HTS_DROME
ID HTS_DROME Reviewed; 1156 AA.
AC Q02645; A1ZBK8; A4UZP6; E1JGM4; E1JGM6; Q8MQX6; Q9GNA8; Q9GZC1; Q9V8U4;
AC Q9V8U5;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Protein hu-li tai shao;
DE AltName: Full=Adducin-like protein;
GN Name=hts; ORFNames=CG9325;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RC TISSUE=Egg;
RX PubMed=1340461; DOI=10.1101/gad.6.12b.2443;
RA Yue L., Spradling A.C.;
RT "hu-li tai shao, a gene required for ring canal formation during Drosophila
RT oogenesis, encodes a homolog of adducin.";
RL Genes Dev. 6:2443-2454(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RC TISSUE=Embryo;
RX PubMed=7681599; DOI=10.1073/pnas.90.6.2512;
RA Ding D., Parkhurst S.M., Lipshitz H.D.;
RT "Different genetic requirements for anterior RNA localization revealed by
RT the distribution of Adducin-like transcripts during Drosophila oogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:2512-2516(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C), AND TISSUE SPECIFICITY.
RC TISSUE=Embryo, and Ovary;
RX PubMed=10504343; DOI=10.1242/jcs.112.19.3385;
RA Whittaker K.L., Ding D., Fisher W.W., Lipshitz H.D.;
RT "Different 3' untranslated regions target alternatively processed hu-li tai
RT shao (hts) transcripts to distinct cytoplasmic locations during Drosophila
RT oogenesis.";
RL J. Cell Sci. 112:3385-3398(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [5]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-498, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-478; THR-480; SER-603;
RP TYR-608; THR-609; THR-611; SER-614; TYR-627 AND SER-630, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [9]
RP FUNCTION.
RX PubMed=23836506; DOI=10.1002/ana.23971;
RA Kruer M.C., Jepperson T., Dutta S., Steiner R.D., Cottenie E., Sanford L.,
RA Merkens M., Russman B.S., Blasco P.A., Fan G., Pollock J., Green S.,
RA Woltjer R.L., Mooney C., Kretzschmar D., Paisan-Ruiz C., Houlden H.;
RT "Mutations in gamma adducin are associated with inherited cerebral palsy.";
RL Ann. Neurol. 74:805-814(2013).
CC -!- FUNCTION: Required for assembling actin at ring canals in developing
CC egg chambers. Probably interacts with other developmental proteins
CC involved in nurse cell/oocyte transport through the ring canals.
CC Important for normal neuromotor function (PubMed:23836506).
CC {ECO:0000269|PubMed:23836506}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC Cytoplasmic side {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=A; Synonyms=K, N, N4;
CC IsoId=Q02645-1; Sequence=Displayed;
CC Name=B; Synonyms=I, L, M, R1;
CC IsoId=Q02645-2; Sequence=VSP_000191, VSP_000192;
CC Name=C; Synonyms=H, J, N32, R2;
CC IsoId=Q02645-3; Sequence=VSP_009199, VSP_009200;
CC Name=D;
CC IsoId=Q02645-4; Sequence=VSP_042122, VSP_042123;
CC -!- TISSUE SPECIFICITY: Isoform C is expressed in nurse cells. Isoform A is
CC produced in the nurse cell but transported into the oocyte at stage 1,
CC localizes to the oocyte cortex at stage 8 and to the anterior pole from
CC day 9 onwards. Isoform B is expressed in the somatic follicle cells
CC that surround the germline. {ECO:0000269|PubMed:10504343}.
CC -!- DEVELOPMENTAL STAGE: Oogenesis and early embryogenesis.
CC -!- MISCELLANEOUS: 'Hu-li tai shao' means 'too little nursing' in Chinese.
CC -!- SIMILARITY: Belongs to the aldolase class II family. Adducin subfamily.
CC {ECO:0000305}.
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DR EMBL; L05016; AAA28643.1; -; mRNA.
DR EMBL; AF151708; AAB59182.1; -; mRNA.
