HECW1_MOUSE
ID HECW1_MOUSE Reviewed; 1604 AA.
AC Q8K4P8; D3YZ67; Q6A086; Q8BIA6; Q8BKC2; Q8BKL3; Q8BKZ8;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=E3 ubiquitin-protein ligase HECW1;
DE EC=2.3.2.26;
DE AltName: Full=HECT, C2 and WW domain-containing protein 1;
DE AltName: Full=HECT-type E3 ubiquitin transferase HECW1;
DE AltName: Full=NEDD4-like E3 ubiquitin-protein ligase 1;
DE Short=mNEDL1;
GN Name=Hecw1; Synonyms=Kiaa0322, Nedl1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1212-1604 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Corpus striatum, Diencephalon, and Eye;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 22-1604 (ISOFORM 1), FUNCTION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=14684739; DOI=10.1074/jbc.m312389200;
RA Miyazaki K., Fujita T., Ozaki T., Kato C., Kurose Y., Sakamoto M., Kato S.,
RA Goto T., Itoyama Y., Aoki M., Nakagawara A.;
RT "NEDL1, a novel ubiquitin-protein isopeptide ligase for dishevelled-1,
RT targets mutant superoxide dismutase-1.";
RL J. Biol. Chem. 279:11327-11335(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 414-1604 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-871; SER-935 AND SER-937, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and
CC subsequent degradation of DVL1. {ECO:0000250,
CC ECO:0000269|PubMed:14684739}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.26;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with DVL1 and SSR3. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14684739}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Named isoforms=2.;
CC Name=1;
CC IsoId=Q8K4P8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K4P8-2; Sequence=VSP_023076;
CC Name=3;
CC IsoId=Q8K4P8-3; Sequence=VSP_023074, VSP_023075;
CC Name=4;
CC IsoId=Q8K4P8-4; Sequence=VSP_023075;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in neurons of the spinal
CC cord.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC28516.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK033922; BAC28516.1; ALT_INIT; mRNA.
DR EMBL; AK047678; BAC33122.1; -; mRNA.
DR EMBL; AK051569; BAC34677.1; -; mRNA.
DR EMBL; AK053694; BAC35477.1; -; mRNA.
DR EMBL; AC092710; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154511; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154615; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC161249; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT025604; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB083710; BAB97389.1; -; mRNA.
DR EMBL; AK172932; BAD32210.1; -; mRNA.
DR CCDS; CCDS49207.1; -. [Q8K4P8-1]
DR RefSeq; NP_001074817.3; NM_001081348.3. [Q8K4P8-1]
DR RefSeq; XP_006516873.1; XM_006516810.3. [Q8K4P8-1]
DR RefSeq; XP_006516874.1; XM_006516811.1. [Q8K4P8-1]
DR RefSeq; XP_006516875.1; XM_006516812.3. [Q8K4P8-1]
DR AlphaFoldDB; Q8K4P8; -.
DR SMR; Q8K4P8; -.
DR BioGRID; 220495; 2.
DR IntAct; Q8K4P8; 3.
DR MINT; Q8K4P8; -.
DR STRING; 10090.ENSMUSP00000106145; -.
DR iPTMnet; Q8K4P8; -.
DR PhosphoSitePlus; Q8K4P8; -.
DR MaxQB; Q8K4P8; -.
DR PaxDb; Q8K4P8; -.
DR PeptideAtlas; Q8K4P8; -.
DR PRIDE; Q8K4P8; -.
DR ProteomicsDB; 269687; -. [Q8K4P8-1]
DR ProteomicsDB; 269688; -. [Q8K4P8-2]
DR ProteomicsDB; 269689; -. [Q8K4P8-3]
DR ProteomicsDB; 269690; -. [Q8K4P8-4]
DR Antibodypedia; 1996; 52 antibodies from 16 providers.
DR DNASU; 94253; -.
DR Ensembl; ENSMUST00000110516; ENSMUSP00000106145; ENSMUSG00000021301. [Q8K4P8-1]
DR GeneID; 94253; -.
DR KEGG; mmu:94253; -.
DR UCSC; uc007pnd.2; mouse. [Q8K4P8-1]
DR UCSC; uc007png.2; mouse. [Q8K4P8-4]
DR UCSC; uc007pnh.2; mouse. [Q8K4P8-3]
DR UCSC; uc011ywk.1; mouse. [Q8K4P8-2]
DR CTD; 23072; -.
DR MGI; MGI:2444115; Hecw1.
DR VEuPathDB; HostDB:ENSMUSG00000021301; -.
DR eggNOG; KOG0940; Eukaryota.
DR GeneTree; ENSGT00940000158294; -.
DR HOGENOM; CLU_002173_14_0_1; -.
DR InParanoid; Q8K4P8; -.
DR OMA; AGPWHDE; -.
DR OrthoDB; 117748at2759; -.
DR PhylomeDB; Q8K4P8; -.
DR TreeFam; TF313938; -.
DR Reactome; R-MMU-4641258; Degradation of DVL.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 94253; 4 hits in 73 CRISPR screens.
DR PRO; PR:Q8K4P8; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8K4P8; protein.
DR Bgee; ENSMUSG00000021301; Expressed in cortical plate and 115 other tissues.
DR ExpressionAtlas; Q8K4P8; baseline and differential.
DR Genevisible; Q8K4P8; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:2000650; P:negative regulation of sodium ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; IBA:GO_Central.
DR CDD; cd08691; C2_NEDL1-like; 1.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd00201; WW; 2.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037795; C2_HECW.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR040524; HECW1_helix.
DR InterPro; IPR032348; HECW_N.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF18436; HECW1_helix; 1.
