UPL2_ARATH
ID UPL2_ARATH Reviewed; 3658 AA.
AC Q8H0T4; O64604; O64605; Q0WL35; Q9M7K6;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 3.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=E3 ubiquitin-protein ligase UPL2;
DE Short=Ubiquitin-protein ligase 2;
DE EC=2.3.2.26;
DE AltName: Full=HECT-type E3 ubiquitin transferase UPL2;
GN Name=UPL2; OrderedLocusNames=At1g70320; ORFNames=F17O7.14/F17O7.15;
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], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
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 2526-3658.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3298-3658.
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2582, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2582, 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:0000250}.
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=AAC18812.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes.; Evidence={ECO:0000305};
CC Sequence=AAC18813.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes.; Evidence={ECO:0000305};
CC Sequence=AAN72076.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF127565; AAF36455.1; -; Genomic_DNA.
DR EMBL; AC003671; AAC18812.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC003671; AAC18813.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35045.1; -; Genomic_DNA.
DR EMBL; AK230373; BAF02172.1; -; mRNA.
DR EMBL; BT002065; AAN72076.1; ALT_INIT; mRNA.
DR EMBL; BT008830; AAP68269.1; -; mRNA.
DR PIR; T01490; T01490.
DR PIR; T01491; T01491.
DR RefSeq; NP_177189.1; NM_105700.3.
DR SMR; Q8H0T4; -.
DR BioGRID; 28588; 5.
DR IntAct; Q8H0T4; 1.
DR STRING; 3702.AT1G70320.1; -.
DR iPTMnet; Q8H0T4; -.
DR PaxDb; Q8H0T4; -.
DR PRIDE; Q8H0T4; -.
DR ProteomicsDB; 234117; -.
DR EnsemblPlants; AT1G70320.1; AT1G70320.1; AT1G70320.
DR GeneID; 843368; -.
DR Gramene; AT1G70320.1; AT1G70320.1; AT1G70320.
DR KEGG; ath:AT1G70320; -.
DR Araport; AT1G70320; -.
DR TAIR; locus:2016174; AT1G70320.
DR eggNOG; KOG0939; Eukaryota.
DR HOGENOM; CLU_000215_1_0_1; -.
DR InParanoid; Q8H0T4; -.
DR OMA; LAHATCT; -.
DR OrthoDB; 25515at2759; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q8H0T4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8H0T4; baseline and differential.
DR Genevisible; Q8H0T4; 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:0061630; F:ubiquitin protein ligase 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 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; 1.
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..3658
FT /note="E3 ubiquitin-protein ligase UPL2"
FT /id="PRO_0000120344"
FT DOMAIN 1271..1312
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 1318..1337
FT /note="UIM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 3317..3658
