UPL1_ARATH
ID UPL1_ARATH Reviewed; 3681 AA.
AC Q8GY23; F4I1Y3; Q9LG27; Q9M7K7;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=E3 ubiquitin-protein ligase UPL1;
DE Short=Ubiquitin-protein ligase 1;
DE EC=2.3.2.26;
DE AltName: Full=HECT-type E3 ubiquitin transferase UPL1;
GN Name=UPL1; OrderedLocusNames=At1g55860; ORFNames=F14J16.14, F14J16.37;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROBABLE FUNCTION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND MUTAGENESIS OF CYS-3648.
RC STRAIN=cv. Columbia;
RX PubMed=10571878; DOI=10.1046/j.1365-313x.1999.00590.x;
RA Bates P.W., Vierstra R.D.;
RT "UPL1 and 2, two 405 kDa ubiquitin-protein ligases from Arabidopsis
RT thaliana related to the HECT-domain protein family.";
RL Plant J. 20:183-195(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3533-3681.
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP GENE FAMILY ORGANIZATION.
RX PubMed=12969426; DOI=10.1046/j.1365-313x.2003.01844.x;
RA Downes B.P., Stupar R.M., Gingerich D.J., Vierstra R.D.;
RT "The HECT ubiquitin-protein ligase (UPL) family in Arabidopsis: UPL3 has a
RT specific role in trichome development.";
RL Plant J. 35:729-742(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2598, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2598, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: Probable E3 ubiquitin-protein ligase which mediates
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins. {ECO:0000303|PubMed:10571878}.
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 -!- TISSUE SPECIFICITY: Widely expressed. Expressed in root, stem, cauline
CC and rosette leaf, seedling and flower (at protein level).
CC {ECO:0000269|PubMed:10571878}.
CC -!- DEVELOPMENTAL STAGE: Constitutively expressed throughout development
CC post-germination (at protein level). {ECO:0000269|PubMed:10571878}.
CC -!- SIMILARITY: Belongs to the UPL family. TOM1/PTR1 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79338.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAC42550.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF127564; AAF36454.1; -; Genomic_DNA.
DR EMBL; AC002304; AAF79338.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33309.2; -; Genomic_DNA.
DR EMBL; AK117912; BAC42550.1; ALT_INIT; mRNA.
DR PIR; H96599; H96599.
DR RefSeq; NP_001185245.1; NM_001198316.2.
DR SMR; Q8GY23; -.
DR BioGRID; 27261; 1.
DR STRING; 3702.AT1G55860.1; -.
DR iPTMnet; Q8GY23; -.
DR PaxDb; Q8GY23; -.
DR PRIDE; Q8GY23; -.
DR ProteomicsDB; 234116; -.
DR EnsemblPlants; AT1G55860.1; AT1G55860.1; AT1G55860.
DR GeneID; 842036; -.
DR Gramene; AT1G55860.1; AT1G55860.1; AT1G55860.
DR KEGG; ath:AT1G55860; -.
DR Araport; AT1G55860; -.
DR TAIR; locus:2012060; AT1G55860.
DR eggNOG; KOG0939; Eukaryota.
DR HOGENOM; CLU_000215_1_0_1; -.
DR InParanoid; Q8GY23; -.
DR OMA; ADEMKYG; -.
DR OrthoDB; 25515at2759; -.
DR PhylomeDB; Q8GY23; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q8GY23; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8GY23; baseline and differential.
DR Genevisible; Q8GY23; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISS:TAIR.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
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; ISS:TAIR.
DR CDD; cd00078; HECTc; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR010309; E3_Ub_ligase_DUF908.
DR InterPro; IPR010314; E3_Ub_ligase_DUF913.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR025527; HUWE1/Rev1_UBM.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR003903; UIM_dom.
DR Pfam; PF06012; DUF908; 2.
DR Pfam; PF06025; DUF913; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00627; UBA; 1.
DR Pfam; PF14377; UBM; 3.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
DR SUPFAM; SSF56204; SSF56204; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS50330; UIM; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome; Transferase; Ubl conjugation pathway.
FT CHAIN 1..3681
FT /note="E3 ubiquitin-protein ligase UPL1"
FT /id="PRO_0000120343"
FT DOMAIN 1269..1310
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 1316..1335
FT /note="UIM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 3340..3681
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT REGION 882..912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1332..1358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1768..1802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2015..2094
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2125..2151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2253..2287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2401..2435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2483..2505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2537..2606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2975..3003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3228..3254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1336..1358
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1773..1802
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2019..2042
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2043..2089
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2131..2151
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2550..2587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2985..3003
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 3648
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT MOD_RES 2598
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19376835"
FT MUTAGEN 3648
FT /note="C->S,A: Abolishes ability to conjugate ubiquitin in
FT vitro."
