TERT_MOUSE
ID TERT_MOUSE Reviewed; 1122 AA.
AC O70372; O35432; Q9JK99;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Telomerase reverse transcriptase;
DE EC=2.7.7.49;
DE AltName: Full=Telomerase catalytic subunit;
GN Name=Tert;
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], FUNCTION, DEVELOPMENTAL STAGE, INDUCTION, AND
RP TISSUE SPECIFICITY.
RX PubMed=9582020; DOI=10.1038/sj.onc.1201933;
RA Greenberg R.A., Allsopp R.C., Chin L., Morin G.B., DePinho R.A.;
RT "Expression of mouse telomerase reverse transcriptase during development,
RT differentiation and proliferation.";
RL Oncogene 16:1723-1730(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=9724727; DOI=10.1073/pnas.95.18.10471;
RA Martin-Rivera L., Herrera E., Albar J.P., Blasco M.A.;
RT "Expression of mouse telomerase catalytic subunit in embryos and adult
RT tissues.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:10471-10476(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 548-1122, AND TISSUE SPECIFICITY.
RX PubMed=13679242; DOI=10.1016/s0024-3205(03)00670-2;
RA Wong S.C., Ong L.L., Er C.P., Gao S., Yu H., So J.B.;
RT "Cloning of rat telomerase catalytic subunit functional domains,
RT reconstitution of telomerase activity and enzymatic profile of pig and
RT chicken tissues.";
RL Life Sci. 73:2749-2760(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 550-616.
RA Drissi R., Cleveland J.L.;
RT "Partial sequence of Mus musculus telomerase catalytic subunit homolog.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INTERACTION WITH PIF1, AND FUNCTION.
RX PubMed=17130244; DOI=10.1128/mcb.01866-06;
RA Snow B.E., Mateyak M., Paderova J., Wakeham A., Iorio C., Zakian V.,
RA Squire J., Harrington L.;
RT "Murine Pif1 interacts with telomerase and is dispensable for telomere
RT function in vivo.";
RL Mol. Cell. Biol. 27:1017-1026(2007).
RN [6]
RP INTERACTION WITH GNL3L.
RX PubMed=19487455; DOI=10.1083/jcb.200812121;
RA Zhu Q., Meng L., Hsu J.K., Lin T., Teishima J., Tsai R.Y.;
RT "GNL3L stabilizes the TRF1 complex and promotes mitotic transition.";
RL J. Cell Biol. 185:827-839(2009).
RN [7]
RP INTERACTION WITH SMARCA4, AND FUNCTION.
RX PubMed=19571879; DOI=10.1038/nature08137;
RA Park J.I., Venteicher A.S., Hong J.Y., Choi J., Jun S., Shkreli M.,
RA Chang W., Meng Z., Cheung P., Ji H., McLaughlin M., Veenstra T.D.,
RA Nusse R., McCrea P.D., Artandi S.E.;
RT "Telomerase modulates Wnt signalling by association with target gene
RT chromatin.";
RL Nature 460:66-72(2009).
CC -!- FUNCTION: Telomerase is a ribonucleoprotein enzyme essential for the
CC replication of chromosome termini in most eukaryotes. Active in
CC progenitor and cancer cells. Inactive, or very low activity, in normal
CC somatic cells. Catalytic component of the teleromerase holoenzyme
CC complex whose main activity is the elongation of telomeres by acting as
CC a reverse transcriptase that adds simple sequence repeats to chromosome
CC ends by copying a template sequence within the RNA component of the
CC enzyme. Catalyzes the RNA-dependent extension of 3'-chromosomal termini
CC with the 6-nucleotide telomeric repeat unit, 5'-TTAGGG-3'. The
CC catalytic cycle involves primer binding, primer extension and release
CC of product once the template boundary has been reached or nascent
CC product translocation followed by further extension. More active on
CC substrates containing 2 or 3 telomeric repeats. Telomerase activity is
CC regulated by a number of factors including telomerase complex-
CC associated proteins, chaperones and polypeptide modifiers. Modulates
CC Wnt signaling. Plays important roles in aging and antiapoptosis (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:17130244,
CC ECO:0000269|PubMed:19571879, ECO:0000269|PubMed:9582020}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00405};
CC -!- SUBUNIT: Catalytic component of the telomerase holoenzyme complex
CC composed of one molecule of TERT, one molecule of WRAP53/TCAB1, two
CC molecules of H/ACA ribonucleoprotein complex subunits DKC1, NOP10, NHP2
CC and GAR1, and a telomerase RNA template component (TERC). The
CC telomerase holoenzyme complex is associated with TEP1, SMG6/EST1A and
CC POT1. The molecular chaperone HSP90/P23 complex is required for correct
CC assembly and stabilization of the active telomerase. Interacts directly
CC with HSP90A and PTGES3. Interacts with HSPA1A; the interaction occurs
CC in the absence of TERC and dissociates once the complex has formed.
