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TLP3_ARATH
ID   TLP3_ARATH              Reviewed;         406 AA.
AC   Q8VY21; O82257;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Tubby-like F-box protein 3;
DE            Short=AtTLP3;
GN   Name=TULP3; OrderedLocusNames=At2g47900; ORFNames=F17A22.29;
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 [MRNA], TISSUE SPECIFICITY, GENE FAMILY, AND
RP   NOMENCLATURE.
RX   PubMed=15064372; DOI=10.1104/pp.103.037820;
RA   Lai C.-P., Lee C.-L., Chen P.-H., Wu S.-H., Yang C.-C., Shaw J.-F.;
RT   "Molecular analyses of the Arabidopsis TUBBY-like protein gene family.";
RL   Plant Physiol. 134:1586-1597(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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].
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   [5]
RP   FUNCTION, DISRUPTION PHENOTYPE, 3D-STRUCTURE MODELING, TISSUE SPECIFICITY,
RP   INDUCTION BY H(2)O(2), SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-187 AND
RP   ARG-189.
RC   STRAIN=cv. Columbia;
RX   PubMed=22751378; DOI=10.1104/pp.112.201319;
RA   Reitz M.U., Bissue J.K., Zocher K., Attard A., Huckelhoven R., Becker K.,
RA   Imani J., Eichmann R., Schafer P.;
RT   "The subcellular localization of Tubby-like proteins and participation in
RT   stress signaling and root colonization by the mutualist Piriformospora
RT   indica.";
RL   Plant Physiol. 160:349-364(2012).
CC   -!- FUNCTION: Involved in abiotic stress signaling. Tethered to plasma
CC       membrane (PM) and probably bound to phosphatidylinositol 4,5-
CC       bisphosphate. Abiotic stresses (drought, salt, H(2)O(2)) trigger
CC       phospholipase C mediated PM dislogement and plastidial and
CC       nucleocytosolic relocation of TULP3. {ECO:0000269|PubMed:22751378}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22751378};
CC       Peripheral membrane protein {ECO:0000269|PubMed:22751378}. Plastid
CC       {ECO:0000269|PubMed:22751378}. Nucleus, nucleoplasm
CC       {ECO:0000269|PubMed:22751378}. Cytoplasm {ECO:0000269|PubMed:22751378}.
CC       Note=Phospholipase C activity mediates the release from the plasma
CC       membrane and the relocation to plastids, cytoplasm and nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q8VY21-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Ubiquitous at low levels. Not detected in mature
CC       siliques. {ECO:0000269|PubMed:15064372, ECO:0000269|PubMed:22751378}.
CC   -!- INDUCTION: Down-regulated by H(2)O(2) treatment.
CC       {ECO:0000269|PubMed:22751378}.
CC   -!- DISRUPTION PHENOTYPE: Reduced colonization of the roots by the
CC       mutualistic fungus Piriformospora indica.
CC       {ECO:0000269|PubMed:22751378}.
CC   -!- SIMILARITY: Belongs to the TUB family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC63644.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAM15124.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AY045774; AAK98802.1; -; mRNA.
DR   EMBL; AC005309; AAC63644.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC006072; AAM15124.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC10907.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC10908.1; -; Genomic_DNA.
DR   EMBL; AY074273; AAL66970.1; -; mRNA.
DR   EMBL; AY096604; AAM20254.1; -; mRNA.
DR   PIR; H84920; H84920.
DR   RefSeq; NP_001031558.1; NM_001036481.1. [Q8VY21-1]
DR   RefSeq; NP_001189775.1; NM_001202846.1.
DR   RefSeq; NP_850481.1; NM_180150.2. [Q8VY21-1]
DR   AlphaFoldDB; Q8VY21; -.
DR   SMR; Q8VY21; -.
DR   BioGRID; 4737; 6.
DR   IntAct; Q8VY21; 2.
DR   STRING; 3702.AT2G47900.3; -.
DR   iPTMnet; Q8VY21; -.
DR   PaxDb; Q8VY21; -.
DR   PRIDE; Q8VY21; -.
DR   EnsemblPlants; AT2G47900.1; AT2G47900.1; AT2G47900. [Q8VY21-1]
DR   EnsemblPlants; AT2G47900.2; AT2G47900.2; AT2G47900. [Q8VY21-1]
DR   GeneID; 819402; -.
DR   Gramene; AT2G47900.1; AT2G47900.1; AT2G47900. [Q8VY21-1]
DR   Gramene; AT2G47900.2; AT2G47900.2; AT2G47900. [Q8VY21-1]
DR   KEGG; ath:AT2G47900; -.
DR   Araport; AT2G47900; -.
DR   eggNOG; KOG2502; Eukaryota.
DR   HOGENOM; CLU_028236_3_0_1; -.
DR   InParanoid; Q8VY21; -.
DR   OrthoDB; 1445357at2759; -.
DR   PhylomeDB; Q8VY21; -.
DR   PRO; PR:Q8VY21; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q8VY21; baseline and differential.
DR   Genevisible; Q8VY21; AT.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009536; C:plastid; IEA:UniProtKB-SubCell.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProt.
DR   Gene3D; 3.20.90.10; -; 1.
DR   InterPro; IPR001810; F-box_dom.
DR   InterPro; IPR025659; Tubby-like_C.
DR   InterPro; IPR000007; Tubby_C.
DR   Pfam; PF00646; F-box; 1.
DR   Pfam; PF01167; Tub; 1.
DR   PRINTS; PR01573; SUPERTUBBY.
DR   SUPFAM; SSF54518; SSF54518; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Cytoplasm; Membrane; Nucleus; Plastid;
KW   Reference proteome; Stress response.
FT   CHAIN           1..406
FT                   /note="Tubby-like F-box protein 3"
FT                   /id="PRO_0000272231"
FT   DOMAIN          50..105
FT                   /note="F-box"
FT   MUTAGEN         187
FT                   /note="K->A: Loss of plasma membrane tethering; when
FT                   associated with A-189."
FT                   /evidence="ECO:0000269|PubMed:22751378"
FT   MUTAGEN         189
FT                   /note="R->A: Loss of plasma membrane tethering; when
FT                   associated with A-187."
FT                   /evidence="ECO:0000269|PubMed:22751378"
SQ   SEQUENCE   406 AA;  45312 MW;  C8A8188C0A0D77D4 CRC64;
     MSFKSLIQDM RGELGSISRK GFDVRFGYGR SRSQRVVQDT SVPVDAFKQS CWASMPPELL
     RDVLMRIEQS EDTWPSRKNV VSCAGVCRNW REIVKEIVRV PELSSKLTFP ISLKQPGPRG
     SLVQCYIMRN RSNQTYYLYL GLNQAASNDD GKFLLAAKRF RRPTCTDYII SLNCDDVSRG
     SNTYIGKLRS NFLGTKFTVY DAQPTNPGTQ VTRTRSSRLL SLKQVSPRIP SGNYPVAHIS
     YELNVLGSRG PRRMQCVMDA IPASAVEPGG TAPTQTELVH SNLDSFPSFS FFRSKSIRAE
     SLPSGPSSAA QKEGLLVLKN KAPRWHEQLQ CWCLNFNGRV TVASVKNFQL VAAPENGPAG
     PEHENVILQF GKVGKDVFTM DYQYPISAFQ AFTICLSSFD TKIACE
 
 
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