ID LMOD2_HUMAN Reviewed; 547 AA. AC Q6P5Q4; A4D0W9; A4D0Y2; Q8WVJ8; DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot. DT 13-NOV-2007, sequence version 2. DT 12-OCT-2022, entry version 130. DE RecName: Full=Leiomodin-2; DE AltName: Full=Cardiac leiomodin; DE Short=C-LMOD; DE AltName: Full=Leiomodin {ECO:0000303|PubMed:18403713}; GN Name=LMOD2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12690205; DOI=10.1126/science.1083423; RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D., RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., RA Adams M.D., Tsui L.-C.; RT "Human chromosome 7: DNA sequence and biology."; RL Science 300:767-772(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC TISSUE=Skeletal muscle; 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 [3] RP TISSUE SPECIFICITY. RX PubMed=11318603; DOI=10.1006/geno.2000.6501; RA Conley C.A., Fritz-Six K.L., Almenar-Queralt A., Fowler V.M.; RT "Leiomodins: larger members of the tropomodulin (Tmod) gene family."; RL Genomics 73:127-139(2001). RN [4] RP FUNCTION, SUBCELLULAR LOCATION, ACTIN-BINDING, AND SUBUNIT. RX PubMed=18403713; DOI=10.1126/science.1155313; RA Chereau D., Boczkowska M., Skwarek-Maruszewska A., Fujiwara I., Hayes D.B., RA Rebowski G., Lappalainen P., Pollard T.D., Dominguez R.; RT "Leiomodin is an actin filament nucleator in muscle cells."; RL Science 320:239-243(2008). RN [5] RP FUNCTION, INTERACTION WITH TPM1/2, AND TISSUE SPECIFICITY. RX PubMed=25250574; DOI=10.1172/jci75199; RA Yuen M., Sandaradura S.A., Dowling J.J., Kostyukova A.S., Moroz N., RA Quinlan K.G., Lehtokari V.L., Ravenscroft G., Todd E.J., Ceyhan-Birsoy O., RA Gokhin D.S., Maluenda J., Lek M., Nolent F., Pappas C.T., Novak S.M., RA D'Amico A., Malfatti E., Thomas B.P., Gabriel S.B., Gupta N., Daly M.J., RA Ilkovski B., Houweling P.J., Davidson A.E., Swanson L.C., Brownstein C.A., RA Gupta V.A., Medne L., Shannon P., Martin N., Bick D.P., Flisberg A., RA Holmberg E., Van den Bergh P., Lapunzina P., Waddell L.B., Sloboda D.D., RA Bertini E., Chitayat D., Telfer W.R., Laquerriere A., Gregorio C.C., RA Ottenheijm C.A., Boennemann C.G., Pelin K., Beggs A.H., Hayashi Y.K., RA Romero N.B., Laing N.G., Nishino I., Wallgren-Pettersson C., Melki J., RA Fowler V.M., MacArthur D.G., North K.N., Clarke N.F.; RT "Leiomodin-3 dysfunction results in thin filament disorganization and RT nemaline myopathy."; RL J. Clin. Invest. 124:4693-4708(2014). RN [6] RP SUBCELLULAR LOCATION, AND ACTIN-BINDING. RX PubMed=20685966; DOI=10.1091/mbc.e10-02-0109; RA Skwarek-Maruszewska A., Boczkowska M., Zajac A.L., Kremneva E., RA Svitkina T., Dominguez R., Lappalainen P.; RT "Different localizations and cellular behaviors of leiomodin and RT tropomodulin in mature cardiomyocyte sarcomeres."; RL Mol. Biol. Cell 21:3352-3361(2010). RN [7] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=26370058; DOI=10.1038/ncomms9314; RA Boczkowska M., Rebowski G., Kremneva E., Lappalainen P., Dominguez R.; RT "How Leiomodin and Tropomodulin use a common fold for different actin RT assembly functions."; RL Nat. Commun. 