LOCUS       NP_001365257            3019 aa            linear   PRI 30-APR-2025
DEFINITION  cadherin EGF LAG seven-pass G-type receptor 1 isoform 1 precursor
            [Homo sapiens].
ACCESSION   NP_001365257 XP_006724446
VERSION     NP_001365257.1
DBSOURCE    REFSEQ: accession NM_001378328.1
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 3019)
  AUTHORS   de Koning,M.A., Pimienta Ramirez,P.A., Haak,M.C., Han,X.,
            Ruiterkamp-Versteeg,M.H., de Leeuw,N., Schatz,U.A., Shoukier,M.,
            Rieger-Fackeldey,E., Ortiz,J.U., van Duinen,S.G., Klein,W.M.,
            Witlox,R.S.G.M., Finnell,R.H., Santen,G.W.E., Lei,Y. and Suerink,M.
  TITLE     De novo heterozygous missense variants in CELSR1 as cause of fetal
            pleural effusions and progressive fetal hydrops
  JOURNAL   J Med Genet 61 (6), 549-552 (2024)
   PUBMED   38272662
  REMARK    GeneRIF: De novo heterozygous missense variants in CELSR1 as cause
            of fetal pleural effusions and progressive fetal hydrops.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 3019)
  AUTHORS   Tamilselvan,E. and Sotomayor,M.
  TITLE     CELSR1, a core planar cell polarity protein, features a weakly
            adhesive and flexible cadherin ectodomain
  JOURNAL   Structure 32 (4), 476-491 (2024)
   PUBMED   38307021
  REMARK    GeneRIF: CELSR1, a core planar cell polarity protein, features a
            weakly adhesive and flexible cadherin ectodomain.
REFERENCE   3  (residues 1 to 3019)
  AUTHORS   Zuo,J., Zheng,A., Wang,X., Luo,Z., Chen,Y., Cheng,X., Zhao,Y.,
            Zhou,X., Tang,K.F. and Du,X.
  TITLE     Upregulation of CELSR1 expression promotes ovarian cancer cell
            proliferation, migration, and invasion
  JOURNAL   Med Oncol 41 (1), 10 (2023)
   PUBMED   38070011
  REMARK    GeneRIF: Upregulation of CELSR1 expression promotes ovarian cancer
            cell proliferation, migration, and invasion.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 3019)
  AUTHORS   Alpaslan,M., Mestre-Godin,S., Lay,A., Giacalone,G., Helaers,R.,
            Adham,S., Kovacsik,H., Guillemard,S., Mercier,E., Boon,L.,
            Revencu,N., Brouillard,P., Quere,I. and Vikkula,M.
  TITLE     Ureteropelvic junction obstruction with primary lymphoedema
            associated with CELSR1 variants
  JOURNAL   J Med Genet 60 (12), 1161-1168 (2023)
   PUBMED   37225411
  REMARK    GeneRIF: Ureteropelvic junction obstruction with primary
            lymphoedema associated with CELSR1 variants.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 3019)
  AUTHORS   Smith,M.S., Sarasua,S.M., Rogers,C., Phelan,K. and Boccuto,L.
  TITLE     Lymphedema is associated with CELSR1 in Phelan-McDermid syndrome
  JOURNAL   Clin Genet 104 (4), 472-478 (2023)
   PUBMED   37232218
  REMARK    GeneRIF: Lymphedema is associated with CELSR1 in Phelan-McDermid
            syndrome.
REFERENCE   6  (residues 1 to 3019)
  AUTHORS   Georgieva,L., Nikolov,I., Poriazova,N., Jones,G., Toncheva,D.,
            Kirov,G. and Owen,M.J.
  TITLE     Genetic variation in the seven-pass transmembrane cadherin CELSR1:
            lack of association with schizophrenia
  JOURNAL   Psychiatr Genet 13 (2), 103-106 (2003)
   PUBMED   12782967
  REMARK    GeneRIF: Variations in the nine ectodomains of CELSR1 do not
            increase susceptibility to schizophrenia.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 3019)
  AUTHORS   Gross,J., Grimm,O., Ortega,G., Teuber,I., Lesch,K.P. and Meyer,J.
  TITLE     Mutational analysis of the neuronal cadherin gene CELSR1 and
            exclusion as a candidate for catatonic schizophrenia in a large
            family
  JOURNAL   Psychiatr Genet 11 (4), 197-200 (2001)
   PUBMED   11807409
  REMARK    GeneRIF: exclusion as a candidate gene for schizophrenia-- a
            cadhrin gene
REFERENCE   8  (residues 1 to 3019)
  AUTHORS   Ghosh,A.
