Highly expressed in the liver, heart
CC and kidney. {ECO:0000269|PubMed:10625688, ECO:0000269|PubMed:16040613}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Highly expressed in the liver
CC (PubMed:10625688, PubMed:20559429, PubMed:16040613). Expressed at lower
CC levels in the kidney (PubMed:10625688). {ECO:0000269|PubMed:10625688,
CC ECO:0000269|PubMed:16040613, ECO:0000269|PubMed:20559429}.
CC -!- DOMAIN: [Isoform 1]: The N-terminal extension, may be the regulatory
CC domain. {ECO:0000269|PubMed:12095677}.
CC -!- DISRUPTION PHENOTYPE: Pank1 single knockout mice exhibit reduced
CC hepatic CoA levels, a reduced rate of CoA-dependent fatty acid
CC oxidation in the fasting state, impaired gluconeogenesis, and mild
CC hypoglycemia in the fasting state (PubMed:20559429). Show a reduction
CC in pantothenate kinase (PANK) activity of about 50% and 40% in the
CC liver and brain respectively (PubMed:22815849). Pank1 and Pank2 double
CC knockout mice develop progressively severe hypoglycemia and
CC hyperketonemia by postnatal day 10 leading to their death by day 17
CC (PubMed:22815849). A reduction in PANK activity of about 90-95% seen in
CC the liver and brain and hepatocytes show reduced levels of NADH
CC (PubMed:22815849). {ECO:0000269|PubMed:20559429,
CC ECO:0000269|PubMed:22815849}.
CC -!- SIMILARITY: Belongs to the type II pantothenate kinase family.
CC {ECO:0000305}.
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DR EMBL; AF200357; AAF23952.1; -; mRNA.
DR EMBL; AF347700; AAM77216.1; -; mRNA.
DR EMBL; AK017345; BAB30700.1; -; mRNA.
DR EMBL; BC023496; AAH23496.1; -; mRNA.
DR CCDS; CCDS37966.1; -. [Q8K4K6-2]
DR CCDS; CCDS50424.1; -. [Q8K4K6-1]
DR RefSeq; NP_001107811.1; NM_001114339.2. [Q8K4K6-1]
DR RefSeq; NP_076281.1; NM_023792.2. [Q8K4K6-2]
DR AlphaFoldDB; Q8K4K6; -.
DR SMR; Q8K4K6; -.
DR STRING; 10090.ENSMUSP00000043562; -.
DR iPTMnet; Q8K4K6; -.
DR PhosphoSitePlus; Q8K4K6; -.
DR jPOST; Q8K4K6; -.
DR MaxQB; Q8K4K6; -.
DR PaxDb; Q8K4K6; -.
DR PeptideAtlas; Q8K4K6; -.
DR PRIDE; Q8K4K6; -.
DR ProteomicsDB; 294243; -. [Q8K4K6-1]
DR ProteomicsDB; 294244; -. [Q8K4K6-2]
DR Antibodypedia; 35332; 248 antibodies from 28 providers.
DR DNASU; 75735; -.
DR Ensembl; ENSMUST00000036584; ENSMUSP00000043562; ENSMUSG00000033610. [Q8K4K6-1]
DR Ensembl; ENSMUST00000112460; ENSMUSP00000108079; ENSMUSG00000033610. [Q8K4K6-2]
DR GeneID; 75735; -.
DR KEGG; mmu:75735; -.
DR UCSC; uc008hgw.3; mouse. [Q8K4K6-1]
DR CTD; 53354; -.
DR MGI; MGI:1922985; Pank1.
DR VEuPathDB; HostDB:ENSMUSG00000033610; -.
DR eggNOG; KOG2201; Eukaryota.
DR GeneTree; ENSGT00940000157373; -.
DR HOGENOM; CLU_011154_4_1_1; -.
DR InParanoid; Q8K4K6; -.
DR OMA; KQRSFPW; -.
DR OrthoDB; 865329at2759; -.
DR PhylomeDB; Q8K4K6; -.
DR TreeFam; TF314866; -.
DR BRENDA; 2.7.1.33; 3474.
DR Reactome; R-MMU-196783; Coenzyme A biosynthesis.
DR SABIO-RK; Q8K4K6; -.
DR UniPathway; UPA00241; UER00352.
DR BioGRID-ORCS; 75735; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Pank1; mouse.
DR PRO; PR:Q8K4K6; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8K4K6; protein.
DR Bgee; ENSMUSG00000033610; Expressed in indifferent gonad and 257 other tissues.
DR ExpressionAtlas; Q8K4K6; baseline and differential.
DR Genevisible; Q8K4K6; MM.
DR GO; GO:0071944; C:cell periphery; IDA:MGI.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:1905502; F:acetyl-CoA binding; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004594; F:pantothenate kinase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IMP:MGI.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR004567; Type_II_PanK.
DR PANTHER; PTHR12280; PTHR12280; 1.
DR Pfam; PF03630; Fumble; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR00555; panK_eukar; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Coenzyme A biosynthesis; Cytoplasm;
KW Cytoplasmic vesicle; Endosome; Kinase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..548
FT /note="Pantothenate kinase 1"
FT /id="PRO_0000161803"
FT REGION 1..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1..8
FT /note="Nucleolar localization signal"
FT /evidence="ECO:0000269|PubMed:23152917"
FT MOTIF 168..185
FT /note="Nucleolar localization signal"
FT /evidence="ECO:0000269|PubMed:23152917"
FT COMPBIAS 67..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 313
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9H999"
FT BINDING 367
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q8TE04"
FT BINDING 370
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q8TE04"
FT BINDING 382
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q8TE04"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..175
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10625688,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_004522"
FT VAR_SEQ 176..185
FT /note="MDSGRKNRPP -> MKLVNGRKQT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10625688,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_004523"
FT MUTAGEN 4..5
FT /note="RR->AA: Loss of nuclear localization."
FT /evidence="ECO:0000269|PubMed:23152917"
FT MUTAGEN 168..183
FT /note="KKCRLRRRMDSGRKNR->AACALAAAMDSGAANA: Loss of nuclear
FT localization."
FT /evidence="ECO:0000269|PubMed:23152917"
SQ SEQUENCE 548 AA; 60091 MW; C916709D048E429B CRC64;
MRGRRAPRPG STEVPAAARD ADTLRARAAS PVRGAQLAED VGTPTGGGEE RRGHQLPTAA
PRLRESKPQG GSEDRGTADR DLQRGCQSRS PRTAPPVPGM GDRGAQHERA ALQSPGAPEG
AAAAVNGLLH NGFHPSAASS RDPPAPRFQL PSELQPQPLF AQHDSPAKKC RLRRRMDSGR
KNRPPFPWFG MDIGGTLVKL VYFEPKDITA EEEQEEVENL KSIRKYLTSN TAYGKTGIRD
VHLELKNLTM CGRKGNLHFI RFPTCAMHLF IQMGSEKNFS SLHTTLCATG GGAFKFEEDF
RMIADLQLHK LDELDCLIQG LLYVDSVGFN GKPECYYFEN PTNPELCQKK PYCLDNPYPM
LLVNMGSGVS ILAVYSKDNY KRVTGTSLGG GTFLGLCCLL TGCETFEEAL DMAAKGDSTN
VDKLVKDIYG GDYERFGLQG SAVASSFGNM MSKEKRESIS KEDLARATLV TITNNIGSIA
RMCALNENID RVVFVGNFLR INMVSMKLLA YAMDFWSKGQ LKALFLEHEG YFGAVGALLE
LFKMTDTQ
