PTI1_YEAST
ID PTI1_YEAST Reviewed; 425 AA.
AC P39927; D6VUT6;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Protein PTI1;
GN Name=PTI1; OrderedLocusNames=YGR156W; ORFNames=G6670;
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].
RC STRAIN=A5-8-1A;
RA Ono B., Inoue T., Kijima K., Matsuda A., Negishi K., Shinoda S.;
RL Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8585325; DOI=10.1002/yea.320111410;
RA Skala J., Nawrocki A., Goffeau A.;
RT "The sequence of a 27 kb segment on the right arm of chromosome VII from
RT Saccharomyces cerevisiae reveals MOL1, NAT2, RPL30B, RSR1, CYS4, PEM1/CHO2,
RT NSR1 genes and ten new open reading frames.";
RL Yeast 11:1421-1427(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP FUNCTION IN SNORNA 3-END FORMATION.
RX PubMed=12773397; DOI=10.1093/emboj/cdg253;
RA Dheur S., Vo le T.A., Voisinet-Hakil F., Minet M., Schmitter J.-M.,
RA Lacroute F., Wyers F., Minvielle-Sebastia L.;
RT "Pti1p and Ref2p found in association with the mRNA 3' end formation
RT complex direct snoRNA maturation.";
RL EMBO J. 22:2831-2840(2003).
RN [7]
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 [8]
RP IDENTIFICATION IN THE CPF COMPLEX, COMPOSITION OF THE APT COMPLEX,
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12819204; DOI=10.1074/jbc.m304454200;
RA Nedea E., He X., Kim M., Pootoolal J., Zhong G., Canadien V., Hughes T.,
RA Buratowski S., Moore C.L., Greenblatt J.;
RT "Organization and function of APT, a subcomplex of the yeast cleavage and
RT polyadenylation factor involved in the formation of mRNA and small
RT nucleolar RNA 3'-ends.";
RL J. Biol. Chem. 278:33000-33010(2003).
RN [9]
RP IDENTIFICATION BY 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 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-272, 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).
CC -!- FUNCTION: Component of the cleavage and polyadenylation factor (CPF)
CC complex, which plays a key role in polyadenylation-dependent pre-mRNA
CC 3'-end formation and cooperates with cleavage factors including the
CC CFIA complex and NAB4/CFIB. Component of the APT complex, which may be
CC involved in polyadenylation-independent transcript 3'-end formation.
CC PTI1 is required for 3'-end formation of snoRNAs.
CC {ECO:0000269|PubMed:12773397}.
CC -!- SUBUNIT: Component of the cleavage and polyadenylation factor (CPF)
CC complex, which is composed of PTI1, SYC1, SSU72, GLC7, MPE1, REF2,
CC PFS2, PTA1, YSH1/BRR5, SWD2, CFT2/YDH1, YTH1, CFT1/YHH1, FIP1 and PAP1.
CC Component of the APT complex, which is a subcomplex of CPF, and is
CC composed of PTI1, SYC1, SSU72, GLC7, REF2, PTA1 and SWD2.
CC {ECO:0000269|PubMed:12819204}.
CC -!- INTERACTION:
CC P39927; Q01329: PTA1; NbExp=3; IntAct=EBI-23382, EBI-14145;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12819204}.
CC -!- MISCELLANEOUS: Present with 937 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; D16502; BAA03953.1; -; Genomic_DNA.
DR EMBL; X85807; CAA59813.1; -; Genomic_DNA.
DR EMBL; Z72941; CAA97170.1; -; Genomic_DNA.
DR EMBL; AY557841; AAS56167.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08247.1; -; Genomic_DNA.
DR PIR; S60446; S60446.
DR RefSeq; NP_011672.1; NM_001181285.1.
DR AlphaFoldDB; P39927; -.
DR SMR; P39927; -.
DR BioGRID; 33404; 540.
DR ComplexPortal; CPX-1053; Cleavage and polyadenylation specificity factor complex.
DR DIP; DIP-4402N; -.
DR IntAct; P39927; 16.
DR MINT; P39927; -.
DR STRING; 4932.YGR156W; -.
DR iPTMnet; P39927; -.
DR MaxQB; P39927; -.
DR PaxDb; P39927; -.
DR PRIDE; P39927; -.
DR EnsemblFungi; YGR156W_mRNA; YGR156W; YGR156W.
DR GeneID; 853060; -.
DR KEGG; sce:YGR156W; -.
DR SGD; S000003388; PTI1.
DR VEuPathDB; FungiDB:YGR156W; -.
DR eggNOG; KOG0108; Eukaryota.
DR HOGENOM; CLU_040439_0_0_1; -.
DR InParanoid; P39927; -.
DR OMA; EMGFINY; -.
DR BioCyc; YEAST:G3O-30857-MON; -.
DR PRO; PR:P39927; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P39927; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0006378; P:mRNA polyadenylation; IDA:ComplexPortal.
DR GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IDA:ComplexPortal.
DR GO; GO:0031126; P:sno(s)RNA 3'-end processing; IMP:SGD.
DR GO; GO:0030847; P:termination of RNA polymerase II transcription, exosome-dependent; IMP:SGD.
DR GO; GO:0030846; P:termination of RNA polymerase II transcription, poly(A)-coupled; IC:ComplexPortal.
DR Gene3D; 1.10.20.70; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR025742; CSTF2_hinge.
DR InterPro; IPR026896; CSTF_C.
DR InterPro; IPR038192; CSTF_C_sf.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF14327; CSTF2_hinge; 1.
DR Pfam; PF14304; CSTF_C; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
PE 1: Evidence at protein level;
KW mRNA processing; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..425
FT /note="Protein PTI1"
FT /id="PRO_0000076294"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 300
FT /note="N -> Y (in Ref. 1; BAA03953)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 425 AA; 46983 MW; F6564311A2B1F240 CRC64;
MTDPRRRTGR HFLTPENLSS TLQITNLPPE WNQDIITSVV AGSGPVIDIK AKNDPRTGKL
TGVLFDYLTS KDCKRAWEIL NRIENFPVKI EQIIPPNYKD HLRETANKNS QKQVLQLNRD
SYPFEAGLEL PFEMVTEVPI PRRPPPPQAA NNTNSVSNNT NIQFPDILSK ASKHLPSFQD
GSIIAPDKIS QNLSKIPPLQ LIEIISNLKI LSNQENIQKS QLESFLDTNS DITISVTQAL
LEMGFIDYSV VTKVLKSQVG EAPSLLSSNN TSNSNTPVSV IRNNTPLHVP SNEVSNNPNN
MPLNVAMPMP MSTPPFIPLP LQQQPFGFAP PGPFMPPAQG PSMGQPVLAN QLGQVQQQNI
SSTEGPSNAN KANDSGTINM AKLQLLPENQ QDMIKQVLTL TPAQIQSLPS DQQLMVENFR
KEYII