  TITLE     Dentritic growth: don't go says flamingo
  JOURNAL   Neuron 28 (1), 3-4 (2000)
   PUBMED   11086974
REFERENCE   9  (residues 1 to 3019)
  AUTHORS   Nollet,F., Kools,P. and van Roy,F.
  TITLE     Phylogenetic analysis of the cadherin superfamily allows
            identification of six major subfamilies besides several solitary
            members
  JOURNAL   J Mol Biol 299 (3), 551-572 (2000)
   PUBMED   10835267
  REMARK    Review article
REFERENCE   10 (residues 1 to 3019)
  AUTHORS   Hadjantonakis,A.K., Sheward,W.J., Harmar,A.J., de Galan,L.,
            Hoovers,J.M. and Little,P.F.
  TITLE     Celsr1, a neural-specific gene encoding an unusual seven-pass
            transmembrane receptor, maps to mouse chromosome 15 and human
            chromosome 22qter
  JOURNAL   Genomics 45 (1), 97-104 (1997)
   PUBMED   9339365
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL021392.5, AL031597.7 and
            AL031588.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 7, 2020 this sequence version replaced XP_006724446.1.
            
            Summary: The protein encoded by this gene is a member of the
            flamingo subfamily, part of the cadherin superfamily. The flamingo
            subfamily consists of nonclassic-type cadherins; a subpopulation
            that does not interact with catenins. The flamingo cadherins are
            located at the plasma membrane and have nine cadherin domains,
            seven epidermal growth factor-like repeats and two laminin A G-type
            repeats in their ectodomain. They also have seven transmembrane
            domains, a characteristic unique to this subfamily. It is
            postulated that these proteins are receptors involved in
            contact-mediated communication, with cadherin domains acting as
            homophilic binding regions and the EGF-like domains involved in
            cell adhesion and receptor-ligand interactions. This particular
            member is a developmentally regulated, neural-specific gene which
            plays an unspecified role in early embryogenesis. [provided by
            RefSeq, Jul 2008].
            
            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 :: SRR18074969.1537087.1,
                                           SRR14038194.2205577.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000674500.2/ ENSP00000501367.2
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..3019
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.31"
     Protein         1..3019
                     /product="cadherin EGF LAG seven-pass G-type receptor 1
                     isoform 1 precursor"
                     /note="protocadherin flamingo 2; cadherin, EGF LAG
                     seven-pass G-type receptor 1 (flamingo homolog,
                     Drosophila); adhesion G protein-coupled receptor C1;
                     flamingo homolog 2; cadherin family member 9"
                     /calculated_mol_wt=327577
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2392
     Region          205..242
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYQ6.1)"
     Region          250..349
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(256..257,312,314,345,347..348)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          357..455
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(364..365,416,418,451,453..454)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            403
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NYQ6.1)"
     Region          464..561
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(470..471,523,525,557,559..560)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            546
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NYQ6.1)"
     Region          569..683
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(576..577,646,648,679,681..682)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            634
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NYQ6.1)"
     Region          691..785
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(698..699,751,753,781,783..784)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            778
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NYQ6.1)"
     Region          793..888
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(800..801,851,853,884,886..887)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          897..995
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(903..904,957,959,991,993..994)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          1003..1097
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(1010..1011,1063,1065,1093,1095..1096)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            1114
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NYQ6.1)"
     Region          1117..1198
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            1139
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NYQ6.1)"
     Site            1213
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NYQ6.1)"
     Site            1249
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NYQ6.1)"
     Site            1259
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NYQ6.1)"