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT REGION 884..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1331..1360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1702..1733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2004..2038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2052..2072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2113..2204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2293..2313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2417..2487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2503..2591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2958..2987
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1338..1360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2012..2031
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2118..2144
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2160..2204
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2294..2313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2417..2436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2503..2518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2534..2571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2968..2987
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 3625
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT MOD_RES 2582
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19376835"
FT CONFLICT 153..154
FT /note="NL -> ES (in Ref. 1; AAF36455)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="Q -> R (in Ref. 1; AAF36455)"
FT /evidence="ECO:0000305"
FT CONFLICT 1759
FT /note="R -> S (in Ref. 1; AAF36455)"
FT /evidence="ECO:0000305"
FT CONFLICT 1771
FT /note="D -> N (in Ref. 1; AAF36455)"
FT /evidence="ECO:0000305"
FT CONFLICT 2322
FT /note="S -> I (in Ref. 1; AAF36455)"
FT /evidence="ECO:0000305"
FT CONFLICT 3298
FT /note="I -> F (in Ref. 5; AAN72076)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3658 AA; 403616 MW; C6D74894C0264444 CRC64;
MKLRRRRASE VPTKISLFIN SVTSVPLELI QEPLASFRWE FDKGDFHHWV DLFYHFDTFF
EKHVKVRKDL RIEEEFDESD PPFPKDAVLQ VLRVIRLVLE NCTNKQFYTS YEQHLSLLLA
STDADVVEAC LQTLAAFLKR PTGKYSIRDA SLNLKLFSLA QGWGGKEEGL GLTSCATEHS
CDQLFLQLGC TLLFEFYASD ESPSELPGGL QVIHVPDVSM RSESDLELLN KLVIDHNVPP
SLRFALLTRL RFARAFSSLA TRQQYTCIRL YAFIVLVQAS GDTENVVSFF NGEPEFVNEL
VTLVSYEDTV PAKIRILCLQ SLVALSQDRT RQPTVLTAVT SGGHRGLLSG LMQKAIDSVI
CNTSKWSLAF AEALLSLVTV LVSSSSGCSA MREAGLIPTL VPLIKDTDPQ HLHLVSTAVH
ILEVFMDYSN PAAALFRDLG GLDDTIFRLK QEVSRTEDDV KEIVCCSGSN GPEDDTEQLP
YSEALISYHR RLLLKALLRA ISLGTYAPGN TNLYGSEESL LPECLCIIFR RAKDFGGGVF
SLAATVMSDL IHKDPTCFNA LDSAGLTSAF LDAISDEVIC SAEAITCIPQ CLDALCLNNS
GLQAVKDRNA LRCFVKIFSS PSYLKALTSD TPGSLSSGLD ELLRHQSSLR TYGVDMFIEI
LNSILIIGSG MEATTSKSAD VPTDAAPVPM EIDVDEKSLA VSDEAEPSSD TSPANIELFL
PDCVCNVARL FETVLQNAEV CSLFVEKKGI DTVLQLFSLP LMPLSTSLGQ SFSVAFKNFS
PQHSAGLARI LCSYLREHLK KTNNLLVSIE GTQLLKLESA VQTKILRSLS CLEGMLSLSN
FLLKGSASVI SELSAANADV LKELGITYKQ TIWQMALCND TKEDEKKSVD RASDNSVSAS
SSTAERESDE DSSNALAVRY TNPVSIRSSS SQSIWGGHRE FLSVVRSGRG VHGHTRHAIA
RMRGGRTRRH LESFNFDSEI PADLPVTSSS HELKKKSTEV LIAEILNKLN CTLRFFFTSL