DR EMBL; AF151705; AAG01377.1; -; mRNA.
DR EMBL; AF151706; AAG01378.1; -; mRNA.
DR EMBL; AF151707; AAG01379.1; -; mRNA.
DR EMBL; AE013599; AAF57565.3; -; Genomic_DNA.
DR EMBL; AE013599; AAF57566.4; -; Genomic_DNA.
DR EMBL; AE013599; AAM70850.2; -; Genomic_DNA.
DR EMBL; AE013599; AAM70851.2; -; Genomic_DNA.
DR EMBL; AE013599; AAN16130.2; -; Genomic_DNA.
DR EMBL; AE013599; AAN16131.2; -; Genomic_DNA.
DR EMBL; AE013599; ACZ94475.1; -; Genomic_DNA.
DR EMBL; AE013599; ACZ94476.1; -; Genomic_DNA.
DR EMBL; AE013599; ACZ94477.1; -; Genomic_DNA.
DR EMBL; AE013599; ACZ94478.1; -; Genomic_DNA.
DR EMBL; AY122245; AAM52757.1; -; mRNA.
DR PIR; A47397; A47397.
DR RefSeq; NP_001163203.1; NM_001169732.2. [Q02645-3]
DR RefSeq; NP_001163204.1; NM_001169733.2. [Q02645-3]
DR RefSeq; NP_001163205.1; NM_001169734.2. [Q02645-1]
DR RefSeq; NP_001163206.1; NM_001169735.2. [Q02645-1]
DR RefSeq; NP_476877.1; NM_057529.4. [Q02645-1]
DR RefSeq; NP_725886.2; NM_166347.3. [Q02645-2]
DR RefSeq; NP_725887.2; NM_166348.3. [Q02645-2]
DR RefSeq; NP_725888.2; NM_166349.3. [Q02645-2]
DR RefSeq; NP_725889.1; NM_166350.2. [Q02645-4]
DR RefSeq; NP_725890.1; NM_166351.2. [Q02645-3]
DR AlphaFoldDB; Q02645; -.
DR SMR; Q02645; -.
DR BioGRID; 62894; 23.
DR DIP; DIP-23013N; -.
DR IntAct; Q02645; 16.
DR iPTMnet; Q02645; -.
DR PRIDE; Q02645; -.
DR EnsemblMetazoa; FBtr0309102; FBpp0301110; FBgn0263391. [Q02645-4]
DR EnsemblMetazoa; FBtr0309103; FBpp0301111; FBgn0263391. [Q02645-3]
DR EnsemblMetazoa; FBtr0309104; FBpp0301112; FBgn0263391. [Q02645-1]
DR EnsemblMetazoa; FBtr0309105; FBpp0301113; FBgn0263391. [Q02645-3]
DR EnsemblMetazoa; FBtr0309106; FBpp0301114; FBgn0263391. [Q02645-2]
DR EnsemblMetazoa; FBtr0309107; FBpp0301115; FBgn0263391. [Q02645-3]
DR EnsemblMetazoa; FBtr0309108; FBpp0301116; FBgn0263391. [Q02645-1]
DR EnsemblMetazoa; FBtr0309109; FBpp0301117; FBgn0263391. [Q02645-2]
DR EnsemblMetazoa; FBtr0309110; FBpp0301118; FBgn0263391. [Q02645-2]
DR EnsemblMetazoa; FBtr0309111; FBpp0301119; FBgn0263391. [Q02645-1]
DR GeneID; 37230; -.
DR KEGG; dme:Dmel_CG43443; -.
DR UCSC; CG9325-RD; d. melanogaster.
DR UCSC; CG9325-RE; d. melanogaster.
DR CTD; 116529; -.
DR FlyBase; FBgn0263391; hts.
DR VEuPathDB; VectorBase:FBgn0263391; -.
DR GeneTree; ENSGT00940000168292; -.
DR InParanoid; Q02645; -.
DR PhylomeDB; Q02645; -.
DR Reactome; R-DME-264870; Caspase-mediated cleavage of cytoskeletal proteins.
