LOCUS       NP_510880               2054 aa            linear   PRI 29-APR-2025
DEFINITION  unconventional myosin-XVIIIa isoform a [Homo sapiens].
ACCESSION   NP_510880
VERSION     NP_510880.2
DBSOURCE    REFSEQ: accession NM_078471.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2054)
  AUTHORS   Yau,E., Yang,L., Chen,Y., Umstead,T.M., Stanley,A.E.,
            Halstead,E.S., Gandhi,C.K., Yewdell,J.W. and Chroneos,Z.C.
  TITLE     SP-R210 isoforms of Myosin18A modulate endosomal sorting and
            recognition of influenza A virus infection in macrophages
  JOURNAL   Microbes Infect 26 (3), 105280 (2024)
   PUBMED   38135024
  REMARK    GeneRIF: SP-R210 isoforms of Myosin18A modulate endosomal sorting
            and recognition of influenza A virus infection in macrophages.
REFERENCE   2  (residues 1 to 2054)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 2054)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 2054)
  AUTHORS   Buschman,M.D. and Field,S.J.
  TITLE     MYO18A: An unusual myosin
  JOURNAL   Adv Biol Regul 67, 84-92 (2018)
   PUBMED   28942352
  REMARK    GeneRIF: a high proportion of MYO18A is found in complex with
            GOLPH3 at the trans Golgi, where it functions to promote vesicle
            budding for Golgi-to-plasma membrane trafficking.
            Review article
REFERENCE   5  (residues 1 to 2054)
  AUTHORS   Xing,M., Peterman,M.C., Davis,R.L., Oegema,K., Shiau,A.K. and
            Field,S.J.
  TITLE     GOLPH3 drives cell migration by promoting Golgi reorientation and
            directional trafficking to the leading edge
  JOURNAL   Mol Biol Cell 27 (24), 3828-3840 (2016)
   PUBMED   27708138
REFERENCE   6  (residues 1 to 2054)
  AUTHORS   Brajenovic,M., Joberty,G., Kuster,B., Bouwmeester,T. and Drewes,G.
  TITLE     Comprehensive proteomic analysis of human Par protein complexes
            reveals an interconnected protein network
  JOURNAL   J Biol Chem 279 (13), 12804-12811 (2004)
   PUBMED   14676191
REFERENCE   7  (residues 1 to 2054)
  AUTHORS   Schultz,L., Khera,S., Sleve,D., Heath,J. and Chang,N.S.
  TITLE     TIAF1 and p53 functionally interact in mediating apoptosis and
            silencing of TIAF1 abolishes nuclear translocation of serine
            15-phosphorylated p53
  JOURNAL   DNA Cell Biol 23 (1), 67-74 (2004)
   PUBMED   14965474
  REMARK    GeneRIF: TIAF1 and p53 functionally interact in regulating
            apoptosis, and TIAF1 is likely to participate in the nuclear
            translocation of activated p53.
REFERENCE   8  (residues 1 to 2054)
  AUTHORS   van der Leij,J., van den Berg,A., Albrecht,E.W., Blokzijl,T.,
            Roozendaal,R., Gouw,A.S., de Jong,K.P., Stegeman,C.A., van Goor,H.,
            Chang,N.S. and Poppema,S.
  TITLE     High expression of TIAF-1 in chronic kidney and liver allograft
            rejection and in activated T-helper cells
  JOURNAL   Transplantation 75 (12), 2076-2082 (2003)
   PUBMED   12829915
  REMARK    GeneRIF: Expression of TIAF-1 in the lymphocytes during chronic
            allograft rejection may be related to the predominance of a Th2
            response in this condition and may protect these cells from
            apoptosis
REFERENCE   9  (residues 1 to 2054)
  AUTHORS   Mori,K., Furusawa,T., Okubo,T., Inoue,T., Ikawa,S., Yanai,N.,
            Mori,K.J. and Obinata,M.
  TITLE     Genome structure and differential expression of two isoforms of a
            novel PDZ-containing myosin (MysPDZ) (Myo18A)
  JOURNAL   J Biochem 133 (4), 405-413 (2003)
   PUBMED   12761286
REFERENCE   10 (residues 1 to 2054)
  AUTHORS   Chroneos,Z.C., Abdolrasulnia,R., Whitsett,J.A., Rice,W.R. and
            Shepherd,V.L.
  TITLE     Purification of a cell-surface receptor for surfactant protein A
  JOURNAL   J Biol Chem 271 (27), 16375-16383 (1996)
   PUBMED   8663107
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005412.8, D86970.2,
            BM544214.1 and AC024619.16.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 19, 2003 this sequence version replaced NP_510880.1.
            
            Summary: The protein encoded by this gene can bind GOLPH3, linking
            the Golgi to the cytoskeleton and influencing Golgi membrane
            trafficking. The encoded protein is also part of a complex that
            assembles lamellar actomyosin bundles and may be required for cell
            migration. [provided by RefSeq, Oct 2016].
