PANK4_MOUSE
ID PANK4_MOUSE Reviewed; 820 AA.
AC Q80YV4; B1AZN5; B1AZN6; Q7M751; Q8BQE9;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=4'-phosphopantetheine phosphatase {ECO:0000250|UniProtKB:Q9NVE7};
DE EC=3.1.3.- {ECO:0000250|UniProtKB:Q9NVE7};
DE AltName: Full=Inactive pantothenic acid kinase 4 {ECO:0000250|UniProtKB:Q9NVE7};
DE Short=mPanK4 {ECO:0000305};
GN Name=Pank4;
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 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-820 (ISOFORM 3).
RX PubMed=11479594; DOI=10.1038/ng572;
RA Zhou B., Westaway S.K., Levinson B., Johnson M.A., Gitschier J.,
RA Hayflick S.J.;
RT "A novel pantothenate kinase gene (PANK2) is defective in Hallervorden-
RT Spatz syndrome.";
RL Nat. Genet. 28:345-349(2001).
RN [5]
RP NITRATION [LARGE SCALE ANALYSIS] AT TYR-320, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16800626; DOI=10.1021/bi060474w;
RA Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H., Lacan G.,
RA Melega W.P., Camp D.G. II, Smith R.D., Smith D.J., Squier T.C.,
RA Bigelow D.J.;
RT "Endogenously nitrated proteins in mouse brain: links to neurodegenerative
RT disease.";
RL Biochemistry 45:8009-8022(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-404 AND THR-406, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and 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 [7]
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=30585370; DOI=10.1002/humu.23696;
RA Sun M., Chen C., Hou S., Li X., Wang H., Zhou J., Chen X., Liu P.,
RA Kijlstra A., Lin S., Ye J.;
RT "A novel mutation of PANK4 causes autosomal dominant congenital posterior
RT cataract.";
RL Hum. Mutat. 40:380-391(2019).
CC -!- FUNCTION: Phosphatase which shows a preference for 4'-
CC phosphopantetheine and its oxidatively damaged forms (sulfonate or S-
CC sulfonate), providing strong indirect evidence that the phosphatase
CC activity pre-empts damage in the coenzyme A (CoA) pathway. Hydrolyzing
CC excess 4'-phosphopantetheine could constitute a directed overflow
CC mechanism to prevent its oxidation to the S-sulfonate, sulfonate, or
CC other forms. Hydrolyzing 4'-phosphopantetheine sulfonate or S-sulfonate
CC would forestall their conversion to inactive forms of CoA and acyl
CC carrier protein. May play a role in the physiological regulation of CoA
CC intracellular levels. {ECO:0000250|UniProtKB:Q9NVE7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-4'-phosphopantetheine + H2O = (R)-pantetheine + phosphate;
CC Xref=Rhea:RHEA:68328, ChEBI:CHEBI:15377, ChEBI:CHEBI:16753,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:61723;
CC Evidence={ECO:0000250|UniProtKB:Q9NVE7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68329;
CC Evidence={ECO:0000250|UniProtKB:Q9NVE7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-4'-phosphopantetheine sulfonate + H2O = (R)-pantetheine
CC sulfonate + phosphate; Xref=Rhea:RHEA:68336, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:177300, ChEBI:CHEBI:177301;
CC Evidence={ECO:0000250|UniProtKB:Q9NVE7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68337;
CC Evidence={ECO:0000250|UniProtKB:Q9NVE7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-4'-phospho-S-sulfopantetheine + H2O = (R)-S-
CC sulfopantetheine + phosphate; Xref=Rhea:RHEA:68340,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:177302,
CC ChEBI:CHEBI:177303; Evidence={ECO:0000250|UniProtKB:Q9NVE7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68341;
CC Evidence={ECO:0000250|UniProtKB:Q9NVE7};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9NVE7};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000250|UniProtKB:Q9NVE7};
CC -!- ACTIVITY REGULATION: Activity is strongly promoted by Co(2+), Ni(2+),
CC Mg(2+) and Mn(2+). Activity is inhibited by EDTA.
CC {ECO:0000250|UniProtKB:Q9NVE7}.
CC -!- SUBUNIT: Homodimer. Interacts with PKM. {ECO:0000250|UniProtKB:Q923S8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q923S8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q80YV4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80YV4-2; Sequence=VSP_020381;
CC Name=3;
CC IsoId=Q80YV4-3; Sequence=VSP_020379, VSP_020380;
CC -!- TISSUE SPECIFICITY: Expressed in liver, kidney, brain cortex and eye
CC lens (at protein level). {ECO:0000269|PubMed:30585370}.
