LOCUS       NP_001106192            2792 aa            linear   ROD 28-APR-2025
DEFINITION  E3 ubiquitin-protein ligase UBR5 isoform 2 [Mus musculus].
ACCESSION   NP_001106192
VERSION     NP_001106192.1
DBSOURCE    REFSEQ: accession NM_001112721.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 2792)
  AUTHORS   Yang,D., Geng,T., Harrison,A.G., Cahoon,J.G., Xing,J., Jiao,B.,
            Wang,M., Cheng,C., Hill,R.E., Wang,H., Vella,A.T., Cheng,G.,
            Wang,Y. and Wang,P.
  TITLE     UBR5 promotes antiviral immunity by disengaging the transcriptional
            brake on RIG-I like receptors
  JOURNAL   Nat Commun 15 (1), 780 (2024)
   PUBMED   38278841
  REMARK    GeneRIF: UBR5 promotes antiviral immunity by disengaging the
            transcriptional brake on RIG-I like receptors.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 2792)
  AUTHORS   Mellis,D., Staines,K.A., Peluso,S., Georgiou,I.C., Dora,N.,
            Kubiak,M., Van't Hof,R., Grillo,M., Farquharson,C., Kinsella,E.,
            Thornburn,A., Ralston,S.H., Salter,D.M., Riobo-Del Galdo,N.A.,
            Hill,R.E. and Ditzel,M.
  TITLE     Ubiquitin-protein ligase Ubr5 cooperates with hedgehog signalling
            to promote skeletal tissue homeostasis
  JOURNAL   PLoS Genet 17 (4), e1009275 (2021)
   PUBMED   33819267
  REMARK    GeneRIF: Ubiquitin-protein ligase Ubr5 cooperates with hedgehog
            signalling to promote skeletal tissue homeostasis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2792)
  AUTHORS   Hughes,D.C., Turner,D.C., Baehr,L.M., Seaborne,R.A., Viggars,M.,
            Jarvis,J.C., Gorski,P.P., Stewart,C.E., Owens,D.J., Bodine,S.C. and
            Sharples,A.P.
  TITLE     Knockdown of the E3 ubiquitin ligase UBR5 and its role in skeletal
            muscle anabolism
  JOURNAL   Am J Physiol Cell Physiol 320 (1), C45-C56 (2021)
   PUBMED   33052072
  REMARK    GeneRIF: Knockdown of the E3 ubiquitin ligase UBR5 and its role in
            skeletal muscle anabolism.
REFERENCE   4  (residues 1 to 2792)
  AUTHORS   Song,M., Yeku,O.O., Rafiq,S., Purdon,T., Dong,X., Zhu,L., Zhang,T.,
            Wang,H., Yu,Z., Mai,J., Shen,H., Nixon,B., Li,M., Brentjens,R.J.
            and Ma,X.
  TITLE     Tumor derived UBR5 promotes ovarian cancer growth and metastasis
            through inducing immunosuppressive macrophages
  JOURNAL   Nat Commun 11 (1), 6298 (2020)
   PUBMED   33293516
  REMARK    GeneRIF: Tumor derived UBR5 promotes ovarian cancer growth and
            metastasis through inducing immunosuppressive macrophages.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2792)
  AUTHORS   Loupe,J.M., Pinto,R.M., Kim,K.H., Gillis,T., Mysore,J.S.,
            Andrew,M.A., Kovalenko,M., Murtha,R., Seong,I., Gusella,J.F.,
            Kwak,S., Howland,D., Lee,R., Lee,J.M., Wheeler,V.C. and
            MacDonald,M.E.
  TITLE     Promotion of somatic CAG repeat expansion by Fan1 knock-out in
            Huntington's disease knock-in mice is blocked by Mlh1 knock-out
  JOURNAL   Hum Mol Genet 29 (18), 3044-3053 (2020)
   PUBMED   32876667
REFERENCE   6  (residues 1 to 2792)
  AUTHORS   Saunders,D.N., Hird,S.L., Withington,S.L., Dunwoodie,S.L.,
            Henderson,M.J., Biben,C., Sutherland,R.L., Ormandy,C.J. and
            Watts,C.K.
  TITLE     Edd, the murine hyperplastic disc gene, is essential for yolk sac
            vascularization and chorioallantoic fusion
  JOURNAL   Mol Cell Biol 24 (16), 7225-7234 (2004)
   PUBMED   15282321
  REMARK    GeneRIF: Results suggest that Edd has an essential role in
            extraembryonic development.
