KLF10_HUMAN
ID KLF10_HUMAN Reviewed; 480 AA.
AC Q13118; A8MVH0; B2R794; L0R4P6; L0R679; O75411; Q503B2;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Krueppel-like factor 10;
DE AltName: Full=EGR-alpha;
DE AltName: Full=Transforming growth factor-beta-inducible early growth response protein 1;
DE Short=TGFB-inducible early growth response protein 1;
DE Short=TIEG-1;
GN Name=KLF10; Synonyms=TIEG, TIEG1;
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 2), AND FUNCTION.
RX PubMed=8584037; DOI=10.1210/mend.9.11.8584037;
RA Blok L.J., Grossmann M.E., Perry J.E., Tindall D.J.;
RT "Characterization of an early growth response gene, which encodes a zinc
RT finger transcription factor, potentially involved in cell cycle
RT regulation.";
RL Mol. Endocrinol. 9:1610-1620(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INDUCTION.
RX PubMed=8532536; DOI=10.1093/nar/23.23.4907;
RA Subramaniam M., Harris S.A., Oursler M.J., Rasmussen K., Riggs B.L.,
RA Spelsberg T.C.;
RT "Identification of a novel TGF-beta-regulated gene encoding a putative zinc
RT finger protein in human osteoblasts.";
RL Nucleic Acids Res. 23:4907-4912(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9721211; DOI=10.1006/geno.1998.5388;
RA Fautsch M.P., Vrabel A., Subramaniam M., Hefferen T.E., Spelsberg T.C.,
RA Wieben E.D.;
RT "TGFbeta-inducible early gene (TIEG) also codes for early growth response
RT alpha (EGRalpha): evidence of multiple transcripts from alternate
RT promoters.";
RL Genomics 51:408-416(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), AND ALTERNATIVE SPLICING.
RX PubMed=23134681; DOI=10.1096/fj.12-220319;
RA Camacho-Vanegas O., Till J., Miranda-Lorenzo I., Ozturk B., Camacho S.C.,
RA Martignetti J.A.;
RT "Shaking the family tree: Identification of novel and biologically active
RT alternatively spliced isoforms across the KLF family of transcription
RT factors.";
RL FASEB J. 27:432-436(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Amygdala;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Eye, and Placenta;
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 [10]
RP INTERACTION WITH SIAH1, UBIQUITINATION, AND PROTEASOMAL DEGRADATION.
RX PubMed=12072443; DOI=10.1074/jbc.m204812200;
RA Johnsen S.A., Subramaniam M., Monroe D.G., Janknecht R., Spelsberg T.C.;
RT "Modulation of transforming growth factor beta (TGFbeta)/Smad
RT transcriptional responses through targeted degradation of TGFbeta-inducible
RT early gene-1 by human seven in absentia homologue.";
RL J. Biol. Chem. 277:30754-30759(2002).
RN [11]
RP DNA-BINDING.
RX PubMed=12804117; DOI=10.1089/104454903321655819;
RA Chrisman H.R., Tindall D.J.;
RT "Identification and characterization of a consensus DNA binding element for
RT the zinc finger transcription factor TIEG/EGRalpha.";
RL DNA Cell Biol. 22:187-199(2003).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP STRUCTURE BY NMR OF 353-423.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the first and second ZF-C2H2 domains from human
RT krueppel-like factor 10.";
RL Submitted (APR-2008) to the PDB data bank.
CC -!- FUNCTION: Transcriptional repressor which binds to the consensus
CC sequence 5'-GGTGTG-3'. Plays a role in the regulation of the circadian
CC clock; binds to the GC box sequence in the promoter of the core clock
CC component ARTNL/BMAL1 and represses its transcriptional activity.
CC Regulates the circadian expression of genes involved in lipogenesis,
CC gluconeogenesis, and glycolysis in the liver. Represses the expression
CC of PCK2, a rate-limiting step enzyme of gluconeogenesis (By
CC similarity). May play a role in the cell cycle regulation.
CC {ECO:0000250|UniProtKB:O89091, ECO:0000269|PubMed:8584037}.
