ID   ABCF1_PIG               Reviewed;         807 AA.
AC   Q767L0;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=ATP-binding cassette sub-family F member 1;
GN   Name=ABCF1;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Large white;
RX   PubMed=14673549; DOI=10.1007/s00251-003-0627-0;
RA   Shigenari A., Ando A., Renard C., Chardon P., Shiina T., Kulski J.K.,
RA   Yasue H., Inoko H.;
RT   "Nucleotide sequencing analysis of the swine 433-kb genomic segment located
RT   between the non-classical and classical SLA class I gene clusters.";
RL   Immunogenetics 55:695-705(2004).
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-110 and Ser-141 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}.
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DR   EMBL; AB113357; BAD08439.1; -; Genomic_DNA.
DR   RefSeq; NP_001116541.1; NM_001123069.1.
DR   AlphaFoldDB; Q767L0; -.
DR   SMR; Q767L0; -.
DR   STRING; 9823.ENSSSCP00000001420; -.
DR   PaxDb; Q767L0; -.
DR   PeptideAtlas; Q767L0; -.
DR   PRIDE; Q767L0; -.
DR   Ensembl; ENSSSCT00015047857; ENSSSCP00015018968; ENSSSCG00015034086.
DR   Ensembl; ENSSSCT00030086951; ENSSSCP00030040123; ENSSSCG00030061982.
DR   Ensembl; ENSSSCT00035087430; ENSSSCP00035036503; ENSSSCG00035064746.
DR   Ensembl; ENSSSCT00040098572; ENSSSCP00040044051; ENSSSCG00040071140.
DR   Ensembl; ENSSSCT00045068613; ENSSSCP00045048833; ENSSSCG00045039380.
DR   Ensembl; ENSSSCT00055061136; ENSSSCP00055049024; ENSSSCG00055030656.
DR   Ensembl; ENSSSCT00065084428; ENSSSCP00065036820; ENSSSCG00065061355.
DR   Ensembl; ENSSSCT00070049248; ENSSSCP00070041599; ENSSSCG00070024670.
DR   GeneID; 100144452; -.
DR   KEGG; ssc:100144452; -.
DR   CTD; 23; -.
DR   eggNOG; KOG0066; Eukaryota.
DR   HOGENOM; CLU_000604_36_5_1; -.
DR   InParanoid; Q767L0; -.
DR   OMA; RYFMDKI; -.
DR   OrthoDB; 580544at2759; -.
DR   TreeFam; TF105207; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Chromosome 7.
DR   Genevisible; Q767L0; SS.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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: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; 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   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   3: Inferred from homology;
KW   Activator; ATP-binding; Cytoplasm; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..807
FT                   /note="ATP-binding cassette sub-family F member 1"
FT                   /id="PRO_0000093321"
FT   DOMAIN          266..510
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          587..802
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   REGION          1..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          521..564
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        83..121
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..163
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..197
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..227
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         298..305
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         620..627
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         106
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NE71"
FT   MOD_RES         110
FT                   /note="Phosphoserine; by CK2"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NE71"
FT   MOD_RES         141
FT                   /note="Phosphoserine; by CK2"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NE71"
FT   MOD_RES         167
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NE71"
FT   MOD_RES         557
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NE71"
SQ   SEQUENCE   807 AA;  91637 MW;  A12F61517E5C7987 CRC64;
     MPKGPKQQPP EPEWIGDGES TSPTDKVVKK GKKDKKTKKT FFEELAVEDR QAGEEEKVLK
     EKEQQQQHQQ QQQKKKRDTR KGRRKKDVDD DDGEEKELME RLKKLSVPAS DEEEEAPAPV
     PRGGKKNKGG NVFAALIQDQ SEEEEEEEKH PPKPAKPEKN RINKAVSQEQ QPGPKGRKGK
     EEKSKGKAKP QNKFAALDDE EEQDEEEIKE KEPPKQGKEK AKKAEQMEYE RQVASLKAAN
     AAENDFSVSQ AEMSSRQAML ENASDIKLEK FSISAHGKEL FVNADLYIVA GRRYGLVGPN
     GKGKTTLLKH IANRALSIPP NIDVLLCEQE VVADETPAVQ AVLRADTKRL KLLEEERRLQ
     GQLEQGDDTA ADRLEKVYEE LRATGAAAAE AKARRILAGL GFDPEMQNRP TQKFSGGWRM
     RVSLARALFM EPTLLMLDEP TNHLDLNAVI WLNNYLQGWR KTLLIVSHDQ GFLDDVCTDI
     IHLDAQRLHY YRGNYMTFKK MYQQKQKELL KQYEKQEKKL KELKAGGKST KQAEKQTKEA
     LTRKQQKCRR KNQDEESQEA PELLKRPKEY TVRFTFPDPP PLSPPVLGLH GVTFGYEGQK
     PLFKNLDFGI DMDSRICIVG PNGVGKSTLL LLLTGKLTPT RGEMRKNHRL KIGFFNQQYA
     EQLRMEETPT EYLQRGFNLP YQDARKCLGR FGLESHAHTI QICKLSGGQK ARVVFAELAC
     REPDVLILDE PTNNLDIESI DALGEAINEY KGAVIVVSHD ARLITETNCQ LWVVEEQSVS
     QIDGDFDDYK REVLEALGEV MVSRPRE