ABCF1_MOUSE
ID ABCF1_MOUSE Reviewed; 837 AA.
AC Q6P542; Q6NV71;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=ATP-binding cassette sub-family F member 1;
GN Name=Abcf1;
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].
RC STRAIN=ICR; TISSUE=Limb, and Trophoblast stem cell;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103; SER-107 AND SER-138, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-103; SER-138 AND
RP SER-194, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107 AND SER-194, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103; SER-107; SER-138 AND
RP SER-194, AND 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: Required for efficient Cap- and IRES-mediated mRNA
CC translation initiation. Not involved in the ribosome biogenesis (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via N-terminus) with EIF2S1; the interaction is
CC independent of its phosphorylated status. Associates (via both ABC
CC transporter domains) with the ribosomes (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8NE71}.
CC Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q8NE71}. Nucleus envelope
CC {ECO:0000250|UniProtKB:Q8NE71}.
CC -!- PTM: Phosphorylated at phosphoserine and phosphothreonine.
CC Phosphorylation on Ser-107 and Ser-138 by CK2; inhibits association of
CC EIF2 with ribosomes (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family.
CC EF3 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC063094; AAH63094.1; -; mRNA.
DR EMBL; BC068282; AAH68282.1; -; mRNA.
DR CCDS; CCDS28713.1; -.
DR RefSeq; NP_038882.1; NM_013854.1.
DR AlphaFoldDB; Q6P542; -.
DR SMR; Q6P542; -.
DR BioGRID; 230310; 5.
DR IntAct; Q6P542; 54.
DR MINT; Q6P542; -.
DR STRING; 10090.ENSMUSP00000036881; -.
DR iPTMnet; Q6P542; -.
DR PhosphoSitePlus; Q6P542; -.
DR EPD; Q6P542; -.
DR jPOST; Q6P542; -.
DR MaxQB; Q6P542; -.
DR PaxDb; Q6P542; -.
DR PeptideAtlas; Q6P542; -.
DR PRIDE; Q6P542; -.
DR ProteomicsDB; 285904; -.
DR Antibodypedia; 2796; 309 antibodies from 33 providers.
DR DNASU; 224742; -.
DR Ensembl; ENSMUST00000043757; ENSMUSP00000036881; ENSMUSG00000038762.
DR GeneID; 224742; -.
DR KEGG; mmu:224742; -.
DR UCSC; uc008cjk.1; mouse.
DR CTD; 23; -.
DR MGI; MGI:1351658; Abcf1.
DR VEuPathDB; HostDB:ENSMUSG00000038762; -.
DR eggNOG; KOG0066; Eukaryota.
DR GeneTree; ENSGT00940000158329; -.
DR HOGENOM; CLU_000604_36_5_1; -.
DR InParanoid; Q6P542; -.
DR OMA; RYFMDKI; -.
DR OrthoDB; 580544at2759; -.
DR PhylomeDB; Q6P542; -.
DR TreeFam; TF105207; -.
DR Reactome; R-MMU-382556; ABC-family proteins mediated transport.
DR BioGRID-ORCS; 224742; 15 hits in 72 CRISPR screens.
DR ChiTaRS; Abcf1; mouse.
DR PRO; PR:Q6P542; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q6P542; protein.
DR Bgee; ENSMUSG00000038762; Expressed in retinal neural layer and 259 other tissues.
DR ExpressionAtlas; Q6P542; baseline and differential.
DR Genevisible; Q6P542; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0042788; C:polysomal ribosome; ISS:UniProtKB.
DR GO; GO:0005840; C:ribosome; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
DR GO; GO:0008494; F:translation activator activity; ISS:UniProtKB.
DR GO; GO:0045727; P:positive regulation of translation; ISS:UniProtKB.
DR GO; GO:0006413; P:translational initiation; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR032781; ABC_tran_Xtn.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF12848; ABC_tran_Xtn; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW Activator; ATP-binding; Cytoplasm; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..837
FT /note="ATP-binding cassette sub-family F member 1"
FT /id="PRO_0000093319"
FT DOMAIN 296..540
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 617..832
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 328..335
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 650..657
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NE71"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"
FT MOD_RES 107
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 138
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:21183079"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6MG08"
FT MOD_RES 587
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NE71"
SQ SEQUENCE 837 AA; 94945 MW; 9CCD1753D5357944 CRC64;
MPKGPKQQPP EPEWIGDGEG TSPADKVVKK GKKDKKTKKT FFEELAVEDK QAGEEEKLQK
EKEQQQQQQQ QKKKRDTRKG RRKKDVDDDS DERVLMERLK QLSVPASDEE DEVPAPIPRG
RKKAKGGNVF EALIQDDSEE EEEEEENRVL KPAKPEKNRI NKAVAEEPPG LRSKKGKEEK
SKGKAKSKPA AADSEGEEEE EDTAKEKEPP QQGKDRDKKE AEQGSGEEKE EKEGDLKAND
PYANLSKKEK KKLKKQMDYE RQVESLKAAN AAENDFSVSQ AEVSSRQAML ENASDIKLEK
FSISAHGKEL FVNADLYIVA GRRYGLVGPN GKGKTTLLKH IANRALSIPP NIDVLLCEQE
VVADETPAVQ AVLRADTKRL RLLEEERRLQ GQLEQGDDTA AEKLEKVYEE LRATGAAAAE
AKARRILAGL GFDPEMQNRP TQKFSGGWRM RVSLARALFM EPTLLMLDEP TNHLDLNAVI
WLNNYLQGWR KTLLIVSHDQ GFLDDVCTDI IHLDTQRLHY YRGNYMTFKK MYQQKQKELL
KQYEKQEKKL KELKAGGKST KQAEKQTKEV LTRKQQKCRR KNQDEESQEP PELLKRPKEY
TVRFTFPDPP PLSPPVLGLH GVTFGYEGQK PLFKNLDFGI DMDSRICIVG PNGVGKSTLL
LLLTGKLTPT NGEMRKNHRL KIGFFNQQYA EQLHMEETPT EYLQRSFNLP YQDARKCLGR
FGLESHAHTI QICKLSGGQK ARVVFAELAC REPDVLILDE PTNNLDIESI DALGEAINDY
KGAVIVVSHD ARLITETNCQ LWVVEEQGVS QIDGDFDDYK REVLEALGEV MVNRPRD