CC -!- INTERACTION:
CC Q13118; P08047: SP1; NbExp=2; IntAct=EBI-1389509, EBI-298336;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O89091}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q13118-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13118-2; Sequence=VSP_042653;
CC Name=3;
CC IsoId=Q13118-3; Sequence=VSP_042653, VSP_047483, VSP_047484;
CC Name=4;
CC IsoId=Q13118-4; Sequence=VSP_042653, VSP_047482, VSP_047485;
CC -!- INDUCTION: By TGFB1 and BMP2. {ECO:0000269|PubMed:8532536}.
CC -!- PTM: Ubiquitinated; mediated by SIAH1 and leading to its subsequent
CC proteasomal degradation. {ECO:0000269|PubMed:12072443}.
CC -!- SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; S81439; AAB36088.1; -; mRNA.
DR EMBL; U21847; AAC50340.1; -; mRNA.
DR EMBL; AF050110; AAC34293.1; -; Genomic_DNA.
DR EMBL; AF050110; AAC34294.1; -; Genomic_DNA.
DR EMBL; HF546210; CCO02796.1; -; mRNA.
DR EMBL; HF546211; CCO02797.1; -; mRNA.
DR EMBL; BT006634; AAP35280.1; -; mRNA.
DR EMBL; AK312894; BAG35741.1; -; mRNA.
DR EMBL; AP002851; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471060; EAW91850.1; -; Genomic_DNA.
DR EMBL; BC011538; AAH11538.1; -; mRNA.
DR EMBL; BC095399; AAH95399.1; -; mRNA.
DR CCDS; CCDS47905.1; -. [Q13118-2]
DR CCDS; CCDS6294.1; -. [Q13118-1]
DR RefSeq; NP_001027453.1; NM_001032282.3. [Q13118-2]
DR RefSeq; NP_005646.1; NM_005655.3. [Q13118-1]
DR PDB; 2EPA; NMR; -; A=359-423.
DR PDBsum; 2EPA; -.
DR AlphaFoldDB; Q13118; -.
DR SMR; Q13118; -.
DR BioGRID; 112927; 37.
DR CORUM; Q13118; -.
DR ELM; Q13118; -.
DR IntAct; Q13118; 32.
DR MINT; Q13118; -.
DR STRING; 9606.ENSP00000285407; -.
DR BindingDB; Q13118; -.
DR ChEMBL; CHEMBL3407312; -.
DR DrugCentral; Q13118; -.
DR iPTMnet; Q13118; -.
DR PhosphoSitePlus; Q13118; -.
DR BioMuta; KLF10; -.
DR DMDM; 11387050; -.
DR jPOST; Q13118; -.
DR MassIVE; Q13118; -.
DR MaxQB; Q13118; -.
DR PaxDb; Q13118; -.
DR PeptideAtlas; Q13118; -.
DR PRIDE; Q13118; -.
DR ProteomicsDB; 59171; -. [Q13118-1]
DR ProteomicsDB; 59172; -. [Q13118-2]
DR TopDownProteomics; Q13118-1; -. [Q13118-1]
DR Antibodypedia; 26326; 324 antibodies from 34 providers.
DR DNASU; 7071; -.
DR Ensembl; ENST00000285407.11; ENSP00000285407.6; ENSG00000155090.15. [Q13118-1]
DR Ensembl; ENST00000395884.3; ENSP00000379222.3; ENSG00000155090.15. [Q13118-2]
DR GeneID; 7071; -.
DR KEGG; hsa:7071; -.
DR MANE-Select; ENST00000285407.11; ENSP00000285407.6; NM_005655.4; NP_005646.1.
DR UCSC; uc011lhj.3; human. [Q13118-1]
DR CTD; 7071; -.
DR DisGeNET; 7071; -.
DR GeneCards; KLF10; -.
DR HGNC; HGNC:11810; KLF10.
DR HPA; ENSG00000155090; Low tissue specificity.
DR MIM; 601878; gene.
DR neXtProt; NX_Q13118; -.
DR OpenTargets; ENSG00000155090; -.
DR PharmGKB; PA36517; -.
DR VEuPathDB; HostDB:ENSG00000155090; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000159405; -.
DR HOGENOM; CLU_046370_1_0_1; -.