CC Interacts with RAN; the interaction promotes nuclear export of TERT.
CC Interacts with XPO1. Interacts with PTPN11; the interaction retains
CC TERT in the nucleus. Interacts with NCL (via RRM1 and C-terminal
CC RRM4/Arg/Gly-rich domains); the interaction is important for nucleolar
CC localization of TERT (By similarity). Interacts with SMARCA4 (via the
CC bromodomain); the interaction regulates Wnt-mediated signaling
CC (PubMed:19571879). Interacts with MCRS1 (isoform MCRS2); the
CC interaction inhibits in vitro telomerase activity (By similarity).
CC Interacts with PIF1; the interaction has no effect on the elongation
CC activity of TERT (PubMed:17130244). Interacts with PML; the interaction
CC recruits TERT to PML bodies and inhibits telomerase activity (By
CC similarity). Interacts with GNL3L (PubMed:19487455). Interacts with
CC isoform 1 and isoform 2 of NVL (By similarity). Interacts with DHX36
CC (By similarity). Interacts with ATF7 (By similarity).
CC {ECO:0000250|UniProtKB:O14746, ECO:0000269|PubMed:17130244,
CC ECO:0000269|PubMed:19487455, ECO:0000269|PubMed:19571879}.
CC -!- INTERACTION:
CC O70372; Q3TKT4: Smarca4; NbExp=2; IntAct=EBI-9662790, EBI-1210244;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:O14746}. Nucleus, nucleoplasm {ECO:0000250}.
CC Nucleus. Chromosome, telomere. Cytoplasm {ECO:0000250}. Nucleus, PML
CC body {ECO:0000250}. Note=Shuttling between nuclear and cytoplasm
CC depends on cell cycle, phosphorylation states, transformation and DNA
CC damage. Diffuse localization in the nucleoplasm. Enriched in nucleoli
CC of certain cell types. Translocated to the cytoplasm via nuclear pores
CC in a CRM1/RAN-dependent manner involving oxidative stress-mediated
CC phosphorylation at Tyr-697. Dephosphorylation at this site by SHP2
CC retains TERT in the nucleus. Translocated to the nucleus by
CC phosphorylation by AKT (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: High activity in intestine, liver and testis,
CC moderate in lung, very low in muscle, heart and brain.
CC {ECO:0000269|PubMed:13679242, ECO:0000269|PubMed:9582020,
CC ECO:0000269|PubMed:9724727}.
CC -!- DEVELOPMENTAL STAGE: Highest levels in midgestational stages, 9.5 dpc
CC to 15.5 dpc. {ECO:0000269|PubMed:9582020}.
CC -!- DOMAIN: The primer grip sequence in the RT domain is required for
CC telomerase activity and for stable association with short telomeric
CC primers. {ECO:0000250}.
CC -!- DOMAIN: The RNA-interacting domain 1 (RD1)/N-terminal extension (NTE)
CC is required for interaction with the pseudoknot-template domain of each
CC of TERC dimers. It contains anchor sites that bind primer nucleotides
CC upstream of the RNA-DNA hybrid and is thus an essential determinant of
CC repeat addition processivity (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The RNA-interacting domain 2 (RD2) is essential for both
CC interaction with the CR4-CR5 domain of TERC and for DNA synthesis.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylation at Tyr-697 under oxidative stress leads to
CC translocation of TERT to the cytoplasm and reduces its antiapoptotic
CC activity. Dephosphorylated by SHP2/PTPN11 leading to nuclear retention.
