LIMK1_DROME
ID LIMK1_DROME Reviewed; 1257 AA.
AC Q8IR79; Q8IR78; Q9GV18; Q9GV19; Q9VYL6;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=LIM domain kinase 1;
DE Short=LIMK-1;
DE EC=2.7.11.1 {ECO:0000269|PubMed:11027607};
DE AltName: Full=dLIMK;
GN Name=LIMK1; Synonyms=LIMK; ORFNames=CG1848;
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] (ISOFORMS 1 AND 2), FUNCTION, CATALYTIC
RP ACTIVITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP ASP-522.
RX PubMed=11027607; DOI=10.1006/bbrc.2000.3599;
RA Ohashi K., Hosoya T., Takahashi K., Hing H., Mizuno K.;
RT "A Drosophila homolog of LIM-kinase phosphorylates cofilin and induces
RT actin cytoskeletal reorganization.";
RL Biochem. Biophys. Res. Commun. 276:1178-1185(2000).
RN [2]
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 [3]
RP GENOME REANNOTATION.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [5]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP ASP-522.
RX PubMed=14972681; DOI=10.1016/j.cub.2004.01.056;
RA Chen G.-C., Gajowniczek P., Settleman J.;
RT "Rho-LIM kinase signaling regulates ecdysone-induced gene expression and
RT morphogenesis during Drosophila metamorphosis.";
RL Curr. Biol. 14:309-313(2004).
RN [6]
RP FUNCTION, INTERACTION WITH LATS1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP ASP-522.
RX PubMed=15220930; DOI=10.1038/ncb1140;
RA Yang X., Yu K., Hao Y., Li D.-M., Stewart R.A., Insogna K.L., Xu T.;
RT "LATS1 tumour suppressor affects cytokinesis by inhibiting LIMK1.";
RL Nat. Cell Biol. 6:609-617(2004).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF ASP-522.
RX PubMed=15572110; DOI=10.1016/j.neuron.2004.11.014;
RA Ng J., Luo L.;
RT "Rho GTPases regulate axon growth through convergent and divergent
RT signaling pathways.";
RL Neuron 44:779-793(2004).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF ASP-522.
RX PubMed=15657426; DOI=10.1128/mcb.25.3.979-987.2005;
RA Chen G.-C., Turano B., Ruest P.J., Hagel M., Settleman J., Thomas S.M.;
RT "Regulation of Rho and Rac signaling to the actin cytoskeleton by paxillin
RT during Drosophila development.";
RL Mol. Cell. Biol. 25:979-987(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1000, 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).
CC -!- FUNCTION: Protein kinase which regulates actin filament dynamics.
CC Phosphorylates and inactivates the actin binding/depolymerizing factor
CC tsr/cofilin, thereby stabilizing the actin cytoskeleton. Modulation of
CC actin cytoskeleton dynamics may be essential for imaginal disk
CC morphogenesis and axon guidance. {ECO:0000269|PubMed:11027607,
CC ECO:0000269|PubMed:14972681, ECO:0000269|PubMed:15220930,
CC ECO:0000269|PubMed:15572110, ECO:0000269|PubMed:15657426}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:11027607};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:11027607};
CC -!- SUBUNIT: Interacts with LATS1, and this interaction inhibits
CC phosphorylation of tsr/cofilin. {ECO:0000269|PubMed:15220930}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cleavage furrow. Midbody.
CC Note=Localizes to the cleavage furrow and the midbody at cytokinesis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8IR79-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IR79-2; Sequence=VSP_016309;
CC Name=3;
CC IsoId=Q8IR79-3; Sequence=VSP_016308, VSP_016310;
CC -!- TISSUE SPECIFICITY: Expressed throughout the imaginal disks of the eye,
CC leg and wing. {ECO:0000269|PubMed:14972681}.
CC -!- DEVELOPMENTAL STAGE: Expressed from early third instar to late pupal
CC stages. {ECO:0000269|PubMed:11027607, ECO:0000269|PubMed:14972681}.
CC -!- PTM: Phosphorylated on serine and/or threonine residues by ROCK1.
CC Phosphorylated by PAK4 resulting in increased LIMK1 ability to
CC phosphorylate cofilin. May be dephosphorylated and inactivated by SSH1
CC (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AB042816; BAB17233.1; -; mRNA.
DR EMBL; AB042818; BAB17234.1; -; mRNA.
DR EMBL; AE014298; AAF48176.2; -; Genomic_DNA.
DR EMBL; AE014298; AAN09311.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09312.1; -; Genomic_DNA.
DR EMBL; AY119587; AAM50241.1; -; mRNA.
DR RefSeq; NP_001162733.1; NM_001169262.1. [Q8IR79-2]
DR RefSeq; NP_511139.2; NM_078584.3. [Q8IR79-1]
DR RefSeq; NP_727621.1; NM_167326.2. [Q8IR79-2]
DR RefSeq; NP_727622.1; NM_167327.2. [Q8IR79-3]
DR AlphaFoldDB; Q8IR79; -.
DR SMR; Q8IR79; -.
DR BioGRID; 58605; 45.
DR IntAct; Q8IR79; 9.
DR STRING; 7227.FBpp0073493; -.
DR iPTMnet; Q8IR79; -.
DR PaxDb; Q8IR79; -.
DR PRIDE; Q8IR79; -.
DR DNASU; 32207; -.
DR EnsemblMetazoa; FBtr0073659; FBpp0073492; FBgn0283712. [Q8IR79-2]
DR EnsemblMetazoa; FBtr0073660; FBpp0073493; FBgn0283712. [Q8IR79-1]
DR EnsemblMetazoa; FBtr0073661; FBpp0073494; FBgn0283712. [Q8IR79-3]
DR EnsemblMetazoa; FBtr0301830; FBpp0291044; FBgn0283712. [Q8IR79-2]
DR GeneID; 32207; -.
