Full text data of ABCE1
ABCE1
(RLI, RNASEL1, RNASELI, RNS4I)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
ATP-binding cassette sub-family E member 1 (2'-5'-oligoadenylate-binding protein; HuHP68; RNase L inhibitor; Ribonuclease 4 inhibitor; RNS4I)
ATP-binding cassette sub-family E member 1 (2'-5'-oligoadenylate-binding protein; HuHP68; RNase L inhibitor; Ribonuclease 4 inhibitor; RNS4I)
UniProt
P61221
ID ABCE1_HUMAN Reviewed; 599 AA.
AC P61221; O88793; Q13181; Q13864; Q6NR76; Q96AL0; Q96B10; Q99K66;
read moreDT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 22-JAN-2014, entry version 112.
DE RecName: Full=ATP-binding cassette sub-family E member 1;
DE AltName: Full=2'-5'-oligoadenylate-binding protein;
DE AltName: Full=HuHP68;
DE AltName: Full=RNase L inhibitor;
DE AltName: Full=Ribonuclease 4 inhibitor;
DE Short=RNS4I;
GN Name=ABCE1; Synonyms=RLI, RNASEL1, RNASELI, RNS4I;
GN ORFNames=OK/SW-cl.40;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND INTERACTION WITH
RP RNASEL.
RX PubMed=7539425; DOI=10.1074/jbc.270.22.13308;
RA Bisbal C., Martinand C., Silhol M., Lebleu B., Salehzada T.;
RT "Cloning and characterization of a RNase L inhibitor. A new component
RT of the interferon-regulated 2-5A pathway.";
RL J. Biol. Chem. 270:13308-13317(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8641422; DOI=10.1016/0014-5793(96)00099-3;
RA Aubry F., Mattei M.-G., Barque J.-P., Galibert F.;
RT "Chromosomal localization and expression pattern of the RNase L
RT inhibitor gene.";
RL FEBS Lett. 381:135-139(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon adenocarcinoma;
RA Shichijo S., Itoh K.;
RT "Identification of immuno-peptidmics that are recognized by tumor-
RT reactive CTL generated from TIL of colon cancer patients.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG SeattleSNPs variation discovery resource;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Duodenum, and Uterus;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP INDUCTION BY EMCV, AND FUNCTION.
RX PubMed=9660177; DOI=10.1046/j.1432-1327.1998.2540248.x;
RA Martinand C., Salehzada T., Silhol M., Lebleu B., Bisbal C.;
RT "RNase L inhibitor (RLI) antisense constructions block partially the
RT down regulation of the 2-5A/RNase L pathway in encephalomyocarditis-
RT virus-(EMCV)-infected cells.";
RL Eur. J. Biochem. 254:248-255(1998).
RN [8]
RP INDUCTION BY HIV-1, AND FUNCTION.
RX PubMed=9847332;
RA Martinand C., Montavon C., Salehzada T., Silhol M., Lebleu B.,
RA Bisbal C.;
RT "RNase L inhibitor is induced during human immunodeficiency virus type
RT 1 infection and down regulates the 2-5A/RNase L pathway in human T
RT cells.";
RL J. Virol. 73:290-296(1999).
RN [9]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=11585831; DOI=10.1074/jbc.M107482200;
RA Le Roy F., Bisbal C., Silhol M., Martinand C., Lebleu B.,
RA Salehzada T.;
RT "The 2-5A/RNase L/RNase L inhibitor (RNI) pathway regulates
RT mitochondrial mRNAs stability in interferon alpha-treated H9 cells.";
RL J. Biol. Chem. 276:48473-48482(2001).
RN [10]
RP INTERACTION WITH HIV-1 VIF AND GAG PROTEINS.
RX PubMed=11780123; DOI=10.1038/415088a;
RA Zimmerman C., Klein K.C., Kiser P.K., Singh A.R., Firestein B.L.,
RA Riba S.C., Lingappa J.R.;
RT "Identification of a host protein essential for assembly of immature
RT HIV-1 capsids.";
RL Nature 415:88-92(2002).
RN [11]
RP INTERACTION WITH HIV-2 AND SIV GAG PROTEINS.
RX PubMed=14747530; DOI=10.1128/JVI.78.4.1645-1656.2004;
RA Dooher J.E., Lingappa J.R.;
RT "Conservation of a stepwise, energy-sensitive pathway involving HP68
RT for assembly of primate lentivirus capsids in cells.";
RL J. Virol. 78:1645-1656(2004).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP VARIANT CYS-489, AND MASS SPECTROMETRY.