REFERENCE   7  (residues 1 to 2792)
  AUTHORS   Okazaki,N., Kikuno,R., Ohara,R., Inamoto,S., Aizawa,H., Yuasa,S.,
            Nakajima,D., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: II. The complete nucleotide sequences of 400 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 10 (1), 35-48 (2003)
   PUBMED   12693553
REFERENCE   8  (residues 1 to 2792)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   9  (residues 1 to 2792)
  AUTHORS   Henderson,M.J., Russell,A.J., Hird,S., Munoz,M., Clancy,J.L.,
            Lehrbach,G.M., Calanni,S.T., Jans,D.A., Sutherland,R.L. and
            Watts,C.K.
  TITLE     EDD, the human hyperplastic discs protein, has a role in
            progesterone receptor coactivation and potential involvement in DNA
            damage response
  JOURNAL   J Biol Chem 277 (29), 26468-26478 (2002)
   PUBMED   12011095
REFERENCE   10 (residues 1 to 2792)
  AUTHORS   Nelson,P.S., Pritchard,C., Abbott,D. and Clegg,N.
  TITLE     The human (PEDB) and mouse (mPEDB) Prostate Expression Databases
  JOURNAL   Nucleic Acids Res 30 (1), 218-220 (2002)
   PUBMED   11752298
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CJ063125.1, AY550908.1, AK162029.1, CB527808.1 and AK014485.1.
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the central coding region, compared to variant 1.
            The encoded isoform (2) is shorter, compared to 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##
            Transcript exon combination :: AY550908.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2792
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="15"
                     /map="15 15.1 cM"
     Protein         1..2792
                     /product="E3 ubiquitin-protein ligase UBR5 isoform 2"
                     /EC_number="2.3.2.26"
                     /note="extraembryonic development; E3 ubiquitin-protein
                     ligase UBR5; hyperplastic discs protein homolog; E3
                     ubiquitin-protein ligase, HECT domain-containing 1;
                     HECT-type E3 ubiquitin transferase UBR5"
                     /calculated_mol_wt=308189
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylthreonine.
                     /evidence=ECO:0000250|UniProtKB:O95071; propagated from
                     UniProtKB/Swiss-Prot (Q80TP3.2)"
     Region          77..175
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80TP3.2)"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O95071; propagated from
                     UniProtKB/Swiss-Prot (Q80TP3.2)"
     Region          184..230
                     /region_name="CUE_UBR5"
                     /note="CUE domain found in E3 ubiquitin-protein ligase
                     UBR5 and similar proteins; cd14423"
                     /db_xref="CDD:270606"
     Site            order(192,195..196,198,216..217,220..221,224..225)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270606"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q80TP3.2)"
     Region          322..347
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80TP3.2)"
     Site            346
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O95071; propagated from
                     UniProtKB/Swiss-Prot (Q80TP3.2)"
     Site            572
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O95071; propagated from
                     UniProtKB/Swiss-Prot (Q80TP3.2)"
     Region          577..642
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80TP3.2)"
     Site            606
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O95071; propagated from
                     UniProtKB/Swiss-Prot (Q80TP3.2)"
     Site            631
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O95071; propagated from
                     UniProtKB/Swiss-Prot (Q80TP3.2)"
     Site            802
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O95071; propagated from
                     UniProtKB/Swiss-Prot (Q80TP3.2)"
     Site            922
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O95071; propagated from
                     UniProtKB/Swiss-Prot (Q80TP3.2)"
     Region          993..1029
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80TP3.2)"
     Site            1012
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O95071; propagated from
                     UniProtKB/Swiss-Prot (Q80TP3.2)"
     Region          1046..1069
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80TP3.2)"
     Site            1109
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O95071; propagated from
                     UniProtKB/Swiss-Prot (Q80TP3.2)"
     Site            1129
