UBR3_DROME
ID UBR3_DROME Reviewed; 2219 AA.
AC Q9W3M3; M9PGM3;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 4.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=E3 ubiquitin-protein ligase Ubr3 {ECO:0000303|PubMed:25146930};
DE EC=2.3.2.27 {ECO:0000269|PubMed:26383956};
DE AltName: Full=E3 ubiquitin-protein transferase Ubr3 {ECO:0000305};
GN Name=Ubr3 {ECO:0000303|PubMed:25146930, ECO:0000312|FlyBase:FBgn0260970};
GN ORFNames=CG42593 {ECO:0000312|FlyBase:FBgn0260970};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH DIAP1, UBR-TYPE DOMAIN, RING-TYPE DOMAIN, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=25146930; DOI=10.1038/cdd.2014.115;
RA Huang Q., Tang X., Wang G., Fan Y., Ray L., Bergmann A., Belenkaya T.Y.,
RA Ling X., Yan D., Lin Y., Ye X., Shi W., Zhou X., Lu F., Qu J., Lin X.;
RT "Ubr3 E3 ligase regulates apoptosis by controlling the activity of DIAP1 in
RT Drosophila.";
RL Cell Death Differ. 21:1961-1970(2014).
RN [4] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INTERACTION WITH DIAP1; OVO; RRP1
RP AND TAL, AND SUBCELLULAR LOCATION.
RX PubMed=26383956; DOI=10.1126/science.aac5677;
RA Zanet J., Benrabah E., Li T., Pelissier-Monier A., Chanut-Delalande H.,
RA Ronsin B., Bellen H.J., Payre F., Plaza S.;
RT "Pri sORF peptides induce selective proteasome-mediated protein
RT processing.";
RL Science 349:1356-1358(2015).
RN [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH CAD99C; CK AND SANS, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND MUTAGENESIS OF PHE-949.
RX PubMed=27331610; DOI=10.7554/elife.15258;
RA Li T., Giagtzoglou N., Eberl D.F., Jaiswal S.N., Cai T., Godt D.,
RA Groves A.K., Bellen H.J.;
RT "The E3 ligase Ubr3 regulates Usher syndrome and MYH9 disorder proteins in
RT the auditory organs of Drosophila and mammals.";
RL Elife 5:E15258-E15258(2016).
RN [6] {ECO:0000305}
RP FUNCTION, INTERACTION WITH COS, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP UBR-TYPE DOMAIN, UBIQUITINATION, AND MUTAGENESIS OF PHE-949.
RX PubMed=27195754; DOI=10.1371/journal.pgen.1006054;
RA Li T., Fan J., Blanco-Sanchez B., Giagtzoglou N., Lin G., Yamamoto S.,
RA Jaiswal M., Chen K., Zhang J., Wei W., Lewis M.T., Groves A.K.,
RA Westerfield M., Jia J., Bellen H.J.;
RT "Ubr3, a Novel Modulator of Hh Signaling Affects the Degradation of Costal-
RT 2 and Kif7 through Poly-ubiquitination.";
RL PLoS Genet. 12:E1006054-E1006054(2016).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which is a component of the N-end
CC rule pathway (PubMed:26383956, PubMed:27195754). Recognizes and binds
CC to proteins bearing specific N-terminal residues, leading to their
CC ubiquitination and subsequent degradation (PubMed:26383956,
CC PubMed:27195754). Binds to the E3 ubiquitin-protein ligase Diap1 and
CC enhances its ubiquitination and anti-apoptotic functions
CC (PubMed:25146930). Essential during trichome development for the
CC ubiquitination of the N-terminus of ovo isoform B (svb), converting it
CC from a transcriptional inhibitor to an activator (PubMed:26383956).
CC Positively regulates a hh-signaling pathway which functions in
CC photoreceptor differentiation (PubMed:27195754). Activation of hh up-
CC regulates transcription of Ubr3, which in turn promotes hh signaling by
CC mediating the ubiquitination and degradation of cos (PubMed:27195754).
CC Necessary for auditory transduction: plays a role in Johnston's organ
CC organization by acting in the regulation of zip and ck function in
CC scolopidial apical attachment (PubMed:27331610). Likely to function by
CC acting in a pathway that negatively regulates the ubiquitination of
CC zip, consequently affecting its interaction with ck (PubMed:27331610).
