LMOD2_HUMAN
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 03-AUG-2022, entry version 129.
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};
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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 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