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O95071; propagated from
                     UniProtKB/Swiss-Prot (Q80TP3.2)"
     Region          1165..1240
                     /region_name="UBR-box_UBR5"
                     /note="UBR-box found in HECT-type E3 ubiquitin-protein
                     ligase UBR5 and similar proteins; cd19675"
                     /db_xref="CDD:439073"
     Site            order(1190,1193,1202,1205,1209..1210,1213,1226,1228,1234)
                     /site_type="other"
                     /note="putative Zn binding site [ion binding]"
                     /db_xref="CDD:439073"
     Site            1221
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O95071; propagated from
                     UniProtKB/Swiss-Prot (Q80TP3.2)"
     Region          1293..1312
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80TP3.2)"
     Site            1302
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O95071; propagated from
                     UniProtKB/Swiss-Prot (Q80TP3.2)"
     Site            1349
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O95071; propagated from
                     UniProtKB/Swiss-Prot (Q80TP3.2)"
     Site            1369
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O95071; propagated from
                     UniProtKB/Swiss-Prot (Q80TP3.2)"
     Site            1475
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O95071; propagated from
                     UniProtKB/Swiss-Prot (Q80TP3.2)"
     Region          1509..1734
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80TP3.2)"
     Site            1543
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O95071; propagated from
                     UniProtKB/Swiss-Prot (Q80TP3.2)"
     Site            1730
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O95071; propagated from
                     UniProtKB/Swiss-Prot (Q80TP3.2)"
     Site            1735
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O95071; propagated from
                     UniProtKB/Swiss-Prot (Q80TP3.2)"
     Site            1740
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:O95071; propagated from
                     UniProtKB/Swiss-Prot (Q80TP3.2)"
     Site            1774
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O95071; propagated from
                     UniProtKB/Swiss-Prot (Q80TP3.2)"
     Region          1853..1884
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80TP3.2)"
     Site            1963
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O95071; propagated from
                     UniProtKB/Swiss-Prot (Q80TP3.2)"
     Region          1978..2015
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80TP3.2)"
     Site            1984
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O95071; propagated from
                     UniProtKB/Swiss-Prot (Q80TP3.2)"
     Site            2020
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O95071; propagated from
                     UniProtKB/Swiss-Prot (Q80TP3.2)"
     Site            2022
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O95071; propagated from
                     UniProtKB/Swiss-Prot (Q80TP3.2)"
     Site            2024
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O95071; propagated from
                     UniProtKB/Swiss-Prot (Q80TP3.2)"
     Site            2070
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O95071; propagated from
                     UniProtKB/Swiss-Prot (Q80TP3.2)"
     Region          2111..2137
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80TP3.2)"
     Site            2207
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O95071; propagated from
                     UniProtKB/Swiss-Prot (Q80TP3.2)"
     Site            2235
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O95071; propagated from
                     UniProtKB/Swiss-Prot (Q80TP3.2)"
     Site            2283
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O95071; propagated from
                     UniProtKB/Swiss-Prot (Q80TP3.2)"
     Region          2317..2387
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80TP3.2)"
     Region          2383..2446
                     /region_name="PolyA"
                     /note="C-terminal domain of Poly(A)-binding protein.
                     Present also in Drosophila hyperplastics discs protein;
                     smart00517"
                     /db_xref="CDD:197769"
     Region          2461..2789
                     /region_name="HECTc"
                     /note="Domain Homologous to E6-AP Carboxyl Terminus with;
                     smart00119"
                     /db_xref="CDD:214523"
     Site            2463
