LOCUS NP_079350 4012 aa linear PRI 09-OCT-2024
DEFINITION extracellular matrix organizing protein FRAS1 isoform 1 precursor
[Homo sapiens].
ACCESSION NP_079350
VERSION NP_079350.5
DBSOURCE REFSEQ: accession NM_025074.7
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 4012)
AUTHORS Tang,Z.Y., Wang,X.M., Xu,C.W., Sun,Q.Q., Hua,Y.X., Zhou,Q.Y.,
Hu,H.Y., Liu,S.B., Guo,Y.J., Ao,L., Che,X., Zhang,X.C., Heger,M.,
Zheng,X., Liu,A.J., Wang,Q., Zhan,Z.J., Cheng,S.Q. and Pan,W.W.
TITLE DCAF13 promotes ovarian cancer progression by activating
FRAS1-mediated FAK signaling pathway
JOURNAL Cell Mol Life Sci 81 (1), 421 (2024)
PUBMED 39367995
REMARK GeneRIF: DCAF13 promotes ovarian cancer progression by activating
FRAS1-mediated FAK signaling pathway.
Publication Status: Online-Only
REFERENCE 2 (residues 1 to 4012)
AUTHORS Wang,V., Geybels,M.S., Jordahl,K.M., Gerke,T., Hamid,A.,
Penney,K.L., Markt,S.C., Freedman,M., Pomerantz,M., Lee,G.M.,
Rana,H., Bornigen,D., Rebbeck,T.R., Huttenhower,C., Eeles,R.A.,
Stanford,J.L., Consortium,P., Berndt,S.I., Claessens,F.,
Sorensen,K.D., Park,J.Y., Vega,A., Usmani,N., Mucci,L. and
Sweeney,C.J.
TITLE A polymorphism in the promoter of FRAS1 is a candidate SNP
associated with metastatic prostate cancer
JOURNAL Prostate 81 (10), 683-693 (2021)
PUBMED 33956343
REMARK GeneRIF: A polymorphism in the promoter of FRAS1 is a candidate SNP
associated with metastatic prostate cancer.
REFERENCE 3 (residues 1 to 4012)
AUTHORS Al-Hamed,M.H., Sayer,J.A., Alsahan,N., Tulbah,M., Kurdi,W.,
Ambusaidi,Q., Ali,W. and Imtiaz,F.
TITLE Novel loss of function variants in FRAS1 AND FREM2 underlie renal
agenesis in consanguineous families
JOURNAL J Nephrol 34 (3), 893-900 (2021)
PUBMED 32643034
REMARK GeneRIF: Novel loss of function variants in FRAS1 AND FREM2
underlie renal agenesis in consanguineous families.
REFERENCE 4 (residues 1 to 4012)
AUTHORS Umeda,S., Kanda,M., Miwa,T., Tanaka,H., Tanaka,C., Kobayashi,D.,
Hayashi,M., Yamada,S., Nakayama,G., Koike,M. and Kodera,Y.
TITLE Fraser extracellular matrix complex subunit 1 promotes liver
metastasis of gastric cancer
JOURNAL Int J Cancer 146 (10), 2865-2876 (2020)
PUBMED 31597194
REMARK GeneRIF: Fraser extracellular matrix complex subunit 1 promotes
liver metastasis of gastric cancer.
REFERENCE 5 (residues 1 to 4012)
AUTHORS Midro,A.T., Stasiewicz-Jarocka,B., Borys,J., Hubert,E.,
Skotnicka,B., Hassmann-Poznanska,E., Sierpinska,T., Panasiuk,B.,
Schanze,D. and Zenker,M.
TITLE Two unrelated families with variable expression of Fraser syndrome
due to the same pathogenic variant in the FRAS1 gene
JOURNAL Am J Med Genet A 182 (4), 773-779 (2020)
PUBMED 31999076
REMARK GeneRIF: Two unrelated families with variable expression of Fraser
syndrome due to the same pathogenic variant in the FRAS1 gene.
REFERENCE 6 (residues 1 to 4012)
AUTHORS Short,K., Wiradjaja,F. and Smyth,I.