RX PubMed=17488105; DOI=10.1021/pr0700908;
RA Bunger M.K., Cargile B.J., Sevinsky J.R., Deyanova E., Yates N.A.,
RA Hendrickson R.C., Stephenson J.L. Jr.;
RT "Detection and validation of non-synonymous coding SNPs from
RT orthogonal analysis of shotgun proteomics data.";
RL J. Proteome Res. 6:2331-2340(2007).
CC -!- FUNCTION: Antagonizes the binding of 2-5A (5'-phosphorylated
CC 2',5'-linked oligoadenylates) by RNase L through direct
CC interaction with RNase L and therefore inhibits its
CC endoribonuclease activity. May play a central role in the
CC regulation of mRNA turnover. Antagonizes the anti-viral effect of
CC the interferon-regulated 2-5A/RNase L pathway. May act as a
CC chaperone for post-translational events during HIV-1 capsid
CC assembly.
CC -!- SUBUNIT: Probably heterodimerizes with RNASEL; this interaction
CC inhibits the RNASEL. Associates with HIV-1 Vif and HIV-1, HIV-2
CC and SIV Gag proteins.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion. Note=Localized to
CC clusters of virus formation at the plasma membrane.
CC -!- INDUCTION: Activated by encephalomyocarditis virus (EMCV) and HIV-
CC 1.
CC -!- MISCELLANEOUS: The ABC transporter domains seem not to be
CC functional.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCE
CC family.
CC -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains.
CC -!- SIMILARITY: Contains 2 ABC transporter domains.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/abce1/";
CC -!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC
CC proteins;
CC URL="http://abcmutations.hegelab.org/proteinDetails?uniprot_id=P61221";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X76388; CAA53972.1; -; mRNA.
DR EMBL; X74987; CAA52920.1; -; mRNA.
DR EMBL; AB062293; BAB93476.1; -; mRNA.
DR EMBL; BT009779; AAP88781.1; -; mRNA.
DR EMBL; DQ148409; AAZ38723.1; -; Genomic_DNA.
DR EMBL; BC016283; AAH16283.1; -; mRNA.
DR EMBL; BC016988; AAH16988.1; -; mRNA.
DR PIR; A57017; A57017.
DR PIR; S63672; S63672.
DR RefSeq; NP_001035809.1; NM_001040876.1.
DR RefSeq; NP_002931.2; NM_002940.2.
DR UniGene; Hs.12013; -.
DR ProteinModelPortal; P61221; -.
DR SMR; P61221; 7-597.
DR IntAct; P61221; 4.
DR MINT; MINT-5004380; -.
DR STRING; 9606.ENSP00000296577; -.
DR PhosphoSite; P61221; -.
DR DMDM; 47117664; -.
DR PaxDb; P61221; -.
DR PeptideAtlas; P61221; -.
DR PRIDE; P61221; -.
DR DNASU; 6059; -.
DR Ensembl; ENST00000296577; ENSP00000296577; ENSG00000164163.
DR GeneID; 6059; -.
DR KEGG; hsa:6059; -.
DR UCSC; uc003ijx.3; human.
DR CTD; 6059; -.
DR GeneCards; GC04P146019; -.
DR HGNC; HGNC:69; ABCE1.
DR HPA; CAB012476; -.
DR MIM; 601213; gene.
DR neXtProt; NX_P61221; -.
DR PharmGKB; PA24404; -.
DR eggNOG; COG1245; -.
DR HOVERGEN; HBG050439; -.
DR InParanoid; P61221; -.
DR KO; K06174; -.
DR OMA; ISYKPQY; -.
DR OrthoDB; EOG70GMF4; -.
DR PhylomeDB; P61221; -.
DR ChiTaRS; ABCE1; human.
DR GenomeRNAi; 6059; -.
DR NextBio; 23613; -.
DR PRO; PR:P61221; -.
DR ArrayExpress; P61221; -.
DR Bgee; P61221; -.
DR CleanEx; HS_ABCE1; -.
DR Genevestigator; P61221; -.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATPase activity; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR GO; GO:0008428; F:ribonuclease inhibitor activity; TAS:ProtInc.
DR GO; GO:0006200; P:ATP catabolic process; IEA:GOC.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0009615; P:response to virus; TAS:ProtInc.
