PTA1_YEAST
ID PTA1_YEAST Reviewed; 785 AA.
AC Q01329; D6VPH3;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Pre-tRNA-processing protein PTA1;
GN Name=PTA1; OrderedLocusNames=YAL043C; ORFNames=FUN39;
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].
RX PubMed=1508188; DOI=10.1128/mcb.12.9.3843-3856.1992;
RA O'Connor J.P., Peebles C.L.;
RT "PTA1, an essential gene of Saccharomyces cerevisiae affecting pre-tRNA
RT processing.";
RL Mol. Cell. Biol. 12:3843-3856(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA Storms R.K.;
RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
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 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 [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 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-500, 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: Essential in pre-tRNA processing. Component of the cleavage
CC and polyadenylation factor (CPF) complex, which plays a key role in
CC polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with
CC cleavage factors including the CFIA complex and NAB4/CFIB. Component of
CC the APT complex, which may be involved in polyadenylation-independent
CC transcript 3'-end formation.
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 Q01329; Q12102: CFT2; NbExp=5; IntAct=EBI-14145, EBI-31412;
CC Q01329; P45976: FIP1; NbExp=5; IntAct=EBI-14145, EBI-6940;
CC Q01329; P29468: PAP1; NbExp=8; IntAct=EBI-14145, EBI-12917;
CC Q01329; P39927: PTI1; NbExp=3; IntAct=EBI-14145, EBI-23382;
CC Q01329; P53538: SSU72; NbExp=6; IntAct=EBI-14145, EBI-18134;
CC Q01329; Q06224: YSH1; NbExp=4; IntAct=EBI-14145, EBI-38345;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12819204}.
CC -!- MISCELLANEOUS: Present with 3730 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; M95673; AAA34919.1; -; Genomic_DNA.
DR EMBL; U12980; AAC04988.1; -; Genomic_DNA.
DR EMBL; BK006935; DAA06943.1; -; Genomic_DNA.
DR PIR; S31299; S31299.
DR RefSeq; NP_009356.1; NM_001178188.1.
DR AlphaFoldDB; Q01329; -.
DR SMR; Q01329; -.
DR BioGRID; 31784; 164.
DR ComplexPortal; CPX-1053; Cleavage and polyadenylation specificity factor complex.
DR DIP; DIP-2469N; -.
DR IntAct; Q01329; 31.
DR MINT; Q01329; -.
DR STRING; 4932.YAL043C; -.
DR iPTMnet; Q01329; -.
DR MaxQB; Q01329; -.
DR PaxDb; Q01329; -.
DR PRIDE; Q01329; -.
DR EnsemblFungi; YAL043C_mRNA; YAL043C; YAL043C.
DR GeneID; 851255; -.
DR KEGG; sce:YAL043C; -.
DR SGD; S000000041; PTA1.
DR VEuPathDB; FungiDB:YAL043C; -.
DR eggNOG; KOG1895; Eukaryota.
DR GeneTree; ENSGT00390000017045; -.
DR HOGENOM; CLU_021804_0_0_1; -.
DR InParanoid; Q01329; -.
DR OMA; AREMCLN; -.
DR BioCyc; YEAST:G3O-28851-MON; -.
DR Reactome; R-SCE-77595; Processing of Intronless Pre-mRNAs.
DR PRO; PR:Q01329; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; Q01329; protein.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
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:0030846; P:termination of RNA polymerase II transcription, poly(A)-coupled; IPI:SGD.
DR GO; GO:0008033; P:tRNA processing; IMP:SGD.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR021850; Symplekin/Pta1.
DR InterPro; IPR032460; Symplekin/Pta1_N.
DR PANTHER; PTHR15245:SF20; PTHR15245:SF20; 1.
DR Pfam; PF11935; SYMPK_PTA1_N; 1.
PE 1: Evidence at protein level;
KW mRNA processing; Nucleus; Phosphoprotein; Reference proteome;
KW tRNA processing.
FT CHAIN 1..785
FT /note="Pre-tRNA-processing protein PTA1"
FT /id="PRO_0000097086"
FT REGION 487..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 500
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 785 AA; 88473 MW; E2AB1F468B7BC8D0 CRC64;
MSSAEMEQLL QAKTLAMHNN PTEMLPKVLE TTASMYHNGN LSKLKLPLAK FFTQLVLDVV
SMDSPIANTE RPFIAAQYLP LLLAMAQSTA DVLVYKNIVL IMCASYPLVL DLVAKTSNQE
MFDQLCMLKK FVLSHWRTAY PLRATVDDET DVEQWLAQID QNIGVKLATI KFISEVVLSQ
TKSPSGNEIN SSTIPDNHPV LNKPALESEA KRLLDMLLNY LIEEQYMVSS VFIGIINSLS
FVIKRRPQTT IRILSGLLRF NVDAKFPLEG KSDLNYKLSK RFVERAYKNF VQFGLKNQII
TKSLSSGSGS SIYSKLTKIS QTLHVIGEET KSKGILNFDP SKGNSKKTLS RQDKLKYISL
WKRQLSALLS TLGVSTKTPT PVSAPATGSS TENMLDQLKI LQKYTLNKAS HQGNTFFNNS
PKPISNTYSS VYSLMNSSNS NQDVTQLPND ILIKLSTEAI LQMDSTKLIT GLSIVASRYT
DLMNTYINSV PSSSSSKRKS DDDDDGNDNE EVGNDGPTAN SKKIKMETEP LAEEPEEPED
DDRMQKMLQE EESAQEISGD ANKSTSAIKE IAPPFEPDSL TQDEKLKYLS KLTKKLFELS
GRQDTTRAKS SSSSSILLDD DDSSSWLHVL IRLVTRGIEA QEASDLIREE LLGFFIQDFE
QRVSLIIEWL NEEWFFQTSL HQDPSNYKKW SLRVLESLGP FLENKHRRFF IRLMSELPSL
QSDHLEALKP ICLDPARSSL GFQTLKFLIM FRPPVQDTVR DLLHQLKQED EGLHKQCDSL
LDRLK
