ID   ARB1_YEAST              Reviewed;         610 AA.
AC   P40024; D3DLT5;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 188.
DE   RecName: Full=ABC transporter ATP-binding protein ARB1;
DE            EC=3.6.5.- {ECO:0000269|PubMed:16260602, ECO:0000305|PubMed:31189955};
DE   AltName: Full=ATP-binding cassette protein involved in ribosome biogenesis 1;
GN   Name=ARB1; OrderedLocusNames=YER036C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169868;
RA   Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA   Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA   Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA   Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA   Botstein D., Davis R.W.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL   Nature 387:78-81(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP   LSG1.
RX   PubMed=16260602; DOI=10.1128/mcb.25.22.9859-9873.2005;
RA   Dong J., Lai R., Jennings J.L., Link A.J., Hinnebusch A.G.;
RT   "The novel ATP-binding cassette protein ARB1 is a shuttling factor that
RT   stimulates 40S and 60S ribosome biogenesis.";
RL   Mol. Cell. Biol. 25:9859-9873(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43; SER-65; SER-196 AND
RP   THR-446, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [7] {ECO:0007744|PDB:6R84}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) OF 85-603 IN COMPLEX WITH
RP   60S RIBOSOME AND VMS1, FUNCTION, AND MUTAGENESIS OF 229-GLY-GLY-230;
RP   TYR-346 AND GLY-519.
RX   PubMed=31189955; DOI=10.1038/s41586-019-1307-z;
RA   Su T., Izawa T., Thoms M., Yamashita Y., Cheng J., Berninghausen O.,
RA   Hartl F.U., Inada T., Neupert W., Beckmann R.;
RT   "Structure and function of Vms1 and Arb1 in RQC and mitochondrial proteome
RT   homeostasis.";
RL   Nature 570:538-542(2019).
CC   -!- FUNCTION: ATPase that stimulates 40S and 60S ribosome biogenesis
CC       (PubMed:16260602). Also involved in ribosome-associated quality control
CC       (RQC) pathway, a pathway that mediates ubiquitination and extraction of
CC       incompletely synthesized nascent chains for proteasomal degradation:
CC       localizes to the ribosomal E-site and stimulates VMS1-dependent tRNA
CC       cleavage (PubMed:31189955). {ECO:0000269|PubMed:16260602,
CC       ECO:0000269|PubMed:31189955}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000269|PubMed:16260602, ECO:0000305|PubMed:31189955};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC         Evidence={ECO:0000269|PubMed:16260602, ECO:0000305|PubMed:31189955};
CC   -!- SUBUNIT: Interacts with LSG1. {ECO:0000269|PubMed:16260602}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16260602}. Nucleus
CC       {ECO:0000269|PubMed:16260602}. Note=Shuttles between the cytoplasm and
CC       the nucleus. {ECO:0000269|PubMed:16260602}.
CC   -!- MISCELLANEOUS: Present with 17600 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family.
CC       EF3 subfamily. {ECO:0000305}.
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DR   EMBL; U18796; AAB64571.1; -; Genomic_DNA.
DR   EMBL; BK006939; DAA07689.1; -; Genomic_DNA.
DR   PIR; S50539; S50539.
DR   RefSeq; NP_010953.1; NM_001178927.1.
DR   PDB; 6R84; EM; 3.60 A; A=85-603.
DR   PDBsum; 6R84; -.
DR   AlphaFoldDB; P40024; -.
DR   EMDB; EMD-4751; -.
DR   SMR; P40024; -.
DR   BioGRID; 36771; 133.
DR   DIP; DIP-4341N; -.
DR   IntAct; P40024; 27.
DR   MINT; P40024; -.
DR   STRING; 4932.YER036C; -.
DR   iPTMnet; P40024; -.
DR   MaxQB; P40024; -.
DR   PaxDb; 4932-YER036C; -.
DR   PeptideAtlas; P40024; -.
DR   EnsemblFungi; YER036C_mRNA; YER036C; YER036C.
DR   GeneID; 856758; -.
DR   KEGG; sce:YER036C; -.