DR GO; GO:0006401; P:RNA catabolic process; TAS:ProtInc.
DR InterPro; IPR001450; 4Fe4S-bd_dom.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013283; ABC_E.
DR InterPro; IPR003439; ABC_transporter-like.
DR InterPro; IPR017871; ABC_transporter_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR007209; RNaseL-inhib_metal-bd_dom.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF00037; Fer4; 1.
DR Pfam; PF04068; RLI; 1.
DR PRINTS; PR01868; ABCEFAMILY.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Complete proteome; Cytoplasm;
KW Host-virus interaction; Mitochondrion; Nucleotide-binding;
KW Polymorphism; Reference proteome; Repeat.
FT CHAIN 1 599 ATP-binding cassette sub-family E member
FT 1.
FT /FTId=PRO_0000093316.
FT DOMAIN 7 37 4Fe-4S ferredoxin-type 1.
FT DOMAIN 46 75 4Fe-4S ferredoxin-type 2.
FT DOMAIN 79 315 ABC transporter 1.
FT DOMAIN 342 562 ABC transporter 2.
FT NP_BIND 110 117 ATP 1 (Potential).
FT NP_BIND 379 386 ATP 2 (Potential).
FT VARIANT 489 489 S -> C (polymorphism confirmed at protein
FT level; dbSNP:rs3816497).
FT /FTId=VAR_068914.
FT CONFLICT 118 118 T -> A (in Ref. 1; CAA53972).
FT CONFLICT 174 179 DQIPKA -> ARFLRL (in Ref. 1; CAA53972).
FT CONFLICT 471 473 ALA -> RLR (in Ref. 1; CAA53972/
FT CAA52920).
SQ SEQUENCE 599 AA; 67314 MW; 5D582B62E95BC7A6 CRC64;
MADKLTRIAI VNHDKCKPKK CRQECKKSCP VVRMGKLCIE VTPQSKIAWI SETLCIGCGI
CIKKCPFGAL SIVNLPSNLE KETTHRYCAN AFKLHRLPIP RPGEVLGLVG TNGIGKSTAL
KILAGKQKPN LGKYDDPPDW QEILTYFRGS ELQNYFTKIL EDDLKAIIKP QYVDQIPKAA
KGTVGSILDR KDETKTQAIV CQQLDLTHLK ERNVEDLSGG ELQRFACAVV CIQKADIFMF
DEPSSYLDVK QRLKAAITIR SLINPDRYII VVEHDLSVLD YLSDFICCLY GVPSAYGVVT
MPFSVREGIN IFLDGYVPTE NLRFRDASLV FKVAETANEE EVKKMCMYKY PGMKKKMGEF
ELAIVAGEFT DSEIMVMLGE NGTGKTTFIR MLAGRLKPDE GGEVPVLNVS YKPQKISPKS
TGSVRQLLHE KIRDAYTHPQ FVTDVMKPLQ IENIIDQEVQ TLSGGELQRV ALALCLGKPA
DVYLIDEPSA YLDSEQRLMA ARVVKRFILH AKKTAFVVEH DFIMATYLAD RVIVFDGVPS
KNTVANSPQT LLAGMNKFLS QLEITFRRDP NNYRPRINKL NSIKDVEQKK SGNYFFLDD
//
ID ABCE1_HUMAN Reviewed; 599 AA.
AC P61221; O88793; Q13181; Q13864; Q6NR76; Q96AL0; Q96B10; Q99K66;
read moreDT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 22-JAN-2014, entry version 112.
DE RecName: Full=ATP-binding cassette sub-family E member 1;
DE AltName: Full=2'-5'-oligoadenylate-binding protein;
DE AltName: Full=HuHP68;
DE AltName: Full=RNase L inhibitor;
DE AltName: Full=Ribonuclease 4 inhibitor;
DE Short=RNS4I;
GN Name=ABCE1; Synonyms=RLI, RNASEL1, RNASELI, RNS4I;
GN ORFNames=OK/SW-cl.40;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND INTERACTION WITH
RP RNASEL.