DR KEGG; dme:Dmel_CG1848; -.
DR CTD; 3984; -.
DR FlyBase; FBgn0283712; LIMK1.
DR VEuPathDB; VectorBase:FBgn0283712; -.
DR eggNOG; KOG1187; Eukaryota.
DR GeneTree; ENSGT00940000170287; -.
DR InParanoid; Q8IR79; -.
DR PhylomeDB; Q8IR79; -.
DR Reactome; R-DME-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-DME-399954; Sema3A PAK dependent Axon repulsion.
DR Reactome; R-DME-5627123; RHO GTPases activate PAKs.
DR GenomeRNAi; 32207; -.
DR PRO; PR:Q8IR79; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0283712; Expressed in brain and 22 other tissues.
DR ExpressionAtlas; Q8IR79; baseline and differential.
DR Genevisible; Q8IR79; DM.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; IDA:UniProtKB.
DR GO; GO:0007560; P:imaginal disc morphogenesis; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00412; LIM; 2.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00132; LIM; 2.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 2.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Kinase; LIM domain;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; Transferase; Zinc.
FT CHAIN 1..1257
FT /note="LIM domain kinase 1"
FT /id="PRO_0000075808"
FT DOMAIN 31..93
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 94..154
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 174..274
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 401..686
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..147
FT /note="Interaction with LATS1"
FT /evidence="ECO:0000269|PubMed:15220930"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 881..900
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1010..1037
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1085..1182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1212..1257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..811
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1037
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1085..1100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1221..1235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 522
FT /evidence="ECO:0000250"
FT BINDING 407..415
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 430
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 1000
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT VAR_SEQ 1..205
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_016308"
FT VAR_SEQ 203..225
FT /note="DLFCNFFLWLTSMAEQCCGAPYR -> E (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11027607,
FT ECO:0000303|PubMed:12537569"
FT /id="VSP_016309"
FT VAR_SEQ 206..225
FT /note="CNFFLWLTSMAEQCCGAPYR -> MSFWLHFVLKKILPWLKSTK (in
FT isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_016310"
FT MUTAGEN 522
FT /note="D->A: Abrogates kinase activity."
FT /evidence="ECO:0000269|PubMed:11027607,
FT ECO:0000269|PubMed:14972681, ECO:0000269|PubMed:15220930,
FT ECO:0000269|PubMed:15572110, ECO:0000269|PubMed:15657426"
FT CONFLICT 613
FT /note="V -> L (in Ref. 1; BAB17233/BAB17234)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1257 AA; 139304 MW; 3B3C988A69D07C69 CRC64;
MHHQQRLRAN GGRGGTGLGA GSGPVSGGHS PLCAHCRGQL LPHPEEPIVM ALGQQWHCDC
FRCSVCEGHL HNWYFEREGL LYCREDYYGR FGDACQQCMA VITGPVMVAG EHKFHPECFC
CTACGSFIGE GESYALVERS KLYCGQCYGK RSCQPADAKA RITTAGKPMH SIRLVEIPKD
ATPGLRVDGV ALDDGCPTVR ITDLFCNFFL WLTSMAEQCC GAPYRIDVNL TNLHIGDRIL
EVNGTPVSDS SVEQIDKLIR SNEKMLQLTV EHDPVQVCRS CSQADIQRAM SASTLILPLS
TSASSVEVGR ERLYKTPGEQ GTKARKLRQA TNASTTIPPA AGATAMTQLK EKERCSSLSK
LLDEQHQAQQ HSAHPQLYDL SRTQSCRVVQ KPQRIFRATD LVIGEKLGEG FFGKVFKVTH
RQSGEVMVLK ELHRADEEAQ RNFIKEVAVL RLLDHRHVLK FIGVLYKDKK LHMVTEYVAG
GCLKELIHDP AQVLPWPQRV RLARDIACGM SYLHSMNIIH RDLNSMNCLV REDRSVIVAD
FGLARSVDAP RLPSGNMTPG GYGSGANSDA PMSPSGTLRR SKSRQRRQRY TVVGNPYWMA
PEMMKGLKYD EKVDVFSFGI MLCEIIGRVE ADPDFMPRNS DFSLNQQEFR EKFCAQCPEP
FVKVAFVCCD LNPDMRPCFE TLHVWLQRLA DDLAADRVPP ERLLHEIETF QEWYASSEDA
LSPTSQRSLN NLDELVKSAV DSEISPVEKE KENMVIKPQD IPKSPHLGKD FSPSGERLRD
SMRARRRQRF LGAQEERRNL TPDTESKERA LKKALKKCRP FGERGYLVDL RAGAELQLED
VRDLNTYSDV DSSCDTSLNY HDVNNLPAAQ EDENTVKPGK EELLEESTNK PSNQESQHHR
LAIDDMRTRL NQCRSKFEHL EEASRRNFNQ SQHSMKNFFK TPPVALKMFQ RLEHEAAALN
GGNNCPPPPP RTQRINQTPI FGRKNPPVAI VGQKLQHAES LEDLASSGVA KQLATPAPKR
SKATATTKGG QSSNPPLFLP PSLNISVALN SNGNVTTTTN TNSSCPPSAS DWLPKKHKLT
LPLPSAQQQR TSSNHRLPMC NNKGKTLKPL PSRTGSQGIP ASNCVSPTRS SRPGSPTKHL
AQRHTAATAQ RLTNAAATHQ QQHQQQSSKT TRLNILSPEK VHRLGARLTD QKQKMREEAA
ATASSVGGAG CAAGTAAGSL NGHRTIGSSG TPNSAVGERR RRAAPSPPVR THFNTRC
