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SAC3B_ARATH
ID   SAC3B_ARATH             Reviewed;        1697 AA.
AC   F4JAU2; Q9M8I9;
DT   17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=SAC3 family protein B {ECO:0000303|PubMed:19843313};
GN   Name=SAC3B {ECO:0000303|PubMed:19843313};
GN   OrderedLocusNames=At3g06290 {ECO:0000312|Araport:AT3G06290};
GN   ORFNames=F28L1.23 {ECO:0000312|EMBL:AAF30322.1};
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 {ECO:0000312|Proteomes:UP000006548};
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 {ECO:0000312|Proteomes:UP000006548};
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   INTERACTION WITH EER5; SAC3A AND CML19, SUBCELLULAR LOCATION, DISRUPTION
RP   PHENOTYPE, AND FUNCTION.
RX   PubMed=19843313; DOI=10.1111/j.1365-313x.2009.04048.x;
RA   Lu Q., Tang X., Tian G., Wang F., Liu K., Nguyen V., Kohalmi S.E.,
RA   Keller W.A., Tsang E.W., Harada J.J., Rothstein S.J., Cui Y.;
RT   "Arabidopsis homolog of the yeast TREX-2 mRNA export complex: components
RT   and anchoring nucleoporin.";
RL   Plant J. 61:259-270(2010).
RN   [4]
RP   INTERACTION WITH UCH1 AND UCH2.
RX   PubMed=22951400; DOI=10.4161/psb.21899;
RA   Tian G., Lu Q., Kohalmi S.E., Rothstein S.J., Cui Y.;
RT   "Evidence that the Arabidopsis Ubiquitin C-terminal Hydrolases 1 and 2
RT   associate with the 26S proteasome and the TREX-2 complex.";
RL   Plant Signal. Behav. 7:1415-1419(2012).
CC   -!- FUNCTION: Component of the TREX-2 complex (transcription and export
CC       complex 2), a muliprotein complex that functions in docking export-
CC       competent ribonucleoprotein particles (mRNPs) to the nuclear entrance
CC       of the nuclear pore complex (nuclear basket). TREX-2 participates in
CC       mRNA export and accurate chromatin positioning in the nucleus by
CC       tethering genes to the nuclear periphery (PubMed:19843313).
CC       {ECO:0000269|PubMed:19843313}.
CC   -!- SUBUNIT: Interacts with SAC3A, EER5 and CML19 (PubMed:19843313).
CC       Interacts with UCH1 and UCH2 (PubMed:22951400).
CC       {ECO:0000269|PubMed:19843313, ECO:0000269|PubMed:22951400}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19843313}.
CC       Note=Apparent concentration to the nuclear periphery.
CC       {ECO:0000269|PubMed:19843313}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype. Sac3a, sac3b and sac3c
CC       triple mutants show no visible phenotype.
CC       {ECO:0000269|PubMed:19843313}.
CC   -!- SIMILARITY: Belongs to the SAC3 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF30322.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC018907; AAF30322.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE74369.1; -; Genomic_DNA.
DR   RefSeq; NP_187280.3; NM_111504.3.
DR   AlphaFoldDB; F4JAU2; -.
DR   SMR; F4JAU2; -.
DR   IntAct; F4JAU2; 4.
DR   STRING; 3702.AT3G06290.1; -.
DR   iPTMnet; F4JAU2; -.
DR   PaxDb; F4JAU2; -.
DR   PRIDE; F4JAU2; -.
DR   ProteomicsDB; 232835; -.
DR   EnsemblPlants; AT3G06290.1; AT3G06290.1; AT3G06290.
DR   GeneID; 819803; -.
DR   Gramene; AT3G06290.1; AT3G06290.1; AT3G06290.
DR   KEGG; ath:AT3G06290; -.
DR   Araport; AT3G06290; -.
DR   TAIR; locus:2082485; AT3G06290.
DR   eggNOG; KOG1860; Eukaryota.
DR   HOGENOM; CLU_003928_0_0_1; -.
DR   InParanoid; F4JAU2; -.
DR   OrthoDB; 1593971at2759; -.
DR   PRO; PR:F4JAU2; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; F4JAU2; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0034399; C:nuclear periphery; IDA:TAIR.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0070390; C:transcription export complex 2; IBA:GO_Central.
DR   GO; GO:0006406; P:mRNA export from nucleus; IBA:GO_Central.
DR   GO; GO:0044030; P:regulation of DNA methylation; IMP:TAIR.
DR   InterPro; IPR031907; MCM3AP_GANP.
DR   InterPro; IPR000717; PCI_dom.
DR   InterPro; IPR045107; SAC3/GANP/THP3.
DR   InterPro; IPR005062; SAC3/GANP/THP3_conserved.
DR   PANTHER; PTHR12436; PTHR12436; 1.
