TERT_ORYLA
ID TERT_ORYLA Reviewed; 1090 AA.
AC Q1PS67; A7J3B2; H2BIT2; H2BIT3; H2BIT4; H2BIT5; H2MFU0;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 24-JUN-2015, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Telomerase reverse transcriptase {ECO:0000303|PubMed:18312429};
DE EC=2.7.7.49 {ECO:0000255|PROSITE-ProRule:PRU00405, ECO:0000269|PubMed:18039659, ECO:0000269|PubMed:22123986};
DE AltName: Full=Telomerase catalytic subunit {ECO:0000305};
GN Name=tert {ECO:0000303|PubMed:18312429};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000312|EMBL:ABB76648.1};
RN [1] {ECO:0000312|EMBL:ABI74619.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM F), AND TISSUE SPECIFICITY.
RC STRAIN=D-rR.YHNI {ECO:0000312|EMBL:ABI74619.1};
RC TISSUE=Testis {ECO:0000312|EMBL:ABI74619.1};
RX PubMed=18312429; DOI=10.1111/j.1440-169x.2008.00986.x;
RA Pfennig F., Kind B., Zieschang F., Busch M., Gutzeit H.O.;
RT "Tert expression and telomerase activity in gonads and somatic cells of the
RT Japanese medaka (Oryzias latipes).";
RL Dev. Growth Differ. 50:131-141(2008).
RN [2] {ECO:0000312|EMBL:ADZ28508.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B; C; D AND E), TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=21547060; DOI=10.7150/ijbs.7.426;
RA Rao F., Wang T., Li M., Li Z., Hong N., Zhao H., Yan Y., Lu W., Chen T.,
RA Wang W., Lim M., Yuan Y., Liu L., Zeng L., Wei Q., Guan G., Li C., Hong Y.;
RT "Medaka tert produces multiple variants with differential expression during
RT differentiation in vitro and in vivo.";
RL Int. J. Biol. Sci. 7:426-439(2011).
RN [3] {ECO:0000312|EMBL:ABB76648.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Orange {ECO:0000312|EMBL:ABB76648.1};
RA Rao F., Li M., Hong Y.;
RT "Telomerase reverse transcriptase and telomerase activity in the model fish
RT medaka.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000312|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000312|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [5] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND RECONSTITUTION OF THE TELOMERASE
RP HOLOENZYME COMPLEX.
RX PubMed=18039659; DOI=10.1074/jbc.m708032200;
RA Xie M., Mosig A., Qi X., Li Y., Stadler P.F., Chen J.J.;
RT "Structure and function of the smallest vertebrate telomerase RNA from
RT teleost fish.";
RL J. Biol. Chem. 283:2049-2059(2008).
RN [6] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, RECONSTITUTION OF THE TELOMERASE HOLOENZYME
RP COMPLEX, SUBUNIT, AND MUTAGENESIS OF PHE-355; TRP-477 AND TYR-503.
RX PubMed=22123986; DOI=10.1073/pnas.1100270108;
RA Bley C.J., Qi X., Rand D.P., Borges C.R., Nelson R.W., Chen J.J.;
RT "RNA-protein binding interface in the telomerase ribonucleoprotein.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20333-20338(2011).
RN [7] {ECO:0007744|PDB:4O26}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 318-572 IN COMPLEX WITH RNA
RP TEMPLATE, AND MUTAGENESIS OF PHE-376 AND TYR-503.
RX PubMed=24793650; DOI=10.1038/nsmb.2819;
RA Huang J., Brown A.F., Wu J., Xue J., Bley C.J., Rand D.P., Wu L., Zhang R.,
RA Chen J.J., Lei M.;
RT "Structural basis for protein-RNA recognition in telomerase.";
RL Nat. Struct. Mol. Biol. 21:507-512(2014).
CC -!- FUNCTION: Telomerase is a ribonucleoprotein enzyme essential for the
CC replication of chromosome termini in most eukaryotes. It elongates
CC telomeres. It is a reverse transcriptase that adds simple sequence
CC repeats to chromosome ends by copying a template sequence within the
CC RNA component of the enzyme. {ECO:0000269|PubMed:18039659,
CC ECO:0000269|PubMed:22123986}.