6:8314-8314(2015). RN [8] RP INTERACTION WITH TPM1. RX PubMed=26873245; DOI=10.1016/j.bbapap.2016.02.009; RA Colpan M., Tolkatchev D., Grover S., Helms G.L., Cort J.R., Moroz N., RA Kostyukova A.S.; RT "Localization of the binding interface between leiomodin-2 and alpha- RT tropomyosin."; RL Biochim. Biophys. Acta 1864:523-530(2016). RN [9] {ECO:0007744|PDB:4RWT} RP X-RAY CRYSTALLOGRAPHY (2.98 ANGSTROMS) OF 1-547 IN COMPLEX WITH ACTIN, RP FUNCTION, ACTIN-BINDING, SUBUNIT, AND MUTAGENESIS OF PHE-64; LEU-69; RP 72-TYR-TRP-73; GLY-284; HIS-304; HIS-334; ARG-356; 525-LEU--ILE-529 AND RP 537-LEU--VAL-540. RX PubMed=26417072; DOI=10.1073/pnas.1512464112; RA Chen X., Ni F., Kondrashkina E., Ma J., Wang Q.; RT "Mechanisms of leiomodin 2-mediated regulation of actin filament in muscle RT cells."; RL Proc. Natl. Acad. Sci. U.S.A. 112:12687-12692(2015). CC -!- FUNCTION: Mediates nucleation of actin filaments and thereby promotes CC actin polymerization (PubMed:18403713, PubMed:26370058, CC PubMed:25250574, PubMed:26417072). Plays a role in the regulation of CC actin filament length (By similarity). Required for normal sarcomere CC organization in the heart, and for normal heart function CC (PubMed:18403713). {ECO:0000250|UniProtKB:Q3UHZ5, CC ECO:0000269|PubMed:18403713, ECO:0000269|PubMed:25250574, CC ECO:0000269|PubMed:26370058, ECO:0000269|PubMed:26417072}. CC -!- SUBUNIT: Can bind at least three actin monomers and thereby provides a CC nucleus for actin filament formation (PubMed:18403713, CC PubMed:26417072). Interacts (via N-terminus) with tropomyosin alpha CC (TPM1) (via N-terminus) (PubMed:25250574, PubMed:26873245). May also CC interact with TPM2 (via N-terminus) (PubMed:25250574). CC {ECO:0000269|PubMed:18403713, ECO:0000269|PubMed:25250574, CC ECO:0000269|PubMed:26417072, ECO:0000269|PubMed:26873245}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere CC {ECO:0000269|PubMed:18403713, ECO:0000269|PubMed:20685966, CC ECO:0000269|PubMed:26370058}. Cytoplasm, myofibril CC {ECO:0000269|PubMed:20685966}. Cytoplasm, myofibril, sarcomere, M line CC {ECO:0000269|PubMed:18403713, ECO:0000269|PubMed:20685966}. Cytoplasm, CC cytoskeleton {ECO:0000269|PubMed:26370058}. Note=Colocalizes with actin CC filaments in sarcomeres. Detected close to the M line. CC {ECO:0000269|PubMed:18403713, ECO:0000269|PubMed:20685966, CC ECO:0000269|PubMed:26370058}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q6P5Q4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q6P5Q4-2; Sequence=VSP_029526, VSP_029528; CC Name=3; CC IsoId=Q6P5Q4-3; Sequence=VSP_029525, VSP_029527; CC -!- TISSUE SPECIFICITY: Specifically expressed in heart and skeletal CC muscles, with higher levels in heart (at protein level). Not expressed CC in other tissues. {ECO:0000269|PubMed:11318603, CC ECO:0000269|PubMed:25250574}. CC -!- SIMILARITY: Belongs to the tropomodulin family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH17911.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAH62765.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAH62765.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=EAL24334.