CC May also negatively regulate a component of the SCF (SKP1-CUL1-F-box
CC protein) E3 ubiquitin-protein ligase complex Cul1, which also appears
CC to function in the negative regulation of the zip-ck interaction and
CC scolopidial apical attachment (PubMed:27331610).
CC {ECO:0000269|PubMed:25146930, ECO:0000269|PubMed:26383956,
CC ECO:0000269|PubMed:27195754, ECO:0000269|PubMed:27331610}.
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=2.3.2.27; Evidence={ECO:0000269|PubMed:26383956};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:26383956}.
CC -!- SUBUNIT: Selectively interacts (via UBR-type zinc finger) with the
CC cleaved form of Diap1; this interaction is enhanced by tal
CC (PubMed:25146930, PubMed:26383956). Interacts with tal and Rrp1
CC (PubMed:26383956). Interacts with ovo isoform B (via N-terminus)
CC (PubMed:26383956). Interacts with Cad99C (via the cytoplasmic domain)
CC (PubMed:27331610). Interacts with ck and Sans (PubMed:27331610).
CC Interacts with cos (via Kinesin motor domain) (PubMed:27195754).
CC {ECO:0000269|PubMed:25146930, ECO:0000269|PubMed:26383956,
CC ECO:0000269|PubMed:27195754, ECO:0000269|PubMed:27331610}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26383956,
CC ECO:0000269|PubMed:27195754}. Nucleus {ECO:0000269|PubMed:26383956}.
CC Note=In Johnston's organ, high expression at the apical tips of neurons
CC and scolopale cells (PubMed:27331610). In the cytoplasm expressed in
CC puncta (PubMed:27195754). {ECO:0000269|PubMed:27195754,
CC ECO:0000269|PubMed:27331610}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A {ECO:0000312|FlyBase:FBgn0260970};
CC IsoId=Q9W3M3-1; Sequence=Displayed;
CC Name=C {ECO:0000312|FlyBase:FBgn0260970};
CC IsoId=Q9W3M3-2; Sequence=VSP_059031;
CC -!- DEVELOPMENTAL STAGE: Ubiquitously expressed in the second and third
CC segments of the pupal antenna (at protein level) (PubMed:27331610). In
CC the eye imaginal disks of 3rd instar larvae, expression is highest in
CC the morphogenetic furrow (PubMed:27195754).
CC {ECO:0000269|PubMed:27195754, ECO:0000269|PubMed:27331610}.
CC -!- DOMAIN: The UBR-type zinc finger domain is necessary for interaction
CC with Diap1 and anti-apoptotic activity (PubMed:25146930). Domain is
CC also sufficient for interaction with cos (PubMed:27195754).
CC {ECO:0000269|PubMed:25146930, ECO:0000269|PubMed:27195754}.
CC -!- DOMAIN: The RING-type zinc finger domain is not necessary for
CC interaction with Diap1 and anti-apoptotic activity.
CC {ECO:0000269|PubMed:25146930}.
CC -!- PTM: In vitro, self-ubiquitination in the presence of E1, E2 and
CC ubiquitin. {ECO:0000269|PubMed:27195754}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in the eye results in
CC small rough eyes. {ECO:0000269|PubMed:25146930}.
CC -!- SIMILARITY: Belongs to the UBR1 family. {ECO:0000305}.
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DR EMBL; AE014298; AAF46302.4; -; Genomic_DNA.
DR EMBL; AE014298; AGB95163.1; -; Genomic_DNA.
DR RefSeq; NP_001259318.1; NM_001272389.1. [Q9W3M3-2]
DR RefSeq; NP_572428.3; NM_132200.4. [Q9W3M3-1]
DR AlphaFoldDB; Q9W3M3; -.
DR SMR; Q9W3M3; -.
DR IntAct; Q9W3M3; 4.
DR STRING; 7227.FBpp0290962; -.
DR EnsemblMetazoa; FBtr0301748; FBpp0290962; FBgn0260970. [Q9W3M3-1]
DR EnsemblMetazoa; FBtr0331299; FBpp0303731; FBgn0260970. [Q9W3M3-2]
DR GeneID; 31713; -.
