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SMD1B_ARATH
ID   SMD1B_ARATH             Reviewed;         116 AA.
AC   Q9SY09; F4JHV8;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 155.
DE   RecName: Full=Small nuclear ribonucleoprotein SmD1b {ECO:0000303|PubMed:15575968};
DE            Short=AtSmD1-b {ECO:0000303|PubMed:15575968};
GN   Name=SMD1B {ECO:0000303|PubMed:15575968};
GN   OrderedLocusNames=At4g02840 {ECO:0000312|Araport:AT4G02840};
GN   ORFNames=T5J8.16 {ECO:0000312|EMBL:AAD15345.1};
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
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] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RA   Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT   "Arabidopsis ORF Clones.";
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=15575968; DOI=10.1186/gb-2004-5-12-r102;
RA   Wang B.B., Brendel V.;
RT   "The ASRG database: identification and survey of Arabidopsis thaliana genes
RT   involved in pre-mRNA splicing.";
RL   Genome Biol. 5:R102.1-R102.23(2004).
RN   [7]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX   PubMed=26842463; DOI=10.1105/tpc.15.01045;
RA   Elvira-Matelot E., Bardou F., Ariel F., Jauvion V., Bouteiller N.,
RA   Le Masson I., Cao J., Crespi M.D., Vaucheret H.;
RT   "The nuclear ribonucleoprotein SmD1 interplays with splicing, RNA quality
RT   control, and posttranscriptional gene silencing in Arabidopsis.";
RL   Plant Cell 28:426-438(2016).
CC   -!- FUNCTION: Involved in splicing regulation. Facilitates post-
CC       transcriptional gene silencing (PTGS) by limiting the degradation of
CC       transgene aberrant RNAs by the RNA quality control (RQC) machinery,
CC       thus favoring their entry into cytoplasmic siRNA bodies where they can
CC       trigger PTGS. Does not participate in the production of small RNAs.
CC       {ECO:0000269|PubMed:26842463}.
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:26842463}.
CC       Nucleus, nucleolus {ECO:0000269|PubMed:26842463}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9SY09-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9SY09-2; Sequence=VSP_058955;
CC   -!- DISRUPTION PHENOTYPE: Post-transcriptional gene silencing deficiency
CC       and developmental defects, including reduced stature, leaf serration
CC       and early flowering (PubMed:26842463). Smd1a and smd2b double mutants
CC       are embryo lethal (PubMed:26842463). {ECO:0000269|PubMed:26842463}.
CC   -!- MISCELLANEOUS: SMD1A and SMD1B have redundant activity, but consistent
CC       with their expression level, SMD1B is more important than SMD1A and
CC       either one copy of SMD1B or two copies of SMD1A is necessary for the
CC       plant to survive. {ECO:0000305|PubMed:26842463}.
CC   -!- SIMILARITY: Belongs to the snRNP core protein family. {ECO:0000305}.
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DR   EMBL; AC004044; AAD15345.1; -; Genomic_DNA.
DR   EMBL; AL161495; CAB77769.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE82236.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE82237.1; -; Genomic_DNA.
DR   EMBL; AK117672; BAC42325.1; -; mRNA.
DR   EMBL; BT028879; ABI49426.1; -; mRNA.
DR   EMBL; AY084707; AAM61281.1; -; mRNA.
DR   PIR; B85036; B85036.
DR   RefSeq; NP_001190664.1; NM_001203735.1. [Q9SY09-2]
DR   RefSeq; NP_192193.1; NM_116518.4. [Q9SY09-1]
DR   AlphaFoldDB; Q9SY09; -.
DR   SMR; Q9SY09; -.
DR   IntAct; Q9SY09; 3.
DR   STRING; 3702.AT4G02840.2; -.
DR   PRIDE; Q9SY09; -.
DR   ProteomicsDB; 234530; -. [Q9SY09-1]
DR   EnsemblPlants; AT4G02840.1; AT4G02840.1; AT4G02840. [Q9SY09-1]
DR   EnsemblPlants; AT4G02840.2; AT4G02840.2; AT4G02840. [Q9SY09-2]
DR   GeneID; 828163; -.
DR   Gramene; AT4G02840.1; AT4G02840.1; AT4G02840. [Q9SY09-1]
DR   Gramene; AT4G02840.2; AT4G02840.2; AT4G02840. [Q9SY09-2]
DR   KEGG; ath:AT4G02840; -.