FT /evidence="ECO:0000269|PubMed:10571878"
FT CONFLICT 865
FT /note="T -> S (in Ref. 1; AAF36454)"
FT /evidence="ECO:0000305"
FT CONFLICT 1186
FT /note="A -> T (in Ref. 1; AAF36454)"
FT /evidence="ECO:0000305"
FT CONFLICT 1207
FT /note="N -> K (in Ref. 1; AAF36454)"
FT /evidence="ECO:0000305"
FT CONFLICT 3027
FT /note="L -> S (in Ref. 1; AAF36454)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3681 AA; 405000 MW; 3954A6ABDD574189 CRC64;
MKLRRRRASE VPSKIKSFIN SVTSVPLELI HEPLACFRWE FDKGDFHHWV DLFNYFDTFF
EKHVQVRKDL HIEENFEESD PPFPKDAVLQ VLRVIRVVLE NCTNKHFYSS YEQHLSLLLA
STDADVVEAC LQTLAAFLKR QIGKYSIRDA SLNSKLFSLA QGWGGKEEGL GLTSCAAENS
CDQVSLQLGR TLHFEFYPSD ESPSELPGGL QVIHVPDVSI CAESDLELLN KLVIDHNVPP
SLRFALLTRM RFARAFSSLA TRQQFTCIRL YAFVVLVQAS GDTENVVSFF NGEPEFVNEL
VTLVSYEDTV PEKIRILCLL SLVALSQDRT RQPTVLTAVT SGGHRGLLSG LMQKAIDSVV
CITSKWSLAF AEALLSLVTV LVSSSSGCSA MREAGLIPTL VPLIKDTDPQ HLHLVSAAVH
ILEAFMDYSN PAAALFRDLG GLDDTIFRLK LEVSRTEDDV KEKNCSSDSN GPDTEQLPYS
EALISYHRRL LLKALLRAIS LGTYAPGNTN LYGSEESLLP ECLCIIFRRA KDFGGGVFSL
AATVMSDLIH KDPTCFNALD SAGLTSTFLD AISDEVICSA EAITCIPQCL DALCLNNSGL
QAVKDRNALR CFVKIFTSPS YLRALTGDTP GSLSSGLDEL LRHQSSLRTY GVDMFIEILN
SMLIIGSGME ATTSKSADVP TSAAPVPMEI DVDEKSLAVS DEAEPSSDTS PANIELFLPD
CVCNVARLFE TVLQNAEVCS LFVEKKGIDA VLQLFSLPLM PLSTSLGQSF SVAFKNFSPQ
HSAGLARIVC SYLREHLKKT KILLVSIEGT QLLKLESAIQ TKILRSLSCL EGMLSLSNFL
LKGSASVISE LSAADADVLK ELGITYKQTI WQMALCNDTK EDEKKSVDRG SDNSVSASSS
TAERESDEDS SNALAVRYTN PVSIRSSSSQ SIWGGDREFL SIVRSGEGIH GRTRHAIARM
RGGRTRRHLE SFNFDSEIPA DLPVTSSSHE LKKKSTEVLI AEILNKLNCT LRFFFTALVK
GFTSANRRRI DGASLSSASK TLGTALAKVF LEALNFDGYG AAAGHEKSLS VKCRYLGKVV
DDITFLSFDT RRRVCFTAMV NSFYVHGTFK ELLTTFEATS QLLWTVPFSI PASSTENEKP
GERNIWSHSK WLVDTLQNYC RALDYFVNST YLLSPTSQTQ LLVQPASVGL SIGLFPVPRE
PETFVRNLQS QVLDVILPIW NHPMFPDCNP NFVASVTSLV THIYSGVVDA RENRSGVTRG
INQRALPLQL DESIVGMIVE MGFSRSRAEI ALRRVGTNSV EMAMDWLFTN PEQPVQEDDE
LAQALALSLG NSSETPKLED TEKPVDVPQE EAEPKEPPVD EVIAASVKLF QSDDSMAFPL
MDLFVTLCNR NKGEDRPKIV SYLIQQLKLV QLDFSKDTGA LTMIPHILAL VLSEDDNTRE
IAAQDGIVTV AIGILTDFNL KSESETEILA PKCISALLLV LSMMLQAQTK LSSEYVEGNQ
GGSLVPSDSP QDSTAALKDA LSSDVAKGES NQALELIFGK STGYLTMEEG HKALLIACGL
IKQHVPAMIM QAVLQLCARL TKSHALAIQF LENGGLSSLF NLPKKCCFPG YDTVASVIVR
