ARX1_YEAST
ID ARX1_YEAST Reviewed; 593 AA.
AC Q03862; D6VS88;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Probable metalloprotease ARX1;
DE EC=3.-.-.-;
DE AltName: Full=Associated with ribosomal export complex protein 1;
GN Name=ARX1; OrderedLocusNames=YDR101C; ORFNames=YD8557.10c;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE
RP PRE-60S RIBOSOMAL PARTICLES, AND SUBCELLULAR LOCATION.
RX PubMed=12374754; DOI=10.1093/emboj/cdf547;
RA Nissan T.A., Bassler J., Petfalski E., Tollervey D., Hurt E.;
RT "60S pre-ribosome formation viewed from assembly in the nucleolus until
RT export to the cytoplasm.";
RL EMBO J. 21:5539-5547(2002).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
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 [6]
RP FUNCTION, INTERACTION WITH REI1, AND ASSOCIATION WITH PRE-60S PARTICLES.
RX PubMed=16648468; DOI=10.1128/mcb.26.10.3718-3727.2006;
RA Hung N.J., Johnson A.W.;
RT "Nuclear recycling of the pre-60S ribosomal subunit-associated factor Arx1
RT depends on Rei1 in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 26:3718-3727(2006).
CC -!- FUNCTION: Probable metalloprotease involved in proper assembly of pre-
CC ribosomal particles during the biogenesis of the 60S ribosomal subunit.
CC Accompanies the pre-60S particles to the cytoplasm.
CC {ECO:0000269|PubMed:12374754, ECO:0000269|PubMed:16648468}.
CC -!- SUBUNIT: Component of the nucleoplasmic and cytoplasmic pre-60S
CC ribosomal particles. Interacts directly with REI1.
CC {ECO:0000269|PubMed:12374754, ECO:0000269|PubMed:16648468}.
CC -!- INTERACTION:
CC Q03862; P47019: ALB1; NbExp=3; IntAct=EBI-31385, EBI-26061;
CC Q03862; Q12080: NOP53; NbExp=3; IntAct=EBI-31385, EBI-29395;
CC Q03862; P38344: REI1; NbExp=5; IntAct=EBI-31385, EBI-21136;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- MISCELLANEOUS: Present with 45100 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peptidase M24 family. {ECO:0000305}.
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DR EMBL; Z47746; CAA87677.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11948.1; -; Genomic_DNA.
DR PIR; S51252; S51252.
DR RefSeq; NP_010386.1; NM_001180409.1.
DR PDB; 3JCT; EM; 3.08 A; 4=1-593.
DR PDB; 4V7F; EM; 8.70 A; l=1-593.
DR PDB; 4V8T; EM; 8.10 A; t=1-593.
DR PDB; 5APN; EM; 3.91 A; x=1-593.
DR PDB; 5APO; EM; 3.41 A; x=1-593.
DR PDB; 5JCS; EM; 9.50 A; u=1-593.
DR PDB; 6FT6; EM; 3.90 A; 4=1-593.
DR PDB; 6M62; EM; 3.20 A; 4=1-593.
DR PDB; 6RZZ; EM; 3.20 A; r=1-593.
DR PDB; 6YLG; EM; 3.00 A; 4=1-593.
DR PDB; 6YLH; EM; 3.10 A; 4=1-593.
DR PDBsum; 3JCT; -.
DR PDBsum; 4V7F; -.
DR PDBsum; 4V8T; -.
DR PDBsum; 5APN; -.
DR PDBsum; 5APO; -.
DR PDBsum; 5JCS; -.
DR PDBsum; 6FT6; -.
DR PDBsum; 6M62; -.
DR PDBsum; 6RZZ; -.
DR PDBsum; 6YLG; -.
DR PDBsum; 6YLH; -.
DR AlphaFoldDB; Q03862; -.
DR SMR; Q03862; -.
DR BioGRID; 32159; 334.
DR DIP; DIP-5819N; -.
DR IntAct; Q03862; 69.
DR MINT; Q03862; -.
DR STRING; 4932.YDR101C; -.
DR MaxQB; Q03862; -.
DR PaxDb; Q03862; -.
DR PRIDE; Q03862; -.
DR EnsemblFungi; YDR101C_mRNA; YDR101C; YDR101C.
DR GeneID; 851678; -.
DR KEGG; sce:YDR101C; -.
DR SGD; S000002508; ARX1.
DR VEuPathDB; FungiDB:YDR101C; -.
DR eggNOG; KOG2776; Eukaryota.
DR HOGENOM; CLU_477525_0_0_1; -.
DR InParanoid; Q03862; -.
DR OMA; KPSWVHS; -.
DR BioCyc; YEAST:G3O-29704-MON; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR PRO; PR:Q03862; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q03862; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005654; C:nucleoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0000055; P:ribosomal large subunit export from nucleus; IMP:SGD.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.90.230.10; -; 1.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF00557; Peptidase_M24; 1.
DR SUPFAM; SSF55920; SSF55920; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Metal-binding; Metalloprotease;
KW Nucleus; Protease; Reference proteome.
FT CHAIN 1..593
FT /note="Probable metalloprotease ARX1"
FT /id="PRO_0000148999"
SQ SEQUENCE 593 AA; 65213 MW; E68A7896FAFA6A0C CRC64;
MALAISHEDT QILLKDKNIL QESVLNKYRT AGQIAQTALK YVTSLINDSY HSKTTQRQLT
VPELCLLTDS FILTRLEQYY KNKVNERGIA IPTTIDIDQI SGGWCPEIDD TQNLLNWNKG
KDSTFASSVT GTLRPGDLVK ITLGVHIDGY TSEVSHTMVI YPVDETKPIL QPTGPLLGGK
ADAVAAAHIA METVVALLAC ALTPEKLPAS LGGTSSGITG QLIRTIVDTI ARSYNCGVVP
GSRVRRIRRF LAGQNEGIVA EREYKGVVWT ESHQEADLLS NTDAKDLTVV DRGQSTPFTN
VSAIPSDDFV VQSGEVYLID LKMASLEHCT KKGLVTLETV DSYTGKSHKA GELIARPGAY
VRDFAQTHIL KLKTSRQLLT KIDKQGVYPF KLSHLSSNFP FVHENEEELQ SLKKDLKSFR
LGMSEISNNY LCVESPIQIA RWVPWDHILK ATNPNGNLSY DATSTLTLPG HELPLPKLGV
SAIKLKSLMN STKESISLPV ARECNTIVLC DSSVSTTDRP ELLRLTGGSK TCQPSWIHSQ
HELNPQDSIV QGIFQLATLA KDKRFGLLLK ETQPMKQKSV ETSNGGVEET MKM