DR   Araport; AT4G02840; -.
DR   TAIR; locus:2140240; AT4G02840.
DR   eggNOG; KOG3428; Eukaryota.
DR   HOGENOM; CLU_123956_3_0_1; -.
DR   OMA; SVTPQMN; -.
DR   OrthoDB; 1579192at2759; -.
DR   PhylomeDB; Q9SY09; -.
DR   PRO; PR:Q9SY09; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9SY09; baseline and differential.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR   GO; GO:0000243; C:commitment complex; IBA:GO_Central.
DR   GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR   GO; GO:0034715; C:pICln-Sm protein complex; IBA:GO_Central.
DR   GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR   GO; GO:0071011; C:precatalytic spliceosome; IBA:GO_Central.
DR   GO; GO:0034719; C:SMN-Sm protein complex; IBA:GO_Central.
DR   GO; GO:0097526; C:spliceosomal tri-snRNP complex; IBA:GO_Central.
DR   GO; GO:0005685; C:U1 snRNP; IBA:GO_Central.
DR   GO; GO:0005689; C:U12-type spliceosomal complex; IBA:GO_Central.
DR   GO; GO:0005686; C:U2 snRNP; IBA:GO_Central.
DR   GO; GO:0005687; C:U4 snRNP; IBA:GO_Central.
DR   GO; GO:0005682; C:U5 snRNP; IBA:GO_Central.
DR   GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0035194; P:post-transcriptional gene silencing by RNA; IMP:UniProtKB.
DR   GO; GO:0043484; P:regulation of RNA splicing; IMP:UniProtKB.
DR   GO; GO:0008380; P:RNA splicing; IMP:TAIR.
DR   GO; GO:0000387; P:spliceosomal snRNP assembly; IBA:GO_Central.
DR   CDD; cd01724; Sm_D1; 1.
DR   InterPro; IPR027141; LSm4/Sm_D1/D3.
DR   InterPro; IPR001163; LSM_dom_euk/arc.
DR   InterPro; IPR010920; LSM_dom_sf.
DR   InterPro; IPR034102; Sm_D1.
DR   PANTHER; PTHR23338; PTHR23338; 1.
DR   Pfam; PF01423; LSM; 1.
DR   SMART; SM00651; Sm; 1.
DR   SUPFAM; SSF50182; SSF50182; 1.
PE   3: Inferred from homology;
KW   Alternative splicing; Nucleus; Reference proteome; Repeat;
KW   Ribonucleoprotein.
FT   CHAIN           1..116
FT                   /note="Small nuclear ribonucleoprotein SmD1b"
FT                   /id="PRO_0000440136"
FT   REPEAT          100..101
FT                   /note="1"
FT                   /evidence="ECO:0000305"
FT   REPEAT          102..103
FT                   /note="2"
FT                   /evidence="ECO:0000305"
FT   REPEAT          104..105
FT                   /note="3"
FT                   /evidence="ECO:0000305"
FT   REPEAT          106..107
FT                   /note="4"
FT                   /evidence="ECO:0000305"
FT   REPEAT          108..109
FT                   /note="5"
FT                   /evidence="ECO:0000305"
FT   REPEAT          110..111
FT                   /note="6"
FT                   /evidence="ECO:0000305"
FT   REPEAT          112..113
FT                   /note="7"
FT                   /evidence="ECO:0000305"
FT   REPEAT          114..116
FT                   /note="8; approximate"
FT                   /evidence="ECO:0000305"
FT   REGION          85..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          100..116
FT                   /note="8 X 2 AA approximate tandem repeats of G-R"
FT                   /evidence="ECO:0000305"
FT   COMPBIAS        102..116
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         30
FT                   /note="T -> TDEYTRFYLNR (in isoform 2)"
FT                   /id="VSP_058955"
SQ   SEQUENCE   116 AA;  12750 MW;  4ABA07CBD18F2152 CRC64;
     MKLVRFLMKL NNETVSIELK NGTIVHGTIT GVDVSMNTHL KAVKLTLKGK NPVTLDHLSV
     RGNNIRYYIL PDSLNLETLL VEDTPRIKPK KPTAGKIPAG RGRGRGRGRG RGRGGR
 
 
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