FIR1_YEAST
ID FIR1_YEAST Reviewed; 876 AA.
AC P40020; D3DLT1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 3.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Factor interacting with REF2;
DE AltName: Full=PAP1-interacting protein;
DE AltName: Full=Polymerase-interacting protein 1;
GN Name=FIR1; Synonyms=PIP1; OrderedLocusNames=YER032W;
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 [GENOMIC DNA], INTERACTION WITH PAP1, AND VARIANT
RP ARG-614.
RC STRAIN=ATCC 200060 / W303;
RX PubMed=9236779; DOI=10.1007/s004380050491;
RA del Olmo M., Mizrahi N., Gross S., Moore C.L.;
RT "The Uba2 and Ufd1 proteins of Saccharomyces cerevisiae interact with
RT poly(A) polymerase and affect the polyadenylation activity of cell
RT extracts.";
RL Mol. Gen. Genet. 255:209-218(1997).
RN [2]
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 [3]
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 [4]
RP FUNCTION, AND INTERACTION WITH REF2.
RX PubMed=9196079;
RA Russnak R., Pereira S., Platt T.;
RT "RNA binding analysis of yeast REF2 and its two-hybrid interaction with a
RT new gene product, FIR1.";
RL Gene Expr. 6:241-258(1996).
RN [5]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [6]
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 [7]
RP PHOSPHORYLATION BY CDC28.
RX PubMed=14574415; DOI=10.1038/nature02062;
RA Ubersax J.A., Woodbury E.L., Quang P.N., Paraz M., Blethrow J.D., Shah K.,
RA Shokat K.M., Morgan D.O.;
RT "Targets of the cyclin-dependent kinase Cdk1.";
RL Nature 425:859-864(2003).
RN [8]
RP FUNCTION, AND INTERACTION WITH PBP1.
RX PubMed=15121841; DOI=10.1128/mcb.24.10.4196-4206.2004;
RA Mangus D.A., Smith M.M., McSweeney J.M., Jacobson A.;
RT "Identification of factors regulating poly(A) tail synthesis and
RT maturation.";
RL Mol. Cell. Biol. 24:4196-4206(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81; SER-172 AND SER-225, AND
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: Involved in 3' mRNA processing. Positively regulates poly(A)
CC synthesis. {ECO:0000269|PubMed:15121841, ECO:0000269|PubMed:9196079}.
CC -!- SUBUNIT: Interacts with PAP1, REF2 and PBP1.
CC {ECO:0000269|PubMed:15121841, ECO:0000269|PubMed:9196079,
CC ECO:0000269|PubMed:9236779}.
CC -!- INTERACTION:
CC P40020; P38041: BOI1; NbExp=2; IntAct=EBI-13431, EBI-3719;
CC P40020; P39969: BOI2; NbExp=2; IntAct=EBI-13431, EBI-3727;
CC P40020; Q12038: SRO7; NbExp=2; IntAct=EBI-13431, EBI-17573;
CC -!- SUBCELLULAR LOCATION: Bud neck {ECO:0000269|PubMed:14562095}.
CC -!- PTM: Phosphorylated by CDC28. {ECO:0000269|PubMed:14574415}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB46625.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAB64565.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U17262; AAB46625.1; ALT_INIT; Genomic_DNA.
DR EMBL; U18778; AAB64565.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006939; DAA07685.1; -; Genomic_DNA.
DR PIR; S50490; S50490.
DR RefSeq; NP_010949.4; NM_001178923.3.
DR AlphaFoldDB; P40020; -.
DR SMR; P40020; -.
DR BioGRID; 36767; 97.
DR DIP; DIP-844N; -.
DR ELM; P40020; -.
DR IntAct; P40020; 16.
DR MINT; P40020; -.
DR STRING; 4932.YER032W; -.
DR iPTMnet; P40020; -.
DR MaxQB; P40020; -.
DR PaxDb; P40020; -.
DR PRIDE; P40020; -.
DR EnsemblFungi; YER032W_mRNA; YER032W; YER032W.
DR GeneID; 856754; -.
DR KEGG; sce:YER032W; -.
DR SGD; S000000834; FIR1.
DR VEuPathDB; FungiDB:YER032W; -.
DR eggNOG; ENOG502RI27; Eukaryota.
DR HOGENOM; CLU_007020_0_0_1; -.
DR InParanoid; P40020; -.
DR OMA; DVPEDIW; -.
DR BioCyc; YEAST:G3O-30213-MON; -.
DR PRO; PR:P40020; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P40020; protein.
DR GO; GO:0005935; C:cellular bud neck; IEA:UniProtKB-SubCell.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW mRNA processing; Phosphoprotein; Reference proteome.
FT CHAIN 1..876
FT /note="Factor interacting with REF2"
FT /id="PRO_0000058446"
FT REGION 49..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 826..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..742
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT VARIANT 614
FT /note="P -> R (in strain: ATCC 200060 / W303)"
FT /evidence="ECO:0000269|PubMed:9236779"
SQ SEQUENCE 876 AA; 98812 MW; DFD2AB3684EBC1D2 CRC64;
MSLPVTPVKS KVCSTLSIQH EMDHDQCRDV LCPRENLLAI NRTNNIESVA IPRQRSSKNK
KPHEHTQSQV RFSIPDPNEI SQDSPLKIVF PKSGNETERR MSTSSLLMNS HGHLVDMHSK
ILVDVPKEVW KFHHNRRKKC ESRHRKTRSD VRSNTSSSGK EPNHSRSKSL QSIIVDTMNT
YRATEVETSI NENTSNISQV SPLNLSFDRP PPLTPEKNLY LTPESPLNRY HLPVPLEISL
PPYLSPQNKD KKRSSLVYDG DGYSQFQEGN TSSSTESSLE QPSSSYSDED DSIPYAHHDV
SFELNNADAD KLLGIDENAN VNLKIQRRNL KNPQHIKSKT DRECEEKNTE KNVSLKILST
PNKLIDIPDL EHMKSPPSTG LNGTLKFFQQ FEPSEEPTSP TRQVNPESLD KLDMSFKFPS
STTNNNVDKV HENRNSGDTN NEDFLKVDTS PVNQSFESRR QMLIDLQKSP TNNNPRIHKH
RRSRSVHNID DISLNFEATS TPPAPTSAPS IPVEHSNPCT SIEIPKRSPL RFTSSPKTSD
IPPEAQSPKN GSFLQEISVP SIQIIPDESI SHTREPSPSL IECPEDENEA FSTEVADHSI
AIISETKSVP SIEPFKPLSS FNSFGQEIQN KEPTPLNQTP TDLIGKQRNC VNPHSIPFSV
LSSNSQSSQS GSSKSSYNSE FSSNTAITDT TSQPSVTINR STLEHNFIEE KRSIKNLGHG
PPSQKNNYSF PRNKNTPSNR HDLDFNTIYE KRDGKMVEVI LLDEDEDVGL KNNDISRTRV
CHAQKAKNEQ QKKRLSHCNE ILGMCDKTAD DAKRIIYQLV NEKHKFSEKG QQTKPKKSRV
LPPLPFPLYD EKGNSLIPNK YQSSIHNDIP SHRKLK