TITLE Let's stick together: the role of the Fras1 and Frem proteins in
epidermal adhesion
JOURNAL IUBMB Life 59 (7), 427-435 (2007)
PUBMED 17654118
REMARK GeneRIF: In this review, recent studies support direct interactions
between Fras1 and Frem proteins and shed new light on their role in
the regulation of epidermal-basement membrane adhesion and
organogenesis during development.
Review article
REFERENCE 7 (residues 1 to 4012)
AUTHORS Vrontou,S., Petrou,P., Meyer,B.I., Galanopoulos,V.K., Imai,K.,
Yanagi,M., Chowdhury,K., Scambler,P.J. and Chalepakis,G.
TITLE Fras1 deficiency results in cryptophthalmos, renal agenesis and
blebbed phenotype in mice
JOURNAL Nat Genet 34 (2), 209-214 (2003)
PUBMED 12766770
REFERENCE 8 (residues 1 to 4012)
AUTHORS McGregor,L., Makela,V., Darling,S.M., Vrontou,S., Chalepakis,G.,
Roberts,C., Smart,N., Rutland,P., Prescott,N., Hopkins,J.,
Bentley,E., Shaw,A., Roberts,E., Mueller,R., Jadeja,S., Philip,N.,
Nelson,J., Francannet,C., Perez-Aytes,A., Megarbane,A., Kerr,B.,
Wainwright,B., Woolf,A.S., Winter,R.M. and Scambler,P.J.
TITLE Fraser syndrome and mouse blebbed phenotype caused by mutations in
FRAS1/Fras1 encoding a putative extracellular matrix protein
JOURNAL Nat Genet 34 (2), 203-208 (2003)
PUBMED 12766769
REMARK GeneRIF: Locus FS1 at chromosome 4q21 is associated with Fraser
syndrome. Mutation analysis identified five frameshift mutations in
FRAS1, which encodes one member of a family of novel proteins
related to an extracellular matrix (ECM) protein found in sea
urchin.
REFERENCE 9 (residues 1 to 4012)
AUTHORS Longoni,M., Pober,B.R. and High,F.A.
TITLE Congenital Diaphragmatic Hernia Overview
JOURNAL (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
Amemiya A (Eds.);
GENEREVIEWS(R);
(1993)
PUBMED 20301533
REFERENCE 10 (residues 1 to 4012)
AUTHORS Gattuso,J., Patton,M.A. and Baraitser,M.
TITLE The clinical spectrum of the Fraser syndrome: report of three new
cases and review
JOURNAL J Med Genet 24 (9), 549-555 (1987)
PUBMED 3118036
REMARK Review article
COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The
reference sequence was derived from AC093652.5, DA725113.1,
DA881824.1, BC131820.1, AC093886.2, AB040933.2, AC104808.4,
BX647949.1 and BX647420.1.
This sequence is a reference standard in the RefSeqGene project.
On Aug 18, 2009 this sequence version replaced NP_079350.4.
Summary: This gene encodes an extracellular matrix protein that
appears to function in the regulation of epidermal-basement
membrane adhesion and organogenesis during development. Mutations
in this gene cause Fraser syndrome, a multisystem malformation that
can include craniofacial, urogenital and respiratory system
abnormalities. Alternative splicing results in multiple transcript
variants. [provided by RefSeq, Oct 2009].
Transcript Variant: This variant (1) represents the longer
transcript and encodes the longer isoform (1).
