ABCF1_RAT
ID ABCF1_RAT Reviewed; 839 AA.
AC Q6MG08; Q9ERQ2;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=ATP-binding cassette sub-family F member 1;
DE AltName: Full=ATP-binding cassette 50;
GN Name=Abcf1; Synonyms=Abc50;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15060004; DOI=10.1101/gr.1987704;
RA Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T., Inoko H.,
RA Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.;
RT "The genomic sequence and comparative analysis of the rat major
RT histocompatibility complex.";
RL Genome Res. 14:631-639(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 26-839, FUNCTION, ASSOCIATION WITH RIBOSOMES,
RP AND INTERACTION WITH EIF2.
RC STRAIN=Wistar; TISSUE=Skeletal muscle;
RX PubMed=10931828; DOI=10.1074/jbc.m002868200;
RA Tyzack J.K., Wang X., Belsham G.J., Proud C.G.;
RT "ABC50 interacts with eukaryotic initiation factor 2 and associates with
RT the ribosome in an ATP-dependent manner.";
RL J. Biol. Chem. 275:34131-34139(2000).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109; SER-140; THR-195;
RP SER-197 AND SER-227, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Required for efficient Cap- and IRES-mediated mRNA
CC translation initiation. Not involved in the ribosome biogenesis (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:10931828}.
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-109 and Ser-140 by CK2; inhibits association of
CC EIF2 with ribosomes (By similarity). {ECO:0000250}.
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DR EMBL; BX883048; CAE84039.1; -; Genomic_DNA.
DR EMBL; AF293383; AAG23960.1; -; mRNA.
DR RefSeq; NP_001103353.1; NM_001109883.2.
DR AlphaFoldDB; Q6MG08; -.
DR SMR; Q6MG08; -.
DR IntAct; Q6MG08; 3.
DR STRING; 10116.ENSRNOP00000001049; -.
DR iPTMnet; Q6MG08; -.
DR PhosphoSitePlus; Q6MG08; -.
DR jPOST; Q6MG08; -.
DR PaxDb; Q6MG08; -.
DR PRIDE; Q6MG08; -.
DR GeneID; 85493; -.
DR KEGG; rno:85493; -.
DR UCSC; RGD:620286; rat.
DR CTD; 23; -.
DR RGD; 620286; Abcf1.
DR VEuPathDB; HostDB:ENSRNOG00000000799; -.
DR eggNOG; KOG0066; Eukaryota.
DR HOGENOM; CLU_000604_36_5_1; -.
DR InParanoid; Q6MG08; -.
DR OMA; RYFMDKI; -.
DR OrthoDB; 580544at2759; -.
DR PhylomeDB; Q6MG08; -.
DR Reactome; R-RNO-382556; ABC-family proteins mediated transport.
DR PRO; PR:Q6MG08; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000000799; Expressed in pancreas and 20 other tissues.
DR Genevisible; Q6MG08; RN.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IDA:RGD.
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:0006412; P:translation; NAS:RGD.
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..839
FT /note="ATP-binding cassette sub-family F member 1"
FT /id="PRO_0000093322"
FT DOMAIN 298..542
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 619..834
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..600
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..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 330..337
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 652..659
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 105
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NE71"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 195
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 589
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NE71"
FT CONFLICT 201
FT /note="D -> DK (in Ref. 2; AAG23960)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 839 AA; 95252 MW; 0EB651DD0B3F5B24 CRC64;
MPKGPKQQPP EPEWIGDGEG TSPADKVVKK GKKDKKTKKT FFEELAVEDK QAGEEEKLQK
EKEQQQQQQQ QKKKRDTRKG RRKKDVDDDD DGDERVLMER LKQLSVPASD EEDEVPVPVP
RGRKKAKGGN VFEALIQDES EEEKEEEEEK PVLKPAKPEK NRINKAVAEE PPGLRNKKGK
EEKSKGKAKN KPSATDSEGE DDEDMTKEKE PPRPGKDKDK KGAEQGSEEE KEEKEGEVKA
NDPYAHLSKK EKKKLKKQMD YERQVESLKA ANAAENDFSV SQAEVSSRQA MLENASDIKL
EKFSISAHGK ELFVNADLYI VAGRRYGLVG PNGKGKTTLL KHIANRALSI PPNIDVLLCE
QEVVADETPA VQAVLRADTK RLRLLEEEKR LQGQLEQGDD TAAEKLEKVY EELRATGAAA
AEAKARRILA GLGFDPEMQN RPTQKFSGGW RMRVSLARAL FMEPTLLMLD EPTNHLDLNA
VIWLNNYLQG WRKTLLIVSH DQGFLDDVCT DIIHLDTQRL HYYRGNYMTF KKMYQQKQKE
LLKQYEKQEK KLKELKAGGK STKQAEKQTK EVLTRKQQKC RRKNQDEESQ DPPELLKRPR
EYTVRFTFPD PPPLSPPVLG LHGVTFGYEG QKPLFKNLDF GIDMDSRICI VGPNGVGKST
LLLLLTGKLT PTNGEMRKNH RLKIGFFNQQ YAEQLHMEET PTEYLQRGFN LPYQDARKCL
GRFGLESHAH TIQICKLSGG QKARVVFAEL ACREPDVLIL DEPTNNLDIE SIDALGEAIN
EYKGAVIVVS HDARLITETN CQLWVVEEQS VSQIDGDFDD YKREVLEALG EVMVNRPRD
