OVOL2_MOUSE
ID OVOL2_MOUSE Reviewed; 274 AA.
AC Q8CIV7; Q505Q7; Q6F661; Q8CIV6; Q8K0D6; Q9D949;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Transcription factor Ovo-like 2;
DE Short=mOvo2;
DE AltName: Full=Zinc finger OVO2;
DE AltName: Full=Zinc finger protein 339;
DE AltName: Full=Zinc finger protein mOVO;
GN Name=Ovol2; Synonyms=Ovo2, Zfp339, Znf339;
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] (ISOFORMS 1 AND 3), TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=9468311; DOI=10.1016/s0014-5793(97)01567-6;
RA Masu Y., Ikeda S., Okuda-Ashitaka E., Sato E., Ito S.;
RT "Expression of murine novel zinc finger proteins highly homologous to
RT Drosophila ovo gene product in testis.";
RL FEBS Lett. 421:224-228(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC STRAIN=CD-1;
RX PubMed=12213202; DOI=10.1006/geno.2002.6831;
RA Li B., Dai Q., Li L., Nair M., Mackay D.R., Dai X.;
RT "Ovol2, a mammalian homolog of Drosophila ovo: gene structure, chromosomal
RT mapping, and aberrant expression in blind-sterile mice.";
RL Genomics 80:319-325(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, DEVELOPMENTAL
RP STAGE, AND TISSUE SPECIFICITY.
RC STRAIN=ICR; TISSUE=Liver, and Testis;
RX PubMed=15225875; DOI=10.1016/j.gene.2004.03.013;
RA Unezaki S., Nishizawa M., Okuda-Ashitaka E., Masu Y., Mukai M.,
RA Kobayashi S., Sawamoto K., Okano H., Ito S.;
RT "Characterization of the isoforms of MOVO zinc finger protein, a mouse
RT homologue of Drosophila Ovo, as a transcription factors.";
RL Gene 336:47-58(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Pancreas;
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N, and NMRI; TISSUE=Colon, and Mammary tumor;
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 [8]
RP DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND FUNCTION.
RX PubMed=16423343; DOI=10.1016/j.ydbio.2005.12.003;
RA Mackay D.R., Hu M., Li B., Rheaume C., Dai X.;
RT "The mouse Ovol2 gene is required for cranial neural tube development.";
RL Dev. Biol. 291:38-52(2006).
RN [9]
RP INDUCTION, AND FUNCTION.
RX PubMed=23319585; DOI=10.1074/jbc.m112.418376;
RA Zhang T., Zhu Q., Xie Z., Chen Y., Qiao Y., Li L., Jing N.;
RT "The zinc finger transcription factor Ovol2 acts downstream of the bone
RT morphogenetic protein pathway to regulate the cell fate decision between
RT neuroectoderm and mesendoderm.";
RL J. Biol. Chem. 288:6166-6177(2013).
RN [10]
RP FUNCTION.
RX PubMed=24735878; DOI=10.1016/j.devcel.2014.03.005;
RA Lee B., Villarreal-Ponce A., Fallahi M., Ovadia J., Sun P., Yu Q.C.,
RA Ito S., Sinha S., Nie Q., Dai X.;
RT "Transcriptional mechanisms link epithelial plasticity to adhesion and
RT differentiation of epidermal progenitor cells.";
RL Dev. Cell 29:47-58(2014).
RN [11]
RP FUNCTION.
RX PubMed=24735879; DOI=10.1016/j.devcel.2014.03.006;
RA Watanabe K., Villarreal-Ponce A., Sun P., Salmans M.L., Fallahi M.,
RA Andersen B., Dai X.;
RT "Mammary morphogenesis and regeneration require the inhibition of EMT at
RT terminal end buds by Ovol2 transcriptional repressor.";
RL Dev. Cell 29:59-74(2014).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28059165; DOI=10.1038/srep40056;
RA Hayashi M., Shinozuka Y., Shigenobu S., Sato M., Sugimoto M., Ito S.,
RA Abe K., Kobayashi S.;
RT "Conserved role of Ovo in germline development in mouse and Drosophila.";
RL Sci. Rep. 7:40056-40056(2017).
CC -!- FUNCTION: Zinc-finger transcription repressor factor (PubMed:15225875,
CC PubMed:23319585). Plays a critical role in maintaining the identity of
CC epithelial lineages by suppressing epithelial-to mesenchymal transition
CC (EMT) mainly through the repression of ZEB1, an EMT inducer
CC (PubMed:24735878, PubMed:24735879). Positively regulates neuronal
CC differentiation (PubMed:16423343, PubMed:23319585). Suppresses cell
CC cycling and terminal differentiation of keratinocytes by directly
CC repressing MYC and NOTCH1 (By similarity). Important for the correct
CC development of primordial germ cells in embryos (PubMed:28059165).
