HIRA_MOUSE
ID HIRA_MOUSE Reviewed; 1015 AA.
AC Q61666; O08845; Q3TFY0; Q3UX35; Q62365; Q7TMW4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 3.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Protein HIRA;
DE AltName: Full=TUP1-like enhancer of split protein 1;
GN Name=Hira; Synonyms=Tuple1;
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] (ISOFORM LONG).
RC STRAIN=DBA/2J;
RX PubMed=8611624; DOI=10.1016/0167-4781(96)00010-3;
RA Scamps C., Lorain S., Lamour V., Lipinski M.;
RT "The HIR protein family: isolation and characterization of a complete
RT murine cDNA.";
RL Biochim. Biophys. Acta 1306:5-8(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND DEVELOPMENTAL STAGE.
RC STRAIN=ICR X Swiss Webster; TISSUE=Embryo;
RX PubMed=9063745; DOI=10.1093/hmg/6.2.247;
RA Wilming L.G., Snoeren C.A.S., van Rijswijk A., Grosveld F., Meijers C.;
RT "The murine homologue of HIRA, a DiGeorge syndrome candidate gene, is
RT expressed in embryonic structures affected in human CATCH22 patients.";
RL Hum. Mol. Genet. 6:247-258(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 45-562 (ISOFORM SHORT).
RC STRAIN=BALB/cJ, and C57BL/6J; TISSUE=Embryo, and Kidney;
RX PubMed=8111380; DOI=10.1093/hmg/2.12.2099;
RA Halford S., Wadey R., Roberts C., Daw S.C.M., Whiting J.A., O'Donnell H.,
RA Dunham I., Bentley D., Lindsay E., Baldini A., Francis F., Lehrach H.,
RA Williamson R., Wilson D.I., Goodship J., Cross I., Burn J., Scambler P.J.;
RT "Isolation of a putative transcriptional regulator from the region of 22q11
RT deleted in DiGeorge syndrome, Shprintzen syndrome and familial congenital
RT heart disease.";
RL Hum. Mol. Genet. 2:2099-2107(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 748-1015 (ISOFORMS LONG/4).
RC STRAIN=C57BL/6J; TISSUE=Egg;
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 MRNA] (ISOFORM 3).
RC STRAIN=C3H/He; TISSUE=Mesenchymal stem cell;
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 [6]
RP INTERACTION WITH HISTONE H2B; HISTONE H3-3B; PAX3 AND PAX7, SUBCELLULAR
RP LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=9731536; DOI=10.1038/1739;
RA Magnaghi P., Roberts C., Lorain S., Lipinski M., Scambler P.J.;
RT "HIRA, a mammalian homologue of Saccharomyces cerevisiae transcriptional
RT co-repressors, interacts with Pax3.";
RL Nat. Genet. 20:74-77(1998).
RN [7]
RP PHOSPHORYLATION AT THR-554.
RX PubMed=11238922; DOI=10.1128/mcb.21.5.1854-1865.2001;
RA Hall C., Nelson D.M., Ye X., Baker K., DeCaprio J.A., Seeholzer S.,
RA Lipinski M., Adams P.D.;
RT "HIRA, the human homologue of yeast Hir1p and Hir2p, is a novel cyclin-cdk2
RT substrate whose expression blocks S-phase progression.";
RL Mol. Cell. Biol. 21:1854-1865(2001).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=15922569; DOI=10.1016/j.mod.2005.04.009;
RA van der Heijden G.W., Dieker J.W., Derijck A.A.H.A., Muller S.,
RA Berden J.H.M., Braat D.D.M., van der Vlag J., de Boer P.;
RT "Asymmetry in histone H3 variants and lysine methylation between paternal
RT and maternal chromatin of the early mouse zygote.";
RL Mech. Dev. 122:1008-1022(2005).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16399082; DOI=10.1016/j.devcel.2005.10.017;
RA Meshorer E., Yellajoshula D., George E., Scambler P.J., Brown D.T.,
RA Misteli T.;
RT "Hyperdynamic plasticity of chromatin proteins in pluripotent embryonic
RT stem cells.";
RL Dev. Cell 10:105-116(2006).
