TLE6_HUMAN
ID TLE6_HUMAN Reviewed; 572 AA.
AC Q9H808; J3KMZ1;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Transducin-like enhancer protein 6;
GN Name=TLE6;
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 [LARGE SCALE MRNA] (ISOFORM 2).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung;
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 REVIEW.
RX PubMed=18254933; DOI=10.1186/gb-2008-9-1-205;
RA Jennings B.H., Ish-Horowicz D.;
RT "The Groucho/TLE/Grg family of transcriptional co-repressors.";
RL Genome Biol. 9:R205.1-R205.7(2008).
RN [5]
RP FUNCTION, INTERACTION WITH KHDC3L AND OOEP, PHOSPHORYLATION AT SER-510,
RP VARIANT PREMBL1 TYR-510, AND CHARACTERIZATION OF VARIANT PREMBL1 TYR-510.
RX PubMed=26537248; DOI=10.1186/s13059-015-0792-0;
RA Alazami A.M., Awad S.M., Coskun S., Al-Hassan S., Hijazi H.,
RA Abdulwahab F.M., Poizat C., Alkuraya F.S.;
RT "TLE6 mutation causes the earliest known human embryonic lethality.";
RL Genome Biol. 16:R240.1-R240.8(2015).
RN [6]
RP IDENTIFICATION IN THE SCMC COMPLEX, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=25542835; DOI=10.1093/molehr/gau116;
RA Zhu K., Yan L., Zhang X., Lu X., Wang T., Yan J., Liu X., Qiao J., Li L.;
RT "Identification of a human subcortical maternal complex.";
RL Mol. Hum. Reprod. 21:320-329(2015).
RN [7]
RP VARIANTS PREMBL1 HIS-74; GLY-240; ARG-298; HIS-338; 446-TRP--TYR-572 DEL
RP AND HIS-522.
RX PubMed=33020905; DOI=10.1111/cge.13858;
RA Zheng W., Hu H., Dai J., Zhang S., Gu Y., Dai C., Guo J., Xu X., Li Y.,
RA Zhang S., Hu L., Gong F., Lu G., Lin G.;
RT "Expanding the genetic and phenotypic spectrum of the subcortical maternal
RT complex genes in recurrent preimplantation embryonic arrest.";
RL Clin. Genet. 99:286-291(2021).
RN [8]
RP VARIANTS PREMBL1 ASN-130; GLN-409; ILE-503 AND LYS-541.
RX PubMed=31897846; DOI=10.1007/s10815-019-01653-0;
RA Lin J., Xu H., Chen B., Wang W., Wang L., Sun X., Sang Q.;
RT "Expanding the genetic and phenotypic spectrum of female infertility caused
RT by TLE6 mutations.";
RL J. Assist. Reprod. Genet. 37:437-442(2020).
CC -!- FUNCTION: Regulates spermatogonia proliferation and cell cycle
CC progression, potentially via regulation of cell cycle regulatory genes
CC such as; CEBPB, CEBPA, CSF3, PCNA, and CDK4 (By similarity). Suppresses
CC FOXG1/BF-1-mediated transcriptional repression by inhibiting
CC interaction of the transcriptional corepressor TLE1 with FOXG1 which
CC promotes cortical neuron differentiation (By similarity). Acts as a
CC transcriptional corepressor of NFATC1-mediated gene expression by
CC contributing to PAX6-mediated repression (By similarity).
CC {ECO:0000250|UniProtKB:Q9WVB3}.
CC -!- FUNCTION: [Isoform 1]: As a member of the subcortical maternal complex
CC (SCMC), plays an essential role for zygotes to progress beyond the
CC first embryonic cell divisions via regulation of actin dynamics
CC (PubMed:26537248). Required for the formation of F-actin cytoplasmic
CC lattices in oocytes which in turn are responsible for symmetric
CC division of zygotes via the regulation of mitotic spindle formation and
CC positioning (By similarity). {ECO:0000250|UniProtKB:Q9WVB3,
CC ECO:0000269|PubMed:26537248}.