CC -!- DOMAIN: Subfamily II proteins have an EGMGR motif about 50 residues
CC from the C-terminus (By similarity). This motif lies near the metal-
CC binding residues in the putative substrate-binding cleft 2 (By
CC similarity). Subfamily II proteins occur only in eukaryotes, in two
CC forms: as a stand-alone unit in plants, and as a C-terminal domain of
CC pantothenate kinases in plants, animals, and chytrid fungi (By
CC similarity). {ECO:0000250|UniProtKB:Q8K4K6}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice have a body weight and a lifespan
CC similar to wild-type animals. About 10% of the animals start developing
CC cataract at 2 months. At 15 months, 50% homozygous animals are
CC affected. Heterozygous animals develop cataract later, with 10% animals
CC affected at 9 months and 25% at 15. {ECO:0000269|PubMed:30585370}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the type II
CC pantothenate kinase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the damage-control
CC phosphatase family. Phosphopantetheine phosphatase II subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Despite belonging to the type II pantothenate kinase family,
CC the pantothenate kinase domain contains a Val residue at position 147
CC and a Trp residue at position 211 instead of the two conserved active
CC site residues, Glu and Arg. Lacks pantothenate kinase activity.
CC {ECO:0000250|UniProtKB:Q9NVE7}.
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DR EMBL; AK050894; BAC34450.1; -; mRNA.
DR EMBL; BX004788; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC050089; AAH50089.1; -; mRNA.
DR EMBL; BK000016; DAA00010.1; -; mRNA.
DR CCDS; CCDS19019.1; -. [Q80YV4-2]
DR CCDS; CCDS84834.1; -. [Q80YV4-1]
DR RefSeq; NP_001292733.1; NM_001305804.1. [Q80YV4-1]
DR RefSeq; NP_766578.2; NM_172990.5. [Q80YV4-2]
DR AlphaFoldDB; Q80YV4; -.
DR SMR; Q80YV4; -.
DR BioGRID; 234679; 10.
DR IntAct; Q80YV4; 7.
DR STRING; 10090.ENSMUSP00000030931; -.
DR iPTMnet; Q80YV4; -.
DR PhosphoSitePlus; Q80YV4; -.
DR EPD; Q80YV4; -.
DR MaxQB; Q80YV4; -.
DR PeptideAtlas; Q80YV4; -.
DR PRIDE; Q80YV4; -.
DR ProteomicsDB; 294155; -. [Q80YV4-1]
DR ProteomicsDB; 294156; -. [Q80YV4-2]
DR ProteomicsDB; 294157; -. [Q80YV4-3]
DR Antibodypedia; 1627; 140 antibodies from 21 providers.
DR DNASU; 269614; -.
DR Ensembl; ENSMUST00000030931; ENSMUSP00000030931; ENSMUSG00000029056. [Q80YV4-2]
DR Ensembl; ENSMUST00000070953; ENSMUSP00000064330; ENSMUSG00000029056. [Q80YV4-1]
DR GeneID; 269614; -.
DR KEGG; mmu:269614; -.
DR UCSC; uc008wcl.3; mouse. [Q80YV4-2]
DR UCSC; uc012dqn.2; mouse. [Q80YV4-1]
DR CTD; 55229; -.
DR MGI; MGI:2387466; Pank4.
DR VEuPathDB; HostDB:ENSMUSG00000029056; -.
DR eggNOG; KOG2201; Eukaryota.
DR eggNOG; KOG4584; Eukaryota.
DR GeneTree; ENSGT00940000158896; -.
DR HOGENOM; CLU_012496_1_1_1; -.
DR InParanoid; Q80YV4; -.
DR OMA; NHPLSMH; -.
DR OrthoDB; 865329at2759; -.
DR PhylomeDB; Q80YV4; -.
DR TreeFam; TF342917; -.
DR Reactome; R-MMU-196783; Coenzyme A biosynthesis.
DR BioGRID-ORCS; 269614; 0 hits in 58 CRISPR screens.
DR ChiTaRS; Pank4; mouse.
DR PRO; PR:Q80YV4; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q80YV4; protein.
DR Bgee; ENSMUSG00000029056; Expressed in retinal neural layer and 231 other tissues.
DR ExpressionAtlas; Q80YV4; baseline and differential.
DR Genevisible; Q80YV4; MM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004594; F:pantothenate kinase activity; IBA:GO_Central.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IBA:GO_Central.
DR Gene3D; 1.20.1700.10; -; 1.
DR InterPro; IPR036075; ARMT-1-like_metal-bd_sf.