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##
RNAseq introns :: single sample supports all introns SAMEA2142853,
SAMEA2144120 [ECO:0000348]
##Evidence-Data-END##
##RefSeq-Attributes-START##
inferred exon combination :: based on alignments, homology
MANE Ensembl match :: ENST00000512123.4/ ENSP00000422834.2
RefSeq Select criteria :: based on conservation, expression,
longest protein
##RefSeq-Attributes-END##
FEATURES Location/Qualifiers
source 1..4012
/organism="Homo sapiens"
/db_xref="taxon:9606"
/chromosome="4"
/map="4q21.21"
Protein 1..4012
/product="extracellular matrix organizing protein FRAS1
isoform 1 precursor"
/note="extracellular matrix protein FRAS1; Fraser syndrome
1; fraser syndrome 1 protein; extracellular matrix
organizing protein FRAS1"
/calculated_mol_wt=440898
sig_peptide 1..26
/inference="COORDINATES: ab initio prediction:SignalP:6.0"
/calculated_mol_wt=2759
mat_peptide 27..4012
/product="extracellular matrix organizing protein FRAS1
isoform 1"
/calculated_mol_wt=440898
Region 28..87
/region_name="VWC"
/note="von Willebrand factor (vWF) type C domain;
smart00214"
/db_xref="CDD:214564"
Region 95..152
/region_name="VWC"
/note="von Willebrand factor type C domain; pfam00093"
/db_xref="CDD:278520"
Region 159..216
/region_name="VWC"
/note="von Willebrand factor type C domain; pfam00093"
/db_xref="CDD:278520"
Region 221..278
/region_name="VWC"
/note="von Willebrand factor type C domain; pfam00093"
/db_xref="CDD:278520"
Region 285..342
/region_name="VWC"
/note="von Willebrand factor (vWF) type C domain;
smart00214"
/db_xref="CDD:214564"
Site 344
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:19690332; propagated from
UniProtKB/Swiss-Prot (Q86XX4.2)"
Site 361
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (Q86XX4.2)"
Region 367..416
/region_name="VWC"
/note="von Willebrand factor (vWF) type C domain;
smart00214"
/db_xref="CDD:214564"
Region 396..>673
/region_name="VSP"
/note="Giardia variant-specific surface protein;
pfam03302"
/db_xref="CDD:146106"
Region 409..460
/region_name="FU 1"
/note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
Region 462..505
/region_name="FU 2"
/note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
Region 507..553
/region_name="FU 3"
/note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
Region 555..599
/region_name="FU 4"
/note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
Region 602..647
/region_name="FU 5"
/note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
Region 649..705
/region_name="FU 6"
/note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
Region 691..1060
/region_name="VSP"
/note="Giardia variant-specific surface protein;
pfam03302"
/db_xref="CDD:146106"
Region 708..753
/region_name="FU 7"
/note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
Site 728
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (Q86XX4.2)"
Region 755..800
/region_name="FU 8"
/note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
Region 803..852
/region_name="FU 9"
/note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
Region 854..900
/region_name="FU 10"
/note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
Region 903..948
/region_name="FU 11"
/note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
Region 952..997
/region_name="FU 12"
/note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
Region 999..1042
/region_name="FU 13"
/note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
Region 1046..1089
/region_name="FU 14"
/note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
Region 1046..1087
/region_name="FU"
/note="Furin-like repeats; smart00261"
/db_xref="CDD:214589"
Site 1093
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (Q86XX4.2)"
Region 1102..1198
/region_name="Cadherin_3"
/note="Cadherin-like; pfam16184"
/db_xref="CDD:465048"
Region 1102..1197
/region_name="CSPG 1.
/evidence=ECO:0000255|PROSITE-ProRule:PRU01201"
/note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
Site 1108
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (Q86XX4.2)"
Region 1203..1310
/region_name="Cadherin_3"
/note="Cadherin-like; pfam16184"
/db_xref="CDD:465048"
Region 1217..1308
/region_name="CSPG 2.
/evidence=ECO:0000255|PROSITE-ProRule:PRU01201"
/note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
Region 1314..1438
/region_name="Cadherin_3"
/note="Cadherin-like; pfam16184"
/db_xref="CDD:465048"
Region 1329..1438
/region_name="CSPG 3.
/evidence=ECO:0000255|PROSITE-ProRule:PRU01201"
/note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
Region 1446..1574
/region_name="Cadherin_3"
/note="Cadherin-like; pfam16184"
/db_xref="CDD:465048"
Region 1463..1559
/region_name="CSPG 4.
