ARB1_YEAST
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 03-AUG-2022, entry version 180.
DE RecName: Full=ABC transporter ATP-binding protein ARB1;
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, SUBCELLULAR LOCATION, AND INTERACTION WITH 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).
CC -!- FUNCTION: Stimulates 40S and 60S ribosome biogenesis.
CC {ECO:0000269|PubMed:16260602}.
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.
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 SMR; P40024; -.
DR BioGRID; 36771; 117.
DR DIP; DIP-4341N; -.
DR IntAct; P40024; 27.
DR MINT; P40024; -.
DR STRING; 4932.YER036C; -.
DR iPTMnet; P40024; -.
DR MaxQB; P40024; -.
DR PaxDb; P40024; -.
DR PRIDE; P40024; -.
DR EnsemblFungi; YER036C_mRNA; YER036C; YER036C.
DR GeneID; 856758; -.
DR KEGG; sce:YER036C; -.
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; DKMFLDN; -.
DR BioCyc; YEAST:G3O-30217-MON; -.
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; IMP:SGD.
DR GO; GO:0000056; P:ribosomal small subunit export from nucleus; IMP:SGD.
DR GO; GO:0042254; P:ribosome biogenesis; IMP:SGD.
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; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Nucleotide-binding; Nucleus;
KW 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"
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