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, ECO:0000269|PubMed:18039659,
CC ECO:0000269|PubMed:22123986};
CC -!- SUBUNIT: Catalytic subunit of the telomerase holoenzyme complex
CC composed minimally of TERT and the telomerase RNA template component
CC (TERC). {ECO:0000269|PubMed:18039659, ECO:0000269|PubMed:22123986}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O14746}.
CC Chromosome, telomere {ECO:0000250|UniProtKB:O14746}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=A {ECO:0000303|PubMed:21547060}; Synonyms=Long
CC {ECO:0000303|PubMed:18312429};
CC IsoId=Q1PS67-1; Sequence=Displayed;
CC Name=B {ECO:0000303|PubMed:21547060};
CC IsoId=Q1PS67-2; Sequence=VSP_057764, VSP_057765;
CC Name=C {ECO:0000303|PubMed:21547060};
CC IsoId=Q1PS67-3; Sequence=VSP_057767, VSP_057768;
CC Name=D {ECO:0000303|PubMed:21547060};
CC IsoId=Q1PS67-4; Sequence=VSP_057769, VSP_057771;
CC Name=E {ECO:0000303|PubMed:21547060};
CC IsoId=Q1PS67-5; Sequence=VSP_057766, VSP_057770;
CC Name=F {ECO:0000305}; Synonyms=Short {ECO:0000303|PubMed:18312429};
CC IsoId=Q1PS67-6; Sequence=VSP_057772, VSP_057773;
CC -!- TISSUE SPECIFICITY: Expressed at highest levels in gonads and brain,
CC and at lower levels in heart, spleen, kidney, gill, muscle and skin
CC (PubMed:18312429, PubMed:21547060). Detected in embryonic stem cell
CC lines before and after differentiation (PubMed:21547060). Isoform F is
CC expressed in gonads, with higher levels in testis relative to ovary,
CC but is not detected in other tissues (PubMed:18312429). Isoform B is
CC expressed predominantly in testis (PubMed:21547060). Isoform C is up-
CC regulated in embryonic stem cell lines after differentiation
CC (PubMed:21547060). {ECO:0000269|PubMed:18312429,
CC ECO:0000269|PubMed:21547060}.
CC -!- DEVELOPMENTAL STAGE: Expressed at high levels from the embryonic 2-cell
CC stage through to the blastula stage, possibly due to inheritance of
CC maternal transcripts. During later stages levels gradually decline.
CC {ECO:0000269|PubMed:21547060}.
CC -!- SIMILARITY: Belongs to the reverse transcriptase family. Telomerase
CC subfamily. {ECO:0000305}.
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DR EMBL; DQ248968; ABB76648.1; -; mRNA.
DR EMBL; DQ870623; ABI74619.1; -; mRNA.
DR EMBL; JF326825; ADZ28508.1; -; mRNA.
DR EMBL; JF326826; ADZ28509.1; -; mRNA.
DR EMBL; JF326827; ADZ28510.1; -; mRNA.
DR EMBL; JF326828; ADZ28511.1; -; mRNA.
DR RefSeq; NP_001098286.1; NM_001104816.1.
DR PDB; 4O26; X-ray; 3.00 A; A/B=318-572.
DR PDBsum; 4O26; -.
DR AlphaFoldDB; Q1PS67; -.
DR SMR; Q1PS67; -.
DR STRING; 8090.ENSORLP00000017467; -.
DR Ensembl; ENSORLT00000035913; ENSORLP00000030497; ENSORLG00000013929. [Q1PS67-2]
DR Ensembl; ENSORLT00000044664; ENSORLP00000033801; ENSORLG00000013929. [Q1PS67-5]
DR GeneID; 100049443; -.
DR KEGG; ola:100049443; -.
DR CTD; 7015; -.
DR eggNOG; KOG1005; Eukaryota.
DR GeneTree; ENSGT00390000018531; -.