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=EAL24335.1; Type=Erroneous gene model prediction; Evidence={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; CH236947; EAL24334.1; ALT_SEQ; Genomic_DNA. DR EMBL; CH236947; EAL24335.1; ALT_SEQ; Genomic_DNA. DR EMBL; BC017911; AAH17911.1; ALT_INIT; mRNA. DR EMBL; BC062765; AAH62765.1; ALT_SEQ; mRNA. DR CCDS; CCDS47693.1; -. [Q6P5Q4-1] DR RefSeq; NP_997046.1; NM_207163.2. [Q6P5Q4-1] DR PDB; 4RWT; X-ray; 2.98 A; C/D=1-547. DR PDB; 5WFN; X-ray; 3.00 A; C/D=1-547. DR PDB; 6UT2; NMR; -; A=2-41. DR PDBsum; 4RWT; -. DR PDBsum; 5WFN; -. DR PDBsum; 6UT2; -. DR AlphaFoldDB; Q6P5Q4; -. DR SMR; Q6P5Q4; -. DR BioGRID; 138540; 2. DR IntAct; Q6P5Q4; 1. DR MINT; Q6P5Q4; -. DR STRING; 9606.ENSP00000411932; -. DR GlyGen; Q6P5Q4; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q6P5Q4; -. DR PhosphoSitePlus; Q6P5Q4; -. DR BioMuta; LMOD2; -. DR DMDM; 160395556; -. DR EPD; Q6P5Q4; -. DR jPOST; Q6P5Q4; -. DR MassIVE; Q6P5Q4; -. DR PaxDb; Q6P5Q4; -. DR PeptideAtlas; Q6P5Q4; -. DR PRIDE; Q6P5Q4; -. DR ProteomicsDB; 66999; -. [Q6P5Q4-1] DR ProteomicsDB; 67000; -. [Q6P5Q4-2] DR ProteomicsDB; 67001; -. [Q6P5Q4-3] DR Antibodypedia; 55328; 64 antibodies from 13 providers. DR Ensembl; ENST00000458573.3; ENSP00000411932.2; ENSG00000170807.12. [Q6P5Q4-1] DR GeneID; 442721; -. DR KEGG; hsa:442721; -. DR MANE-Select; ENST00000458573.3; ENSP00000411932.2; NM_207163.3; NP_997046.1. DR UCSC; uc003vky.3; human. [Q6P5Q4-1] DR CTD; 442721; -. DR DisGeNET; 442721; -. DR GeneCards; LMOD2; -. DR HGNC; HGNC:6648; LMOD2. DR HPA; ENSG00000170807; Group enriched (heart muscle, skeletal muscle, tongue). DR MalaCards; LMOD2; -. DR MIM; 608006; gene. DR neXtProt; NX_Q6P5Q4; -. DR OpenTargets; ENSG00000170807; -. DR PharmGKB; PA30414; -. DR VEuPathDB; HostDB:ENSG00000170807; -. DR eggNOG; KOG3735; Eukaryota. DR GeneTree; ENSGT00940000156567; -. DR HOGENOM; CLU_031052_4_0_1; -. DR InParanoid; Q6P5Q4; -. DR OMA; EECFTES; -. DR OrthoDB; 1025132at2759; -. DR PhylomeDB; Q6P5Q4; -. DR TreeFam; TF315841; -. DR PathwayCommons; Q6P5Q4; -. DR SignaLink; Q6P5Q4; -. DR BioGRID-ORCS; 442721; 15 hits in 1071 CRISPR screens. DR ChiTaRS; LMOD2; human. DR GenomeRNAi; 442721; -. DR Pharos; Q6P5Q4; Tbio. DR PRO; PR:Q6P5Q4; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; Q6P5Q4; protein. DR Bgee; ENSG00000170807; Expressed in left ventricle myocardium and 99 other tissues. DR ExpressionAtlas; Q6P5Q4; baseline and differential. DR Genevisible; Q6P5Q4; HS. DR GO; GO:0005884; C:actin filament; IDA:UniProtKB. DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central. DR GO; GO:0031430; C:M band; IEA:UniProtKB-SubCell. DR GO; GO:0030016; C:myofibril; IDA:UniProtKB. DR GO; GO:0030017; C:sarcomere; IDA:UniProtKB. DR GO; GO:0005865; C:striated muscle thin filament; IBA:GO_Central. DR GO; GO:0003779; F:actin binding; IDA:UniProtKB. DR GO; GO:0003785; F:actin monomer binding; IMP:UniProtKB. DR GO; GO:0005523; F:tropomyosin binding; IMP:UniProtKB. DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central. DR GO; GO:0030041; P:actin filament polymerization; IEA:Ensembl. DR GO; GO:0045010; P:actin