            
            Transcript Variant: This variant (1) contains an alternate in-frame
            exon and lacks two alternate in-frame exons compared to variant 3.
            The resulting isoform (a) has the same N- and C-termini but is
            shorter compared to isoform c.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D86970.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000527372.7/ ENSP00000437073.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2054
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..2054
                     /product="unconventional myosin-XVIIIa isoform a"
                     /note="myosin 18A; myosin containing PDZ domain; SP-A
                     receptor subunit SP-R210 alphaS; myosin containing a PDZ
                     domain; molecule associated with JAK3 N-terminus;
                     unconventional myosin-XVIIIa; surfactant protein receptor
                     SP-R210; TGFB1-induced anti-apoptotic factor 1;
                     TGF-beta-1-induced antiapoptotic factor 1; molecule
                     associated with Jak-3 N-terminal; 12 kDa
                     TGF-beta-1-induced antiapoptotic factor; Putative
                     TGFB1-induced anti-apoptotic factor 1"
                     /calculated_mol_wt=232985
     Region          1..398
                     /region_name="Mediates nucleotide-independent binding to
                     F-actin and interaction with GOLPH3.
                     /evidence=ECO:0000269|PubMed:23990465"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92614.3)"
     Region          1..34
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92614.3)"
     Site            35
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92614.3)"
     Site            52
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92614.3)"
     Site            72
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92614.3)"
     Site            74
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92614.3)"
     Site            79
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92614.3)"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92614.3)"
     Site            98
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92614.3)"
     Site            99
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92614.3)"
     Site            102
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JMH9; propagated from
                     UniProtKB/Swiss-Prot (Q92614.3)"
     Site            103
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92614.3)"
     Region          114..118
                     /region_name="Interaction with actin"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92614.3)"
     Region          140..167
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92614.3)"
     Site            140
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q92614.3)"
     Site            145
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92614.3)"
     Site            157
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JMH9; propagated from
                     UniProtKB/Swiss-Prot (Q92614.3)"
     Site            160
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JMH9; propagated from
                     UniProtKB/Swiss-Prot (Q92614.3)"
     Site            164
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92614.3)"
     Region          220..308
                     /region_name="PDZ_MYO18-like"
                     /note="PDZ domain of MYO18A protein, and related domains;
                     cd06747"
                     /db_xref="CDD:467229"
     Site            order(230..236,255,258,289,293,296..297)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467229"
     Site            234
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92614.3)"
     Region          318..338
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92614.3)"
     Region          381..1905
                     /region_name="COG5022"
                     /note="Myosin heavy chain [General function prediction
                     only]"
                     /db_xref="CDD:227355"
     Region          419..1173
                     /region_name="MYSc_Myo18"
                     /note="class XVIII myosin, motor domain; cd01386"
                     /db_xref="CDD:276837"
     Site            order(447,454,498..505,545..555,789..794)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:276837"
     Site            order(447,454)
                     /site_type="other"
                     /note="purine-binding loop"
                     /db_xref="CDD:276837"
     Site            498..505
                     /site_type="other"
                     /note="P-loop"
                     /db_xref="CDD:276837"
     Site            545..555
                     /site_type="other"
                     /note="switch I region"
                     /db_xref="CDD:276837"
     Site            789..794
                     /site_type="other"
                     /note="switch II region"
                     /db_xref="CDD:276837"
     Site            order(824..835,838..847)
                     /site_type="active"
                     /note="relay loop [active]"
                     /db_xref="CDD:276837"
     Site            987
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JMH9; propagated from
                     UniProtKB/Swiss-Prot (Q92614.3)"
     Site            1067
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92614.3)"
     Site            1068
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92614.3)"
     Site            1070
