AIR1_YEAST
ID AIR1_YEAST Reviewed; 360 AA.
AC P40507; D6VVK5;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Protein AIR1;
DE AltName: Full=Arginine methyltransferase-interacting RING finger protein 1;
GN Name=AIR1; OrderedLocusNames=YIL079C;
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=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(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, AND INTERACTION WITH HMT1 AND NPL3.
RX PubMed=10896665; DOI=10.1074/jbc.m004560200;
RA Inoue K., Mizuno T., Wada K., Hagiwara M.;
RT "Novel RING finger proteins, Air1p and Air2p, interact with Hmt1p and
RT inhibit the arginine methylation of Npl3p.";
RL J. Biol. Chem. 275:32793-32799(2000).
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 IDENTIFICATION IN THE TRF4 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY,
RP AND FUNCTION OF THE TRF4 COMPLEX.
RX PubMed=15935759; DOI=10.1016/j.cell.2005.04.030;
RA Wyers F., Rougemaille M., Badis G., Rousselle J.-C., Dufour M.-E.,
RA Boulay J., Regnault B., Devaux F., Namane A., Seraphin B., Libri D.,
RA Jacquier A.;
RT "Cryptic pol II transcripts are degraded by a nuclear quality control
RT pathway involving a new poly(A) polymerase.";
RL Cell 121:725-737(2005).
RN [7]
RP IDENTIFICATION IN THE TRF4 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY,
RP AND FUNCTION OF THE TRF4 COMPLEX.
RX PubMed=15828860; DOI=10.1371/journal.pbio.0030189;
RA Vanacova S., Wolf J., Martin G., Blank D., Dettwiler S., Friedlein A.,
RA Langen H., Keith G., Keller W.;
RT "A new yeast poly(A) polymerase complex involved in RNA quality control.";
RL PLoS Biol. 3:986-997(2005).
RN [8]
RP IDENTIFICATION IN THE TRAMP5 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY,
RP AND FUNCTION OF THE TRAMP5 COMPLEX.
RX PubMed=16374505; DOI=10.1038/sj.embor.7400612;
RA Houseley J., Tollervey D.;
RT "Yeast Trf5p is a nuclear poly(A) polymerase.";
RL EMBO Rep. 7:205-211(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Component of the TRAMP (TRF4) and TRAMP5 complexes which have
CC a poly(A) RNA polymerase activity and are involved in a post-
CC transcriptional quality control mechanism limiting inappropriate
CC expression of genetic information. Polyadenylation is required for the
CC degradative activity of the exosome on several of its nuclear RNA
CC substrates like cryptic transcripts generated by RNA polymerase II and
CC III, or hypomethylated pre-tRNAi-Met. Both complexes polyadenylate RNA
CC processing and degradation intermediates of snRNAs, snoRNAs and mRNAs
CC that accumulate in strains lacking a functional exosome. AIR1 also
CC inhibits the methylation of NPL3 mediated by HMT1 through its
CC interaction with HMT1. {ECO:0000269|PubMed:10896665,
CC ECO:0000269|PubMed:15828860, ECO:0000269|PubMed:15935759,
CC ECO:0000269|PubMed:16374505}.
CC -!- SUBUNIT: Component of the TRAMP complex (also called TRF4 complex)
CC composed of at least HUL4, MTR4, PAP2/TFR4 and either AIR1 or AIR2.
CC Component of the TRAMP5 complex composed of at least AIR1, MTR4 and
CC TRF5. Interacts with HMT1 and NPL3. The interaction with NPL3 requires
CC the presence of HMT1. {ECO:0000269|PubMed:10896665,
CC ECO:0000269|PubMed:15828860, ECO:0000269|PubMed:15935759,
CC ECO:0000269|PubMed:16374505}.
CC -!- INTERACTION:
CC P40507; Q01560: NPL3; NbExp=3; IntAct=EBI-25083, EBI-12114;
CC P40507; P53632: PAP2; NbExp=7; IntAct=EBI-25083, EBI-19517;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1550 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the AIR1 family. {ECO:0000305}.