DR Pfam; PF16562; HECW_N; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF51045; SSF51045; 2.
DR SUPFAM; SSF56204; SSF56204; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 2.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Phosphoprotein;
KW Reference proteome; Repeat; Transferase; Ubl conjugation pathway.
FT CHAIN 1..1604
FT /note="E3 ubiquitin-protein ligase HECW1"
FT /id="PRO_0000277666"
FT DOMAIN 182..318
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 826..859
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 1016..1049
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 1269..1604
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT REGION 350..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..936
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 871..898
FT /evidence="ECO:0000255"
FT COMPBIAS 358..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..517
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..936
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1572
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT MOD_RES 871
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 935
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 937
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..8
FT /note="MLLHLCSV -> MICAQLEAA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023074"
FT VAR_SEQ 316..1604
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023075"
FT VAR_SEQ 782..795
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15368895"
FT /id="VSP_023076"
FT CONFLICT 167
FT /note="S -> R (in Ref. 3; BAB97389)"
FT /evidence="ECO:0000305"
FT CONFLICT 823
FT /note="T -> A (in Ref. 3; BAB97389)"
FT /evidence="ECO:0000305"
FT CONFLICT 1036
FT /note="D -> G (in Ref. 3; BAB97389)"
FT /evidence="ECO:0000305"
FT CONFLICT 1248
FT /note="I -> V (in Ref. 3; BAB97389)"
FT /evidence="ECO:0000305"
FT CONFLICT 1356
FT /note="L -> P (in Ref. 3; BAB97389)"
FT /evidence="ECO:0000305"
FT CONFLICT 1538
FT /note="V -> M (in Ref. 3; BAB97389)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1604 AA; 179467 MW; 0643EE0129A08E0D CRC64;
MLLHLCSVKN LYQNRFLGLA AMASPSRNSQ SRRRCKEPLR YSYNPDQFHN IDIRNGAHDA
ITIPRSTSDT DLVTSDSRST LMVSSSYYSI GHSQDLVIHW DIKEEVDAGD WIGMYLIGEV
SSENFLDYKN RGVNGSHRGQ IIWKIDASSY FVESETKICF KYYHGVSGAL RATTPSVTVK
NSAAPIFKGI GSEETAQSQG SRRLISFSLS DFQAMGLKKG MFFNPDPYLK ISIQPGKHSI
FPALPHHGQE RRSTIIGNTV NPIWQAEHFS FVSLPTDVLE IEVKDKFAKS RPIIKRFLGK
LSMPVQRLLE RHAIGDRVVS YTLGRRLPTD HVSGQLQFRF EITSSIHADD EEISLSAEPE
SSAETQDSIM NSMVGNSNGE PSGDATEFCK DAKPESPSEG NGVNSSENQN QEHAGPVEEA
AGAMEARDGS NVSEAPEEPG ELQDPEQHDT QPTLSAEEVA EGLPLDEDSP SSLLPEENTA
LGSKVEEETV PENGAREEEM QKGKDEEEEE EDVSTLEQGE PGLELRVSVR KKSRPCSLPV
SELETVIASA CGDAETPRTH YIRIHTLLHS MPSAQRGSTT EEEDGLEEES TLKESSEKDG
LSEVDTIAAD PQSMEDGESD GATLCMAPSD CSGGHFSSLS KGIGAGQDGE AHPSTGSESD
SSPQQGADHS CEGCDASCCS PSCYSTSCYS SSCYSSSCYS SSCYNGNNRF ASHTRFSSVD
SAKISESTVF SSQEDEEEEN SAFESVPDSV QSPELDPEST NGAGPWQDEL AAPGGNAARS
TEGLESPMAG PSNRREGECP ILHNSQPISQ LPSLRPEHHH YPTIDEPLPP NWEARIDSHG
RVFYVDHINR TTTWQRPSMA PTPDGMIRSG SVHQMEQLNR RYQNIQRTMA TERAEEDSGN
QNSEQIPDGG GGGGGGSDSE AESSQSSLDL RREGSLSPVN SQKVTLLLQS PAVKFITNPE
FFTVLHANYS AYRVFTSSTC LKHMILKVRR DARNFERYQH NRDLVNFINM FADTRLELPR
GWEIKTDHQG KSFFVDHNSR ATTFIDPRIP LQNGRLPNHL THRQHLQRLR SYSAGEASEV
SRNRGASLLA RPGHSLIAAI RSQHQHESLP LAYNDKIVAF LRQPNIFEML QERQPSLARN
HTLREKIHYI RTEGNHGLDK LSCDADLVIL LSLFEEEIMS YVPLQSAFHP GYSFSPRCSP
CSSPQNSPGL QRASARAPSP YRRDFEAKLR NFYRKLEAKG FGQGPGKIKL IIRRDHLLEG
TFNQVMAYSR KELQRNKLYI TFVGEEGLDY SGPSREFFFL LSQELFNPYY GLFEYSANDT
YTVQISPMSA FVENYLEWFR FSGRILGLAL IHQYLLDAFF TRPFYKGLLK LPCDLSDLEY
LDEEFHQSLQ WMKDNNITDI LDLTFTVNEE VFGQVTEREL KSGGANTQVT EKNKKEYIER
MVKWRVERGV VQQTEALLRG FYEVVDSRLV SVFDARELEL VIAGTAEIDL NDWRNNTEYR
GGYHDGHLVI RWFWAAVERF NNEQRLRLLQ FVTGTSSVPY EGFAALRGSN GLRRFCIEKW
GKITSLPRAH TCFNRLDLPP YPSYSMLYEK LLTAVEETST FGLE