CC -!- FUNCTION: Required for the periodic repression of histone gene
CC transcription during the cell cycle (By similarity). Cooperates with
CC ASF1A to promote replication-independent chromatin assembly. Required
CC for the formation of senescence-associated heterochromatin foci (SAHF)
CC and efficient senescence-associated cell cycle exit. {ECO:0000250,
CC ECO:0000269|PubMed:16399082}.
CC -!- SUBUNIT: Interacts with CCNA1, HIRIP3 and NFU1/HIRIP5 (By similarity).
CC Part of a complex which includes ASF1A, CABIN1, histone H3.3, histone
CC H4 and UBN1 (By similarity). Interacts with histone H2B, histone H3-3B,
CC PAX3 and PAX7 (PubMed:9731536). {ECO:0000250|UniProtKB:P54198,
CC ECO:0000269|PubMed:9731536}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, PML body
CC {ECO:0000250}. Note=Primarily, though not exclusively, localized to the
CC nucleus (By similarity). Localizes to PML bodies immediately prior to
CC onset of senescence (By similarity). Localizes specifically to the male
CC nucleus in fertilized eggs. This localization persists from the
CC initiation of sperm nucleus decondensation to pronucleus formation.
CC {ECO:0000250, ECO:0000269|PubMed:15922569, ECO:0000269|PubMed:9731536}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=Long;
CC IsoId=Q61666-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q61666-2; Sequence=VSP_006773, VSP_006774;
CC Name=3;
CC IsoId=Q61666-3; Sequence=VSP_025050, VSP_025051, VSP_025052;
CC Name=4;
CC IsoId=Q61666-4; Sequence=VSP_025049;
CC -!- TISSUE SPECIFICITY: Expressed in cerebrum, cerebellum, heart, kidney,
CC liver, lung and spleen.
CC -!- DEVELOPMENTAL STAGE: Throughout development the long isoform is more
CC abundant. In embryos, ubiquitously expressed with high levels detected
CC in cranial neural folds, subregions of pharyngeal arches 1 and 2,
CC circumpharyngeal neural crest and limb buds.
CC {ECO:0000269|PubMed:9063745, ECO:0000269|PubMed:9731536}.
CC -!- PTM: Sumoylated. {ECO:0000250}.
CC -!- PTM: Phosphorylated by CDK2/CCNA1 and CDK2/CCNE1 on Thr-554 in vitro
CC (By similarity). Also phosphorylated on Thr-554 in vivo. {ECO:0000250,
CC ECO:0000269|PubMed:11238922}.
CC -!- DISRUPTION PHENOTYPE: Embryonic stem cells (ES cells) exhibit
CC accelerated differentiation in the early stages which may be
CC attributable to increased availability of soluble histones.
CC {ECO:0000269|PubMed:16399082}.
CC -!- SIMILARITY: Belongs to the WD repeat HIR1 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; X92590; CAA63334.1; -; mRNA.
DR EMBL; X99712; CAA68049.1; -; mRNA.
DR EMBL; X75295; CAA53043.1; -; mRNA.
DR EMBL; AK135928; BAE22728.1; -; mRNA.
DR EMBL; AK168963; BAE40768.1; -; mRNA.
DR EMBL; BC052856; AAH52856.1; -; mRNA.
DR CCDS; CCDS28031.1; -. [Q61666-1]
DR PIR; S45345; S45345.
DR PIR; S68141; S68141.
DR RefSeq; NP_034565.2; NM_010435.2. [Q61666-1]
DR AlphaFoldDB; Q61666; -.
DR SMR; Q61666; -.
DR BioGRID; 200309; 17.
DR IntAct; Q61666; 8.
DR MINT; Q61666; -.
DR STRING; 10090.ENSMUSP00000004222; -.
DR iPTMnet; Q61666; -.
DR PhosphoSitePlus; Q61666; -.
DR EPD; Q61666; -.
DR MaxQB; Q61666; -.
DR PaxDb; Q61666; -.
DR PeptideAtlas; Q61666; -.
DR PRIDE; Q61666; -.