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O95071; propagated from
                     UniProtKB/Swiss-Prot (Q80TP3.2)"
     Region          2467..2494
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80TP3.2)"
     Site            2477
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O95071; propagated from
                     UniProtKB/Swiss-Prot (Q80TP3.2)"
     Site            2479
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O95071; propagated from
                     UniProtKB/Swiss-Prot (Q80TP3.2)"
     Site            order(2568,2571..2572,2574..2575,2584,2591,2593,
                     2597..2598,2605,2610,2627,2631)
                     /site_type="active"
                     /note="E2 interaction site [active]"
                     /db_xref="CDD:238033"
     CDS             1..2792
                     /gene="Ubr5"
                     /gene_synonym="Edd; Edd1"
                     /coded_by="NM_001112721.2:430..8808"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS88751.1"
                     /db_xref="GeneID:70790"
                     /db_xref="MGI:MGI:1918040"
ORIGIN      
        1 mtsihfvvhp lpgtedqlnd rlrevsekln kynlnshppl nvleqatikq cvvgpnhaaf
       61 lledgricri gfsvqpdrle lgkpdnndgs klnsssgtgr tsrpgrtsds pwflsgsetl
      121 grlagntlgs rwssgvggsg ggssgrssag ardsrrqtrv irtgrdrgsg llgsqpqpvi
      181 pasvipeeli sqaqvvlqgk srsviirelq rtnldvnlav nnllsrdded gddgddtase
      241 sylpgedlms lldadihsah psviidadam fsedisyfgy psfrrsslsr lgssrerdse
      301 llreresvlr lrerrwldga sfdnergsts kegesnpdkk ntpvqspvsl gedlqwwpdk
      361 dgtkftciga lysellavss kgelyqwkws esepyrnaqn pslhhpratf lgltnekivl
      421 lsansiratv atennkvatw vdetlssvas klehtaqtys elqgerivsl hccalytcaq
      481 lennlywwgv vpfsqrkkml ekaraknkkp kssagissmp nitvgtqvcl rnnplyhaga
      541 vafsisagip kvgvlmesvw nmndscrfql rspeslksme kasktletkp eskqepvkte
      601 mgpppspast csdassiass asmpykrrrs tpapreeekv neeqwplrev vfvedvknvp
      661 vgkvlkvdga yvavkfpgts tnttcqnssg pdadpssllq dcrllridel qvvktggtpk
      721 vpdcfqrtpk klcipektei lavnvdskgv havlktgswv rycvfdlatg kaeqennfpt
      781 ssvaflgqde rsvaiftagq espivlrdgn gtiypmakdc mggirdpdwl dlppisslgm
      841 gvhslinlpa nstikkkaai iimavekqtl mqhilrcdye acrqylvnle qavvleqnlq
      901 mlqtfishrc dgnrnilhac vsvcfptsnk etkeeeeaer serntfaerl saveaianai
      961 svvssngpgn ragssnsrsl rlremmrrsl raaglgrhea gasssdhqdp vsppiappsw
     1021 vpdppsmdpd gdidfilapa vgslttaatg sgqgpststi pgpstepsvv eskdrkanah
     1081 filkllcdsa vlqpylrell sakdargmtp fmsavsgray paaitileta qkiakaevsa
     1141 sekeedvfmg mvcpsgtnpd dsplyvlccn dtcsftwtga ehinqdifec rtcglleslc
     1201 cctecarvch kghdcklkrt sptaycdcwe kckcktliag qksarldlly rlltatnlvt
     1261 lpnsrgehll lflvqtvarq tvehcqyrpp riredrnrkt aspedsdmpd hdlepprfaq
     1321 lalervlqdw nalrsmimfg sqenkdplsa ssrighllpe eqvylnqqsg tirldcfthc
     1381 livkctadil lldtllgtlv kelqnkytpg rreeaiavtm rflrsvarvf vilsvemass
     1441 kkknnfipqp igkckrvfqa llpyaveelc nvaeslivpv rmgiarptap ftlastsida
     1501 mqgseelfsv eplpprpssd qassssqsqs syiirnpqqr risqsqpvrg rdeeqddivs
     1561 adveevevve gvageedhhd eqeehgeena eaeghhdehd edgsdmeldl laaaetesds
     1621 esnhsnqdna sgrrsvvtaa tagseagass vpaffsedds qsndssdsds sssqsddieq
     1681 etfmldeple rttnsshang aaqaprsmqw avrnpqhqra astapsstst paassagliy
     1741 idpsnlrrsg tistsaaaaa aaleasnass yltsasslar aysivirqis dlmglipkyn
     1801 hlvysqipaa vkltyqdavn lqnyveekli ptwnwmvsvm dsteaqlryg salasagdpg
     1861 hpnhplhasq nsarrermta reeaslrtle grrratllsa rqgmmsargd flnyalslmr
     1921 shndehsdvl pvldvcslkh vayvfqaliy wikamnqqtt ldtpqlerkr trellelgid
     1981 nedsehendd dtsqsatlnd kdddslpaet gqnhpffrrs dsmtflgcip pnpfevplae
     2041 aipladqphl lqpnarkedl fgrpsqglys ssagsgkciv evtmdrncle vlptkmsyaa
     2101 nlknvmnmqn rqkkegeeqs llaeeadssk pgpsapdvaa qlkssllaei gltesegppl
     2161 tsfrpqcsfm gmvishdmll grwrlslelf grvfmedvga epgsiltelg gfevkeskfr
     2221 remeklrnqq srdlslevdr drdlliqqtm rqlnnhfgrr cattpmavhr vkvtfkdepg
     2281 egsgvarsfy taiaqaflsn eklpnldciq nankgthtsl mqrlrnrger drerererem
     2341 rrssglrags rrdrdrdfrr qlsidtrpfr pasegnpsdd pdplpahrqa lgerlyprvq
     2401 amqpafaski tgmllelspa qlllllased slrarvdeam eliiahgren gadsildlgl
     2461 ldssekvqen rkrhgssrsv vdmdledtdd gddnaplfyq pgkrgfytpr pgkntearln
     2521 cfrnigrilg lcllqnelcp itlnrhvikv llgrkvnwhd faffdpvmye slrqlilasq
     2581 ssdadavfsa mdlafaidlc keegggqvel ipngvnipvt pqnvyeyvrk yaehrmlvva
     2641 eqplhamrkg lldvlpknsl edltaedfrl lvngcgevnv qmlisftsfn desgenaekl
     2701 lqfkrwfwsi vekmsmterq dlvyfwtssp slpaseegfq pmpsitirpp ddqhlptant
     2761 cisrlyvply sskqilkqkl llaiktknfg fv
//