CC Phosphorylation by the AKT pathway promotes nuclear location.
CC Phosphorylation at the G2/M phase at Ser-447 by DYRK2 promotes
CC ubiquitination by the EDVP complex and degradation (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Ubiquitinated by the EDVP complex, a E3 ligase complex following
CC phosphorylation at Ser-447 by DYRK2. Ubiquitinated leads to proteasomal
CC degradation (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the reverse transcriptase family. Telomerase
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to originate from rat.
CC {ECO:0000305|PubMed:13679242}.
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DR EMBL; AF051911; AAC09323.1; -; mRNA.
DR EMBL; AF073311; AAC34821.1; -; mRNA.
DR EMBL; AF247818; AAF62177.1; -; mRNA.
DR EMBL; AF029235; AAB84200.1; -; mRNA.
DR CCDS; CCDS26633.1; -.
DR RefSeq; NP_033380.1; NM_009354.1.
DR AlphaFoldDB; O70372; -.
DR SMR; O70372; -.
DR BioGRID; 204118; 2.
DR ComplexPortal; CPX-1124; Telomerase holoenzyme complex.
DR ComplexPortal; CPX-19; Telomerase catalytic core complex.
DR ComplexPortal; CPX-22; TERT-RMRP complex.
DR DIP; DIP-60451N; -.
DR IntAct; O70372; 3.
DR STRING; 10090.ENSMUSP00000022104; -.
DR iPTMnet; O70372; -.
DR PhosphoSitePlus; O70372; -.
DR PaxDb; O70372; -.
DR PRIDE; O70372; -.
DR Antibodypedia; 8998; 1000 antibodies from 42 providers.
DR DNASU; 21752; -.
DR Ensembl; ENSMUST00000022104; ENSMUSP00000022104; ENSMUSG00000021611.
DR GeneID; 21752; -.
DR KEGG; mmu:21752; -.
DR UCSC; uc007rdq.1; mouse.
DR CTD; 7015; -.
DR MGI; MGI:1202709; Tert.
DR VEuPathDB; HostDB:ENSMUSG00000021611; -.
DR eggNOG; KOG1005; Eukaryota.
DR GeneTree; ENSGT00390000018531; -.
DR HOGENOM; CLU_001996_2_0_1; -.
DR InParanoid; O70372; -.
DR OMA; FWLMDTY; -.
DR OrthoDB; 1297956at2759; -.
DR PhylomeDB; O70372; -.
DR TreeFam; TF329048; -.
DR Reactome; R-MMU-171319; Telomere Extension By Telomerase.
DR Reactome; R-MMU-201722; Formation of the beta-catenin:TCF transactivating complex.
DR BioGRID-ORCS; 21752; 6 hits in 77 CRISPR screens.
DR ChiTaRS; Tert; mouse.
DR PRO; PR:O70372; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; O70372; protein.
DR Bgee; ENSMUSG00000021611; Expressed in paneth cell and 134 other tissues.
DR ExpressionAtlas; O70372; baseline and differential.
DR Genevisible; O70372; MM.
DR GO; GO:0000781; C:chromosome, telomeric region; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:BHF-UCL.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0016605; C:PML body; ISO:MGI.
DR GO; GO:0031379; C:RNA-directed RNA polymerase complex; ISO:MGI.
DR GO; GO:0000333; C:telomerase catalytic core complex; IMP:BHF-UCL.
DR GO; GO:0005697; C:telomerase holoenzyme complex; ISS:UniProtKB.
DR GO; GO:1990572; C:TERT-RMRP complex; ISO:MGI.
DR GO; GO:0051087; F:chaperone binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IPI:BHF-UCL.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; ISO:MGI.
DR GO; GO:0003964; F:RNA-directed DNA polymerase activity; ISO:MGI.
DR GO; GO:0003720; F:telomerase activity; IDA:MGI.