nucleation; IDA:UniProtKB. DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central. DR GO; GO:0030239; P:myofibril assembly; IBA:GO_Central. DR GO; GO:0051694; P:pointed-end actin filament capping; IEA:InterPro. DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IDA:UniProtKB. DR GO; GO:0045214; P:sarcomere organization; IMP:UniProtKB. DR Gene3D; 3.80.10.10; -; 2. DR InterPro; IPR030132; LMOD2. DR InterPro; IPR032675; LRR_dom_sf. DR InterPro; IPR004934; TMOD. DR InterPro; IPR003124; WH2_dom. DR PANTHER; PTHR10901; PTHR10901; 1. DR PANTHER; PTHR10901:SF12; PTHR10901:SF12; 1. DR Pfam; PF03250; Tropomodulin; 1. DR PROSITE; PS51082; WH2; 1. PE 1: Evidence at protein level; KW 3D-structure; Actin-binding; Alternative splicing; Coiled coil; Cytoplasm; KW Cytoskeleton; Phosphoprotein; Reference proteome. FT CHAIN 1..547 FT /note="Leiomodin-2" FT /id="PRO_0000311340" FT DOMAIN 521..540 FT /note="WH2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406" FT REGION 1..161 FT /note="Interaction with actin 1" FT /evidence="ECO:0000269|PubMed:26417072" FT REGION 1..47 FT /note="Interaction with tropomyosin alpha" FT /evidence="ECO:0000269|PubMed:25250574" FT REGION 91..162 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 162..497 FT /note="Interaction with actin 2" FT /evidence="ECO:0000269|PubMed:26417072" FT REGION 352..533 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 521..540 FT /note="Interaction with actin 3" FT /evidence="ECO:0000269|PubMed:26417072" FT COILED 16..41 FT /evidence="ECO:0000255" FT COILED 113..148 FT /evidence="ECO:0000255" FT COMPBIAS 99..138 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 145..162 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 379..395 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 416..452 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 461..475 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 499..513 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 11 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q3UHZ5" FT MOD_RES 15 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q3UHZ5" FT MOD_RES 24 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:A1A5Q0" FT MOD_RES 400 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:A1A5Q0" FT VAR_SEQ 78..129 FT /note="QKLLEKERLGECGKVAEDKEESEEELIFTESNSEVSEEVYTEEEEEESQEEE FT -> LLLLPLLHSQRKSSLPETLQKSSNNRRVPNGHYKMDKKRKKGKRSRNSQTVF (in FT isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_029525" FT VAR_SEQ 110..138 FT /note="SEVSEEVYTEEEEEESQEEEEEEDSDEEE -> RRSPRRKRRKKTVTKRKEQ FT LKLQKGLMEL (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_029526" FT VAR_SEQ 130..547 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_029527" FT VAR_SEQ 139..547 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_029528" FT MUTAGEN 64 FT /note="F->D: Mildly impaired activity in promoting actin FT polymerization; when associated with D-69." FT /evidence="ECO:0000269|PubMed:26417072" FT MUTAGEN 69 FT /note="L->D: Mildly impaired activity in promoting actin FT polymerization; when associated with D-64." FT /evidence="ECO:0000269|PubMed:26417072" FT MUTAGEN 72..73 FT /note="YW->DD: