HDA10_DANRE
ID HDA10_DANRE Reviewed; 675 AA.
AC F1QCV2; Q803K0;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 14-MAY-2014, sequence version 2.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Polyamine deacetylase HDAC10;
DE EC=3.5.1.48 {ECO:0000269|PubMed:28516954};
DE EC=3.5.1.62 {ECO:0000269|PubMed:28516954};
DE AltName: Full=Histone deacetylase 10;
GN Name=hdac10;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0007744|PDB:5TD7}
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 2-676, FUNCTION, CATALYTIC
RP ACTIVITY, MUTAGENESIS OF ASN-93; ASP-94 AND GLU-274, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND ACTIVE SITE.
RX PubMed=28516954; DOI=10.1038/ncomms15368;
RA Hai Y., Shinsky S.A., Porter N.J., Christianson D.W.;
RT "Histone deacetylase 10 structure and molecular function as a polyamine
RT deacetylase.";
RL Nat. Commun. 8:15368-15368(2017).
CC -!- FUNCTION: Polyamine deacetylase (PDAC), which acts preferentially on
CC N(8)-acetylspermidine, and also on acetylcadaverine and
CC acetylputrescine (PubMed:28516954). Exhibits attenuated catalytic
CC activity toward N(1),N(8)-diacetylspermidine and very low activity, if
CC any, toward N(1)-acetylspermidine (PubMed:28516954). Has a very weak
CC lysine deacetylase, if any (PubMed:28516954).
CC {ECO:0000269|PubMed:28516954}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(8)-acetylspermidine = acetate + spermidine;
CC Xref=Rhea:RHEA:23928, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:57834, ChEBI:CHEBI:58535; EC=3.5.1.48;
CC Evidence={ECO:0000269|PubMed:28516954};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetylputrescine = acetate + putrescine;
CC Xref=Rhea:RHEA:23412, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:58263, ChEBI:CHEBI:326268; EC=3.5.1.62;
CC Evidence={ECO:0000269|PubMed:28516954};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetylcadaverine = acetate + cadaverine;
CC Xref=Rhea:RHEA:51892, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:58384, ChEBI:CHEBI:134408;
CC Evidence={ECO:0000269|PubMed:28516954};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=90 uM for acetylcadaverine {ECO:0000269|PubMed:28516954};
CC KM=160 uM for acetylputrescine {ECO:0000269|PubMed:28516954};
CC KM=130 uM for N(8)-acetylspermidine {ECO:0000269|PubMed:28516954};
CC KM=180 uM for N(1),N(8)-diacetylspermidine
CC {ECO:0000269|PubMed:28516954};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q969S8}. Nucleus
CC {ECO:0000250|UniProtKB:Q969S8}. Note=Excluded from the nucleoli.
CC {ECO:0000250|UniProtKB:Q969S8}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Originally thought to be a histone deacetylase and shown in
CC vitro to have this activity (By similarity). Has also been shown to be
CC involved in MSH2 deacetylation (By similarity). However, protein
CC deacetylase activity is a matter of debate, as 3D structure analysis
CC shows that a glutamate gatekeeper and a sterically constricted active
CC site confer specificity for N(8)-acetylspermidine hydrolysis and
CC disfavour acetyllysine hydrolysis. Supporting this observation, has
CC been shown to exhibit only very low activity, if any, towards acetyl-
CC lysine peptide substrates (By similarity).
CC {ECO:0000250|UniProtKB:Q969S8}.
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DR EMBL; FP102808; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC044446; AAH44446.1; -; mRNA.
DR RefSeq; NP_956069.1; NM_199775.1.
DR PDB; 5TD7; X-ray; 2.85 A; A=2-675.
DR PDB; 6UFN; X-ray; 2.70 A; A=2-675.
DR PDB; 6UFO; X-ray; 2.68 A; A=2-675.
DR PDB; 6UHU; X-ray; 2.80 A; A=2-675.
DR PDB; 6UHV; X-ray; 2.53 A; A=2-675.
DR PDB; 6UII; X-ray; 2.65 A; A=2-675.
DR PDB; 6UIJ; X-ray; 2.90 A; A=2-675.
DR PDB; 6UIL; X-ray; 2.85 A; A=2-675.
DR PDB; 6UIM; X-ray; 2.75 A; A=2-675.