CC {ECO:0000250|UniProtKB:Q9BRP0, ECO:0000269|PubMed:15225875,
CC ECO:0000269|PubMed:16423343, ECO:0000269|PubMed:23319585,
CC ECO:0000269|PubMed:24735878, ECO:0000269|PubMed:24735879,
CC ECO:0000269|PubMed:28059165}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9468311}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=MOVO-A;
CC IsoId=Q8CIV7-1; Sequence=Displayed;
CC Name=2; Synonyms=MOVO-C;
CC IsoId=Q8CIV7-2; Sequence=VSP_013577, VSP_013578;
CC Name=3; Synonyms=MOVO-B;
CC IsoId=Q8CIV7-3; Sequence=VSP_013576;
CC -!- TISSUE SPECIFICITY: Expressed highly in testis, specifically in
CC spermatocytes. Expressed also in skin and at lower levels in the ovary.
CC {ECO:0000269|PubMed:12213202, ECO:0000269|PubMed:15225875,
CC ECO:0000269|PubMed:9468311}.
CC -!- DEVELOPMENTAL STAGE: Expressed during early-mid embryogenesis,
CC particularly in the inner cell mass at 3.5 dpc, in epiblast at 6.5 dpc,
CC and at later stages in ectodermally derived tissues such as the rostral
CC surface ectoderm (PubMed:16423343). Expressed in embryonic stem cells,
CC epiblasts of 6.4 dpc embryos and primordial germ cells (PGCs)
CC (PubMed:28059165). High expression levels in PGCs of 8.5 dpc embryos
CC decrease over embryogenesis (PubMed:28059165). Up-regulated during
CC prepupertal testis development (PubMed:15225875).
CC {ECO:0000269|PubMed:15225875, ECO:0000269|PubMed:16423343,
CC ECO:0000269|PubMed:28059165}.
CC -!- INDUCTION: Down-regulated during embryonic stem cell neural
CC differentiation and up-regulated by BMP4.
CC {ECO:0000269|PubMed:23319585}.
CC -!- DISRUPTION PHENOTYPE: Mutant embryos are small and die at 9.5 dpc-10.5
CC dpc with an open neural tube, impaired extra-embryonic and embryonic
CC vascularization, abnormal cardiogenesis and placental defects
CC (PubMed:16423343). Reduced number of primordial germ cells in 8.0 dpc
CC embryos (PubMed:28059165). {ECO:0000269|PubMed:16423343,
CC ECO:0000269|PubMed:28059165}.
CC -!- MISCELLANEOUS: [Isoform 3]: Major form in the testis. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY090537; AAM11991.1; -; mRNA.
DR EMBL; AY090538; AAM11992.1; -; mRNA.
DR EMBL; AB101294; BAD29939.1; -; mRNA.
DR EMBL; AB101295; BAD29940.1; -; mRNA.
DR EMBL; AB101296; BAD29941.1; -; mRNA.
DR EMBL; AB101299; BAD29942.1; -; Genomic_DNA.
DR EMBL; AB101299; BAD29943.1; -; Genomic_DNA.
DR EMBL; AB101299; BAD29944.1; -; Genomic_DNA.
DR EMBL; AK007360; BAB24985.1; -; mRNA.
DR EMBL; AL808123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466519; EDL28455.1; -; Genomic_DNA.
DR EMBL; BC031771; AAH31771.1; -; mRNA.
DR EMBL; BC057210; AAH57210.1; -; mRNA.
DR EMBL; BC094445; AAH94445.1; -; mRNA.
DR CCDS; CCDS16817.1; -. [Q8CIV7-1]
DR CCDS; CCDS16818.1; -. [Q8CIV7-2]
DR RefSeq; NP_081200.2; NM_026924.3. [Q8CIV7-1]
DR RefSeq; NP_694455.2; NM_152947.2. [Q8CIV7-2]
DR AlphaFoldDB; Q8CIV7; -.
DR SMR; Q8CIV7; -.
DR STRING; 10090.ENSMUSP00000044026; -.
DR iPTMnet; Q8CIV7; -.
DR PhosphoSitePlus; Q8CIV7; -.
DR PaxDb; Q8CIV7; -.
DR PRIDE; Q8CIV7; -.
DR ProteomicsDB; 294138; -. [Q8CIV7-1]
DR ProteomicsDB; 294139; -. [Q8CIV7-2]
DR ProteomicsDB; 294140; -. [Q8CIV7-3]
DR Antibodypedia; 24517; 170 antibodies from 25 providers.
