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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
 
 
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