DR TreeFam; TF329048; -.
DR Proteomes; UP000001038; Chromosome 11.
DR Proteomes; UP000265180; Unplaced.
DR Proteomes; UP000265200; Unplaced.
DR Bgee; ENSORLG00000013929; Expressed in testis and 9 other tissues.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0000333; C:telomerase catalytic core complex; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070034; F:telomerase RNA binding; IPI:UniProtKB.
DR GO; GO:0003721; F:telomerase RNA reverse transcriptase activity; IDA:UniProtKB.
DR GO; GO:0042162; F:telomeric DNA binding; IBA:GO_Central.
DR GO; GO:0022616; P:DNA strand elongation; IDA:UniProtKB.
DR GO; GO:0007004; P:telomere maintenance via telomerase; ISS:UniProtKB.
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 3D-structure; Alternative splicing; Chromosome; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Ribonucleoprotein;
KW RNA-binding; RNA-directed DNA polymerase; Telomere; Transferase.
FT CHAIN 1..1090
FT /note="Telomerase reverse transcriptase"
FT /evidence="ECO:0000305"
FT /id="PRO_0000433391"
FT DOMAIN 569..893
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT REGION 184..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..376
FT /note="Interaction with RNA template"
FT /evidence="ECO:0000269|PubMed:24793650"
FT REGION 477..503
FT /note="Interaction with RNA template"
FT /evidence="ECO:0000269|PubMed:24793650"
FT MOTIF 316..321
FT /note="TFLY; involved in RNA binding"
FT /evidence="ECO:0000250|UniProtKB:Q4KTA7"
FT COMPBIAS 215..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 666
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT BINDING 826
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT BINDING 827
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT VAR_SEQ 73..444
FT /note="TCTFPELLAFILNSLKRKRRRNVLAHGYNFLGVAQEDRDADHFRFQGDLSQS
FT AAYIHSSDLWKKVTARLGTDVTRYLLGSCSVFVLAPPSCVFQICGVPAYDRVSMTTASS
FT GFLLRPPSRKHKSFQVGKKTRSANLTKTGSVGDVEESRKRRRVESEVSTRKRKRESEEE
FT ESRERRRGVHHEERRQHEAVLDESTLSGKSGENDAAAVKPPPETSAAPPPLEGGPSWRS
FT GAFPPLPSSQCFIRTLGFLYGGRGMHGFCLNRKRRTAAGPRRLQGQDLVRLVFFEGLPY
FT LNGQERKPKKLPLRYFNMVPVFGRLLQRHRKCRYSSVLHRMCPVVELSRAAQGELSSLI
FT PQHCAPHRVYLFVRECLTAVVPEEL -> VDFSDGSMGSTSMKGFVMSLQKSSKVHHAV
FT LVEQAFGSNLRGKDALQFFTQMLTGSVVQHGKKTYRQCRGIPQGSVVSSLLCCLCYGHM
FT ENVLFRDIKNKGCLMRLVDDFLLITPDRNQAQSFLSILLAGVPQYGVVANPQKVVVNFQ
FT GSEGGGAFPDIRVLPPHCLFPWCGLLLDTRSLDVCKDYSSYAGLSLRYSLTLGSAHSAG
FT QQMRRKLMSILRIKCHPLFLDLKTNSLESAYKNIHKLVLLQACRFHVCVQSLPFAQTVA