CC -!- SUBUNIT: Homodimers (By similarity). Interacts with FOXG1/BF-1; the
CC interaction inhibits TLE1 interaction with FOXG1/BF-1 (By similarity).
CC Interacts with NFATC1 (By similarity). Interacts with PAX6 (By
CC similarity). {ECO:0000250|UniProtKB:Q9WVB3}.
CC -!- SUBUNIT: [Isoform 1]: Component of the subcortical maternal complex
CC (SCMC), at least composed of NLRP5, KHDC3L, OOEP, and TLE6 isoform 1
CC (PubMed:26537248, PubMed:25542835). Within the complex, interacts with
CC NLRP5, KHDC3L and OOEP (PubMed:26537248, PubMed:25542835). The SCMC may
CC facilitate translocation of its components between the nuclear and
CC cytoplasmic compartments (PubMed:25542835). As part of the SCMC
CC interacts with the SCMC-associated protein ZBED3 (By similarity). As
CC part of the SCMC interacts with the SCMC-associated protein NLRP4F (By
CC similarity). As part of the SCMC interacts with the SCMC-associated
CC protein CFL1/Cofilin-1 (By similarity). {ECO:0000250|UniProtKB:Q9WVB3,
CC ECO:0000269|PubMed:25542835, ECO:0000269|PubMed:26537248}.
CC -!- INTERACTION:
CC Q9H808; P23560-2: BDNF; NbExp=3; IntAct=EBI-3921684, EBI-12275524;
CC Q9H808; Q92876: KLK6; NbExp=3; IntAct=EBI-3921684, EBI-2432309;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9WVB3}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm
CC {ECO:0000269|PubMed:25542835}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:25542835}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H808-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H808-2; Sequence=VSP_047216;
CC -!- DEVELOPMENTAL STAGE: [Isoform 1]: Expressed in oocytes of the fetal
CC ovary (PubMed:25542835). Expressed primarily with other SCMC components
CC in the subcortex of oocytes and early embryos (PubMed:25542835).
CC Expression is excluded from cell-cell contact regions after the 2-cell
CC stage (PubMed:25542835). {ECO:0000269|PubMed:25542835}.
CC -!- DEVELOPMENTAL STAGE: [Isoform 2]: Expressed in the fetal kidney.
CC {ECO:0000269|PubMed:25542835}.
CC -!- DOMAIN: Contrary to other WD repeat Groucho/TLE family members, does
CC not contain any identifiable Q, GP, CcN or SP domains. Only the C-
CC terminal WD-repeat domain is conserved. {ECO:0000305|PubMed:18254933}.
CC -!- DISEASE: Preimplantation embryonic lethality 1 (PREMBL1) [MIM:616814]:
CC A rare cause of female primary infertility. In affected women,
CC ovulation proceeds normally and the retrieved oocytes appear normal,
CC but zygote formation and division are severely impaired. Inheritance is
CC autosomal recessive. {ECO:0000269|PubMed:26537248,
CC ECO:0000269|PubMed:31897846, ECO:0000269|PubMed:33020905}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the WD repeat Groucho/TLE family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH20206.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK024071; BAB14815.1; -; mRNA.
DR EMBL; AC006277; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC007766; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007215; AAH07215.1; -; mRNA.
DR EMBL; BC020206; AAH20206.1; ALT_INIT; mRNA.
DR CCDS; CCDS12100.1; -. [Q9H808-2]
DR CCDS; CCDS45910.1; -. [Q9H808-1]
DR RefSeq; NP_001137458.1; NM_001143986.1. [Q9H808-1]
DR RefSeq; NP_079036.1; NM_024760.2. [Q9H808-2]
DR RefSeq; XP_005259702.1; XM_005259645.2. [Q9H808-1]
DR RefSeq; XP_011526602.1; XM_011528300.2. [Q9H808-1]
DR RefSeq; XP_011526603.1; XM_011528301.1. [Q9H808-2]
DR AlphaFoldDB; Q9H808; -.