DR ProteomicsDB; 269756; -. [Q61666-1]
DR ProteomicsDB; 269757; -. [Q61666-2]
DR ProteomicsDB; 269758; -. [Q61666-3]
DR ProteomicsDB; 269759; -. [Q61666-4]
DR Antibodypedia; 34961; 278 antibodies from 30 providers.
DR DNASU; 15260; -.
DR Ensembl; ENSMUST00000004222; ENSMUSP00000004222; ENSMUSG00000022702. [Q61666-1]
DR Ensembl; ENSMUST00000120532; ENSMUSP00000112614; ENSMUSG00000022702. [Q61666-3]
DR GeneID; 15260; -.
DR KEGG; mmu:15260; -.
DR UCSC; uc007yoq.1; mouse. [Q61666-1]
DR UCSC; uc007yor.1; mouse. [Q61666-3]
DR CTD; 7290; -.
DR MGI; MGI:99430; Hira.
DR VEuPathDB; HostDB:ENSMUSG00000022702; -.
DR eggNOG; KOG0973; Eukaryota.
DR GeneTree; ENSGT00550000074919; -.
DR HOGENOM; CLU_604037_0_0_1; -.
DR InParanoid; Q61666; -.
DR OMA; RGSWDGD; -.
DR OrthoDB; 685536at2759; -.
DR PhylomeDB; Q61666; -.
DR TreeFam; TF323161; -.
DR Reactome; R-MMU-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
DR BioGRID-ORCS; 15260; 32 hits in 78 CRISPR screens.
DR ChiTaRS; Hira; mouse.
DR PRO; PR:Q61666; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q61666; protein.
DR Bgee; ENSMUSG00000022702; Expressed in ventricular zone and 187 other tissues.
DR ExpressionAtlas; Q61666; baseline and differential.
DR Genevisible; Q61666; MM.
DR GO; GO:0000785; C:chromatin; IDA:MGI.
DR GO; GO:0000417; C:HIR complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0042393; F:histone binding; ISO:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0006336; P:DNA replication-independent chromatin assembly; ISO:MGI.
DR GO; GO:0007369; P:gastrulation; IMP:MGI.
DR GO; GO:0042692; P:muscle cell differentiation; IGI:MGI.
DR GO; GO:0001649; P:osteoblast differentiation; IGI:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR031120; HIR1.
DR InterPro; IPR011494; Hira.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR13831; PTHR13831; 1.
DR Pfam; PF07569; Hira; 1.
DR Pfam; PF00400; WD40; 4.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromatin regulator; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; WD repeat.
FT CHAIN 1..1015
FT /note="Protein HIRA"
FT /id="PRO_0000051020"
FT REPEAT 11..53
FT /note="WD 1"
FT REPEAT 68..107
FT /note="WD 2"
FT REPEAT 129..168
FT /note="WD 3"
FT REPEAT 172..211
FT /note="WD 4"
FT REPEAT 220..263
FT /note="WD 5"
FT REPEAT 266..322
FT /note="WD 6"
FT REPEAT 326..367
FT /note="WD 7"
FT REGION 408..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..727
FT /note="Interaction with CCNA1"
FT /evidence="ECO:0000250"
FT REGION 421..479
FT /note="Interaction with ASF1A"
FT /evidence="ECO:0000250"
FT REGION 439..475
FT /note="Required for repression of histone gene
FT transcription"
FT /evidence="ECO:0000250"
FT REGION 494..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..737
FT /note="Interaction with PAX3"
FT /evidence="ECO:0000269|PubMed:9731536"
FT REGION 594..824
FT /note="Interaction with histone H2B"
FT /evidence="ECO:0000250"
FT REGION 603..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..1015
FT /note="Interaction with histone H4"
FT /evidence="ECO:0000250"
FT REGION 738..826
FT /note="Interaction with PAX3"
FT /evidence="ECO:0000269|PubMed:9731536"
FT COMPBIAS 494..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54198"