FT KNPTYFQQMIWDMAHYANALIRRSNTGLVLGDGAQKGSVQYEAVELLFCLAFLRVLSKH
FT RPVYKDLLPRLHKWKRRLERLLGDLRLARVRQAANPRALLDFLAMQM (in isoform
FT B)"
FT /id="VSP_057764"
FT VAR_SEQ 445..1090
FT /note="Missing (in isoform B)"
FT /id="VSP_057765"
FT VAR_SEQ 609..666
FT /note="LHHKRIRDLMSMLQARVRSAPALLGSTVWGMTDIHKVLRSLAPAQKDKPQPL
FT YFVKVD -> EHPMFSFLHPSLTGSPVGWAEGGCERRLRQSAARQTQGGDHRGFVTRPR
FT GSLHRPPLR (in isoform E)"
FT /id="VSP_057766"
FT VAR_SEQ 609..619
FT /note="LHHKRIRDLMS -> VHTDEISSVLS (in isoform C)"
FT /id="VSP_057767"
FT VAR_SEQ 620..1090
FT /note="Missing (in isoform C)"
FT /id="VSP_057768"
FT VAR_SEQ 666..690
FT /note="DVSGAYDSLPHDKLKEVITEALSPV -> NLVLPGTSDVFLSPPVSDGLTCG
FT LG (in isoform D)"
FT /id="VSP_057769"
FT VAR_SEQ 667..1090
FT /note="Missing (in isoform E)"
FT /id="VSP_057770"
FT VAR_SEQ 691..1090
FT /note="Missing (in isoform D)"
FT /id="VSP_057771"
FT VAR_SEQ 1057..1063
FT /note="WKRRLER -> CGCSTKH (in isoform F)"
FT /id="VSP_057772"
FT VAR_SEQ 1064..1090
FT /note="Missing (in isoform F)"
FT /id="VSP_057773"
FT MUTAGEN 355
FT /note="F->L: Mildly impaired RNA template binding."
FT /evidence="ECO:0000269|PubMed:22123986"
FT MUTAGEN 355
FT /note="F->Y: Impaired RNA template binding."
FT /evidence="ECO:0000269|PubMed:22123986"
FT MUTAGEN 376
FT /note="F->A: Impaired RNA template binding."
FT /evidence="ECO:0000269|PubMed:24793650"
FT MUTAGEN 477
FT /note="W->F: No effect on RNA template binding."
FT /evidence="ECO:0000269|PubMed:22123986"
FT MUTAGEN 477
FT /note="W->L: Impaired RNA template binding."
FT /evidence="ECO:0000269|PubMed:22123986"
FT MUTAGEN 503
FT /note="Y->A: Impaired RNA template binding."
FT /evidence="ECO:0000269|PubMed:24793650"
FT MUTAGEN 503
FT /note="Y->F: No effect on RNA template binding."
FT /evidence="ECO:0000269|PubMed:22123986"
FT MUTAGEN 503
FT /note="Y->S: Impaired RNA template binding."
FT /evidence="ECO:0000269|PubMed:22123986"
FT CONFLICT 164
FT /note="V -> I (in Ref. 1; ABB76648 and 3; ADZ28508/
FT ADZ28509/ADZ28510/ADZ28511)"
FT CONFLICT 203
FT /note="T -> R (in Ref. 1; ABB76648 and 3; ADZ28508/
FT ADZ28509/ADZ28510/ADZ28511)"
FT CONFLICT 211
FT /note="T -> R (in Ref. 1; ABB76648 and 3; ADZ28508/
FT ADZ28509/ADZ28511)"
FT CONFLICT 229
FT /note="E -> G (in Ref. 1; ABB76648 and 3; ADZ28508/
FT ADZ28509/ADZ28511)"
FT CONFLICT 232
FT /note="T -> A (in Ref. 1; ABB76648 and 3; ADZ28508/
FT ADZ28509/ADZ28511)"
FT CONFLICT 239
FT /note="S -> P (in Ref. 1; ABB76648 and 3; ADZ28508/
FT ADZ28509/ADZ28511)"
FT CONFLICT 820