DR   AGR; SGD:S000000838; -.
DR   SGD; S000000838; ARB1.
DR   VEuPathDB; FungiDB:YER036C; -.
DR   eggNOG; KOG0927; Eukaryota.
DR   GeneTree; ENSGT00630000089910; -.
DR   HOGENOM; CLU_000604_36_6_1; -.
DR   InParanoid; P40024; -.
DR   OMA; QYEGTML; -.
DR   OrthoDB; 25181at2759; -.
DR   BioCyc; YEAST:G3O-30217-MONOMER; -.
DR   BioGRID-ORCS; 856758; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P40024; -.
DR   Proteomes; UP000002311; Chromosome V.
DR   RNAct; P40024; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR   GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IDA:UniProtKB.
DR   GO; GO:0000056; P:ribosomal small subunit export from nucleus; IMP:SGD.
DR   GO; GO:0042254; P:ribosome biogenesis; IMP:SGD.
DR   CDD; cd03221; ABCF_EF-3; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   PANTHER; PTHR19211:SF15; ATP-BINDING CASSETTE SUB-FAMILY F MEMBER 2; 1.
DR   PANTHER; PTHR19211; ATP-BINDING TRANSPORT PROTEIN-RELATED; 1.
DR   Pfam; PF00005; ABC_tran; 2.
DR   Pfam; PF12848; ABC_tran_Xtn; 1.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cytoplasm; Hydrolase; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..610
FT                   /note="ABC transporter ATP-binding protein ARB1"
FT                   /id="PRO_0000093463"
FT   DOMAIN          82..323
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          393..610
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..43
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         114..121
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         428..435
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   MOD_RES         43
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         65
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         196
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         446
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MUTAGEN         229..230
FT                   /note="GG->DE: Abolished ATPase activity, leading to
FT                   impaired ability to stimulate VMS1 activity; when
FT                   associated with D-519."
FT                   /evidence="ECO:0000269|PubMed:31189955"
FT   MUTAGEN         346
FT                   /note="Y->A: Abolished ATPase activity, leading to impaired
FT                   ability to stimulate VMS1 activity."
FT                   /evidence="ECO:0000269|PubMed:31189955"
FT   MUTAGEN         519
FT                   /note="G->D: Abolished ATPase activity, leading to impaired
FT                   ability to stimulate VMS1 activity; when associated with
FT                   229-D-E-230."
FT                   /evidence="ECO:0000269|PubMed:31189955"
SQ   SEQUENCE   610 AA;  68377 MW;  0E5DB4A33059B4F0 CRC64;
     MPPVSASKAK RDAKKAEREA KKAAAGKTIR KLGRKKEAAA EESEVDAAAR EIKMMKLQQD
     KDGLSDRVVT GVLSSLETSR DIKLSSVSLL FHGKVLIQDS GLELNYGRRY GLLGENGCGK
     STFLKALATR EYPIPEHIDI YLLDEPAEPS ELSALDYVVT EAQHELKRIE DLVEKTILED
     GPESELLEPL YERMDSLDPD TFESRAAIIL IGLGFNKKTI LKKTKDMSGG WKMRVALAKA
     LFVKPTLLLL DDPTAHLDLE ACVWLEEYLK RFDRTLVLVS HSQDFLNGVC TNMIDMRAQK
     LTAYGGNYDS YHKTRSELET NQMKQYNKQQ EEIQHIKKFI ASAGTYANLV KQAKSRQKIL
     DKMEADGLVQ PVVPDKVFSF RFPQVERLPP PVLAFDDISF HYESNPSENL YEHLNFGVDM
     DSRIALVGPN GVGKSTLLKI MTGELTPQSG RVSRHTHVKL GVYSQHSQDQ LDLTKSALEF
     VRDKYSNISQ DFQFWRGQLG RYGLTGEGQT VQMATLSEGQ RSRVVFALLA LEQPNVLLLD
     EPTNGLDIPT IDSLADAINE FNGGVVVVSH DFRLLDKIAQ DIFVVENKTA TRWDGSILQY
     KNKLAKNVVL
//