DR SMR; Q9H808; -.
DR BioGRID; 122911; 21.
DR CORUM; Q9H808; -.
DR IntAct; Q9H808; 4.
DR STRING; 9606.ENSP00000246112; -.
DR iPTMnet; Q9H808; -.
DR PhosphoSitePlus; Q9H808; -.
DR BioMuta; TLE6; -.
DR DMDM; 519668658; -.
DR MassIVE; Q9H808; -.
DR PaxDb; Q9H808; -.
DR PeptideAtlas; Q9H808; -.
DR PRIDE; Q9H808; -.
DR ProteomicsDB; 81165; -. [Q9H808-1]
DR Antibodypedia; 23085; 74 antibodies from 18 providers.
DR DNASU; 79816; -.
DR Ensembl; ENST00000246112.9; ENSP00000246112.3; ENSG00000104953.20. [Q9H808-1]
DR Ensembl; ENST00000452088.5; ENSP00000406893.1; ENSG00000104953.20. [Q9H808-2]
DR GeneID; 79816; -.
DR KEGG; hsa:79816; -.
DR MANE-Select; ENST00000246112.9; ENSP00000246112.3; NM_001143986.2; NP_001137458.1.
DR UCSC; uc002lwt.3; human. [Q9H808-1]
DR CTD; 79816; -.
DR DisGeNET; 79816; -.
DR GeneCards; TLE6; -.
DR HGNC; HGNC:30788; TLE6.
DR HPA; ENSG00000104953; Tissue enhanced (thyroid).
DR MalaCards; TLE6; -.
DR MIM; 612399; gene.
DR MIM; 616814; phenotype.
DR neXtProt; NX_Q9H808; -.
DR OpenTargets; ENSG00000104953; -.
DR PharmGKB; PA134948893; -.
DR VEuPathDB; HostDB:ENSG00000104953; -.
DR eggNOG; KOG0639; Eukaryota.
DR GeneTree; ENSGT01030000234519; -.
DR HOGENOM; CLU_007612_1_0_1; -.
DR InParanoid; Q9H808; -.
DR OMA; PLGQWWV; -.
DR OrthoDB; 1025572at2759; -.
DR PhylomeDB; Q9H808; -.
DR TreeFam; TF314167; -.
DR PathwayCommons; Q9H808; -.
DR SignaLink; Q9H808; -.
DR SIGNOR; Q9H808; -.
DR BioGRID-ORCS; 79816; 12 hits in 1074 CRISPR screens.
DR ChiTaRS; TLE6; human.
DR GenomeRNAi; 79816; -.
DR Pharos; Q9H808; Tbio.
DR PRO; PR:Q9H808; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9H808; protein.
DR Bgee; ENSG00000104953; Expressed in oocyte and 109 other tissues.
DR ExpressionAtlas; Q9H808; baseline and differential.
DR Genevisible; Q9H808; HS.
DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IMP:UniProtKB.
DR GO; GO:0106333; C:subcortical maternal complex; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; ISS:UniProtKB.
DR GO; GO:0060136; P:embryonic process involved in female pregnancy; IMP:UniProtKB.
DR GO; GO:0051643; P:endoplasmic reticulum localization; ISS:UniProtKB.
DR GO; GO:0051293; P:establishment of spindle localization; ISS:UniProtKB.
DR GO; GO:0051646; P:mitochondrion localization; ISS:UniProtKB.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0040019; P:positive regulation of embryonic development; ISS:UniProtKB.
DR GO; GO:0051302; P:regulation of cell division; ISS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR009146; Groucho_enhance.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR10814; PTHR10814; 1.
DR PRINTS; PR01850; GROUCHOFAMLY.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Disease variant; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW WD repeat.