DR InterPro; IPR002791; ARMT1-like_metal-bd.
DR InterPro; IPR035073; At2g17340_3_helix_bundle.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR015844; PanK_long.
DR InterPro; IPR004567; Type_II_PanK.
DR PANTHER; PTHR12280; PTHR12280; 2.
DR Pfam; PF01937; ARMT1-like_dom; 1.
DR Pfam; PF03630; Fumble; 1.
DR PIRSF; PIRSF036939; PanK_long; 1.
DR SUPFAM; SSF111321; SSF111321; 2.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR00555; panK_eukar; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Coenzyme A biosynthesis;
KW Cytoplasm; Hydrolase; Manganese; Metal-binding; Nickel; Nitration;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NVE7"
FT CHAIN 2..820
FT /note="4'-phosphopantetheine phosphatase"
FT /id="PRO_0000249248"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..402
FT /note="Pantothenate kinase"
FT /evidence="ECO:0000250|UniProtKB:Q9NVE7"
FT REGION 403..820
FT /note="4'-phosphopantetheine phosphatase"
FT /evidence="ECO:0000250|UniProtKB:Q9NVE7"
FT MOTIF 771..775
FT /note="Subfamily II EGMGR motif"
FT /evidence="ECO:0000250|UniProtKB:Q9NVE7"
FT BINDING 196
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
FT BINDING 623
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic; for phosphatase activity"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 624
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic; for phosphatase activity"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 659
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic; for phosphatase activity"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9NVE7"
FT MOD_RES 320
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0007744|PubMed:16800626"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NVE7"
FT MOD_RES 404
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 406
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 373..374
FT /note="NP -> SE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11479594"
FT /id="VSP_020379"
FT VAR_SEQ 375..820
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11479594"
FT /id="VSP_020380"
FT VAR_SEQ 703..749
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020381"
FT CONFLICT 81
FT /note="I -> T (in Ref. 3; AAH50089)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="D -> G (in Ref. 3; AAH50089)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="S -> A (in Ref. 4; DAA00010)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="T -> I (in Ref. 3; AAH50089)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="S -> F (in Ref. 3; AAH50089)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="L -> P (in Ref. 3; AAH50089)"
FT /evidence="ECO:0000305"
FT CONFLICT 479
FT /note="K -> E (in Ref. 1; BAC34450)"
FT /evidence="ECO:0000305"
FT CONFLICT 635
FT /note="P -> T (in Ref. 1; BAC34450)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 820 AA; 91522 MW; 0D88CA48A8B87D3A CRC64;
MAERGASGGG SGGDSLDKSI TLPPDEIFRN LENAKRFAID IGGSLTKLAY YSTVQHKVAK
VRSFDHPGKD VEQDHEPPYE ISVQEEITAR LHFIKFENTY MEACLDFIRD HLVNTETKVI
QATGGGAYKF KDLIEEKLRL KVDKEDVMTC LIKGCNFVLK NIPHEAFMYQ KDSDPEFRFQ
TNHPNIFPYL LVNIGSGVSI VKVETEDRFE WIGGSSIGGG TFWGLGALLT KTKKFDELLQ
LASRGRHANV DMLVQDIYGG AHQTLGLSGN LIASSFGKSA TADREFSKED MAKSLLHMIS
NDIGQLACLY AKLHGLDRVY FGGFFIRGHP VTMRTITYSI NFFSKGEVQA LFLRHEGYLG
AIGAFLKGAE QDNPNQYSWG ENYAASSGLM STSPELCPTQ RARSGTFDLL EMDRLERPLV
NLPLLLDPSS YVPDTVDLTD DALARQYWLT CFEEALDGVV KRAVASQPES MDAVERAEKF
RQKYWGKLQT LRHQPFAYGT LTVRSLLDTR EHCLNEFNFP DPYSKVKQKE NGLALKCFQS
VTRSLDSLGW EERQLALVKG LLAGNVFDWG AKAVSDVLES DPQFGFEEAK RKLQERPWLV
DSYTKWLQRL KGPPHKCALI FADNSGIDII LGVFPFVREL LFRGTEVILA CNSGPALNDV
TYSESLIVAE RIAAMDPIIC TALREDRLLL VQTGSSSPCL DLSLCTSRTT TCMVLPFAMW
VLWTKLKSLV EKCLSPLSIL LACSVLSAKS RLDKGLAVLV RERGADLVVI EGMGRAIHTN
YHALLRCESL KLAVVKNAWL AERLGGQLFS VIFKYEVPTK