DR KEGG; dme:Dmel_CG42593; -.
DR UCSC; CG1531-RD; d. melanogaster. [Q9W3M3-1]
DR CTD; 130507; -.
DR FlyBase; FBgn0260970; Ubr3.
DR VEuPathDB; VectorBase:FBgn0260970; -.
DR eggNOG; KOG1139; Eukaryota.
DR GeneTree; ENSGT00950000183075; -.
DR InParanoid; Q9W3M3; -.
DR OMA; GNKDELH; -.
DR PhylomeDB; Q9W3M3; -.
DR SignaLink; Q9W3M3; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 31713; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 31713; -.
DR PRO; PR:Q9W3M3; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0260970; Expressed in cleaving embryo and 21 other tissues.
DR ExpressionAtlas; Q9W3M3; baseline and differential.
DR Genevisible; Q9W3M3; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0043025; C:neuronal cell body; IMP:FlyBase.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; ISM:FlyBase.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:FlyBase.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IMP:FlyBase.
DR GO; GO:0051865; P:protein autoubiquitination; IDA:FlyBase.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:FlyBase.
DR GO; GO:0016567; P:protein ubiquitination; IMP:FlyBase.
DR GO; GO:0007605; P:sensory perception of sound; IMP:FlyBase.
DR GO; GO:0071596; P:ubiquitin-dependent protein catabolic process via the N-end rule pathway; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR044046; E3_ligase_UBR-like_C.
DR InterPro; IPR039164; UBR1-like.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR21497; PTHR21497; 1.
DR Pfam; PF18995; PRT6_C; 1.
DR Pfam; PF02207; zf-UBR; 1.
DR SMART; SM00396; ZnF_UBR1; 1.
DR PROSITE; PS51157; ZF_UBR; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Metal-binding; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..2219
FT /note="E3 ubiquitin-protein ligase Ubr3"
FT /id="PRO_0000441157"
FT ZN_FING 222..293
FT /note="UBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00508"
FT ZN_FING 1607..1643
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1348..1367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1440..1464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1872..1902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1935..1954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1689
FT /note="Missing (in isoform C)"
FT /id="VSP_059031"
FT MUTAGEN 949
FT /note="F->L: In eye imaginal disks, hh signaling is
FT impaired resulting in delayed differentiation of
FT photoreceptors in the morphogenetic furrow. In Johnston's
FT organs, results in reduced auditory transduction. Often the
FT filamentous structure of NompA at the apical junction of
FT the neuronal cilium and antennal cuticle collapses into