DR PDB; 6VNQ; X-ray; 2.05 A; A=2-675.
DR PDB; 6WBQ; X-ray; 2.00 A; A=2-675.
DR PDB; 6WDV; X-ray; 2.40 A; A=2-675.
DR PDB; 6WDW; X-ray; 2.20 A; A=2-675.
DR PDB; 6WDX; X-ray; 2.65 A; A=2-675.
DR PDB; 6WDY; X-ray; 2.65 A; A=2-675.
DR PDB; 7KUQ; X-ray; 2.10 A; A=2-675.
DR PDB; 7KUR; X-ray; 2.10 A; A=2-675.
DR PDB; 7KUS; X-ray; 2.00 A; A=2-675.
DR PDB; 7KUT; X-ray; 2.05 A; A=2-675.
DR PDB; 7KUV; X-ray; 2.15 A; A=2-675.
DR PDB; 7U3M; X-ray; 2.10 A; A=2-675.
DR PDB; 7U69; X-ray; 2.50 A; A=2-675.
DR PDB; 7U6A; X-ray; 2.25 A; A=2-675.
DR PDB; 7U6B; X-ray; 2.60 A; B=2-675.
DR PDBsum; 5TD7; -.
DR PDBsum; 6UFN; -.
DR PDBsum; 6UFO; -.
DR PDBsum; 6UHU; -.
DR PDBsum; 6UHV; -.
DR PDBsum; 6UII; -.
DR PDBsum; 6UIJ; -.
DR PDBsum; 6UIL; -.
DR PDBsum; 6UIM; -.
DR PDBsum; 6VNQ; -.
DR PDBsum; 6WBQ; -.
DR PDBsum; 6WDV; -.
DR PDBsum; 6WDW; -.
DR PDBsum; 6WDX; -.
DR PDBsum; 6WDY; -.
DR PDBsum; 7KUQ; -.
DR PDBsum; 7KUR; -.
DR PDBsum; 7KUS; -.
DR PDBsum; 7KUT; -.
DR PDBsum; 7KUV; -.
DR PDBsum; 7U3M; -.
DR PDBsum; 7U69; -.
DR PDBsum; 7U6A; -.
DR PDBsum; 7U6B; -.
DR AlphaFoldDB; F1QCV2; -.
DR SMR; F1QCV2; -.
DR STRING; 7955.ENSDARP00000109870; -.
DR BindingDB; F1QCV2; -.
DR ChEMBL; CHEMBL4802002; -.
DR PaxDb; F1QCV2; -.
DR Ensembl; ENSDART00000127600; ENSDARP00000109870; ENSDARG00000086458.
DR GeneID; 327253; -.
DR KEGG; dre:327253; -.
DR CTD; 83933; -.
DR ZFIN; ZDB-GENE-030131-5464; hdac10.
DR eggNOG; KOG1343; Eukaryota.
DR GeneTree; ENSGT00940000160061; -.
DR HOGENOM; CLU_007727_6_0_1; -.
DR InParanoid; F1QCV2; -.
DR OrthoDB; 1484694at2759; -.
DR TreeFam; TF106173; -.
DR BRENDA; 3.5.1.48; 928.
DR Reactome; R-DRE-3214815; HDACs deacetylate histones.
DR Reactome; R-DRE-350054; Notch-HLH transcription pathway.
DR PRO; PR:F1QCV2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 25.
DR Bgee; ENSDARG00000086458; Expressed in mature ovarian follicle and 25 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:ZFIN.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0047609; F:acetylputrescine deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0047611; F:acetylspermidine deacetylase activity; IDA:ZFIN.
DR GO; GO:0019213; F:deacetylase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IDA:ZFIN.
DR GO; GO:0035825; P:homologous recombination; ISS:UniProtKB.
DR GO; GO:0016236; P:macroautophagy; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0106047; P:polyamine deacetylation; IDA:ZFIN.
DR GO; GO:0106048; P:spermidine deacetylation; IDA:ZFIN.
DR Gene3D; 3.40.800.20; -; 1.
DR InterPro; IPR000286; His_deacetylse.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PRINTS; PR01270; HDASUPER.
DR SUPFAM; SSF52768; SSF52768; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Metal-binding; Nucleus;
KW Reference proteome; Zinc.
