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PEL1_ARATH
ID   PEL1_ARATH              Reviewed;         378 AA.
AC   Q9ZT87; Q9FPG8;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Protein PELOTA 1;
DE            Short=AtPelota1;
DE            EC=3.1.-.- {ECO:0000250|UniProtKB:P33309};
GN   Name=PEL1; OrderedLocusNames=At4g27650; ORFNames=T29A15.140;
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, AND GENE FAMILY.
RC   STRAIN=cv. Columbia;
RX   AGRICOLA=IND22059670; DOI=10.1007/s004970050200;
RA   Caryl A.P., Lacroix I., Jones G.H., Franklin F.C.H.;
RT   "An Arabidopsis homologue of the Drosophila meiotic gene Pelota.";
RL   Sex. Plant Reprod. 12:310-313(2000).
RN   [2]
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   [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] (ISOFORMS 1 AND 2).
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   IDENTIFICATION.
RX   PubMed=7588080; DOI=10.1242/dev.121.10.3477;
RA   Eberhart C.G., Wasserman S.W.;
RT   "The pelota locus encodes a protein required for meiotic cell division: an
RT   analysis of G2/M arrest in Drosophila spermatogenesis.";
RL   Development 121:3477-3486(1995).
CC   -!- FUNCTION: Required for normal chromosome segregation during cell
CC       division and genomic stability (By similarity). May function in
CC       recognizing stalled ribosomes and triggering endonucleolytic cleavage
CC       of the mRNA, a mechanism to release non-functional ribosomes and
CC       degrade damaged mRNAs. May have ribonuclease activity (Potential).
CC       {ECO:0000250, ECO:0000305}.
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250|UniProtKB:P33309};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Cytoplasm {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9ZT87-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9ZT87-2; Sequence=VSP_055358, VSP_055359;
CC   -!- TISSUE SPECIFICITY: Expressed constitutively in seedlings, buds, stems,
CC       leaves and roots. {ECO:0000269|Ref.1}.
CC   -!- DOMAIN: The N-terminal domain has the RNA-binding Sm fold. It harbors
CC       the endoribonuclease activity. {ECO:0000250|UniProtKB:P33309}.
CC   -!- SIMILARITY: Belongs to the eukaryotic release factor 1 family. Pelota
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF069497; AAC82379.1; -; mRNA.
DR   EMBL; AL035602; CAB38277.1; -; Genomic_DNA.
DR   EMBL; AL161571; CAB81415.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85374.1; -; Genomic_DNA.
DR   EMBL; CP002687; ANM67968.1; -; Genomic_DNA.
DR   EMBL; CP002687; ANM67969.1; -; Genomic_DNA.
DR   EMBL; AF325048; AAG40400.1; -; mRNA.
DR   EMBL; AY074298; AAL66995.1; -; mRNA.
DR   EMBL; AY096569; AAM20219.1; -; mRNA.
DR   PIR; T05870; T05870.
DR   RefSeq; NP_001329759.1; NM_001341876.1. [Q9ZT87-1]
DR   RefSeq; NP_001329760.1; NM_001341877.1. [Q9ZT87-1]
DR   RefSeq; NP_194495.3; NM_118901.5. [Q9ZT87-1]
DR   AlphaFoldDB; Q9ZT87; -.
DR   SMR; Q9ZT87; -.
DR   STRING; 3702.AT4G27650.1; -.
DR   PaxDb; Q9ZT87; -.
DR   PRIDE; Q9ZT87; -.
DR   ProteomicsDB; 236721; -. [Q9ZT87-1]
DR   EnsemblPlants; AT4G27650.1; AT4G27650.1; AT4G27650. [Q9ZT87-1]
DR   EnsemblPlants; AT4G27650.2; AT4G27650.2; AT4G27650. [Q9ZT87-1]
DR   EnsemblPlants; AT4G27650.3; AT4G27650.3; AT4G27650. [Q9ZT87-1]
DR   GeneID; 828876; -.