/evidence=ECO:0000255|PROSITE-ProRule:PRU01201"
/note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
Site 1504
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (Q86XX4.2)"
Region 1577..1691
/region_name="Cadherin_3"
/note="Cadherin-like; pfam16184"
/db_xref="CDD:465048"
Region 1595..1689
/region_name="CSPG 5.
/evidence=ECO:0000255|PROSITE-ProRule:PRU01201"
/note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
Region 1699..1811
/region_name="Cadherin_3"
/note="Cadherin-like; pfam16184"
/db_xref="CDD:465048"
Region 1710..1810
/region_name="CSPG 6.
/evidence=ECO:0000255|PROSITE-ProRule:PRU01201"
/note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
Site 1777
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (Q86XX4.2)"
Region 1816..1938
/region_name="Cadherin_3"
/note="Cadherin-like; pfam16184"
/db_xref="CDD:465048"
Region 1833..1936
/region_name="CSPG 7.
/evidence=ECO:0000255|PROSITE-ProRule:PRU01201"
/note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
Region 1941..2059
/region_name="Cadherin_3"
/note="Cadherin-like; pfam16184"
/db_xref="CDD:465048"
Site 1948
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (Q86XX4.2)"
Region 1957..2057
/region_name="CSPG 8.
/evidence=ECO:0000255|PROSITE-ProRule:PRU01201"
/note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
Site 1978
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (Q86XX4.2)"
Region 2073..2179
/region_name="Cadherin_3"
/note="Cadherin-like; pfam16184"
/db_xref="CDD:465048"
Region 2078..2177
/region_name="CSPG 9.
/evidence=ECO:0000255|PROSITE-ProRule:PRU01201"
/note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
Region 2183..2293
/region_name="Cadherin_3"
/note="Cadherin-like; pfam16184"
/db_xref="CDD:465048"
Region 2199..2291
/region_name="CSPG 10.
/evidence=ECO:0000255|PROSITE-ProRule:PRU01201"
/note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
Region 2297..2406
/region_name="Cadherin_3"
/note="Cadherin-like; pfam16184"
/db_xref="CDD:465048"
Region 2311..2404
/region_name="CSPG 11.
/evidence=ECO:0000255|PROSITE-ProRule:PRU01201"
/note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
Region 2425..2537
/region_name="Cadherin_3"
/note="Cadherin-like; pfam16184"
/db_xref="CDD:465048"
Region 2439..2536
/region_name="CSPG 12.
/evidence=ECO:0000255|PROSITE-ProRule:PRU01201"
/note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
Region <2553..>2803
/region_name="caca"
/note="sodium/calcium exchanger 1; TIGR00845"
/db_xref="CDD:273296"
Region 2555..2650
/region_name="Calx_beta"
/note="Domains in Na-Ca exchangers and integrin-beta4;
smart00237"
/db_xref="CDD:197594"
Site 2563
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (Q86XX4.2)"
Site 2668
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (Q86XX4.2)"
Site 2686
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (Q86XX4.2)"
Region 2798..2894
/region_name="Calx-beta"