VKGFTSANRR RIDGPSLSSA SKTLGTALAK VFLEALNFQG YGAAAGPDTS LSLKCRYLGK
VVDDITFLTF DTRRRVCFTA MVNSFYVHGT FKELLTTFEA TSQLLWKVPF SIRASSTENE
KSGERNLWSH SKWLVDTLQN YCRALDYFVN STYLLSPTSQ TQLLVQPASV DLSIGLFPVP
REPETFVRNL QSQVLEVILP IWNHPMFPDC NPNFVASVTS LVTHIYSGVV DTRENRSGAT
QGTNQRALPL QPDEAIVGMI VEMGFSRSRA EDALRRVGTN SVEMAMDWLF TNPEDPVQED
DELAQALALS LGNSSETPKL EDTEKPVDVP QEEAEPKEPP VDEVIAASVK LFQSDDSIAF
PLVDLFVTLC NRNKGEDRPK IVFYLIQQLK LVQLDFSKDT GALTMIPHIL ALVLSEDDNT
REIAAQDGIV AVAIGILTDF NLKSESETDI LAPKCISALL LVLSMMLQAQ TRLSSEYVEG
NQGGSLVLSD SPQDSTAALK DALSSDVAKG ESNQALESMF GKSTGYLTME ESSKVLLIAC
GLIKQRVPAM IMQAVLQLCA RLTKSHALAI QFLENGGLSS LFNLPKKCFF PGYDTVASVI
VRHLVEDPQT LQIAMETEIR QTLSGKRHIG RVLPRTFLTT MAPVISRDPV VFMKAVASTC
QLESSGGTDF VILTKEKEKP KVSGSEHGFS LNEPLGISEN KLHDGSGKCS KSHRRVPTNF
IQVIDQLIDI VLSFPGLKRQ EGEAANLISM DVDEPTTKVK GKSKVGEPEK AELGSEKSEE
LARVTFILKL LSDIVLMYLH GTSVILRRDT EISQLRGSNL PDDSPGNGGL IYHVIHRLLP
ISLEKFVGPE EWKEKLSEKA SWFLVVLCSR SNEGRKRIIN ELTRVLSVFA SLGRSSSQSV
LLPDKRVLAF ANLVYSILTK NSSSSNFPGC GCSPDVAKSM IDGGTIQCLT SILNVIDLDH
PDAPKLVTLI LKSLETLTRA ANAAEQLKSE VPNEQKNTDS DERHDSHGTS TSTEVDELNQ
NNSSLQQVTD AVDNGQEQPQ VSSQSEGERG SSLTQAMLQE MRIEGDETIL PEPIQMDFFR
EEIEGDQIEM SFHVEDRADD DVDDDMDDEG EDDEGDDEDA DSVEDGAGVM SIAGTDVEDP
EDTGLGDEYN DDMVDEDEED EDEYNDDMVD EDEDDEDEYN DDMVDEDEDD FHETRVIEVR
WREALDGLDH FQIVGRSGGG NGFIDDITAE PFEGVNVDDL FALRRSLGFE RRRQTGRSSF
DRSGSEVHGF QHPLFSRPSQ TGNTASVSAS AGSISRHSEA GSYDVAQFYM FDSPVLPFDQ
VPVDPFSDRL GGGGAPPPLT DYSVVGMDSS RRGVGDSRWT DVGHPQPSSL SASIAQLIEE
HFITNLRASA PVDTVVERET NTTEVQEQQQ PDVPPSVGSE TVLGDGNEGG EQSEEHELLN
NNEVMHPLPL NSTPNEIDRM EVGEGGGAPI EQVDREAVHL ISSAQGQSDT SGIQNVSVTA
IPPPVDDPDS NFQPSVDVDM SSDGAEGNQS VQPSPLDGDN NELSSMEATQ DVRNDEQVDE
GSLDGRAPEV NAIDPTFLEA LPEDLRAEVL ASQQAQSVQP PTYEPPSVDD IDPEFLAALP
PEIQREVLAQ QRAQRMLQQS QGQPVDMDNA SIIATLPADL REEVLLTSSE AVLAALPPPL
LAEAQMLRDR AMRHYQARSR VFGSSHRLNN RRNGLGYRLT GMERGVGVTI GQRDVSSSAD
GLKVKEIEGD PLVNADALKS LIRLLRLAQP LGKGLLQRLL LNLCAHSFTR ANLVQLLLDM
IRPEMETLPS ELALTNPQRL YGCQLNVVYG RSQLLNGLPP LVFRRVLEVL TYLATNHSAV
ADMLFYFDSS LLSQLSSRKG KEKVTHETDS RDLEIPLVVF LKLLNRPQLL QSTSHLALVM
GLLQVVVYTA ASRIEGWSPS SGVPEKLENK PVGEEASSET QKDAESELSV ARRKNCAELY
NIFLQLPQSD LCNLCMLLGY EGLSDKIYSL AGEVLKKLAA VDVTHRKFFT KELSELASGL
SSSTVRVLAT LSTTQKMSQN TCSMAGASIL RVLQVLSSLT STIDDSNVGT DKETDQEEQN
IMQGLKVALE PLWQELGQCI SMTELQLDHT AATSNVNPGD HVLGISPTSS LSPGTQSLLP
LIEAFFVLCE KIQTPSMLQQ DATVTAGEVK ESSTHGSSSK TIVDSQKKID GSVTFSKFVE
KHRRLLNSFV RQNPSLLEKS FSMMLKAPRL IDFDNKKAYF RSRIRHQHDQ HISGPLRISV
RRAYVLEDSY NQLRMRSPQD LKGRLNVQFQ GEEGIDAGGL TREWYQLLSR VIFDKGALLF
TTVGNDATFQ PNPNSVYQTE HLSYFKFVGR MVAKALFDGQ LLDVYFTRSF YKHILGVKVT
YHDIEAVDPD YYKNLKWLLE NDVSDILDLT FSMDADEEKH ILYEKTEVTD YELKPGGRNI
RVTEETKHEY VDLVADHILT SAIRPQINAF LEGLNELIPR ELVSIFNDKE LELLISGLPE
IDFDDLKANT EYTSYTVGSP VIRWFWEVVK AFSKEDMARF LQFVTGTSKV PLEGFKALQG
ISGPQRLQIH KAYGSPERLP SAHTCFNQLD LPEYQSKEQV QERLLLAIHE ANEGFGFA