FT /note="W -> C (in Ref. 1; ABB76648)"
FT HELIX 326..328
FT /evidence="ECO:0007829|PDB:4O26"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:4O26"
FT HELIX 346..354
FT /evidence="ECO:0007829|PDB:4O26"
FT HELIX 373..376
FT /evidence="ECO:0007829|PDB:4O26"
FT HELIX 379..391
FT /evidence="ECO:0007829|PDB:4O26"
FT HELIX 394..401
FT /evidence="ECO:0007829|PDB:4O26"
FT TURN 409..414
FT /evidence="ECO:0007829|PDB:4O26"
FT HELIX 415..417
FT /evidence="ECO:0007829|PDB:4O26"
FT HELIX 425..439
FT /evidence="ECO:0007829|PDB:4O26"
FT HELIX 442..445
FT /evidence="ECO:0007829|PDB:4O26"
FT HELIX 448..461
FT /evidence="ECO:0007829|PDB:4O26"
FT STRAND 468..470
FT /evidence="ECO:0007829|PDB:4O26"
FT TURN 473..475
FT /evidence="ECO:0007829|PDB:4O26"
FT HELIX 481..483
FT /evidence="ECO:0007829|PDB:4O26"
FT HELIX 485..487
FT /evidence="ECO:0007829|PDB:4O26"
FT STRAND 489..491
FT /evidence="ECO:0007829|PDB:4O26"
FT HELIX 498..517
FT /evidence="ECO:0007829|PDB:4O26"
FT HELIX 519..527
FT /evidence="ECO:0007829|PDB:4O26"
FT STRAND 529..532
FT /evidence="ECO:0007829|PDB:4O26"
FT STRAND 535..537
FT /evidence="ECO:0007829|PDB:4O26"
FT STRAND 540..543
FT /evidence="ECO:0007829|PDB:4O26"
FT HELIX 546..568
FT /evidence="ECO:0007829|PDB:4O26"
SQ SEQUENCE 1090 AA; 123387 MW; DF885F35FD57ADAB CRC64;
MTSGDLSSVL NILRSLYKRT RTLEEFADGV VFREGRRAAL LQPSDTHSFK SFVRGVFVCS
DEELQDVPSC NQTCTFPELL AFILNSLKRK RRRNVLAHGY NFLGVAQEDR DADHFRFQGD
LSQSAAYIHS SDLWKKVTAR LGTDVTRYLL GSCSVFVLAP PSCVFQICGV PAYDRVSMTT
ASSGFLLRPP SRKHKSFQVG KKTRSANLTK TGSVGDVEES RKRRRVESEV STRKRKRESE
EEESRERRRG VHHEERRQHE AVLDESTLSG KSGENDAAAV KPPPETSAAP PPLEGGPSWR
SGAFPPLPSS QCFIRTLGFL YGGRGMHGFC LNRKRRTAAG PRRLQGQDLV RLVFFEGLPY
LNGQERKPKK LPLRYFNMVP VFGRLLQRHR KCRYSSVLHR MCPVVELSRA AQGELSSLIP
QHCAPHRVYL FVRECLTAVV PEELWGSDHN RLQFFSRVRG FLKSGKFERI SVAELMWKIK
VMDCDWLKLR RTAGRFPPSE LAYRTRILSQ FLTWLLDGFV VGLVRACFYA TESVGQKNAI
RFYRQEVWSK LQDLAFRRHI AKGEMEELSP AQVASLPKGT VISQLRFIPK TDGMRPITRV
IGADSNTRLH HKRIRDLMSM LQARVRSAPA LLGSTVWGMT DIHKVLRSLA PAQKDKPQPL
YFVKVDVSGA YDSLPHDKLK EVITEALSPV QEEVFTVRHY AKIWADSHEG LKKAFARQVD
FSDGSMGSTS MKGFVMSLQK SSKVHHAVLV EQAFGSNLRG KDALQFFTQM LTGSVVQHGK
KTYRQCRGIP QGSVVSSLLC CLCYGHMENV LFRDIKNKGW LMRLVDDFLL ITPDRNQAQS
FLSILLAGVP QYGVVANPQK VVVNFQGSEG GGAFPDIRVL PPHCLFPWCG LLLDTRSLDV
CKDYSSYAGL SLRYSLTLGS AHSAGQQMRR KLMSILRIKC HPLFLDLKTN SLESAYKNIH
KLVLLQACRF HVCVQSLPFA QTVAKNPTYF QQMIWDMAHY ANALIRRSNT GLVLGDGAQK
GSVQYEAVEL LFCLAFLRVL SKHRPVYKDL LPRLHKWKRR LERLLGDLRL ARVRQAANPR
ALLDFLAMQM