HLVEDPQTLQ IAMETEIRQT LSGKRHIGRV LPRTFLTTMA PVISRDPVVF MKAVASTCQL
ESSGGRDFVI LSKEKEKPKV SGSEHGFSLN EPLGISENKL HDVSGKCSKS HRRVPANFIQ
VIDQLIDLVL SFPRVKRQED GETNLISMEV DEPTTKVKGK SKVGEPEKAS SSRVGEPEKA
EIPEKSEELA RVTFILKLLS DIVLMYSHGT SVILRRDTEI SQLRGSNLPD DSPGNGGLIY
HVIHRLLPIS LEKFVGPEEW KEKLSEKASW FLVVLCSRSN EGRKRIINEL SRVLSVFASL
GRSSSKSVLL PDKRVLAFAN LVYSILTKNS SSSSSNFPGC GCSPDVAKSM MDGGTIQCLT
SILHVIDLDH PDAPKLVTLI LKSLETLTRA ANAAEQLKSE VPNEKKNRDS DERHDSHGNS
TETEADELNQ NNSSLQQVTD AAGNGQEQAQ VSSQSAGERG SSQTQAMPQD MRIEGDETIL
PEPIQMDFMR EEIEGDQIEM SFHVENRADD DVDDDMGDEG EDDEGDDEDA DLVEDGAGVM
SLAGTDVEDP EDTGLGDEYN DDMVDEDDDD FHENRVIEVR WREALDGLDH FQILGRSGGG
NGFIDDITAE PFEGVNVDDL FALRRPLGFE RRRQTGRSSL DRSGSEVHGF QHPLFSRPSQ
TGNTASVSAS AGSISRHSEA GSYDVAQFYM FDTPVLPFDQ VPVDPFSARL AGGGAPPPLT
DYSVVGMDSS RRGVGDSRWT DIGHPQPSSL SASIAQLIEE HFISNLRASA PVNTVVERET
NTTEIQEQLH PDVPPSVGSE TVLGDGNEGG QQSEERELLN NNENVNNPPD VMAESFAQGQ
ANLASPVSQD TGESLQQLEV MQPLPLNSTP NEIDRMEVGE GDGAPIDQVD HEAVHLISTA
QGQPDTSSIQ NVSVTAIAPP VDDPDSNFQP SVDVDMSSDG AEGNQSVQPS PLDGDNNELS
SMEATENVRN DEQVEEGSLD GRAPEVNAID PTFLEALPED LRAEVLASQQ AQSVQPPTYE
PPPVDDIDPE FLAALPPDIQ TEVLAQQRAQ RMVQQSQGQA VDMDNASIIA TLPADLREEV
LLTSSEAVLA ALPSPLLAEA QMLRDRAMSH YQARSSVFGS SHRLNNRRNG LGYNRLTGMD
RGVGVTIGQR AVSSSADGLK VKEIEGDPLV NADALKSLIR LLRLAQPLGK GLLQRLLLNL
CAHSFTRANL VQLLLDMIRP EMETSPSELA ITNPQRLYGC QSNVVYGRSQ LLNGLPPLVF
RRVLEVLTYL ATNHSAVADM LFYFDSSLLS QLSSRKGKEK VTHVTDSRDL EIPLVVFLKL
LNRPQLLQST SHLGLVMGLL QVVVYTAASR IEGWSPSSGV PEKLENKPVG EEASSETRKD
AESELVGEAD LSVARRKNCA EIYNIFLQLP QSDLCNLCIL LGYEGLSDKI YSLAGEVLKK
LAAVDVAHRK FFTKELSELA SSLSSSTVRE LATLSSKQKM SRSTGSMAGA SILRVLQVLS
SLTSPIDESN VGTERETEQE EQNIMQRLNV ALEPLWHELS QCISMTELQL DHTAAASNIN
PGDHVLGISP TSSLSPGTQR LLPLIEAFFV LCEKIQTPSM LQQDTNVTAG EVKESSAHGS
SSKTSVDSQK KTDGSVTFSK FAEKHRRLLN SFIRQNPSLL EKSLSMMLKA PRLIDFDNKK
AYFRSRIRHQ HDQHISGPLR ISVRRAYVLE DSYNQLRMRS PQDLKGRLNV QFQGEEGIDA
GGLTREWYQL LSRVIFDKGA LLFTTVGNDA TFQPNPNSVY QTEHLSYFKF VGRMVAKALF
DGQLLDVYFT RSFYKHILGV KVTYHDIEAV DPDYYKNLKW LLENDVSDIL DLTFSMDADE
EKHILYEKTE VTDYELKPGG RNIRVTEETK HEYVDLVAGH ILTNAIRPQI NAFLEGFNEL
IPRELVSIFN DKELELLISG LPEIDFDDLK ANTEYTSYTA GSPVIHWFWE VVKAFSKEDM
ARFLQFVTGT SKVPLEGFKA LQGISGPQRL QIHKAYGAPE RLPSAHTCFN QLDLPEYQSK
EQLQERLLLA IHEASEGFGF A