/note="Calx-beta domain; cl02522"
/db_xref="CDD:413355"
Region <2907..>3134
/region_name="caca"
/note="sodium/calcium exchanger 1; TIGR00845"
/db_xref="CDD:273296"
Site 2912
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (Q86XX4.2)"
Site 2989
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (Q86XX4.2)"
Site 3074
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (Q86XX4.2)"
Site 3222
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (Q86XX4.2)"
Site 3680
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (Q86XX4.2)"
Site 3879
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (Q86XX4.2)"
Site 3906..3926
/site_type="transmembrane region"
/note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
CDS 1..4012
/gene="FRAS1"
/gene_synonym="FRASRS1"
/coded_by="NM_025074.7:688..12726"
/note="isoform 1 precursor is encoded by transcript
variant 1"
/db_xref="CCDS:CCDS54771.1"
/db_xref="GeneID:80144"
/db_xref="HGNC:HGNC:19185"
/db_xref="MIM:607830"
ORIGIN
1 mgvlkvwlgl alalaefavl phhsegacvy qdslladati wkpdscqscr chgdivickp
61 avcrnpqcaf ekgevlqiaa nqccpecvlr tpgschhekk ihehgtewas spcsvcscnh
121 gevrctpqpc pplscghqel afipegsccp vcvglgkpcs yeghvfqdge dwrlsrcakc
181 lcrngvaqcf taqcqplfcn qdetvvrvpg kccpqcsars csaagqvyeh geqwsenact
241 tcicdrgevr chkqaclplr cgkgqsrarr hgqcceecvs pagscsydgv vryqdemwkg
301 sacefcmcdh gqvtcqtgec akvecardee lihldgkccp ecisrngycv yeetgefmss
361 nasevkripe gekwedgpck vcecrgaqvt cyepscppcp vgtlalevkg qccpdctsvh
421 chpdcltcsq spdhcdlcqd ptkllqngwc vhscglgfyq agslclacqp qcstctsgle
481 csscqppllm rhgqcvptcg dgfyqdrhsc avchescagc wgptekhcla crdplhvlrd
541 ggcesscgkg fynrqgtcsa cdqscdscgp ssprcltcte ktvlhdgkcm secpggyyad
601 atgrckvchn scascsgptp shctacsppk alrqghclpr cgegfysdhg vckachsscl
661 acmgpapshc tgckkpeegl qveqlsdvgi psgeclaqcr ahfylestgi ceachqscfr
721 cagksphnct dcgpshvlld gqclsqcpdg yfhqegscte chptcrqchg plesdciscy
781 phisltngnc rtscreeqfl nlvgycadch hlcqhcaadl hntgsiclrc qnahylllgd
841 hcvpdcpsgy yaergackkc hsscrtcqgr gpfscsscdt nlvlshtgtc sttcfpghyl
901 ddnhvcqpcn thcgscdsqa sctscrdpnk vllfgecqye scapqyyldf stntckecdw
961 scsacsgplk tdclqcmdgy vlqdgacveq clssfyqdsg lckncdsycl qcqgphectr
1021 ckgpflllea qcvqecgkgy fadhakhkct acpqgclqcs hrdrchlcdh gfflksglcv
1081 yncvpgfsvh tsnetcsgki htpslhvngs lilpigsikp ldfsllnvqd qegrvedllf
1141 hvvstptngq lvlsrngkev qldkagrfsw kdvnekkvrf vhskeklrkg ylflkisdqq
1201 ffsepqlini qafstqapyv lrnevlhisr geratittqm ldirdddnpq dvvieiidpp
1261 lhgqllqtlq spatpiyqfq ldelsrgllh yahdgsdsts dvavlqandg hsfhnilfqv
1321 ktvpqndrgl qlvansmvwv peggmlqitn rilqaeapga saeeiiykit qdypqfgevv
1381 llvnmpadsp adegqhlpdg rtatptstft qqdinegivw yrhsgapaqs dsfrfevssa
1441 snaqtrlesh mfniailpqt peapkvslea slhmtaredg ltviqphsls finsekpsgk
1501 ivynitlplh pnqgiiehrd hphspiryft qedinqgkvm yrpppaaphl qelmafsfag
1561 lpesvkfhft vsdgehtspe mvltihllps dqqlpvfqvt aprlavspgg stsvglqvvv