FT MOD_RES 548
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54198"
FT MOD_RES 554
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:11238922"
FT MOD_RES 556
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54198"
FT MOD_RES 575
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P54198"
FT MOD_RES 583
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54198"
FT MOD_RES 608
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54198"
FT MOD_RES 609
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54198"
FT MOD_RES 610
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54198"
FT MOD_RES 612
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54198"
FT MOD_RES 659
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54198"
FT MOD_RES 673
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54198"
FT VAR_SEQ 1..652
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025049"
FT VAR_SEQ 1..44
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025050"
FT VAR_SEQ 473..497
FT /note="DFSTAFFNSIPLSSSLAGTMLSSPS -> YSLLHQAFCGLVWGGLLFFCCQL
FT AS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025051"
FT VAR_SEQ 498..1015
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025052"
FT VAR_SEQ 556..562
FT /note="SKIEPMK -> PQYIICSP (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:8111380"
FT /id="VSP_006773"
FT VAR_SEQ 563..1015
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:8111380"
FT /id="VSP_006774"
FT CONFLICT 216
FT /note="F -> C (in Ref. 1; CAA63334)"
FT /evidence="ECO:0000305"
FT CONFLICT 400
FT /note="E -> G (in Ref. 5; AAH52856)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="R -> S (in Ref. 1; CAA63334)"
FT /evidence="ECO:0000305"
FT CONFLICT 650
FT /note="L -> F (in Ref. 1; CAA63334)"
FT /evidence="ECO:0000305"
FT CONFLICT 712
FT /note="G -> R (in Ref. 2; CAA68049)"
FT /evidence="ECO:0000305"
FT CONFLICT 1007
FT /note="E -> G (in Ref. 1; CAA63334)"
FT /evidence="ECO:0000305"
FT CONFLICT 1013..1014
FT /note="RD -> WG (in Ref. 1; CAA63334)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1015 AA; 111767 MW; 2D84294D45B7A967 CRC64;
MKLLKPTWVN HNGKPIFSVD IHPDGTKFAT GGQGQDSGKV VIWNMSPVLQ EDDEKDENIP
KMLCQMDNHL ACVNCVRWSN SGMYLASGGD DKLIMVWKRA TYIGPSTVFG SSGKLANVEQ
WRCVSILRSH SGDVMDVAWS PHDAWLASCS VDNTVVIWNA VKFPEILATL RGHSGLVKGL
TWDPVGKYIA SQADDRSLKV WRTLDWQLET SITKPFDECG GTTHVLRLSW SPDGHYLVSA
HAMNNSGPTA QIIEREGWKT NMDFVGHRKA VTVVKFNPKI FKKKQKNGSS TKPSCPYCCC
AVGSKDRSLS VWLTCLKRPL VVIHELFDKS IMDISWTLNG LGILVCSMDG SVAFLDFSQD
ELGDPLSEEE KSRIHQSTYG KSLAIMTEAQ LSTAVIENPE MLKYQRRQQQ QQLDQKNATT
RETSSASSVT GVVNGESLED IRKNLLKKQV ETRTADGRRR ITPLCIAQLD TGDFSTAFFN
SIPLSSSLAG TMLSSPSGQQ LLPLDSSTPS FGASKPCTEP VAATSARPTG ESVSKDSMNA
TSTPAASSPS VLTTPSKIEP MKAFDSRFTE RSKATPGAPS LTSVIPTAVE RLKEQNLVKE
LRSRELESSS DSDEKVHLAK PSSLSKRKLE LEVETVEKKK KGRPRKDSRL LPMSLSVQSP
AALSTEKEAM CLSAPALALK LPIPGPQRAF TLQVSSDPSM YIEVENEVTT VGGIRLSRLK
CNREGKEWET VLSSRVLTAA GSCDVVCVAC EKRMLSVFST CGRRLLPPIL LPSPISTLHC
TGPYVMALTA AATLSVWDVH RQVVVVKEES LHSILSGSDM TVSQILLTQH GIPVMNLSDG
KAYCFNPSLS TWNLVSDKQD SLAQCADFRN SLPSQDAMLC SGPLAIIQGR TSNSGRQAAR
LFSVPHVVQQ ETTLAYLENQ VAAALTLQSS HEYRHWLLLY ARYLVNEGFE YRLREICKDL
LGPVHCSTGS QWESTVVGLR KRELLKELLP VIGQNLRFQR LFTECQEQLD ILRDK