FT CHAIN 1..572
FT /note="Transducin-like enhancer protein 6"
FT /id="PRO_0000051286"
FT REPEAT 284..322
FT /note="WD 1"
FT REPEAT 332..372
FT /note="WD 2"
FT REPEAT 377..416
FT /note="WD 3"
FT REPEAT 419..456
FT /note="WD 4"
FT REPEAT 458..497
FT /note="WD 5"
FT REPEAT 499..538
FT /note="WD 6"
FT REPEAT 540..571
FT /note="WD 7"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 510
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:26537248"
FT VAR_SEQ 1..123
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_047216"
FT VARIANT 74
FT /note="Q -> H (in PREMBL1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33020905"
FT /id="VAR_084162"
FT VARIANT 130
FT /note="D -> N (in PREMBL1; unknown pathological
FT significance; dbSNP:rs769137034)"
FT /evidence="ECO:0000269|PubMed:31897846"
FT /id="VAR_084163"
FT VARIANT 240
FT /note="A -> G (in PREMBL1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33020905"
FT /id="VAR_084164"
FT VARIANT 298
FT /note="T -> R (in PREMBL1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33020905"
FT /id="VAR_084165"
FT VARIANT 338
FT /note="R -> H (in PREMBL1; unknown pathological
FT significance; dbSNP:rs763793074)"
FT /evidence="ECO:0000269|PubMed:33020905"
FT /id="VAR_084166"
FT VARIANT 409
FT /note="R -> Q (in PREMBL1; unknown pathological
FT significance; dbSNP:rs1310808966)"
FT /evidence="ECO:0000269|PubMed:31897846"
FT /id="VAR_084167"
FT VARIANT 446..572
FT /note="Missing (in PREMBL1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33020905"
FT /id="VAR_084168"
FT VARIANT 503
FT /note="V -> I (in PREMBL1; unknown pathological
FT significance; dbSNP:rs551247575)"
FT /evidence="ECO:0000269|PubMed:31897846"
FT /id="VAR_084169"
FT VARIANT 510
FT /note="S -> Y (in PREMBL1; almost complete loss of
FT phosphorylation and reduced interaction with KHDC3L and
FT OOEP; dbSNP:rs767222404)"
FT /evidence="ECO:0000269|PubMed:26537248"
FT /id="VAR_076246"
FT VARIANT 522
FT /note="D -> H (in PREMBL1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33020905"
FT /id="VAR_084170"
FT VARIANT 541
FT /note="E -> K (in PREMBL1; unknown pathological
FT significance; dbSNP:rs1176718387)"
FT /evidence="ECO:0000269|PubMed:31897846"
FT /id="VAR_084171"
SQ SEQUENCE 572 AA; 63473 MW; 4C9FF29BEB7DF9FF CRC64;
MTSRDQPRPK GPPKSTSPCP GISNSESSPT LNYQGILNRL KQFPRFSPHF AAELESIYYS
LHKIQQDVAE HHKQIGNVLQ IVESCSQLQG FQSEEVSPAE PASPGTPQQV KDKTLQESSF
EDIMATRSSD WLRRPLGEDN QPETQLFWDK EPWFWHDTLT EQLWRIFAGV HDEKAKPRDR
QQAPGLGQES KAPGSCDPGT DPCPEDASTP RPPEASSSPP EGSQDRNTSW GVVQEPPGRA
SRFLQSISWD PEDFEDAWKR PDALPGQSKR LAVPCKLEKM RILAHGELVL ATAISSFTRH
VFTCGRRGIK VWSLTGQVAE DRFPESHLPI QTPGAFLRTC LLSSNSRSLL TGGYNLASVS
VWDLAAPSLH VKEQLPCAGL NCQALDANLD ANLAFASFTS GVVRIWDLRD QSVVRDLKGY
PDGVKSIVVK GYNIWTGGPD ACLRCWDQRT IMKPLEYQFK SQIMSLSHSP QEDWVLLGMA
NGQQWLQSTS GSQRHMVGQK DSVILSVKFS PFGQWWASVG MDDFLGVYSM PAGTKVFEVP
EMSPVTCCDV SSNNRLVVTG SGEHASVYQI TY
