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ERI3_MOUSE
ID   ERI3_MOUSE              Reviewed;         337 AA.
AC   Q8C460; A2ADW0; A2ADW2; Q149R0; Q68FL7; Q923K5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 157.
DE   RecName: Full=ERI1 exoribonuclease 3;
DE            EC=3.1.-.-;
DE   AltName: Full=Prion interactor 1;
DE   AltName: Full=Prion protein-interacting protein;
GN   Name=Eri3; Synonyms=Pint1, Prnpip, Prnpip1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING
RP   (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 193-337 (ISOFORM 3), TISSUE
RP   SPECIFICITY, AND INTERACTION WITH PRNP.
RC   STRAIN=BALB/cJ;
RX   PubMed=11571277; DOI=10.1074/jbc.m103289200;
RA   Spielhaupter C., Schaetzl H.M.;
RT   "PrPC directly interacts with proteins involved in signaling pathways.";
RL   J. Biol. Chem. 276:44604-44612(2001).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Lung, Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryo;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Interacts with PRNP. {ECO:0000269|PubMed:11571277}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8C460-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8C460-2; Sequence=VSP_031105, VSP_031106;
CC       Name=3;
CC         IsoId=Q8C460-3; Sequence=VSP_031107;
CC   -!- TISSUE SPECIFICITY: Highly expressed in the brain, heart, thyroid and
CC       testis. Expressed at low levels in the muscle cells, liver, pancreas
CC       and kidney. {ECO:0000269|PubMed:11571277}.
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DR   EMBL; AK083017; BAC38733.1; -; mRNA.
DR   EMBL; AK144107; BAE25703.1; -; mRNA.
DR   EMBL; AL645740; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL671520; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC079640; AAH79640.1; -; mRNA.
DR   EMBL; BC116685; AAI16686.1; -; mRNA.
DR   EMBL; BC117540; AAI17541.1; -; mRNA.
DR   EMBL; AY029599; AAK38347.1; -; mRNA.
DR   CCDS; CCDS18535.1; -. [Q8C460-1]
DR   RefSeq; NP_001272828.1; NM_001285899.1. [Q8C460-2]
DR   RefSeq; NP_001272830.1; NM_001285901.1.
DR   RefSeq; NP_001272831.1; NM_001285902.1.
DR   RefSeq; NP_536717.2; NM_080469.4. [Q8C460-1]
DR   AlphaFoldDB; Q8C460; -.
DR   SMR; Q8C460; -.
DR   BioGRID; 228276; 1.
DR   STRING; 10090.ENSMUSP00000042796; -.
DR   iPTMnet; Q8C460; -.
DR   PhosphoSitePlus; Q8C460; -.
DR   EPD; Q8C460; -.
DR   MaxQB; Q8C460; -.
DR   PaxDb; Q8C460; -.
DR   PeptideAtlas; Q8C460; -.
DR   PRIDE; Q8C460; -.
DR   ProteomicsDB; 275535; -. [Q8C460-1]
DR   ProteomicsDB; 275536; -. [Q8C460-2]
DR   ProteomicsDB; 275537; -. [Q8C460-3]
DR   Antibodypedia; 18452; 81 antibodies from 18 providers.
DR   DNASU; 140546; -.
DR   Ensembl; ENSMUST00000037127; ENSMUSP00000042796; ENSMUSG00000033423. [Q8C460-1]
DR   GeneID; 140546; -.
DR   KEGG; mmu:140546; -.
DR   UCSC; uc008uis.2; mouse. [Q8C460-1]
DR   UCSC; uc008uit.2; mouse. [Q8C460-2]
DR   CTD; 79033; -.
DR   MGI; MGI:2153887; Eri3.
DR   VEuPathDB; HostDB:ENSMUSG00000033423; -.
DR   eggNOG; KOG0542; Eukaryota.
DR   GeneTree; ENSGT00530000063205; -.
DR   HOGENOM; CLU_037266_0_0_1; -.
DR   InParanoid; Q8C460; -.
DR   OMA; CGDWDLG; -.
DR   OrthoDB; 809000at2759; -.
DR   PhylomeDB; Q8C460; -.
DR   TreeFam; TF313449; -.
DR   BioGRID-ORCS; 140546; 6 hits in 72 CRISPR screens.
DR   ChiTaRS; Eri3; mouse.
DR   PRO; PR:Q8C460; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q8C460; protein.
DR   Bgee; ENSMUSG00000033423; Expressed in humerus cartilage element and 247 other tissues.
DR   ExpressionAtlas; Q8C460; baseline and differential.
DR   Genevisible; Q8C460; MM.
DR   GO; GO:0005886; C:plasma membrane; TAS:MGI.
DR   GO; GO:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0000467; P:exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR   Gene3D; 3.30.420.10; -; 1.
DR   InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   Pfam; PF00929; RNase_T; 1.
DR   SMART; SM00479; EXOIII; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Exonuclease; Hydrolase; Magnesium; Metal-binding;
KW   Nuclease; Reference proteome.
FT   CHAIN           1..337
FT                   /note="ERI1 exoribonuclease 3"
FT                   /id="PRO_0000317627"
FT   DOMAIN          146..320
FT                   /note="Exonuclease"
FT   ACT_SITE        152
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        307
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
FT   BINDING         150
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         150
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         152
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250"
FT   BINDING         152
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         249
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         307
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250"
FT   BINDING         312
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..45
FT                   /note="MATASPAADGGRGRPWEGGLVSWPPAPPLTLPWTWMGPSWGQHPG -> MCV
FT                   CPQ (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_031105"
FT   VAR_SEQ         71..72
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_031106"
FT   VAR_SEQ         278..337
FT                   /note="AYSFAMGCWPKNGLLDMNKGLSLQHIGRPHSGIDDCKNIANIMKTLAYRGFI
FT                   FKQTSKPF -> VPLSSSQGLWFSCPSPPPPTLVSFCFFSQYSPFSSLGNLY (in
FT                   isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:11571277"
FT                   /id="VSP_031107"
SQ   SEQUENCE   337 AA;  37189 MW;  1AEBD95BCE7EF7AA CRC64;
     MATASPAADG GRGRPWEGGL VSWPPAPPLT LPWTWMGPSW GQHPGHWGFP ALTDPSASPA
     ASLGIFEVRR VLDASGCSML APLQTGAARF SSYLLSRARK VLGSHLLSPC GVPELCSIST
     RKLAAHGFGA AMAAMVPFPP QRYHYFLVLD FEATCDKPQI HPQEIIEFPI LKLNGRTMEI
     ESTFHMYVQP VVHPQLTPFC TELTGIIQAM VDGQPSLQQV LERVDEWMAK EGLLDPNVKS
     IFVTCGDWDL KVMLPGQCHY LGLPVADYFK QWINLKKAYS FAMGCWPKNG LLDMNKGLSL
     QHIGRPHSGI DDCKNIANIM KTLAYRGFIF KQTSKPF
 
 
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