DR GO; GO:0070034; F:telomerase RNA binding; IPI:BHF-UCL.
DR GO; GO:0003721; F:telomerase RNA reverse transcriptase activity; ISO:MGI.
DR GO; GO:0042162; F:telomeric DNA binding; IBA:GO_Central.
DR GO; GO:0098680; F:template-free RNA nucleotidyltransferase; ISO:MGI.
DR GO; GO:0001223; F:transcription coactivator binding; IPI:BHF-UCL.
DR GO; GO:0000049; F:tRNA binding; ISO:MGI.
DR GO; GO:0071456; P:cellular response to hypoxia; ISO:MGI.
DR GO; GO:0071897; P:DNA biosynthetic process; ISO:MGI.
DR GO; GO:0022616; P:DNA strand elongation; ISO:MGI.
DR GO; GO:0062103; P:double-stranded RNA biosynthetic process; ISO:MGI.
DR GO; GO:0070200; P:establishment of protein localization to telomere; ISO:MGI.
DR GO; GO:0007005; P:mitochondrion organization; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:2000773; P:negative regulation of cellular senescence; ISO:MGI.
DR GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; ISO:MGI.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0060253; P:negative regulation of glial cell proliferation; ISO:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:1903704; P:negative regulation of siRNA production; ISO:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:0046326; P:positive regulation of glucose import; IMP:MGI.
DR GO; GO:0042635; P:positive regulation of hair cycle; IMP:BHF-UCL.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:MGI.
DR GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; ISO:MGI.
DR GO; GO:0032092; P:positive regulation of protein binding; ISO:MGI.
DR GO; GO:1904751; P:positive regulation of protein localization to nucleolus; ISO:MGI.
DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IMP:BHF-UCL.
DR GO; GO:1903620; P:positive regulation of transdifferentiation; ISO:MGI.
DR GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; ISO:MGI.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IGI:BHF-UCL.
DR GO; GO:0031647; P:regulation of protein stability; ISO:MGI.
DR GO; GO:0090399; P:replicative senescence; ISO:MGI.
DR GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl.
DR GO; GO:0006278; P:RNA-templated DNA biosynthetic process; ISO:MGI.
DR GO; GO:0030422; P:siRNA processing; ISO:MGI.
DR GO; GO:0007004; P:telomere maintenance via telomerase; ISS:UniProtKB.
DR GO; GO:0001172; P:transcription, RNA-templated; ISO:MGI.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR000477; RT_dom.
DR InterPro; IPR021891; Telomerase_RBD.
DR InterPro; IPR003545; Telomerase_RT.
DR PANTHER; PTHR12066; PTHR12066; 1.
DR Pfam; PF00078; RVT_1; 1.
DR Pfam; PF12009; Telomerase_RBD; 1.
DR PRINTS; PR01365; TELOMERASERT.
DR SMART; SM00975; Telomerase_RBD; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS50878; RT_POL; 1.
PE 1: Evidence at protein level;
KW Chromosome; Cytoplasm; DNA-binding; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; RNA-directed DNA polymerase; Telomere; Transferase;
KW Ubl conjugation.