RX PubMed=7539425; DOI=10.1074/jbc.270.22.13308;
RA Bisbal C., Martinand C., Silhol M., Lebleu B., Salehzada T.;
RT "Cloning and characterization of a RNase L inhibitor. A new component
RT of the interferon-regulated 2-5A pathway.";
RL J. Biol. Chem. 270:13308-13317(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8641422; DOI=10.1016/0014-5793(96)00099-3;
RA Aubry F., Mattei M.-G., Barque J.-P., Galibert F.;
RT "Chromosomal localization and expression pattern of the RNase L
RT inhibitor gene.";
RL FEBS Lett. 381:135-139(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon adenocarcinoma;
RA Shichijo S., Itoh K.;
RT "Identification of immuno-peptidmics that are recognized by tumor-
RT reactive CTL generated from TIL of colon cancer patients.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG SeattleSNPs variation discovery resource;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Duodenum, and Uterus;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP INDUCTION BY EMCV, AND FUNCTION.
RX PubMed=9660177; DOI=10.1046/j.1432-1327.1998.2540248.x;
RA Martinand C., Salehzada T., Silhol M., Lebleu B., Bisbal C.;
RT "RNase L inhibitor (RLI) antisense constructions block partially the
RT down regulation of the 2-5A/RNase L pathway in encephalomyocarditis-
RT virus-(EMCV)-infected cells.";
RL Eur. J. Biochem. 254:248-255(1998).
RN [8]
RP INDUCTION BY HIV-1, AND FUNCTION.
RX PubMed=9847332;
RA Martinand C., Montavon C., Salehzada T., Silhol M., Lebleu B.,
RA Bisbal C.;
RT "RNase L inhibitor is induced during human immunodeficiency virus type
RT 1 infection and down regulates the 2-5A/RNase L pathway in human T
RT cells.";
RL J. Virol. 73:290-296(1999).
RN [9]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=11585831; DOI=10.1074/jbc.M107482200;
RA Le Roy F., Bisbal C., Silhol M., Martinand C., Lebleu B.,
RA Salehzada T.;
RT "The 2-5A/RNase L/RNase L inhibitor (RNI) pathway regulates
RT mitochondrial mRNAs stability in interferon alpha-treated H9 cells.";
RL J. Biol. Chem. 276:48473-48482(2001).
RN [10]
RP INTERACTION WITH HIV-1 VIF AND GAG PROTEINS.
RX PubMed=11780123; DOI=10.1038/415088a;
RA Zimmerman C., Klein K.C., Kiser P.K., Singh A.R., Firestein B.L.,
RA Riba S.C., Lingappa J.R.;
RT "Identification of a host protein essential for assembly of immature
RT HIV-1 capsids.";
RL Nature 415:88-92(2002).
RN [11]
RP INTERACTION WITH HIV-2 AND SIV GAG PROTEINS.
RX PubMed=14747530; DOI=10.1128/JVI.78.4.1645-1656.2004;
RA Dooher J.E., Lingappa J.R.;
RT "Conservation of a stepwise, energy-sensitive pathway involving HP68
RT for assembly of primate lentivirus capsids in cells.";
RL J. Virol. 78:1645-1656(2004).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP VARIANT CYS-489, AND MASS SPECTROMETRY.
RX PubMed=17488105; DOI=10.1021/pr0700908;
RA Bunger M.K., Cargile B.J., Sevinsky J.R., Deyanova E., Yates N.A.,
RA Hendrickson R.C., Stephenson J.L. Jr.;
RT "Detection and validation of non-synonymous coding SNPs from
RT orthogonal analysis of shotgun proteomics data.";
RL J. Proteome Res. 6:2331-2340(2007).
CC -!- FUNCTION: Antagonizes the binding of 2-5A (5'-phosphorylated
CC 2',5'-linked oligoadenylates) by RNase L through direct
CC interaction with RNase L and therefore inhibits its
CC endoribonuclease activity. May play a central role in the
CC regulation of mRNA turnover. Antagonizes the anti-viral effect of
CC the interferon-regulated 2-5A/RNase L pathway. May act as a
CC chaperone for post-translational events during HIV-1 capsid
CC assembly.
CC -!- SUBUNIT: Probably heterodimerizes with RNASEL; this interaction
CC inhibits the RNASEL. Associates with HIV-1 Vif and HIV-1, HIV-2
CC and SIV Gag proteins.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion. Note=Localized to
CC clusters of virus formation at the plasma membrane.
CC -!- INDUCTION: Activated by encephalomyocarditis virus (EMCV) and HIV-
CC 1.
CC -!- MISCELLANEOUS: The ABC transporter domains seem not to be
CC functional.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCE
CC family.
CC -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains.