FT CHAIN 1..675
FT /note="Polyamine deacetylase HDAC10"
FT /id="PRO_0000446065"
FT REGION 362..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 23..26
FT /note="Substrate specificity"
FT /evidence="ECO:0000269|PubMed:28516954"
FT COMPBIAS 382..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 137
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000269|PubMed:28516954,
FT ECO:0007744|PDB:5TD7"
FT BINDING 22
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28516954,
FT ECO:0007744|PDB:5TD7"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28516954,
FT ECO:0007744|PDB:5TD7"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:28516954,
FT ECO:0007744|PDB:5TD7"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:28516954,
FT ECO:0007744|PDB:5TD7"
FT BINDING 267
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:28516954,
FT ECO:0007744|PDB:5TD7"
FT BINDING 307
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28516954,
FT ECO:0007744|PDB:5TD7"
FT SITE 274
FT /note="Substrate specificity"
FT /evidence="ECO:0000269|PubMed:28516954"
FT MUTAGEN 93
FT /note="N->A: No effect on steady-state kinetic parameters."
FT /evidence="ECO:0000269|PubMed:28516954"
FT MUTAGEN 94
FT /note="D->A: No effect on steady-state kinetic parameters."
FT /evidence="ECO:0000269|PubMed:28516954"
FT MUTAGEN 274
FT /note="E->L: Affects substrate specificity, diminishing
FT N(8)-acetyl-spermidine deacetylase activity by 20-fold and
FT enhancing acetyl-lysine deacetylase activity by about 100-
FT fold."
FT /evidence="ECO:0000269|PubMed:28516954"
FT CONFLICT 154
FT /note="I -> F (in Ref. 2; AAH44446)"
FT /evidence="ECO:0000305"
FT CONFLICT 548
FT /note="S -> T (in Ref. 2; AAH44446)"
FT /evidence="ECO:0000305"
FT CONFLICT 586
FT /note="G -> E (in Ref. 2; AAH44446)"
FT /evidence="ECO:0000305"
FT CONFLICT 593..596
FT /note="GLMT -> RLMR (in Ref. 2; AAH44446)"
FT /evidence="ECO:0000305"
FT CONFLICT 613
FT /note="T -> M (in Ref. 2; AAH44446)"
FT /evidence="ECO:0000305"
FT CONFLICT 646
FT /note="L -> P (in Ref. 2; AAH44446)"
FT /evidence="ECO:0000305"
FT CONFLICT 675
FT /note="S -> SW (in Ref. 2; AAH44446)"
FT /evidence="ECO:0000305"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:6WBQ"
FT HELIX 11..14
FT /evidence="ECO:0007829|PDB:6WBQ"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:6WBQ"
FT HELIX 31..42
FT /evidence="ECO:0007829|PDB:6WBQ"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:6WDX"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:6WBQ"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:6WBQ"
FT HELIX 59..62
FT /evidence="ECO:0007829|PDB:6WBQ"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:6WBQ"
FT HELIX 68..75
FT /evidence="ECO:0007829|PDB:6WBQ"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:6WBQ"
FT HELIX 82..89
FT /evidence="ECO:0007829|PDB:6WBQ"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:6WBQ"
FT HELIX 101..120
FT /evidence="ECO:0007829|PDB:6WBQ"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:6WBQ"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:6WBQ"
FT HELIX 151..163
FT /evidence="ECO:0007829|PDB:6WBQ"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:6WBQ"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:6WBQ"
