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MLN51_ARATH
ID   MLN51_ARATH             Reviewed;         605 AA.
AC   Q93ZJ9; Q9S770;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 126.
DE   RecName: Full=Protein MLN51 homolog;
DE   AltName: Full=Protein CASC3 homolog {ECO:0000305};
DE   AltName: Full=Protein barentsz {ECO:0000305};
DE            Short=Btz {ECO:0000305};
GN   Name=MLN51 {ECO:0000303|PubMed:19435936}; Synonyms=CASC3 {ECO:0000305};
GN   OrderedLocusNames=At1g80000 {ECO:0000312|Araport:AT1G80000};
GN   ORFNames=F18B13.8 {ECO:0000312|EMBL:AAD55481.1},
GN   F19K16.3 {ECO:0000312|EMBL:AAG52246.1};
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 [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   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA   Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA   Shinozaki K.;
RT   "Analysis of multiple occurrences of alternative splicing events in
RT   Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL   DNA Res. 16:155-164(2009).
RN   [5]
RP   INTERACTION WITH EIF4A3.
RX   PubMed=19435936; DOI=10.1105/tpc.108.060434;
RA   Koroleva O.A., Calder G., Pendle A.F., Kim S.H., Lewandowska D.,
RA   Simpson C.G., Jones I.M., Brown J.W.S., Shaw P.J.;
RT   "Dynamic behavior of Arabidopsis eIF4A-III, putative core protein of exon
RT   junction complex: fast relocation to nucleolus and splicing speckles under
RT   hypoxia.";
RL   Plant Cell 21:1592-1606(2009).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, 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: Core component of the splicing-dependent multiprotein exon
CC       junction complex (EJC) deposited at splice junctions on mRNAs. The EJC
CC       is a dynamic structure consisting of core proteins and several
CC       peripheral nuclear and cytoplasmic associated factors that join the
CC       complex only transiently either during EJC assembly or during
CC       subsequent mRNA metabolism. The EJC marks the position of the exon-exon
CC       junction in the mature mRNA for the gene expression machinery and the
CC       core components remain bound to spliced mRNAs throughout all stages of
CC       mRNA metabolism thereby influencing downstream processes including
CC       nuclear mRNA export, subcellular mRNA localization, translation
CC       efficiency and nonsense-mediated mRNA decay (NMD). Stimulates the
CC       ATPase and RNA-helicase activities of EIF4A3.
CC       {ECO:0000250|UniProtKB:O15234}.
CC   -!- SUBUNIT: Weekly interacts with EIF4A3. {ECO:0000269|PubMed:19435936}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O15234}. Cytoplasm
CC       {ECO:0000250|UniProtKB:O15234}. Note=Nucleocytoplasmic shuttling
CC       protein. Travels to the cytoplasm as part of the exon junction complex
CC       (EJC) bound to mRNA. {ECO:0000250|UniProtKB:O15234}.
CC   -!- SIMILARITY: Belongs to the CASC3 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD55481.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAG52246.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC009322; AAD55481.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC011717; AAG52246.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE36342.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE36343.1; -; Genomic_DNA.
DR   EMBL; CP002684; ANM60522.1; -; Genomic_DNA.
DR   EMBL; AY057486; AAL09720.1; -; mRNA.
DR   EMBL; BT004550; AAO42796.1; -; mRNA.
DR   EMBL; AK317141; BAH19827.1; -; mRNA.
DR   PIR; D96831; D96831.
DR   RefSeq; NP_001322803.1; NM_001334946.1.
DR   RefSeq; NP_565226.1; NM_106649.3.
DR   RefSeq; NP_974187.1; NM_202458.2.
DR   AlphaFoldDB; Q93ZJ9; -.
DR   IntAct; Q93ZJ9; 15.
DR   STRING; 3702.AT1G80000.2; -.
DR   iPTMnet; Q93ZJ9; -.
DR   PaxDb; Q93ZJ9; -.
DR   PRIDE; Q93ZJ9; -.
DR   ProteomicsDB; 251412; -.
DR   EnsemblPlants; AT1G80000.1; AT1G80000.1; AT1G80000.
DR   EnsemblPlants; AT1G80000.2; AT1G80000.2; AT1G80000.
DR   EnsemblPlants; AT1G80000.3; AT1G80000.3; AT1G80000.
DR   GeneID; 844340; -.
DR   Gramene; AT1G80000.1; AT1G80000.1; AT1G80000.
DR   Gramene; AT1G80000.2; AT1G80000.2; AT1G80000.
DR   Gramene; AT1G80000.3; AT1G80000.3; AT1G80000.
DR   KEGG; ath:AT1G80000; -.
DR   Araport; AT1G80000; -.
DR   TAIR; locus:2016224; AT1G80000.
DR   eggNOG; ENOG502SAIS; Eukaryota.
DR   HOGENOM; CLU_016753_1_0_1; -.
DR   InParanoid; Q93ZJ9; -.
DR   OMA; VDQRQNK; -.
DR   OrthoDB; 675280at2759; -.
DR   PhylomeDB; Q93ZJ9; -.
DR   PRO; PR:Q93ZJ9; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q93ZJ9; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0035145; C:exon-exon junction complex; IEA:InterPro.
DR   GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR018545; Btz_dom.
DR   InterPro; IPR044796; MLN51_plant.
DR   PANTHER; PTHR46837; PTHR46837; 1.
DR   Pfam; PF09405; Btz; 1.
DR   SMART; SM01044; Btz; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; mRNA processing; mRNA splicing; mRNA transport;
KW   Nonsense-mediated mRNA decay; Nucleus; Phosphoprotein; Reference proteome;
KW   RNA-binding; Translation regulation; Transport.
FT   CHAIN           1..605
FT                   /note="Protein MLN51 homolog"
FT                   /id="PRO_0000440128"
FT   REGION          1..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          101..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          151..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          350..380
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          544..605
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..30
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..88
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        151..205
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        207..229
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        248..267
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        366..380
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        550..567
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        577..605
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         30
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19376835"
SQ   SEQUENCE   605 AA;  65693 MW;  7FF61B6C323EE41F CRC64;
     MAPDGVEDSD YESDPDELNR SLATRRREAS DDDEDDEEAD DHDKLRAAIQ IHSDEHSGVV
     VVDSDDNEGL HIEDSYGDDD DEEEDGDYGQ VDDHVEYIAD NNDKTIVAGN GTDDSAATDL
     VDGEEQKKKE PFAVPTAGAF YMHDDRFQEL DAASNRRMRG GRRLWQSRDE RKWGHDKFEE
     MNTQKQQYDR RTSRGRGRGR GQGRGQDRGQ SRGNNSKEFT GNGHQNQFPK AVTRGRGARR
     YEVALRNGNQ APSVQTKQSQ NSSVEVSHVD LGRPPTETAT LETEAIQAKK NVFASSLNSA
     SPPFYPSRSN NNLAQKDVQA GMGRLHINEN PNPTGKKFGN TKSSSLWGRT AQTTSHGRGV
     PPHGQVLYQQ SPNQGDKVSS PMQIRGMPKG TDQSCTQLPG QVFNQHSAVI SLLPSSPPKT
     GSSENPYLSG EIESAVETGA LVAKGKGSLQ PSGRGSFMYG GTQFMGPAGM AAGHGNPNFP
     AFLPVMQFGG QHGGVPTFGM ALPGYFQPEH GTGNPEMTWL PILAGPGALG GSYCPPYTVL
     DGSYQADKPG LPSSAGSSSQ ENSSNNPNDE EPMERPEVTN NGNSQRSNSN PNKQPRRYSE
     MSFSK
 
 
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