DR   Gramene; AT4G27650.1; AT4G27650.1; AT4G27650. [Q9ZT87-1]
DR   Gramene; AT4G27650.2; AT4G27650.2; AT4G27650. [Q9ZT87-1]
DR   Gramene; AT4G27650.3; AT4G27650.3; AT4G27650. [Q9ZT87-1]
DR   KEGG; ath:AT4G27650; -.
DR   Araport; AT4G27650; -.
DR   TAIR; locus:2137732; AT4G27650.
DR   eggNOG; KOG2869; Eukaryota.
DR   HOGENOM; CLU_023334_3_1_1; -.
DR   InParanoid; Q9ZT87; -.
DR   OMA; DDLWHLK; -.
DR   PhylomeDB; Q9ZT87; -.
DR   PRO; PR:Q9ZT87; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9ZT87; baseline and differential.
DR   Genevisible; Q9ZT87; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070651; P:nonfunctional rRNA decay; IBA:GO_Central.
DR   GO; GO:0070966; P:nuclear-transcribed mRNA catabolic process, no-go decay; IEP:TAIR.
DR   GO; GO:0070481; P:nuclear-transcribed mRNA catabolic process, non-stop decay; IEP:TAIR.
DR   GO; GO:0032790; P:ribosome disassembly; IBA:GO_Central.
DR   GO; GO:0071025; P:RNA surveillance; IEA:InterPro.
DR   Gene3D; 2.30.30.870; -; 1.
DR   Gene3D; 3.30.1330.30; -; 1.
DR   Gene3D; 3.30.420.60; -; 1.
DR   InterPro; IPR042226; eFR1_2_sf.
DR   InterPro; IPR005140; eRF1_1_Pelota.
DR   InterPro; IPR005141; eRF1_2.
DR   InterPro; IPR005142; eRF1_3.
DR   InterPro; IPR029064; L30e-like.
DR   InterPro; IPR038069; Pelota/DOM34_N.
DR   InterPro; IPR004405; Transl-rel_pelota.
DR   PANTHER; PTHR10853; PTHR10853; 1.
DR   Pfam; PF03463; eRF1_1; 1.
DR   Pfam; PF03464; eRF1_2; 1.
DR   Pfam; PF03465; eRF1_3; 1.
DR   SMART; SM01194; eRF1_1; 1.
DR   SUPFAM; SSF159065; SSF159065; 1.
DR   SUPFAM; SSF55315; SSF55315; 1.
DR   TIGRFAMs; TIGR00111; pelota; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; Endonuclease; Hydrolase; Metal-binding;
KW   Nuclease; Nucleus; Reference proteome.
FT   CHAIN           1..378
FT                   /note="Protein PELOTA 1"
FT                   /id="PRO_0000429930"
FT   VAR_SEQ         215..251
FT                   /note="DQFHRHLLLEAERRQLRPIIENKSRIILVHTNSGYRH -> VFFLVTQRLSK
FT                   FTWFIIFQIAAGPGLQISHTYMTQTV (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14593172"
FT                   /id="VSP_055358"
FT   VAR_SEQ         252..378
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14593172"
FT                   /id="VSP_055359"
SQ   SEQUENCE   378 AA;  42519 MW;  A6B571D9592EBC43 CRC64;
     MKIVRRDFVR NGPGSVKMVA EDSDDLWYAY NLIAVGDSVM AVTFRKVQRE IPGGGRDSER
     VKLKLEVQVE EVDYDKDGSV LRIRGKNILE NEHVKIGAFH TLELELKRPF VLRKEMWDSM
     ALDTLKQASD PAASADLAVV LMQEGLAQIF LVGRSVTSSR ARIETSIPRK HGPAIAGYES
     ALKKFFENVL QAFVKHVDFS VVRCAVVASP GFTKDQFHRH LLLEAERRQL RPIIENKSRI
     ILVHTNSGYR HSLGEVLHAP NVMNMIKDTK AAKEVKALND FHNMLSTEPD RACYGPKHVE
     VANERMAIQT LLITDELFRN SDVKTRKKYV NLVESVKDSG GDAFIFSAMH VSGEQLAQLT
     GIAALLRFPL PELEDIEM
 
 
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