FT HELIX 179..185
FT /evidence="ECO:0007829|PDB:6WBQ"
FT STRAND 191..198
FT /evidence="ECO:0007829|PDB:6WBQ"
FT TURN 200..203
FT /evidence="ECO:0007829|PDB:6WBQ"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:6WBQ"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:6WBQ"
FT STRAND 224..230
FT /evidence="ECO:0007829|PDB:6WBQ"
FT HELIX 237..246
FT /evidence="ECO:0007829|PDB:6WBQ"
FT HELIX 248..255
FT /evidence="ECO:0007829|PDB:6WBQ"
FT STRAND 258..264
FT /evidence="ECO:0007829|PDB:6WBQ"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:7KUS"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:6WBQ"
FT HELIX 283..291
FT /evidence="ECO:0007829|PDB:6WBQ"
FT HELIX 294..297
FT /evidence="ECO:0007829|PDB:6WBQ"
FT STRAND 299..303
FT /evidence="ECO:0007829|PDB:6WBQ"
FT HELIX 309..323
FT /evidence="ECO:0007829|PDB:6WBQ"
FT HELIX 339..352
FT /evidence="ECO:0007829|PDB:6WBQ"
FT TURN 353..355
FT /evidence="ECO:0007829|PDB:6WBQ"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:6WBQ"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:6VNQ"
FT TURN 365..367
FT /evidence="ECO:0007829|PDB:7KUT"
FT STRAND 412..418
FT /evidence="ECO:0007829|PDB:6WBQ"
FT STRAND 420..422
FT /evidence="ECO:0007829|PDB:6WDV"
FT STRAND 431..433
FT /evidence="ECO:0007829|PDB:6WBQ"
FT HELIX 439..452
FT /evidence="ECO:0007829|PDB:6WBQ"
FT HELIX 459..476
FT /evidence="ECO:0007829|PDB:6WBQ"
FT STRAND 479..489
FT /evidence="ECO:0007829|PDB:6WBQ"
FT HELIX 491..503
FT /evidence="ECO:0007829|PDB:6WBQ"
FT TURN 504..506
FT /evidence="ECO:0007829|PDB:6WBQ"
FT STRAND 510..518
FT /evidence="ECO:0007829|PDB:6WBQ"
FT STRAND 525..537
FT /evidence="ECO:0007829|PDB:6WBQ"
FT STRAND 546..550
FT /evidence="ECO:0007829|PDB:6WBQ"
FT HELIX 557..567
FT /evidence="ECO:0007829|PDB:6WBQ"
FT HELIX 569..576
FT /evidence="ECO:0007829|PDB:6WBQ"
FT STRAND 579..585
FT /evidence="ECO:0007829|PDB:6WBQ"
FT HELIX 587..589
FT /evidence="ECO:0007829|PDB:7KUT"
FT TURN 595..597
FT /evidence="ECO:0007829|PDB:7KUS"
FT HELIX 598..605
FT /evidence="ECO:0007829|PDB:6WBQ"
FT HELIX 609..611
FT /evidence="ECO:0007829|PDB:6WBQ"
FT STRAND 613..619
FT /evidence="ECO:0007829|PDB:6WBQ"
FT HELIX 622..632
FT /evidence="ECO:0007829|PDB:6WBQ"
FT HELIX 648..661
FT /evidence="ECO:0007829|PDB:6WBQ"
FT TURN 662..664
FT /evidence="ECO:0007829|PDB:6WBQ"
FT HELIX 666..668
FT /evidence="ECO:0007829|PDB:6WBQ"
SQ SEQUENCE 675 AA; 74543 MW; 4DDABEA59E275F36 CRC64;
MASGSALIFD EEMSRYKLLW TDPACEIEVP ERLTVSYEAL RTHGLAQRCK AVPVRQATEQ
EILLAHSEEY LEAVKQTPGM NVEELMAFSK KYNDVYFHQN IYHCAKLAAG ATLQLVDSVM
KREVRNGMAL VRPPGHHSQR SAANGFCVFN NVAIAALYAK KNYNLNRILI VDWDVHHGQG
IQYCFEEDPS VLYFSWHRYE HQSFWPNLPE SDYSSVGKGK GSGFNINLPW NKVGMTNSDY
LAAFFHVLLP VAYEFDPELV IVSAGFDSAI GDPEGEMCAL PEIFAHLTHL LMPLAAGKMC
VVLEGGYNLT SLGQSVCQTV HSLLGDPTPR ISGLGTACDS ALESIQNVRN VQSSYWSSFK
HLAQSETNPK RPRLDATNGG PKESSEPASE SNPKKTAQDI VWPEPLKRMP ASVRTVVVPP
PGVELTLPKN CQHSGDISES TAKEVQRIRD KHFHDLTDQN ILRSLGNIIS VLDRMMRSDE
VCNGCVVVSD LSVSVQCALQ HALTEPAERV LVVYVGDGEL PVKTNDGKVF LVQICTKETE
DKCVNRLSLC LREGESLTAG FMQALLGLIL PVAYEFNPAL VLGIVGETAA KTGLMTVWGH
MTCLIQGLAR GRTLTLLQGY DKDLLELTVS ALSGASISPL GPLRALKPED VEMMEKQRQR
LQERWGLLRC TVSES