DR Reactome; R-DME-5223345; Miscellaneous transport and binding events.
DR Reactome; R-DME-9013405; RHOD GTPase cycle.
DR Reactome; R-DME-9035034; RHOF GTPase cycle.
DR SignaLink; Q02645; -.
DR BioGRID-ORCS; 37230; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 37230; -.
DR PRO; PR:Q02645; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0263391; Expressed in wing disc and 24 other tissues.
DR ExpressionAtlas; Q02645; baseline and differential.
DR Genevisible; Q02645; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0035183; C:female germline ring canal inner rim; TAS:FlyBase.
DR GO; GO:0045169; C:fusome; IDA:FlyBase.
DR GO; GO:0045172; C:germline ring canal; IDA:FlyBase.
DR GO; GO:0016328; C:lateral plasma membrane; HDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; IDA:SynGO.
DR GO; GO:0045170; C:spectrosome; IDA:FlyBase.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0061572; P:actin filament bundle organization; IMP:FlyBase.
DR GO; GO:0007527; P:adult somatic muscle development; IMP:FlyBase.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0007098; P:centrosome cycle; IMP:FlyBase.
DR GO; GO:0007282; P:cystoblast division; IMP:FlyBase.
DR GO; GO:0048135; P:female germ-line cyst formation; TAS:FlyBase.
DR GO; GO:0008302; P:female germline ring canal formation, actin assembly; IMP:FlyBase.
DR GO; GO:0045478; P:fusome organization; TAS:FlyBase.
DR GO; GO:0048134; P:germ-line cyst formation; TAS:FlyBase.
DR GO; GO:0007294; P:germarium-derived oocyte fate determination; TAS:FlyBase.
DR GO; GO:0000212; P:meiotic spindle organization; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0030723; P:ovarian fusome organization; IMP:FlyBase.
DR GO; GO:0072499; P:photoreceptor cell axon guidance; IMP:FlyBase.
DR GO; GO:0045214; P:sarcomere organization; IMP:FlyBase.
DR GO; GO:0030724; P:testicular fusome organization; IMP:FlyBase.
DR Gene3D; 3.40.225.10; -; 1.
DR InterPro; IPR001303; Aldolase_II/adducin_N.
DR InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR Pfam; PF00596; Aldolase_II; 1.
DR SMART; SM01007; Aldolase_II; 1.
DR SUPFAM; SSF53639; SSF53639; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cell membrane; Cytoplasm;
KW Cytoskeleton; Developmental protein; Differentiation; Membrane; Oogenesis;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1156
FT /note="Protein hu-li tai shao"
FT /id="PRO_0000218539"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 897..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..929
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 478
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 480
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 498
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 603
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 608
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 609
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 611
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 614
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 627