CC -!- SIMILARITY: Contains 2 ABC transporter domains.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/abce1/";
CC -!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC
CC proteins;
CC URL="http://abcmutations.hegelab.org/proteinDetails?uniprot_id=P61221";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X76388; CAA53972.1; -; mRNA.
DR EMBL; X74987; CAA52920.1; -; mRNA.
DR EMBL; AB062293; BAB93476.1; -; mRNA.
DR EMBL; BT009779; AAP88781.1; -; mRNA.
DR EMBL; DQ148409; AAZ38723.1; -; Genomic_DNA.
DR EMBL; BC016283; AAH16283.1; -; mRNA.
DR EMBL; BC016988; AAH16988.1; -; mRNA.
DR PIR; A57017; A57017.
DR PIR; S63672; S63672.
DR RefSeq; NP_001035809.1; NM_001040876.1.
DR RefSeq; NP_002931.2; NM_002940.2.
DR UniGene; Hs.12013; -.
DR ProteinModelPortal; P61221; -.
DR SMR; P61221; 7-597.
DR IntAct; P61221; 4.
DR MINT; MINT-5004380; -.
DR STRING; 9606.ENSP00000296577; -.
DR PhosphoSite; P61221; -.
DR DMDM; 47117664; -.
DR PaxDb; P61221; -.
DR PeptideAtlas; P61221; -.
DR PRIDE; P61221; -.
DR DNASU; 6059; -.
DR Ensembl; ENST00000296577; ENSP00000296577; ENSG00000164163.
DR GeneID; 6059; -.
DR KEGG; hsa:6059; -.
DR UCSC; uc003ijx.3; human.
DR CTD; 6059; -.
DR GeneCards; GC04P146019; -.
DR HGNC; HGNC:69; ABCE1.
DR HPA; CAB012476; -.
DR MIM; 601213; gene.
DR neXtProt; NX_P61221; -.
DR PharmGKB; PA24404; -.
DR eggNOG; COG1245; -.
DR HOVERGEN; HBG050439; -.
DR InParanoid; P61221; -.
DR KO; K06174; -.
DR OMA; ISYKPQY; -.
DR OrthoDB; EOG70GMF4; -.
DR PhylomeDB; P61221; -.
DR ChiTaRS; ABCE1; human.
DR GenomeRNAi; 6059; -.
DR NextBio; 23613; -.
DR PRO; PR:P61221; -.
DR ArrayExpress; P61221; -.
DR Bgee; P61221; -.
DR CleanEx; HS_ABCE1; -.
DR Genevestigator; P61221; -.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATPase activity; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR GO; GO:0008428; F:ribonuclease inhibitor activity; TAS:ProtInc.
DR GO; GO:0006200; P:ATP catabolic process; IEA:GOC.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0009615; P:response to virus; TAS:ProtInc.
DR GO; GO:0006401; P:RNA catabolic process; TAS:ProtInc.
DR InterPro; IPR001450; 4Fe4S-bd_dom.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013283; ABC_E.
DR InterPro; IPR003439; ABC_transporter-like.
DR InterPro; IPR017871; ABC_transporter_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR007209; RNaseL-inhib_metal-bd_dom.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF00037; Fer4; 1.
DR Pfam; PF04068; RLI; 1.
DR PRINTS; PR01868; ABCEFAMILY.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Complete proteome; Cytoplasm;
KW Host-virus interaction; Mitochondrion; Nucleotide-binding;
KW Polymorphism; Reference proteome; Repeat.
FT CHAIN 1 599 ATP-binding cassette sub-family E member
FT 1.
FT /FTId=PRO_0000093316.
FT DOMAIN 7 37 4Fe-4S ferredoxin-type 1.
FT DOMAIN 46 75 4Fe-4S ferredoxin-type 2.
FT DOMAIN 79 315 ABC transporter 1.
FT DOMAIN 342 562 ABC transporter 2.
FT NP_BIND 110 117 ATP 1 (Potential).
FT NP_BIND 379 386 ATP 2 (Potential).
FT VARIANT 489 489 S -> C (polymorphism confirmed at protein
FT level; dbSNP:rs3816497).
FT /FTId=VAR_068914.
FT CONFLICT 118 118 T -> A (in Ref. 1; CAA53972).
FT CONFLICT 174 179 DQIPKA -> ARFLRL (in Ref. 1; CAA53972).
