ABCE1_MOUSE
ID ABCE1_MOUSE Reviewed; 599 AA.
AC P61222; O88793; Q13181; Q13864; Q96AL0; Q96B10; Q99K66;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=ATP-binding cassette sub-family E member 1;
DE AltName: Full=RNase L inhibitor;
DE AltName: Full=Ribonuclease 4 inhibitor;
DE Short=RNS4I;
GN Name=Abce1; Synonyms=Rli;
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 [MRNA].
RX PubMed=9524254; DOI=10.1016/s0378-1119(98)00040-7;
RA Benoit De Coignac A., Bisbal C., Lebleu B., Salehzada T.;
RT "cDNA cloning and expression analysis of the murine ribonuclease L
RT inhibitor.";
RL Gene 209:149-156(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP FUNCTION.
RX PubMed=10866653; DOI=10.1128/mcb.20.14.4959-4969.2000;
RA Bisbal C., Silhol M., Laubenthal H., Kaluza T., Carnac G., Milligan L.,
RA Le Roy F., Salehzada T.;
RT "The 2'-5' oligoadenylate/RNase L/RNase L inhibitor pathway regulates both
RT MyoD mRNA stability and muscle cell differentiation.";
RL Mol. Cell. Biol. 20:4959-4969(2000).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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).
CC -!- FUNCTION: Cotranslational quality control factor involved in the No-Go
CC Decay (NGD) pathway (By similarity). Together with PELO and HBS1L, is
CC required for 48S complex formation from 80S ribosomes and dissociation
CC of vacant 80S ribosomes (By similarity). Together with PELO and HBS1L,
CC recognizes stalled ribosomes and promotes dissociation of elongation
CC complexes assembled on non-stop mRNAs; this triggers endonucleolytic
CC cleavage of the mRNA, a mechanism to release non-functional ribosomes
CC and to degrade damaged mRNAs as part of the No-Go Decay (NGD) pathway
CC (By similarity). Plays a role in the regulation of mRNA turnover
CC (PubMed:10866653). Plays a role in quality control of translation of
CC mitochondrial outer membrane-localized mRNA (By similarity). As part of
CC the PINK1-regulated signaling, ubiquitinated by CNOT4 upon mitochondria
CC damage; this modification generates polyubiquitin signals that recruit
CC autophagy receptors to the mitochondrial outer membrane and initiate
CC mitophagy (By similarity). RNASEL-specific protein inhibitor which
CC antagonizes the binding of 2-5A (5'-phosphorylated 2',5'-linked
CC oligoadenylates) to RNASEL (By similarity). Negative regulator of the
CC anti-viral effect of the interferon-regulated 2-5A/RNASEL pathway (By
CC similarity). {ECO:0000250|UniProtKB:P61221,
CC ECO:0000269|PubMed:10866653}.
CC -!- SUBUNIT: Interacts with PINK1, CNOT4 and PELO. Probably heterodimerizes
CC with RNASEL; this interaction inhibits RNASEL.
CC {ECO:0000250|UniProtKB:P61221}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Mitochondrion
CC {ECO:0000250}. Note=Localized to clusters of virus formation at the
CC plasma membrane. {ECO:0000250}.
CC -!- PTM: Ubiquitinated by CNOT4 (By similarity). Ubiquitination mediates
CC the recruitment of autophagy receptors to the mitochondrial outer
CC membrane and initiates mitophagy (By similarity).
CC {ECO:0000250|UniProtKB:P61221}.
CC -!- MISCELLANEOUS: The ABC transporter domains seem not to be functional.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCE family.
CC {ECO:0000305}.
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DR EMBL; U90446; AAC24730.1; -; mRNA.
DR EMBL; BC005422; AAH05422.1; -; mRNA.
DR CCDS; CCDS22438.1; -.
DR PIR; JC6555; JC6555.
DR RefSeq; NP_056566.2; NM_015751.2.
DR AlphaFoldDB; P61222; -.
DR SMR; P61222; -.
DR BioGRID; 204855; 42.
DR IntAct; P61222; 1.
DR STRING; 10090.ENSMUSP00000079379; -.
DR iPTMnet; P61222; -.
DR PhosphoSitePlus; P61222; -.
DR SwissPalm; P61222; -.
DR EPD; P61222; -.
DR jPOST; P61222; -.
DR PaxDb; P61222; -.
DR PeptideAtlas; P61222; -.
DR PRIDE; P61222; -.
DR ProteomicsDB; 286047; -.
DR Antibodypedia; 27438; 328 antibodies from 31 providers.
DR DNASU; 24015; -.
DR Ensembl; ENSMUST00000080536; ENSMUSP00000079379; ENSMUSG00000058355.
DR GeneID; 24015; -.
DR KEGG; mmu:24015; -.
DR UCSC; uc009mit.1; mouse.
DR CTD; 6059; -.
DR MGI; MGI:1195458; Abce1.
DR VEuPathDB; HostDB:ENSMUSG00000058355; -.
DR eggNOG; KOG0063; Eukaryota.
DR GeneTree; ENSGT00390000015089; -.
DR HOGENOM; CLU_017344_4_1_1; -.
DR InParanoid; P61222; -.
DR OMA; VCVQQAD; -.
DR OrthoDB; 359213at2759; -.
DR PhylomeDB; P61222; -.
DR TreeFam; TF105206; -.
DR Reactome; R-MMU-8983711; OAS antiviral response.
DR Reactome; R-MMU-909733; Interferon alpha/beta signaling.
DR BioGRID-ORCS; 24015; 24 hits in 72 CRISPR screens.
DR ChiTaRS; Abce1; mouse.
DR PRO; PR:P61222; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P61222; protein.
DR Bgee; ENSMUSG00000058355; Expressed in floor plate of midbrain and 276 other tissues.
DR ExpressionAtlas; P61222; baseline and differential.
DR Genevisible; P61222; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0060698; F:endoribonuclease inhibitor activity; ISO:MGI.
DR GO; GO:0005506; F:iron ion binding; IBA:GO_Central.
DR GO; GO:0043024; F:ribosomal small subunit binding; IBA:GO_Central.
DR GO; GO:0060702; P:negative regulation of endoribonuclease activity; ISO:MGI.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0000054; P:ribosomal subunit export from nucleus; IBA:GO_Central.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
DR GO; GO:0006415; P:translational termination; IBA:GO_Central.
DR CDD; cd03236; ABC_RNaseL_inhibitor_domain1; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013283; RLI1.
DR InterPro; IPR034348; RLI_dom_1.
DR InterPro; IPR007209; RNaseL-inhib-like_metal-bd_dom.
DR PANTHER; PTHR19248; PTHR19248; 1.
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 4Fe-4S; ATP-binding; Chaperone; Cytoplasm; Iron; Iron-sulfur;
KW Metal-binding; Mitochondrion; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Translation regulation; Ubl conjugation.
FT CHAIN 1..599
FT /note="ATP-binding cassette sub-family E member 1"
FT /id="PRO_0000093317"
FT DOMAIN 7..37
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 46..75
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 79..315
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 342..562
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 110..117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 379..386
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61221"
FT MOD_RES 550
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P61221"
FT CONFLICT 153
FT /note="Q -> K (in Ref. 1; AAC24730)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="K -> T (in Ref. 1; AAC24730)"
FT /evidence="ECO:0000305"
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