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 630
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 473..495
FT /note="WVAEGSPTHSTPVRIEDPLQFVP -> VEIITFEDMKQTKTTNLKEIEGK
FT (in isoform C)"
FT /evidence="ECO:0000303|PubMed:10504343"
FT /id="VSP_009199"
FT VAR_SEQ 496..1156
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:10504343"
FT /id="VSP_009200"
FT VAR_SEQ 659..718
FT /note="ALVSQLAQKYAFLYSPGQYMYACMKMAPLMHKVYVIHKVEPVSKHNYPPVND
FT GNMSIHHN -> GENVQNGDHSEAHLSTFSQSSKEFQDVSTDGSPKKDKKKKKGLRTPS
FT FLKKKKEKKKAEA (in isoform B)"
FT /evidence="ECO:0000303|PubMed:10504343,
FT ECO:0000303|PubMed:12537569"
FT /id="VSP_000191"
FT VAR_SEQ 659..668
FT /note="ALVSQLAQKY -> GTNCCTAFIK (in isoform D)"
FT /evidence="ECO:0000305"
FT /id="VSP_042122"
FT VAR_SEQ 669..1156
FT /note="Missing (in isoform D)"
FT /evidence="ECO:0000305"
FT /id="VSP_042123"
FT VAR_SEQ 719..1156
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:10504343,
FT ECO:0000303|PubMed:12537569"
FT /id="VSP_000192"
FT CONFLICT 76
FT /note="Missing (in Ref. 6; AAM52757)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="A -> V (in Ref. 1; AAA28643)"
FT /evidence="ECO:0000305"
FT CONFLICT 680..682
FT /note="ACM -> GCL (in Ref. 1; AAA28643)"
FT /evidence="ECO:0000305"
FT CONFLICT 689
FT /note="H -> Q (in Ref. 1; AAA28643 and 2; AAB59182)"
FT /evidence="ECO:0000305"
FT CONFLICT 725..727
FT /note="MAQ -> LAH (in Ref. 1; AAA28643)"
FT /evidence="ECO:0000305"
FT CONFLICT 746
FT /note="L -> F (in Ref. 1; AAA28643)"
FT /evidence="ECO:0000305"
FT CONFLICT 912
FT /note="N -> D (in Ref. 1; AAA28643)"
FT /evidence="ECO:0000305"
FT CONFLICT 1089
FT /note="G -> C (in Ref. 2; AAB59182)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1156 AA; 127939 MW; 5AA90E8938A84A0A CRC64;
MTEVEQPPQN GIDPTAGEDD DNSKARPADI EQDMREMERR KRVEAIMGSK LFREELERIV
DSARDGGAGA SGILQQLSDI VGVPVSRVGS VFKSSNCMVP INDIRGVESM GYAKGEKILR
CKLAATFRLL DLYGWTQGLG AQITARLKVD QEYFLVNPYG LLYHEITASA LNKVDMQGQI
VEQGTTNFGG NKSHFVLHSV VHAARPDIRC AIYIGCSPVV AISSLKTGLL PLTKDACVLG
EITTHAYTGL FDEEERNRLV RSLGPNSKVI LLTNHGALCC GETIEEAFFA ACHIVQACET
QLKLLPVGLD NLVLIPEESR KAIYEQSRRP PEDLEKKFAA VAAAEDGAAT AEKDAAEAVP
KVGSPPKWRV GGAEFEALMR MLDNAGYRTG YIYRHPLIKS DPPKPKNDVE LPPAVSSLGY
LLEEEELFRQ GIWKKGDIRK GGDRSRWLNS PNVYQKVEVL ETGTPDPKKI TKWVAEGSPT
HSTPVRIEDP LQFVPAGTNP REFKRVQQLI KDNRRADKIS AGPQSHILEG VTWDEASRLK
DATVSQAGDH VVMMGAASKG IIQRGFQHNA TVYKAPYAKN PFDNVTDDEL NEYKRTVERK
KKSVHGEYTD TDFSESEAVL QAGTKKYPQS EPETEHQVIE IQTQQAPVPR QAEVVLSDAL
VSQLAQKYAF LYSPGQYMYA CMKMAPLMHK VYVIHKVEPV SKHNYPPVND GNMSIHHNES
GAGFMAQESS VISSTPVRNA LASVSLPEER NHSILGLSST PYRTISHFGF NCPLITSPTI
LLHPEHRSIW QRVAEQREKV VSFIDLTTLS LDNRKLLNVV TSTHPTQCQS QSQSFISEKH
IQLEVTPPKR KQRVYSATIS SGLDDSLDEL DSLMSGLAIN MPRSREQDSG LYRSYTFLPS
NHALPKDTDA NNRDQTDRER PEAEQEESFH CAGDSGIGDS TGRRPRLATT SNDSSIQEAE
AYTQGKHVKL TLSSSPTPTA TQSPATIEIL INVSLRNAEC VQTVQTHEQE FRAKLERVID
EEIHYISQQL AFKQRQAELH EQQTTSRAPI ATPSFTTMHP PAPASSSSMV HRSNSAPELC
HTYSYVAVGD LSTKQDQASP QLPAEGEPLN DILSSLEKEL ERLLNSVVTA HMLHNKAIIH
ECRARFSQLA DGIVSS