DR InParanoid; Q13118; -.
DR OMA; CQPMVFM; -.
DR OrthoDB; 582598at2759; -.
DR PhylomeDB; Q13118; -.
DR TreeFam; TF315506; -.
DR PathwayCommons; Q13118; -.
DR SignaLink; Q13118; -.
DR SIGNOR; Q13118; -.
DR BioGRID-ORCS; 7071; 23 hits in 1095 CRISPR screens.
DR ChiTaRS; KLF10; human.
DR EvolutionaryTrace; Q13118; -.
DR GeneWiki; KLF10; -.
DR GenomeRNAi; 7071; -.
DR Pharos; Q13118; Tbio.
DR PRO; PR:Q13118; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q13118; protein.
DR Bgee; ENSG00000155090; Expressed in mucosa of paranasal sinus and 202 other tissues.
DR Genevisible; Q13118; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0030282; P:bone mineralization; IEA:Ensembl.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0009267; P:cellular response to starvation; ISS:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; TAS:ProtInc.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IEA:Ensembl.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Biological rhythms; DNA-binding;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..480
FT /note="Krueppel-like factor 10"
FT /id="PRO_0000047177"
FT ZN_FING 369..393
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 399..423
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 429..451
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..12
FT /note="MLNFGASLQQTA -> M (in isoform 2, isoform 3 and
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:23134681, ECO:0000303|PubMed:8584037,
FT ECO:0000303|Ref.5"
FT /id="VSP_042653"
FT VAR_SEQ 91..134
FT /note="CLTPPYSPSDFEPSQVSNLMAPAPSTVHFKSLSDTAKPHIAAPF -> EKSL
FT SAVAGKVVKGGLPVLMNCPDTGEPTRVRRNLRAPCVTGGS (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:23134681"
FT /id="VSP_047482"
FT VAR_SEQ 91..102
FT /note="CLTPPYSPSDFE -> QQKSLLRLIHQG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:23134681"
FT /id="VSP_047483"
FT VAR_SEQ 103..480
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:23134681"
FT /id="VSP_047484"
FT VAR_SEQ 135..480
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:23134681"
FT /id="VSP_047485"
FT VARIANT 249
FT /note="S -> F (in dbSNP:rs4734653)"
FT /id="VAR_052716"
FT TURN 374..376
FT /evidence="ECO:0007829|PDB:2EPA"
FT STRAND 379..382
FT /evidence="ECO:0007829|PDB:2EPA"
FT HELIX 383..393
FT /evidence="ECO:0007829|PDB:2EPA"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:2EPA"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:2EPA"
FT STRAND 409..412
FT /evidence="ECO:0007829|PDB:2EPA"
FT HELIX 413..419
FT /evidence="ECO:0007829|PDB:2EPA"
FT TURN 420..422
FT /evidence="ECO:0007829|PDB:2EPA"
SQ SEQUENCE 480 AA; 52555 MW; 78B1EBB0DB97579D CRC64;
MLNFGASLQQ TAEERMEMIS ERPKESMYSW NKTAEKSDFE AVEALMSMSC SWKSDFKKYV
ENRPVTPVSD LSEEENLLPG TPDFHTIPAF CLTPPYSPSD FEPSQVSNLM APAPSTVHFK
SLSDTAKPHI AAPFKEEEKS PVSAPKLPKA QATSVIRHTA DAQLCNHQTC PMKAASILNY
QNNSFRRRTH LNVEAARKNI PCAAVSPNRS KCERNTVADV DEKASAALYD FSVPSSETVI
CRSQPAPVSP QQKSVLVSPP AVSAGGVPPM PVICQMVPLP ANNPVVTTVV PSTPPSQPPA
VCPPVVFMGT QVPKGAVMFV VPQPVVQSSK PPVVSPNGTR LSPIAPAPGF SPSAAKVTPQ
IDSSRIRSHI CSHPGCGKTY FKSSHLKAHT RTHTGEKPFS CSWKGCERRF ARSDELSRHR
RTHTGEKKFA CPMCDRRFMR SDHLTKHARR HLSAKKLPNW QMEVSKLNDI ALPPTPAPTQ