FT CHAIN 1..1122
FT /note="Telomerase reverse transcriptase"
FT /id="PRO_0000054926"
FT DOMAIN 595..928
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT REGION 1..239
FT /note="RNA-interacting domain 1"
FT /evidence="ECO:0000250"
FT REGION 58..205
FT /note="GQ motif"
FT /evidence="ECO:0000250"
FT REGION 137..141
FT /note="Required for regulating specificity for telomeric
FT DNA and for processivity for primer elongation"
FT /evidence="ECO:0000250"
FT REGION 213..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..328
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 306..528
FT /note="Required for oligomerization"
FT /evidence="ECO:0000250"
FT REGION 329..540
FT /note="RNA-interacting domain 2"
FT /evidence="ECO:0000250"
FT REGION 381..511
FT /note="QFP motif"
FT /evidence="ECO:0000250"
FT REGION 402..422
FT /note="CP motif"
FT /evidence="ECO:0000250"
FT REGION 907..921
FT /note="Required for oligomerization"
FT /evidence="ECO:0000250"
FT REGION 923..927
FT /note="Primer grip sequence"
FT /evidence="ECO:0000250"
FT REGION 929..1122
FT /note="CTE"
FT /evidence="ECO:0000250"
FT MOTIF 332..337
FT /note="TFLY; involved in RNA binding"
FT /evidence="ECO:0000250|UniProtKB:Q4KTA7"
FT BINDING 702
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT BINDING 861
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT BINDING 862
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT SITE 169
FT /note="Required for optimal binding of telomeric ssDNA and
FT incorporation of nucleotides at the second position of the
FT template"
FT /evidence="ECO:0000250"
FT SITE 860
FT /note="Required for nucleotide incorporation and primer
FT extension rate"
FT /evidence="ECO:0000250"
FT MOD_RES 447
FT /note="Phosphoserine; by DYRK2"
FT /evidence="ECO:0000250|UniProtKB:O14746"
FT MOD_RES 697
FT /note="Phosphotyrosine; by SRC-type Tyr-kinases"
FT /evidence="ECO:0000250|UniProtKB:O14746"
FT CONFLICT 553
FT /note="I -> V (in Ref. 4; AAB84200)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1122 AA; 127978 MW; F85266905DD6558C CRC64;
MTRAPRCPAV RSLLRSRYRE VWPLATFVRR LGPEGRRLVQ PGDPKIYRTL VAQCLVCMHW
GSQPPPADLS FHQVSSLKEL VARVVQRLCE RNERNVLAFG FELLNEARGG PPMAFTSSVR
SYLPNTVIET LRVSGAWMLL LSRVGDDLLV YLLAHCALYL LVPPSCAYQV CGSPLYQICA
TTDIWPSVSA SYRPTRPVGR NFTNLRFLQQ IKSSSRQEAP KPLALPSRGT KRHLSLTSTS
VPSAKKARCY PVPRVEEGPH RQVLPTPSGK SWVPSPARSP EVPTAEKDLS SKGKVSDLSL
SGSVCCKHKP SSTSLLSPPR QNAFQLRPFI ETRHFLYSRG DGQERLNPSF LLSNLQPNLT
GARRLVEIIF LGSRPRTSGP LCRTHRLSRR YWQMRPLFQQ LLVNHAECQY VRLLRSHCRF
RTANQQVTDA LNTSPPHLMD LLRLHSSPWQ VYGFLRACLC KVVSASLWGT RHNERRFFKN
LKKFISLGKY GKLSLQELMW KMKVEDCHWL RSSPGKDRVP AAEHRLRERI LATFLFWLMD
TYVVQLLRSF FYITESTFQK NRLFFYRKSV WSKLQSIGVR QHLERVRLRE LSQEEVRHHQ
DTWLAMPICR LRFIPKPNGL RPIVNMSYSM GTRALGRRKQ AQHFTQRLKT LFSMLNYERT
KHPHLMGSSV LGMNDIYRTW RAFVLRVRAL DQTPRMYFVK ADVTGAYDAI PQGKLVEVVA
NMIRHSESTY CIRQYAVVRR DSQGQVHKSF RRQVTTLSDL QPYMGQFLKH LQDSDASALR
NSVVIEQSIS MNESSSSLFD FFLHFLRHSV VKIGDRCYTQ CQGIPQGSSL STLLCSLCFG
DMENKLFAEV QRDGLLLRFV DDFLLVTPHL DQAKTFLSTL VHGVPEYGCM INLQKTVVNF
PVEPGTLGGA APYQLPAHCL FPWCGLLLDT QTLEVFCDYS GYAQTSIKTS LTFQSVFKAG
KTMRNKLLSV LRLKCHGLFL DLQVNSLQTV CINIYKIFLL QAYRFHACVI QLPFDQRVRK
NLTFFLGIIS SQASCCYAIL KVKNPGMTLK ASGSFPPEAA HWLCYQAFLL KLAAHSVIYK
CLLGPLRTAQ KLLCRKLPEA TMTILKAAAD PALSTDFQTI LD