Mildly impaired activity in promoting actin FT polymerization." FT /evidence="ECO:0000269|PubMed:26417072" FT MUTAGEN 284 FT /note="G->R: Strongly impaired activity in promoting actin FT polymerization." FT /evidence="ECO:0000269|PubMed:26417072" FT MUTAGEN 304 FT /note="H->G: Strongly impaired activity in promoting actin FT polymerization; when associated with G-334 and A-356." FT /evidence="ECO:0000269|PubMed:26417072" FT MUTAGEN 334 FT /note="H->G: Strongly impaired activity in promoting actin FT polymerization; when associated with G-304 and A-356." FT /evidence="ECO:0000269|PubMed:26417072" FT MUTAGEN 356 FT /note="R->A: Strongly impaired activity in promoting actin FT polymerization; when associated with G-304 and G-334." FT /evidence="ECO:0000269|PubMed:26417072" FT MUTAGEN 525..529 FT /note="LMEAI->AAEAA: Strongly impaired activity in FT promoting actin polymerization." FT /evidence="ECO:0000269|PubMed:26417072" FT MUTAGEN 537..540 FT /note="LKRV->AEEA: Strongly impaired activity in promoting FT actin polymerization." FT /evidence="ECO:0000269|PubMed:26417072" FT HELIX 3..6 FT /evidence="ECO:0007829|PDB:6UT2" FT TURN 7..9 FT /evidence="ECO:0007829|PDB:6UT2" FT TURN 12..15 FT /evidence="ECO:0007829|PDB:6UT2" FT HELIX 18..21 FT /evidence="ECO:0007829|PDB:6UT2" FT TURN 22..24 FT /evidence="ECO:0007829|PDB:6UT2" FT HELIX 27..40 FT /evidence="ECO:0007829|PDB:6UT2" FT HELIX 199..208 FT /evidence="ECO:0007829|PDB:4RWT" FT STRAND 215..217 FT /evidence="ECO:0007829|PDB:4RWT" FT HELIX 226..235 FT /evidence="ECO:0007829|PDB:4RWT" FT TURN 236..238 FT /evidence="ECO:0007829|PDB:4RWT" FT STRAND 243..250 FT /evidence="ECO:0007829|PDB:4RWT" FT HELIX 254..264 FT /evidence="ECO:0007829|PDB:4RWT" FT STRAND 272..278 FT /evidence="ECO:0007829|PDB:4RWT" FT HELIX 282..291 FT /evidence="ECO:0007829|PDB:4RWT" FT HELIX 292..294 FT /evidence="ECO:0007829|PDB:4RWT" FT STRAND 300..302 FT /evidence="ECO:0007829|PDB:4RWT" FT HELIX 313..321 FT /evidence="ECO:0007829|PDB:4RWT" FT HELIX 322..324 FT /evidence="ECO:0007829|PDB:4RWT" FT STRAND 330..332 FT /evidence="ECO:0007829|PDB:4RWT" FT HELIX 338..362 FT /evidence="ECO:0007829|PDB:4RWT" FT HELIX 460..468 FT /evidence="ECO:0007829|PDB:4RWT" FT HELIX 490..493 FT /evidence="ECO:0007829|PDB:4RWT" FT HELIX 495..497 FT /evidence="ECO:0007829|PDB:4RWT" FT STRAND 502..504 FT /evidence="ECO:0007829|PDB:4RWT" FT HELIX 520..530 FT /evidence="ECO:0007829|PDB:4RWT" FT HELIX 534..536 FT /evidence="ECO:0007829|PDB:4RWT" SQ SEQUENCE 547 AA; 61675 MW; 299A4C8F473E8A34 CRC64; MSTFGYRRGL SKYESIDEDE LLASLSAEEL KELERELEDI EPDRNLPVGL RQKSLTEKTP TGTFSREALM AYWEKESQKL LEKERLGECG KVAEDKEESE EELIFTESNS EVSEEVYTEE EEEESQEEEE EEDSDEEERT IETAKGINGT VNYDSVNSDN SKPKIFKSQI ENINLTNGSN GRNTESPAAI HPCGNPTVIE DALDKIKSND PDTTEVNLNN IENITTQTLT RFAEALKDNT VVKTFSLANT HADDSAAMAI AEMLKVNEHI TNVNVESNFI TGKGILAIMR ALQHNTVLTE LRFHNQRHIM GSQVEMEIVK LLKENTTLLR LGYHFELPGP RMSMTSILTR NMDKQRQKRL QEQKQQEGYD GGPNLRTKVW QRGTPSSSPY VSPRHSPWSS PKLPKKVQTV RSRPLSPVAT PPPPPPPPPP PPPSSQRLPP PPPPPPPPLP EKKLITRNIA EVIKQQESAQ RALQNGQKKK KGKKVKKQPN SILKEIKNSL RSVQEKKMED SSRPSTPQRS AHENLMEAIR GSSIKQLKRV EVPEALR //