     Site            1287
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NYQ6.1)"
     Region          1364..1399
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          1407..1441
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          1444..1627
                     /region_name="LamG"
                     /note="Laminin G domain; Laminin G-like domains are
                     usually Ca++ mediated receptors that can have binding
                     sites for steroids, beta1 integrins, heparin, sulfatides,
                     fibulin-1, and alpha-dystroglycans. Proteins that contain
                     LamG domains serve a variety of...; cd00110"
                     /db_xref="CDD:238058"
     Site            1576
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NYQ6.1)"
     Site            1623
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NYQ6.1)"
     Site            1640
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NYQ6.1)"
     Region          1651..1685
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            1666
                     /site_type="hydroxylation"
                     /note="(3R)-3-hydroxyasparagine. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (Q9NYQ6.1)"
     Region          1719..1849
                     /region_name="Laminin_G_2"
                     /note="Laminin G domain; pfam02210"
                     /db_xref="CDD:460494"
     Region          1874..1908
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          1881..2011
                     /region_name="TNFRSF"
                     /note="Tumor necrosis factor receptor superfamily
                     (TNFRSF); cl22855"
                     /db_xref="CDD:473981"
     Site            1889
                     /site_type="hydroxylation"
                     /note="(3R)-3-hydroxyaspartate. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (Q9NYQ6.1)"
     Region          1898..1934
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276930"
     Site            1979
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NYQ6.1)"
     Region          2002..>2040
                     /region_name="EGF_Lam"
                     /note="Laminin-type epidermal growth factor-like domain;
                     laminins are the major noncollagenous components of
                     basement membranes that mediate cell adhesion, growth
                     migration, and differentiation; the laminin-type epidermal
                     growth factor-like module occurs in...; cd00055"
                     /db_xref="CDD:238012"
     Site            order(2003,2005,2015,2022,2024,2033)
                     /site_type="active"
                     /note="EGF-like motif [active]"
                     /db_xref="CDD:238012"
     Region          2052..2113
                     /region_name="HormR"
                     /note="Domain present in hormone receptors; smart00008"
                     /db_xref="CDD:214468"
     Site            2103
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NYQ6.1)"
     Site            2122
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NYQ6.1)"
     Region          2130..2381
                     /region_name="GAIN"
                     /note="GPCR-Autoproteolysis INducing (GAIN) domain;
                     pfam16489"
                     /db_xref="CDD:465137"
     Site            2257
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NYQ6.1)"
     Region          2291..2328
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYQ6.1)"
     Region          2407..2460
                     /region_name="GPS"
                     /note="G-protein-coupled receptor proteolytic site domain;
                     smart00303"
                     /db_xref="CDD:197639"
     Region          2411..2461
                     /region_name="GPS.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00098"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYQ6.1)"
     Site            2415
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NYQ6.1)"
     Site            2437
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NYQ6.1)"
     Region          2465..2718
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          2468..2492
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320657"
     Site            2470..2490
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYQ6.1)"
     Region          2501..2522
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320657"
     Site            2502..2522
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYQ6.1)"
     Site            2523
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NYQ6.1)"
     Site            2528..2548
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYQ6.1)"
     Region          2532..2554
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320657"
     Site            2573..2593
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYQ6.1)"
     Region          2573..2589
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320657"
     Region          2608..2631
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320657"
     Site            2612..2632
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYQ6.1)"