DR   Pfam; PF16769; MCM3AP_GANP; 1.
DR   Pfam; PF03399; SAC3_GANP; 1.
DR   PROSITE; PS50250; PCI; 1.
PE   1: Evidence at protein level;
KW   Nucleus; Reference proteome.
FT   CHAIN           1..1697
FT                   /note="SAC3 family protein B"
FT                   /id="PRO_0000435404"
FT   DOMAIN          625..813
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   REGION          54..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          167..280
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          306..413
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          491..512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..95
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        110..132
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..280
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        330..383
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1697 AA;  189932 MW;  C70B382BE22E7184 CRC64;
     MAFRPFGKDL GPMSSKPAPF TPFGASSTTR LYLSFLFLHT ANVGFACSDS SIQPPASQNH
     SAFAGQSFGP GGIRSGPSIQ RAPPLSASQN PQLSIGKPYR PGGVQSVPPI NRIPSPSAFQ
     NPSPSSGQPY QPGGIQRIPE PFNGIAWGPE ASRTSPSVRP YQFPGVQRPN LNPQYGHDGS
     RNFLKDHGEH SRATSPPATS HILSRMGTDA VEIGRSQDSK RKSRSDILPD QNMGFSRRNQ
     SPVSGFENGN LVDGFQPLSS RTWMRSPSSA ENNPVRSRSN PNQLIHQEQT GNSSFPYAHE
     VAEIQEATRR KSSAVAPSDK PLGDDPILSQ HDSQRFSTSP PTSGTKSYTL SRSSDSQFPG
     QPSSVNSFNN ARKTNSSPAT KRTRSPPVYP IEEDIPRNSF PSQDCTEGEE QARAKRLARF
     KGELEPIADR PVDIQLTKSP VNKTMKPLDN KQTFNSLESS RDALKGDALP DYENSEQPSL
     IIGVCPDMCP ESERGERERK GDLDHYERVD GDRNQTSKSL AVKKYTRTAE REAILIRPMP
     ILQNTMEYLL SLLDRPYNEN FLGMYNFLWD RMRAIRMDLR MQHIFNQEAI TLLEQMIRLH
     IIAMHELCEY TKGEGFSEGF DAHLNIEQMN KTSVELFQMY DDHRKKGITV PTEKEFRGYY
     ALLKLDKHPG YKVEPSELSL DLANMTPEIR QTSEVLFARN VARACRTGNF IAFFRLARKA
     SYLQACLMHA HFSKLRTQAL ASLHSGLQIN QGLPVSDMSN WIGMEEEDIE ALLEYHGFSI
     KVFEEPYMVK NDLFLHADKD YKTKCSKLVH MKKSRTIVED VSAPTVVEDV STPFPLPSLI
     TEATIGNQQC ITAHKHEMPP ARSLKKQTSM RLFDKEVADS KTSLLAEEDK PMGTFVMNPP
     GPFVINPVVH QEKQNDLTSA GGFHSPVKLY SPFGSPKFPQ TKSSNLEKQP NDDRIGMSPG
     EIKFSIIGDV YTNHVPGPAL QQSPKSMPME IMPVTTIAEC PTSVENKYAL EESVPEAAMI
     CTLEKEFNDI DEEDEDEDGV ILNQYDEEVA KAKLKLIIRL WKRWSSRQSE LRERRQLAAA
     AALNSLSLGT PIRFSKTDQS RACGEFNIDQ AMRRRFEERE KSWSRLNISD VIADILVGRN
     PESKCISWKV VLCTQTKSVN SSSSASQVTH SAASRWLSSK LMPHAEHSSL NDDNLLFSAP
     GVSVWNKWVA NGSDIDFTCC LSVARDVEAE NDMCETTCGA SAVLFLASGG LPLNLQREQL
     NLILESVPNG SVLPLLVVIS SCNGEHMEPD TDIVSGLGLH DIDKSKIASF SIVSIANKSQ
     KGQEVHFFND SRLRDGFKWL ASNSPLQPNL HHVKLRELFL THFSFSLELL KQMPDQEVGP
     NICISAFNDA LETSRRNITS AAEANPIGWP CPETMLLEDN RKECLMVKRY LPNLDWSSAE
     NVELLSSVLE NCKLPDFEDD LTWLTVGCAS GAEIENHTQR LEGCLIEYLT QRSNLMGVSL
     ATKETGVMLE RNTRLELHNS SRYHITPRWI GIFQRIFNWR IMGLFDASSS SAYVLKSDLN
     MSTSSYADKF LAEDASYPSC PPNLPLLHEM IEISCSPLKS PPPYDDKAQR VVETGMLIDD
     HRDIEESMLE KNREACRGID LMITEDDELG ERSWRSKGRE AAEKKTIEKR ESERLDELLE
     KCNMVQNSIA EKLCIYF
 
 
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