FT CONFLICT 471 473 ALA -> RLR (in Ref. 1; CAA53972/
FT CAA52920).
SQ SEQUENCE 599 AA; 67314 MW; 5D582B62E95BC7A6 CRC64;
MADKLTRIAI VNHDKCKPKK CRQECKKSCP VVRMGKLCIE VTPQSKIAWI SETLCIGCGI
CIKKCPFGAL SIVNLPSNLE KETTHRYCAN AFKLHRLPIP RPGEVLGLVG TNGIGKSTAL
KILAGKQKPN LGKYDDPPDW QEILTYFRGS ELQNYFTKIL EDDLKAIIKP QYVDQIPKAA
KGTVGSILDR KDETKTQAIV CQQLDLTHLK ERNVEDLSGG ELQRFACAVV CIQKADIFMF
DEPSSYLDVK QRLKAAITIR SLINPDRYII VVEHDLSVLD YLSDFICCLY GVPSAYGVVT
MPFSVREGIN IFLDGYVPTE NLRFRDASLV FKVAETANEE EVKKMCMYKY PGMKKKMGEF
ELAIVAGEFT DSEIMVMLGE NGTGKTTFIR MLAGRLKPDE GGEVPVLNVS YKPQKISPKS
TGSVRQLLHE KIRDAYTHPQ FVTDVMKPLQ IENIIDQEVQ TLSGGELQRV ALALCLGKPA
DVYLIDEPSA YLDSEQRLMA ARVVKRFILH AKKTAFVVEH DFIMATYLAD RVIVFDGVPS
KNTVANSPQT LLAGMNKFLS QLEITFRRDP NNYRPRINKL NSIKDVEQKK SGNYFFLDD
//
MIM
601213
*RECORD*
*FIELD* NO
601213
*FIELD* TI
*601213 RIBONUCLEASE 4 INHIBITOR; RNS4I
;;RNase L INHIBITOR;;
ATP-BINDING CASSETTE, SUBFAMILY E, MEMBER 1; ABCE1
read more*FIELD* TX
CLONING
The 2-5A/RNase L system is a main pathway for viral interferon (147660)
action and may play a general role in RNA metabolism. In the pathway,
IFN stimulation activates 2-5A synthetases which convert ATP into a set
of unusual oligomers known as 2-5A; these oligomers in turn activate
RNase L (RNase 4; 180435), which leads to inhibition of protein
synthesis by cleaving mRNAs at the 3-prime side of UpNp sequences
(summary by Bisbal et al., 1995).
Bisbal et al. (1995) described the RNase L inhibitor, a potentially
important mediator of the 2-5A/RNase L pathway. RNase L inhibitor blocks
the activity of ribonuclease L. The authors cloned the human RNase L
inhibitor (symbolized RLI by them) from a Daudi cell expression cDNA
library using a radiolabeled 2-5ApCp oligomer. The full-length RLI cDNA
encodes a predicted 599-amino acid protein which contains 2 repeated
ATP/GTP-binding motifs and an internal repeat of 128 amino acids with
53% sequence identity to each other. Northern blots showed 3.5- and
2.8-kb transcripts in HeLa and Daudi cells which differ in their 3-prime
untranslated regions. When the mRNA was expressed in reticulocyte
extracts Bisbal et al. (1995) showed that both 2-5A binding and nuclease
activities of RNase L were abrogated. Furthermore, they found that the
inhibition occurred through association of the inhibitor with RNase L
and both proteins were coprecipitated with a nuclease-specific
monoclonal antibody.
Aubry et al. (1996) also cloned the RNS4I gene and found both a 3.8-kb
and a 2.4-kb transcript expressed differentially in all tissues
examined. Highest expression of the 2.4-kb transcript was found in the
testis, while the 3.8-kb transcript was most abundant in ovaries,
testis, spleen, and pancreas.
MAPPING
Diriong et al. (1996) mapped the gene, symbolized RNS4I, to 4q31 by
fluorescence in situ hybridization. Aubry et al. (1996) confirmed the
mapping to 4q21 by in situ hybridization.
*FIELD* RF
1. Aubry, F.; Mattei, M.-G.; Barque, J.-P.; Galibert, F.: Chromosomal
localization and expression pattern of the RNase L inhibitor gene. FEBS
Lett. 381: 135-139, 1996.