     Region          2654..2676
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320657"
     Site            2656..2676
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYQ6.1)"
     Region          2680..2705
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320657"
     Site            2684..2704
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYQ6.1)"
     Site            2761
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35161; propagated from
                     UniProtKB/Swiss-Prot (Q9NYQ6.1)"
     Site            2764
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9NYQ6.1)"
     Region          2777..2939
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYQ6.1)"
     Site            2871
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35161; propagated from
                     UniProtKB/Swiss-Prot (Q9NYQ6.1)"
     Site            2873
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35161; propagated from
                     UniProtKB/Swiss-Prot (Q9NYQ6.1)"
     CDS             1..3019
                     /gene="CELSR1"
                     /gene_synonym="ADGRC1; CDHF9; FMI2; HFMI2; LMPHM9; ME2"
                     /coded_by="NM_001378328.1:451..9510"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS93179.1"
                     /db_xref="GeneID:9620"
                     /db_xref="HGNC:HGNC:1850"
                     /db_xref="MIM:604523"
ORIGIN      
        1 mapppppvlp vllllaaaaa lpamglraaa weprvpggtr afalrpgcty avgaactpra
       61 prelldvgrd grlagrrrvs gagrplplqv rlvarsapta lsrrlrarth lpgcgararl
      121 cgtgarlcga lcfpvpggca aaqhsalaap ttlpacrcpp rprprcpgrp iclppggsvr
      181 lrllcalrra agavrvglal eaatagtpsa spspspplpp nlpearagpa rrarrgtsgr
      241 gslkfpmpny qvalfenepa gtlilqlhah ytiegeeerv syymeglfde rsrgyfrids
      301 atgavstdsv ldretkethv lrvkavdyst pprsattyit vlvkdtndhs pvfeqseyre
      361 rvrenlevgy evltirasdr dspinanlry rvlggawdvf qlnessgvvs travldreea
      421 aeyqllvean dqgrnpgpls atatvyieve dendnypqfs eqnyvvqvpe dvglntavlr
      481 vqatdrdqgq naaihysils gnvagqfylh slsgildvin pldfedvqky slsikaqdgg
      541 rpplinssgv vsvqvldvnd nepifvsspf qatvlenvpl gypvvhiqav dadsgenarl
      601 hyrlvdtast flgggsagpk npaptpdfpf qihnssgwit vcaeldreev ehysfgveav
      661 dhgsppmsss tsvsitvldv ndndpvftqp tyelrlneda avgssvltlq ardrdansvi
      721 tyqltggntr nrfalssqrg gglitlalpl dykqeqqyvl avtasdgtrs htahvlinvt
      781 danthrpvfq sshytvsvse drpvgtsiat lsandedtge narityviqd pvpqfridpd
      841 sgtmytmmel dyenqvaytl timaqdngip qksdtttlei lildandnap qflwdfyqgs
      901 ifedappsts ilqvsatdrd sgpngrllyt fqggddgdgd fyieptsgvi rtqrrldren
      961 vavynlwala vdrgsptpls asveiqvtil dindnapmfe kdelelfvee nnpvgsvvak
     1021 irandpdegp naqimyqive gdmrhffqld llngdlramv eldfevrrey vlvvqatsap
     1081 lvsratvhil lvdqndnppv lpdfqilfnn yvtnksnsfp tgvigcipah dpdvsdslny
     1141 tfvqgnelrl llldpatgel qlsrdldnnr plealmevsv sdgihsvtaf ctlrvtiitd
     1201 dmltnsitvr lenmsqekfl spllalfveg vaavlsttkd dvfvfnvqnd tdvssnilnv
     1261 tfsallpggv rgqffpsedl qeqiylnrtl lttistqrvl pfddniclre pcenymkcvs
     1321 vlrfdssapf lssttvlfrp ihpinglrcr cppgftgdyc eteidlcysd pcgangrcrs
     1381 reggytcecf edftgehcev darsgrcang vcknggtcvn lliggfhcvc ppgeyerpyc
     1441 evttrsfppq sfvtfrglrq rfhftisltf atqernglll yngrfnekhd fialeivdeq
     1501 vqltfsaget tttvapkvps gvsdgrwhsv qvqyynkpni ghlglphgps gekmavvtvd
     1561 dcdttmavrf gkdignysca aqgtqtgskk sldltgplll ggvpnlpedf pvhnrqfvgc
     1621 mrnlsvdgkn vdmagfiann gtregcaarr nfcdgrrcqn ggtcvnrwnm ylcecplrfg
     1681 gknceqamph pqlfsgesvv swsdlniiis vpwylglmfr trkedsvlme atsggptsfr
     1741 lqilnnylqf evshgpsdve svmlsglrvt dgewhhllie lknvkedsem khlvtmtldy
     1801 gmdqnkadig gmlpgltvrs vvvggasedk vsvrrgfrgc mqgvrmggtp tnvatlnmnn
     1861 alkvrvkdgc dvddpctssp cppnsrchda wedyscvcdk gylgincvda chlnpcenmg
     1921 acvrspgspq gyvcecgpsh ygpycenkld lpcprgwwgn pvcgpchcav skgfdpdcnk
     1981 tngqcqcken yykllaqdtc lpcdcfphgs hsrtcdmatg qcackpgvig rqcnrcdnpf
     2041 aevttlgcev iyngcpkafe agiwwpqtkf gqpaavpcpk gsvgnavrhc sgekgwlppe
     2101 lfncttisfv dlramnekls rnetqvdgar alqlvralrs atqhtgtlfg ndvrtayqll
     2161 ghvlqheswq qgfdlaatqd adfhedvihs gsallapatr aaweqiqrse ggtaqllrrl
     2221 egyfsnvarn vrrtylrpfv ivtanmilav difdkfnftg arvprfdtih eefpreless
     2281 vsfpadffrp peekegpllr pagrrttpqt trpgpgtere apisrrrrhp ddagqfaval
     2341 viiyrtlgql lperydpdrr slrlphrpii ntpmvstlvy segaplprpl erpvlvefal
     2401 leveertkpv cvfwnhslav ggtggwsarg cellsrnrth vacqcshtas favlmdisrr
     2461 engevlplki vtyaavslsl aallvafvll slvrmlrsnl hsihkhlava lflsqlvfvi
     2521 ginqtenpfl ctvvaillhy iymstfawtl veslhvyrml tevrnidtgp mrfyyvvgwg
     2581 ipaivtglav gldpqgygnp dfcwlslqdt liwsfagpig aviiintvts vlsakvscqr
     2641 khhyygkkgi vsllrtafll lllisatwll gllavnrdal sfhylfaifs glqgpfvllf
     2701 hcvlnqevrk hlkgvlggrk lhledsattr atlltrslnc nttfgdgpdm lrtdlgesta
     2761 sldsivrdeg iqklgvssgl vrgshgepda slmprsckdp pghdsdsdse lsldeqsssy
     2821 asshssdsed dgvgaeekwd pargavhstp kgdavanhvp agwpdqslae sdsedpsgkp
     2881 rlkvetkvsv elhreeqgsh rgeyppdqes ggaarlassq ppeqrkgilk nkvtyppplt
     2941 lteqtlkgrl rekladceqs ptssrtsslg sggpdcaitv kspgrepgrd hlngvamnvr
     3001 tgsaqadgsd segsnetsi
//
