ABCF1_PANTR
ID ABCF1_PANTR Reviewed; 807 AA.
AC Q7YR37; Q1XI20;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=ATP-binding cassette sub-family F member 1;
DE AltName: Full=ATP-binding cassette 50;
GN Name=ABCF1; Synonyms=ABC50;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12799463; DOI=10.1073/pnas.1230533100;
RA Anzai T., Shiina T., Kimura N., Yanagiya K., Kohara S., Shigenari A.,
RA Yamagata T., Kulski J.K., Naruse T.K., Fujimori Y., Fukuzumi Y.,
RA Yamazaki M., Tashiro H., Iwamoto C., Umehara Y., Imanishi T., Meyer A.,
RA Ikeo K., Gojobori T., Bahram S., Inoko H.;
RT "Comparative sequencing of human and chimpanzee MHC class I regions unveils
RT insertions/deletions as the major path to genomic divergence.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7708-7713(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16702430; DOI=10.1534/genetics.106.057034;
RA Shiina T., Ota M., Shimizu S., Katsuyama Y., Hashimoto N., Takasu M.,
RA Anzai T., Kulski J.K., Kikkawa E., Naruse T., Kimura N., Yanagiya K.,
RA Watanabe A., Hosomichi K., Kohara S., Iwamoto C., Umehara Y., Meyer A.,
RA Wanner V., Sano K., Macquin C., Ikeo K., Tokunaga K., Gojobori T.,
RA Inoko H., Bahram S.;
RT "Rapid evolution of major histocompatibility complex class I genes in
RT primates generates new disease alleles in humans via hitchhiking
RT diversity.";
RL Genetics 173:1555-1570(2006).
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-109 and Ser-140 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; BA000041; BAC78179.1; -; Genomic_DNA.
DR EMBL; AB210139; BAE92749.1; -; Genomic_DNA.
DR EMBL; AB210140; BAE92750.1; -; Genomic_DNA.
DR RefSeq; NP_001035838.1; NM_001042379.1.
DR AlphaFoldDB; Q7YR37; -.
DR SMR; Q7YR37; -.
DR PaxDb; Q7YR37; -.
DR GeneID; 462543; -.
DR KEGG; ptr:462543; -.
DR CTD; 23; -.
DR eggNOG; KOG0066; Eukaryota.
DR HOGENOM; CLU_000604_36_5_1; -.
DR InParanoid; Q7YR37; -.
DR OrthoDB; 580544at2759; -.
DR TreeFam; TF105207; -.
DR Proteomes; UP000002277; Unplaced.
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_0000093320"
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..221
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..63
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 145..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..221
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 24
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; by CK2"
FT /evidence="ECO:0000250|UniProtKB:Q8NE71"
FT MOD_RES 140
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:Q8NE71"
FT MOD_RES 166
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; 91652 MW; BEA51E035C5F1947 CRC64;
MPKAPKQQPP EPEWIGDGES TSPSDKVVKK GKKDKKIKKT FFEELAVEDK QAGEEEKVLK
EKEQQQQQQQ VQQKKKRDTR KGRRKKDVDD DGEEKELMER LKKLSVPASD EEDEVPAPKP
RGGKKTKGGN VFAALIQDQS EEEEEEEKHP PKPAKPEKNR INKAVSEEQQ PALKGKKGKE
EKSKGKAKPQ NKFAALDNEE EDKEEEIIKE KEPPKQGKEK AKKAEQMEYE RQVASLKAAN
AAENDFSVSQ AEMSSRQAML ENASDIKLEK FSISAHGKEL FVNADLYIVA SRRYGLVGPN
GKGKTTLLKH IANRALSIPP NIDVLLCEQE VVADETPAVQ AVLRADTKRL KLLEEERRLQ
GQLEQGDDTA AERLEKVYEE 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 HGEMRKNHRL KIGFFNQQYA
EQLRMEETPT EYLQRGFNLP YQDARKCLGR FGLESHAHTI QICKLSGGQK ARVVFAELAC
REPDVLILDE PTNNLDIESI DALGEAINEY KGAVIVVSHD ARLITETNCQ LWVVEEQSVS
QIDGDFEDYK REVLEALGEV MVSRPRE