2. Bisbal, C.; Martinand, C.; Silhol, M.; Lebleu, B.; Salehzada, T.
: Cloning and characterization of a RNase L inhibitor: a new component
of the interferon-regulated 2-5A pathway. J. Biol. Chem. 270: 13308-13317,
1995.
3. Diriong, S.; Salehzada, T.; Bisbal, C.; Martinand, C.; Taviaux,
S.: Localization of the ribonuclease L inhibitor gene (RNS4I), a
new member of the interferon-regulated 2-5A pathway, to 4q31 by fluorescence
in situ hybridization. Genomics 32: 488-490, 1996.
*FIELD* CN
Alan F. Scott - updated: 5/20/1996
*FIELD* CD
Alan F. Scott: 4/18/1996
*FIELD* ED
alopez: 11/29/2010
carol: 2/27/2001
mark: 5/20/1996
terry: 5/20/1996
mark: 4/18/1996
terry: 4/18/1996
mark: 4/18/1996
*RECORD*
*FIELD* NO
601213
*FIELD* TI
*601213 RIBONUCLEASE 4 INHIBITOR; RNS4I
;;RNase L INHIBITOR;;
ATP-BINDING CASSETTE, SUBFAMILY E, MEMBER 1; ABCE1
read more*FIELD* TX
CLONING
The 2-5A/RNase L system is a main pathway for viral interferon (147660)
action and may play a general role in RNA metabolism. In the pathway,
IFN stimulation activates 2-5A synthetases which convert ATP into a set
of unusual oligomers known as 2-5A; these oligomers in turn activate
RNase L (RNase 4; 180435), which leads to inhibition of protein
synthesis by cleaving mRNAs at the 3-prime side of UpNp sequences
(summary by Bisbal et al., 1995).
Bisbal et al. (1995) described the RNase L inhibitor, a potentially
important mediator of the 2-5A/RNase L pathway. RNase L inhibitor blocks
the activity of ribonuclease L. The authors cloned the human RNase L
inhibitor (symbolized RLI by them) from a Daudi cell expression cDNA
library using a radiolabeled 2-5ApCp oligomer. The full-length RLI cDNA
encodes a predicted 599-amino acid protein which contains 2 repeated
ATP/GTP-binding motifs and an internal repeat of 128 amino acids with
53% sequence identity to each other. Northern blots showed 3.5- and
2.8-kb transcripts in HeLa and Daudi cells which differ in their 3-prime
untranslated regions. When the mRNA was expressed in reticulocyte
extracts Bisbal et al. (1995) showed that both 2-5A binding and nuclease
activities of RNase L were abrogated. Furthermore, they found that the
inhibition occurred through association of the inhibitor with RNase L
and both proteins were coprecipitated with a nuclease-specific
monoclonal antibody.
Aubry et al. (1996) also cloned the RNS4I gene and found both a 3.8-kb
and a 2.4-kb transcript expressed differentially in all tissues
examined. Highest expression of the 2.4-kb transcript was found in the
testis, while the 3.8-kb transcript was most abundant in ovaries,
testis, spleen, and pancreas.
MAPPING
Diriong et al. (1996) mapped the gene, symbolized RNS4I, to 4q31 by
fluorescence in situ hybridization. Aubry et al. (1996) confirmed the
mapping to 4q21 by in situ hybridization.
*FIELD* RF
1. Aubry, F.; Mattei, M.-G.; Barque, J.-P.; Galibert, F.: Chromosomal
localization and expression pattern of the RNase L inhibitor gene. FEBS
Lett. 381: 135-139, 1996.
2. Bisbal, C.; Martinand, C.; Silhol, M.; Lebleu, B.; Salehzada, T.
: Cloning and characterization of a RNase L inhibitor: a new component
of the interferon-regulated 2-5A pathway. J. Biol. Chem. 270: 13308-13317,
1995.
3. Diriong, S.; Salehzada, T.; Bisbal, C.; Martinand, C.; Taviaux,
S.: Localization of the ribonuclease L inhibitor gene (RNS4I), a
new member of the interferon-regulated 2-5A pathway, to 4q31 by fluorescence
in situ hybridization. Genomics 32: 488-490, 1996.
*FIELD* CN
Alan F. Scott - updated: 5/20/1996
*FIELD* CD
Alan F. Scott: 4/18/1996
*FIELD* ED
alopez: 11/29/2010
carol: 2/27/2001
mark: 5/20/1996
terry: 5/20/1996
mark: 4/18/1996
terry: 4/18/1996
mark: 4/18/1996