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92614.3)"
     Site            1100..1109
                     /site_type="other"
                     /note="SH1 helix"
                     /db_xref="CDD:276837"
     Site            order(1112..1130,1143..1173)
                     /site_type="other"
                     /note="converter subdomain"
                     /db_xref="CDD:276837"
     Region          1450..1480
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92614.3)"
     Site            1501
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92614.3)"
     Site            1640
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92614.3)"
     Region          1824..>1989
                     /region_name="PRK03918"
                     /note="DNA double-strand break repair ATPase Rad50"
                     /db_xref="CDD:235175"
     Site            1843
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92614.3)"
     Region          1852..1901
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92614.3)"
     Site            1922
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92614.3)"
     Site            1942
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92614.3)"
     Site            1959
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92614.3)"
     Region          1962..2054
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92614.3)"
     Site            1970
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q92614.3)"
     Site            1974
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q92614.3)"
     Site            1998
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92614.3)"
     Site            2002
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92614.3)"
     Site            2006
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92614.3)"
     Site            2007
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92614.3)"
     Site            2014
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92614.3)"
     Site            2020
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92614.3)"
     Site            2035
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92614.3)"
     Site            2036
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JMH9; propagated from
                     UniProtKB/Swiss-Prot (Q92614.3)"
     Site            2041
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92614.3)"
     Site            2043
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92614.3)"
     Site            2045
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92614.3)"
     CDS             1..2054
                     /gene="MYO18A"
                     /gene_synonym="MAJN; MYSPDZ; SP-R210; SPR210; TIAF1"
                     /coded_by="NM_078471.4:168..6332"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS45642.1"
                     /db_xref="GeneID:399687"
                     /db_xref="HGNC:HGNC:31104"
                     /db_xref="MIM:609517"
                     /db_xref="MIM:610067"
ORIGIN      
        1 mfnlmkkdkd kdggrkekke kkekkermsa aelrsleems lrrgffnlnr sskresktrl
       61 eisnpipikv asgsdlhltd idsdsnrgsv ildsghlsta sssddlkgee gsfrgsvlqr
      121 aakfgslakq nsqmivkrfs fsqrsrdesa setstpsehs aapspqvevr tlegqlvqhp
      181 gpgiprpghr srapelvtkk fpvdlrlppv vplppptlre lelqrrptgd fgfslrrttm
      241 ldrgpegqac rrvvhfaepg agtkdlalgl vpgdrlvein ghnvesksrd eivemirqsg
      301 dsvrlkvqpi pelselsrsw lrsgegprre psdakteeqi aaeeawnete kvwlvhrdgf
      361 slasqlksee lnlpegkvrv kldhdgaild vdeddvekan apscdrledl aslvylness
      421 vlhtlrqryg asllhtyagp sllvlgprga pavysekvmh mfkgcrredm aphiyavaqt
      481 ayramlmsrq dqsiillgss gsgkttscqh lvqylatiag isgnkvfsve kwqalytlle
      541 afgnsptiin gnatrfsqil sldfdqagqv asasiqtmll eklrvarrpa seatfnvfyy
      601 llacgdgtlr telhlnhlae nnvfgivpla kpeekqkaaq qfsklqaamk vlgispdeqk
      661 acwfilaaiy hlgaagatke aaeagrkqfa rhewaqkaay llgcsleels saifkhqhkg
      721 gtlqrstsfr qgpeesglgd gtgpklsale clegmaagly selftllvsl vnralkssqh
      781 slcsmmivdt pgfqnpeqgg sargasfeel chnytqdrlq rlfhertfvq elerykeeni
      841 elafddlepp tddsvaavdq ashqslvrsl artdeargll wlleeealvp gasedtller
      901 lfsyygpqeg dkkgqspllh sskphhfllg hshgtnwvey nvtgwlnytk qnpatqnapr
      961 llqdsqkkii snlflgrags atvlsgsiag leggsqlalr ratsmrktft tgmaavkkks
     1021 lciqmklqvd alidtikksk lhfvhcflpv aegwageprs assrrvssss eldlpsgdhc
     1081 eagllqldvp llrtqlrgsr lldamrmyrq gypdhmvfse frrrfdvlap hltkkhgrny
     1141 ivvderrave ellecldlek ssccmglsrv ffragtlarl eeqrdeqtsr nltlfqaacr
     1201 gylarqhfkk rkiqdlairc vqknikknkg vkdwpwwklf ttvrplievq lseeqirnkd
     1261 eeiqqlrskl ekaekernel rlnsdrlesr iseltseltd erntgesasq lldaetaerl
     1321 raekemkelq tqydalkkqm evmemevmea rliraaeing evddddagge wrlkyeravr
     1381 evdftkkrlq qefedkleve qqnkrqlerr lgdlqadsee sqralqqlkk kcqrltaelq
     1441 dtklhlegqq vrnhelekkq rrfdselsqa heeaqreklq reklqrekdm llaeafslkq
     1501 qleekdmdia gftqkvvsle aelqdissqe skdeaslakv kkqlrdleak vkdqeeelde
     1561 qagtiqmleq aklrlememe rmrqthskem esrdeeveea rqscqkklkq mevqleeeye
     1621 dkqkvlrekr elegklatls dqvnrrdfes ekrlrkdlkr tkalladaql mldhlknsap
     1681 skreiaqlkn qleeseftca aavkarkame veiedlhlqi ddiakaktal eeqlsrlqre
     1741 kneiqnrlee dqedmnelmk khkaavaqas rdlaqindlq aqleeankek qelqeklqal
     1801 qsqvefleqs mvdkslvsrq eakireletr lefertqvkr leslasrlke nmeklteerd
     1861 qriaaenrek eqnkrlqrql rdtkeemgel arkeaeasrk khelemdles leaanqslqa
     1921 dlklafkrig dlqaaiedem esdenedlin slqdmvtkyq krknklegds dvdseledrv
     1981 dgvkswlskn kgpskaasdd gslkssspts ywkslapdrs ddehdpldnt srpryshsyl
     2041 sdsdteaklt etna
//
