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SAD2H_ARATH
ID   SAD2H_ARATH             Reviewed;        1030 AA.
AC   F4J738; B9DFH6; Q9LYT4;
DT   07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Importin beta-like SAD2 homolog {ECO:0000305};
GN   OrderedLocusNames=At3g59020 {ECO:0000312|Araport:AT3G59020};
GN   ORFNames=F17J16.70 {ECO:0000312|EMBL:CAB86930.1};
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=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(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; TISSUE=Rosette leaf {ECO:0000312|EMBL:BAH19493.1};
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   [4]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=16889648; DOI=10.1111/j.1365-313x.2006.02833.x;
RA   Verslues P.E., Guo Y., Dong C.H., Ma W., Zhu J.K.;
RT   "Mutation of SAD2, an importin beta-domain protein in Arabidopsis, alters
RT   abscisic acid sensitivity.";
RL   Plant J. 47:776-787(2006).
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC   -!- FUNCTION: Functions probably in nuclear protein import, either by
CC       acting as autonomous nuclear transport receptor or as an adapter-like
CC       protein in association with other importin subunits.
CC       {ECO:0000250|UniProtKB:F4IRR2}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:F4IRR2}. Nucleus
CC       {ECO:0000250|UniProtKB:F4IRR2}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoform are produced. According to EST sequences.
CC         {ECO:0000305};
CC       Name=1;
CC         IsoId=F4J738-1; Sequence=Displayed;
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditions. {ECO:0000269|PubMed:16889648}.
CC   -!- SIMILARITY: Belongs to the importin beta family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB86930.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL163527; CAB86930.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE79862.1; -; Genomic_DNA.
DR   EMBL; AK316774; BAH19493.1; -; mRNA.
DR   PIR; T47784; T47784.
DR   RefSeq; NP_001030888.1; NM_001035811.2. [F4J738-1]
DR   AlphaFoldDB; F4J738; -.
DR   SMR; F4J738; -.
DR   STRING; 3702.AT3G59020.2; -.
DR   iPTMnet; F4J738; -.
DR   PaxDb; F4J738; -.
DR   PRIDE; F4J738; -.
DR   ProteomicsDB; 232728; -. [F4J738-1]
DR   EnsemblPlants; AT3G59020.2; AT3G59020.2; AT3G59020. [F4J738-1]
DR   GeneID; 825071; -.
DR   Gramene; AT3G59020.2; AT3G59020.2; AT3G59020. [F4J738-1]
DR   KEGG; ath:AT3G59020; -.
DR   Araport; AT3G59020; -.
DR   TAIR; locus:2077715; AT3G59020.
DR   eggNOG; KOG1991; Eukaryota.
DR   HOGENOM; CLU_004196_0_0_1; -.
DR   InParanoid; F4J738; -.
DR   PhylomeDB; F4J738; -.
DR   PRO; PR:F4J738; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; F4J738; baseline and differential.
DR   Genevisible; F4J738; AT.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR001494; Importin-beta_N.
DR   InterPro; IPR013713; XPO2_central.
DR   Pfam; PF08506; Cse1; 1.
DR   Pfam; PF03810; IBN_N; 1.
DR   SMART; SM00913; IBN_N; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   PROSITE; PS50166; IMPORTIN_B_NT; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm; Nucleus; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..1030
FT                   /note="Importin beta-like SAD2 homolog"
FT                   /id="PRO_0000431578"
FT   DOMAIN          25..99
FT                   /note="Importin N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00115"
FT   REGION          886..928
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          940..964
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        888..921
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        944..963
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CONFLICT        587
FT                   /note="A -> T (in Ref. 3; BAH19493)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1030 AA;  117769 MW;  E37DDA2E9EAA06CB CRC64;
     MDLPSLALIV GAAAFSPNPD ERRAAEQSLN QLQHTPQHLI RILQIIVDGG SDLSVRQSAS
     IHFKNFIAKH WEPHSGDQNI ILPSDKNVVR NQILVFVSQV PPILRVQMGE CLKTIIYADY
     PEQWPELLDW VKQNLQKPQV YGALFVLRIL SSKYEFKSDE DRAPIHRVVE ETFPHLLNIF
     NNLVHVENPS LEVADHIKLI CKIFWSCIYL ELPRPLFDPN FFNAWMGLFL NILERPVPVE
     GQPEDPELRK SWGWWKAKKW IAHILNRLYT RFGDLKLQNP DNKAFAQMFQ INYAAKILEC
     HLKLLNAIRI GGYLPDRVIN LILQYLSNSI SKSSMYNLLQ PHLNTLLFEI VFPLMCFNDN
     DQMLWDEDPH EYVRKGYDII EDLYSPRTAS MDFVTELVRK RGKENFPKFI QFVVDIFKRY
     NEASLENKPY RLKDGALLAV GTLCDKLRQT EPYKSELENM LVQHVFPEFS SPAGHLRAKA
     AWVAGQYANI DFSDQSNFSK ALHCVISGMC DLELPVRVDS VFALRSFIEA CKDLDEIRPV
     LPQLLDEFFK LMKEVENEDL AFTLETIVYK FGEEISPYAL GLCQNLASAF WRCIDTDNGD
     DETDDAGALA AVGCLRAIST ILESISSLPH LYGQIEPQLL PIMRKMLTTD GQDVFEEVLE
     IVSYITTFSP TISLEMWSLW PLMMEALVDW AIDFFPNILV PLHNYISRGT GHYLTCKEPD
     YQQNLWNVIS VLMANKNIDD SDLEPAPKLL GIVLQTCKGQ VDQWVEPYLR ITLDRLRGAE
     KSSFKCLLVE VVANAFYYNT PLALGILQRF GIATEIFTLW FQMLQEKKKS GARSNFKREH
     DKKVCILGLT SLFSLPAGQL PGEVLPHVFR ALLELLVAYK DQLAEAAKAE EEEEDEDGDD
     DDMDEFQTDD EDEDGDDENP DETDGSTLRK LAAQAKDFRS YSDDDDFSDD DFSDDEELES
     PIDEVDPFVL FMDAVTAMQV SDSPRFQSLT QTLDPHYHGL ASTIAQHTEL RRAEILKEKL
     EKQSSATVAS
 
 
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