1621 rdaetapkel ffelrrppqh gvllkhtaef rrpmatgdtf tyedveknal qyihdgsstr
1681 edsmeisvtd gltvtmlevr vevslsedrg prlaagssls itvaskstai itrshlayvd
1741 dsspdpeiwi qlnylpsygt llrisgseve elsevsnftm edinnkkiry savfetdghl
1801 vtdsfyfsvs dmdhnhldnq iftimitpae npppviafad litvdeggra plsfhhffat
1861 ddddnlqrda iiklsalpky gcientgtgd rfgpetasdl easfpiqdvl enyiyyfqsv
1921 hesiepthdi fsfyvsdgts rseihsinit ierkndeppr mtlqplrvql ssgvvisnss
1981 lslqdldtpd nelifvltkk pdhghvlwrq taseplengr vlvqgstfty qdilaglvgy
2041 vpsvpgmvvd efqfsltdgl hvdtgrmkiy telpasdtph lainqglqls agsvariteq
2101 hlkvtdidsd dhqvmyimke dpgagrlqmm khgnleqisi kgpirsftqa disqghveys
2161 hgtgepggsf afkfdvvdge gnrlidksfs isiledkspp vittnkglvl densvkkitt
2221 lqlsatdqds gpteliyrit rqpqlghleh aaspgiqiss ftqadltsrn vqyvhsseae
2281 khsdafsftl sdgvsevtqt fhitlhpvdd slpvvqnlgm rvqegmrkti tefelkavda
2341 dteaesvtft ivqpprhgti ertsngqhfh ltstftmkdi yqnrvsyshd gsnslkdrft
2401 ftvsdgtnpf fiieeggkei mtaapqpfrv dilpvddgtp rivtnlglqw leymdgkatn
2461 litkkelltm dpdtedaqlv yeittgpkhg fvenklqpgr aaatftqedv nlgliryvlh
2521 kekiremmds fqflvkdskp nvvsdnvfhi qwslisfkyt synvsekags vsvtvqrtgn
2581 lnqyaivlcr teqgtassss rvssqpgqqd yveyagqvqf deredtksct ivindddvfe
2641 nvesftvels mpayallgef tqakviindt edeptlefdk kiywvnesag flfapierkg
2701 dassivsaic ytvpksamgs slyalesgsd fksrgmsaas rvifgpgvtm stcdvmlidd
2761 seyeeeeefe ialadasdna rigrvatakv lisgpndast vslgntaftv sedagtvkip
2821 virhgtdlst fasvwcatrp sdpasatpgv dyvpssrkve fgpgvieqyc tltilddtqy
2881 pviegletfv vflssaqgae ltkpfqavia indtfqdvps mqfakdlllv kekegvlhvp
2941 itrsgdlsye ssvrcytqsh saqvmedfee rqnadssrit flkgdkvknc tvyihddsmf
3001 epeeqfrvyl glplgnhwsg arigknnmat itisndedap tiefeeaayq vrepagpdai
3061 ailnikvirr gdqnrtskvr cstrdgsaqs gvdyypksrv lkfspgvdhi ffkveilsne
3121 drewhesfsl vlgpddpvea vlgdvttatv tildqeaags lilpappivv tladydhvee
3181 vtkegvkksp spgyplvcvt pcdphfprya vmkercseag inqtsvqfsw evaaptdgng
3241 arspfetitd ntpftsvnhm vldsiyfsrr fhvrcvakav dkvghvgtpl rsnivtigtd
3301 saichtpvva gtsrgfqaqs fiatlkyldv khkehpnrih isvqiphqdg mlplistmpl
3361 hnlhfllses iyrhqhvcsn lvttydlrgi seagflddvv ydstalgpgy drpfqfdpsv
3421 repktiqlyk hlnlkscvwt fdayydmtel idvcggsvta dfqvrdsaqs fltvhvplyv
3481 syiyvtaprg waslehhtem efsffydtvl wrtgiqtdsv lsarlqiiri yiredgrlvi
3541 efkthakfrg qfvmehhtlp evksfvltpd hlggiefdlq llwsaqtfds phqlwratss
3601 ynrkdysgey tiylipctvq ptqpwvdpge kplactahap erflipiafq qtnrpvpvvy
3661 slntefqlcn nekvflmdpn tsdmslaemd ykgafskgqi lygrvlwnpe qnlnsayklq
3721 lekvylctgk dgyvpffdpt gtiynegpqy gciqpnkhlk hrfllldrnq pevtdkyfhd
3781 vpfeahfase lpdfhvvsnm pgvdgftlkv dalykveagh qwylqviyii gpdtisgprv
3841 qrsltaplrr nrrdlvepdg qlilddsliy dnegdqvkng tnmkslnlem qelavaasls
3901 qtgasigsal aaimllllvf lvacfinrkc qkqrkkkpae dileeyplnt kvevpkrhpd
3961 rveknvnrhy ctvrnvnils epeaaytfkg akvkrlnlev rvhnnlqdgt ev
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