FT puncta resulting in the detachment of scolopidia from the
FT hinge of the second and third antennal segment."
FT /evidence="ECO:0000269|PubMed:27195754,
FT ECO:0000269|PubMed:27331610"
SQ SEQUENCE 2219 AA; 247095 MW; 60CC9F408A3C45B1 CRC64;
MDEDDNLSNA DISIDDEEVV REQTHHPPMQ EDQELDNEDG SSDVDLSSVY VVPPIVSAPS
PASVRIAGGS TIGGGGVAAG AVPTTTDNSH SPFHDWDSSV AAAAAPPPPP PRTGPTTTTS
SGTAAESGAA SALSDDAGAK PSFFFGASSF SLRSRKEVAA LINTECCRGS PTPDLDSIMD
TLFNPGTPID NLDNIEWIRW LIAGGRTPQE FVKIVRSYDN HAKCGLVWVP HVVAYRCRTC
GISPCMSICR DCFKKGNHTN HDFNMFLSQA GGACDCGDTS VMKAEGFCSD HGINNRVNRD
PVPNNLLAVA EAIMPKLLFR LLQHFREHSD TPLEVQAITS YSCEEFANML IDLNNMGEIM
RKVMTRTLIN PEVYAFFMEA PCQDTRNGRF LKANREKYED AVNRFPNPEP PDEYRDLPAL
GDKLVHTTLL EEFIFWTFKF EFPQTLVCFL LNMLPDQDYK EHLTRTFVMH YSRIPSVLEM
SRDPDTLSNR VVHMSVQLFS NESLALKMVN ELSLLHVMII SLKLMMSKIL IQNTLHDPNK
NFHFVIDCTR QVMKDHCYWP LVSDFNNVLS HESVALVFLR DDNLIDMWFQ FLQMLQGMNV
NVRETASHVE FEPNSYYAAF SCELEASAYP MWSIISHLQD GTHAHLAKKI INYCVTTLHE
WLDSIYFMEA RLSMEEMMQA SFHFPLHRYL AAFVCQAVTK MGISLNDVLP SRPYLLPLLM
IHPLRVQSFF YEILAGKWVR NGLQIKGQAM TYIQANFCNS MADMDLFFLQ ICATNLPQYF
FLQNTIELFD VGQWLETAPL KQPQKAEQSS MLEGFLTFLA TLVTSRTNLG NDEATQCIIE
ISALLATENK THSQLLELMP ERSGNVHTKN FETFLKKLSV YKAPSSGSEN LEQGLFTPID
EVWEKHYDPL HVLLRAVHRR DFQSSLDRFT NYVKSKDKMP ASGNLWPPFR LPHALPATSS
FSDPCKILNS RIFHSTILSI FFRAVHTRDV SEHLLALAVF LLEIAVETSD DVGSGTGDRA
PPALAAVVES SSGPGYHGYG TGRHEPPKLF HCYPTDNLSC NLRHVVKKVS LKSRDPQVIT
SSYRSNPFYS DLDFEVEADP EQSMRMIGQG DPEGDEATGG AGLGMGAHSR RNVSQALVPM
RVPGMEVALP PDLSVVAETG VVIRQDSNED DLLREGNHAM DMSPPAALDF HFPLQQITLP
ESGMEVAIRR DLLLAETNNM GAIAGGAGGG ANASATPPAG ASNEMFSPTT PTGSGMLLPF
QRVQPVAVPS SGNMDIVPSN AMGAGGSFTS GVSGSGTGRR MNYETGGARK RSVDIAIGGS
NKDELHLDES ILSLLLKLHS QLSGTLDSFS LSDGEDQSSD DDSTMDVDCN EASTSMAAAE
STALAERGRS KRNYKNIHVS SSRIGDGPFF IGNLLRKIAK QDEQCAQSID DIRARLWPNQ
REKQAEAKAR EAKEKEERRK KARERQQKMM QDFANKQKLF MQSAAASSSG MGYGPEDEDD
EELYEEQPRE KEYDCIICNC TTPSTESNPI GLVVLVESSG IVGHRRRIAE RLPLPINAED
ESRLAHTTRL AAEFNRRTEL LSLKFGDESW YLSNNMAYDN GVHVQSCGHH VHLSCLEAYL
KTLYTTQRQP VQDRGEFYCP VCRQLSNSVL PLSPQLDRPT HLVRSGNQPF ERLVADLTDL
IKENETIPQP TKLTEAMGHA MEVMTNIAQR KVKCSSITFR KLFIFVTSIA RTNLEAEIIQ
RGGSLCTANA TRYKPKRECI VPLLHVLSVH VRVLVEWPLW SSWASLAGLP VTATEPLPAH
CLELIPSILA DPIALLLKFI LLAPLQLDQD YFTCMVKVMY NLLYYQIVVQ LCVTLTDLEC
DHIVKVYGST SVGSDNSAAE SQQQESAAGT TNNRRRAGQQ QQSSSQLGKA MALVLSQTND
LVHLRRDCIP STSSSAAASA AGSSSTTSTN HGASAATASS ATTIEVNLKS MELQLQALCL
PFLRVAALLR QHLYRHEMPE ISAPGLEFVR LVYYLELVTD SMDWDCFNAS KGLCFIPGTE
TTLPQFWCQQ LMEVRPPADT VRELVLINQH SLWQQPRLLE LPREYERLFT YYHERPCLNC
YKVPKESSIC LLCGTIVCLK QNCCAENDCC EAVRHTLSCG GGIGIFLVVT STYIIVIRGR
RACLWGSLYL DDFDEEDRDL KRGKPLYLSK DRFNLLESQW LSHKFAHTKH TWVFHRDLL