DR DNASU; 107586; -.
DR Ensembl; ENSMUST00000037423; ENSMUSP00000044026; ENSMUSG00000037279. [Q8CIV7-1]
DR Ensembl; ENSMUST00000103171; ENSMUSP00000099460; ENSMUSG00000037279. [Q8CIV7-2]
DR GeneID; 107586; -.
DR KEGG; mmu:107586; -.
DR UCSC; uc008mqv.1; mouse. [Q8CIV7-2]
DR UCSC; uc008mqw.1; mouse. [Q8CIV7-1]
DR CTD; 58495; -.
DR MGI; MGI:1338039; Ovol2.
DR VEuPathDB; HostDB:ENSMUSG00000037279; -.
DR eggNOG; KOG3576; Eukaryota.
DR GeneTree; ENSGT00940000159359; -.
DR HOGENOM; CLU_087964_0_0_1; -.
DR InParanoid; Q8CIV7; -.
DR OMA; IPVSLDC; -.
DR OrthoDB; 1419156at2759; -.
DR PhylomeDB; Q8CIV7; -.
DR TreeFam; TF337552; -.
DR BioGRID-ORCS; 107586; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Ovol2; mouse.
DR PRO; PR:Q8CIV7; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8CIV7; protein.
DR Bgee; ENSMUSG00000037279; Expressed in spermatid and 71 other tissues.
DR Genevisible; Q8CIV7; MM.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:ARUK-UCL.
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; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0001525; P:angiogenesis; IMP:MGI.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IDA:ARUK-UCL.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:MGI.
DR GO; GO:0048557; P:embryonic digestive tract morphogenesis; IMP:MGI.
DR GO; GO:0060214; P:endocardium formation; IMP:MGI.
DR GO; GO:0009913; P:epidermal cell differentiation; IMP:UniProtKB.
DR GO; GO:0008544; P:epidermis development; IGI:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0001947; P:heart looping; IMP:MGI.
DR GO; GO:0060347; P:heart trabecula formation; IMP:MGI.
DR GO; GO:0060716; P:labyrinthine layer blood vessel development; IMP:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; IDA:ARUK-UCL.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:ARUK-UCL.
DR GO; GO:0045617; P:negative regulation of keratinocyte differentiation; ISS:UniProtKB.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; ISS:UniProtKB.
DR GO; GO:2000647; P:negative regulation of stem cell proliferation; IGI:MGI.
DR GO; GO:0010944; P:negative regulation of transcription by competitive promoter binding; ISO:MGI.
DR GO; GO:0001755; P:neural crest cell migration; IMP:MGI.
DR GO; GO:0001842; P:neural fold formation; IMP:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:ARUK-UCL.
DR GO; GO:0045618; P:positive regulation of keratinocyte differentiation; IDA:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0010837; P:regulation of keratinocyte proliferation; IMP:BHF-UCL.
DR GO; GO:0060390; P:regulation of SMAD protein signal transduction; IDA:ARUK-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR027756; Ovo-like.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR10032; PTHR10032; 1.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 2: Evidence at transcript level;
KW Alternative splicing; Developmental protein; DNA-binding; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..274
FT /note="Transcription factor Ovo-like 2"
FT /id="PRO_0000047014"
FT ZN_FING 118..140
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 146..168
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 174..197
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 213..236
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRP0"
FT VAR_SEQ 1..95
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15225875,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:9468311"
FT /id="VSP_013576"
FT VAR_SEQ 1..33
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12213202,
FT ECO:0000303|PubMed:15225875"
FT /id="VSP_013577"
FT VAR_SEQ 34
FT /note="V -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12213202,
FT ECO:0000303|PubMed:15225875"
FT /id="VSP_013578"
FT CONFLICT 67
FT /note="A -> S (in Ref. 2; AAM11991/AAM11992)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 274 AA; 30685 MW; 8BE48CE57A9F32E4 CRC64;
MPKVFLVKRR SPGVSVRSWD ELPDDKRADT YIPVSLGCLL RDPPEDCRSD GGSSSGCSSS
AGEPGGAESS SSPRAPEPET PELHDAQGTD GHLAAMQRPV ARSKIKFTTG TCDNSVIHNC
DLCGKSFRLQ RMLNRHLKCH NQVKRHLCTF CGKGFNDTFD LKRHVRTHTG IRPYKCEVCN
KAFTQRCSLE SHLKKIHGVQ QQYAYKQRRD KLYVCEDCGY TGPTQEDLYL HVNSDHPGST
FLKKTSKKLA ALMQNKLTSP LQENSTLSEE EEKK