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DR EMBL; Z37997; CAA86091.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08471.1; -; Genomic_DNA.
DR PIR; S48365; S48365.
DR RefSeq; NP_012186.1; NM_001179429.1.
DR AlphaFoldDB; P40507; -.
DR SMR; P40507; -.
DR BioGRID; 34913; 198.
DR ComplexPortal; CPX-1678; TRAMP complex variant 4-1.
DR ComplexPortal; CPX-1680; TRAMP complex variant 5-1.
DR DIP; DIP-2700N; -.
DR ELM; P40507; -.
DR IntAct; P40507; 20.
DR MINT; P40507; -.
DR STRING; 4932.YIL079C; -.
DR iPTMnet; P40507; -.
DR MaxQB; P40507; -.
DR PaxDb; P40507; -.
DR PRIDE; P40507; -.
DR EnsemblFungi; YIL079C_mRNA; YIL079C; YIL079C.
DR GeneID; 854731; -.
DR KEGG; sce:YIL079C; -.
DR SGD; S000001341; AIR1.
DR VEuPathDB; FungiDB:YIL079C; -.
DR eggNOG; KOG4400; Eukaryota.
DR GeneTree; ENSGT00950000183041; -.
DR HOGENOM; CLU_049076_1_0_1; -.
DR InParanoid; P40507; -.
DR OMA; CNENGHY; -.
DR BioCyc; YEAST:G3O-31344-MON; -.
DR PRO; PR:P40507; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40507; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0031499; C:TRAMP complex; IDA:SGD.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0043629; P:ncRNA polyadenylation; IDA:SGD.
DR GO; GO:0071031; P:nuclear mRNA surveillance of mRNA 3'-end processing; IGI:SGD.
DR GO; GO:0071039; P:nuclear polyadenylation-dependent CUT catabolic process; IGI:SGD.
DR GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; IGI:SGD.
DR GO; GO:0071036; P:nuclear polyadenylation-dependent snoRNA catabolic process; IGI:SGD.
DR GO; GO:0071037; P:nuclear polyadenylation-dependent snRNA catabolic process; IGI:SGD.
DR GO; GO:0071038; P:nuclear polyadenylation-dependent tRNA catabolic process; IDA:SGD.
DR GO; GO:0000292; P:RNA fragment catabolic process; IC:ComplexPortal.
DR InterPro; IPR016713; Air1/2_Saccharomycetales.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF00098; zf-CCHC; 3.
DR PIRSF; PIRSF018162; PolyA_pol_Air1/2; 1.
DR SMART; SM00343; ZnF_C2HC; 5.
DR SUPFAM; SSF57756; SSF57756; 3.
DR PROSITE; PS50158; ZF_CCHC; 3.
PE 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Zinc; Zinc-finger.
FT CHAIN 1..360
FT /note="Protein AIR1"
FT /id="PRO_0000202979"
FT ZN_FING 74..91
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 112..129
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 134..151
FT /note="CCHC-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 173..190
FT /note="CCHC-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 265..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 360 AA; 41631 MW; 3CA920FA1204EC9C CRC64;
MSTLLSEVES IDTLPYVKDT TPTGSDSSSF NKLLAPSIED VDANPEELRT LRGQGRYFGI
TDYDSNGAIM EAEPKCNNCS QRGHLKRNCP HVICTYCGFM DDHYSQHCPK AIICTNCNAN
GHYKSQCPHK WKKVFCTLCN SKRHSRERCP SIWRSYLLKT KDANQGDFDF QTVFCYNCGN
AGHFGDDCAE RRSSRVPNTD GSAFCGDNLA TKFKQHYFNQ LKDYKREASQ RQHFDNEHEF
NLLDYEYNDD AYDLPGSRTY RDKMKWKGKV QSTRNKNSSN NRYESSNNRK KKSPFSAQNY
KVTKNKRVQT HPLDFPRSSQ NNRTNDYSSQ FSYNRDDFPK GPKNKRGRSS SNKSQRNGRY
