AIR2_YEAST
ID AIR2_YEAST Reviewed; 344 AA.
AC Q12476; D6VRH7;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Protein AIR2;
DE AltName: Full=Arginine methyltransferase-interacting RING finger protein 2;
GN Name=AIR2; OrderedLocusNames=YDL175C;
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, 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 TRAMP COMPLEX, AND FUNCTION OF THE TRAMP COMPLEX.
RX PubMed=15935758; DOI=10.1016/j.cell.2005.04.029;
RA LaCava J., Houseley J., Saveanu C., Petfalski E., Thompson E., Jacquier A.,
RA Tollervey D.;
RT "RNA degradation by the exosome is promoted by a nuclear polyadenylation
RT complex.";
RL Cell 121:713-724(2005).
RN [7]
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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31 AND SER-49, AND
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 118-198 IN COMPLEX WITH PAP2 AND
RP ZINC IONS, FUNCTION, AND INTERACTION WITH PAP2.
RX PubMed=20696927; DOI=10.1073/pnas.1003505107;
RA Hamill S., Wolin S.L., Reinisch K.M.;
RT "Structure and function of the polymerase core of TRAMP, a RNA surveillance
RT complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:15045-15050(2010).
CC -!- FUNCTION: Component of the TRAMP (TRF4) complex which has a poly(A) RNA
CC polymerase activity and is involved in a post-transcriptional quality
CC control mechanism limiting inappropriate expression of genetic
CC information. Polyadenylation is required for the degradative activity
CC of the exosome on several of its nuclear RNA substrates like cryptic
CC transcripts generated by RNA polymerase II and III, or hypomethylated
CC pre-tRNAi-Met. Both complexes polyadenylate RNA processing and
CC degradation intermediates of snRNAs, snoRNAs and mRNAs that accumulate
CC in strains lacking a functional exosome. AIR2 also inhibits the
CC methylation of NPL3 mediated by HMT1 through its interaction with HMT1.
CC {ECO:0000269|PubMed:10896665, ECO:0000269|PubMed:15828860,
CC ECO:0000269|PubMed:15935758, ECO:0000269|PubMed:15935759,
CC ECO:0000269|PubMed:20696927}.
CC -!- SUBUNIT: Component of the TRAMP complex (also called TRF4 complex)
CC composed of at least HUL4, MTR4, PAP2/TRF4 and either AIR1 or AIR2.
CC Interacts with HMT1 and NPL3. The interaction with NPL3 requires the
CC presence of HMT1. Interacts directly with PAP2.
CC {ECO:0000269|PubMed:10896665, ECO:0000269|PubMed:15828860,
CC ECO:0000269|PubMed:15935758, ECO:0000269|PubMed:15935759,
CC ECO:0000269|PubMed:20696927}.
CC -!- INTERACTION:
CC Q12476; P47047: MTR4; NbExp=7; IntAct=EBI-31475, EBI-11592;
CC Q12476; P53632: PAP2; NbExp=21; IntAct=EBI-31475, EBI-19517;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1800 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; Z74223; CAA98749.1; -; Genomic_DNA.
DR EMBL; Z67750; CAA91570.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11687.1; -; Genomic_DNA.
DR PIR; S61037; S61037.
DR RefSeq; NP_010106.1; NM_001180235.1.
DR PDB; 2LLI; NMR; -; A=57-180.
DR PDB; 3NYB; X-ray; 2.70 A; B=118-198.
DR PDB; 4U4C; X-ray; 2.40 A; B=1-62.
DR PDBsum; 2LLI; -.
DR PDBsum; 3NYB; -.
DR PDBsum; 4U4C; -.
DR AlphaFoldDB; Q12476; -.
DR BMRB; Q12476; -.
DR SMR; Q12476; -.
DR BioGRID; 31891; 185.
DR ComplexPortal; CPX-1679; TRAMP complex variant 4-2.
DR DIP; DIP-2543N; -.
DR ELM; Q12476; -.
DR IntAct; Q12476; 24.
DR MINT; Q12476; -.
DR STRING; 4932.YDL175C; -.
DR iPTMnet; Q12476; -.
DR MaxQB; Q12476; -.
DR PaxDb; Q12476; -.
DR PRIDE; Q12476; -.
DR EnsemblFungi; YDL175C_mRNA; YDL175C; YDL175C.
DR GeneID; 851379; -.
DR KEGG; sce:YDL175C; -.
DR SGD; S000002334; AIR2.
DR VEuPathDB; FungiDB:YDL175C; -.
DR eggNOG; KOG4400; Eukaryota.
DR HOGENOM; CLU_049076_1_0_1; -.
DR InParanoid; Q12476; -.
DR OMA; PLCDNCH; -.
DR BioCyc; YEAST:G3O-29563-MON; -.
DR EvolutionaryTrace; Q12476; -.
DR PRO; PR:Q12476; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12476; protein.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0031499; C:TRAMP complex; IDA:SGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IMP:SGD.
DR GO; GO:0003723; F:RNA binding; IDA:SGD.
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 GO; GO:0006400; P:tRNA modification; IMP:SGD.
DR DisProt; DP02464; -.
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 3D-structure; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Zinc; Zinc-finger.
FT CHAIN 1..344
FT /note="Protein AIR2"
FT /id="PRO_0000227604"
FT ZN_FING 61..78
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 99..116
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 162..179
FT /note="CCHC-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT STRAND 19..22
FT /evidence="ECO:0007829|PDB:4U4C"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:4U4C"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:4U4C"
FT HELIX 36..40
FT /evidence="ECO:0007829|PDB:4U4C"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:2LLI"
FT TURN 73..77
FT /evidence="ECO:0007829|PDB:2LLI"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:2LLI"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:2LLI"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:2LLI"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:2LLI"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:2LLI"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:2LLI"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:2LLI"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:3NYB"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:3NYB"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:3NYB"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:3NYB"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:2LLI"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:3NYB"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:3NYB"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:3NYB"
SQ SEQUENCE 344 AA; 39344 MW; 5915C97FA39D6AFC CRC64;
MEKNTAPFVV DTAPTTPPDK LVAPSIEEVN SNPNELRALR GQGRYFGVSD DDKDAIKEAA
PKCNNCSQRG HLKKDCPHII CSYCGATDDH YSRHCPKAIQ CSKCDEVGHY RSQCPHKWKK
VQCTLCKSKK HSKERCPSIW RAYILVDDNE KAKPKVLPFH TIYCYNCGGK GHFGDDCKEK
RSSRVPNEDG SAFTGSNLSV ELKQEYYRHM NRNSDENEDY QFSESIYDED PLPRPSHKRH
SQNDHSHSGR NKRRASNFHP PPYQKSNVIQ PTIRGETLSL NNNISKNSRY QNTKVNVSSI
SENMYGSRYN PSTYVDNNSI SNSSNYRNYN SYQPYRSGTL GKRR
