THP1_YEAST
ID THP1_YEAST Reviewed; 455 AA.
AC Q08231; D6W1Z5;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Nuclear mRNA export protein THP1;
DE AltName: Full=Bud site selection protein 29;
GN Name=THP1; Synonyms=BUD29; OrderedLocusNames=YOL072W; ORFNames=O1140;
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=ATCC 96604 / S288c / FY1679;
RX PubMed=9178509;
RX DOI=10.1002/(sici)1097-0061(199705)13:6<583::aid-yea111>3.0.co;2-y;
RA Tzermia M., Katsoulou C., Alexandraki D.;
RT "Sequence analysis of a 33.2 kb segment from the left arm of yeast
RT chromosome XV reveals eight known genes and ten new open reading frames
RT including homologues of ABC transporters, inositol phosphatases and human
RT expressed sequence tags.";
RL Yeast 13:583-589(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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.
RX PubMed=11139493; DOI=10.1093/genetics/157.1.79;
RA Gallardo M., Aguilera A.;
RT "A new hyperrecombination mutation identifies a novel yeast gene, THP1,
RT connecting transcription elongation with mitotic recombination.";
RL Genetics 157:79-89(2001).
RN [5]
RP FUNCTION, INTERACTION WITH SAC3, AND SUBCELLULAR LOCATION.
RX PubMed=12411502; DOI=10.1093/emboj/cdf590;
RA Fischer T., Straesser K., Racz A., Rodriguez-Navarro S., Oppizzi M.,
RA Ihrig P., Lechner J., Hurt E.;
RT "The mRNA export machinery requires the novel Sac3p-Thp1p complex to dock
RT at the nucleoplasmic entrance of the nuclear pores.";
RL EMBO J. 21:5843-5852(2002).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=12206772; DOI=10.1016/s0022-2836(02)00652-6;
RA Teixeira M.T., Dujon B., Fabre E.;
RT "Genome-wide nuclear morphology screen identifies novel genes involved in
RT nuclear architecture and gene-silencing in Saccharomyces cerevisiae.";
RL J. Mol. Biol. 321:551-561(2002).
RN [7]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=12702719; DOI=10.1074/jbc.m302900200;
RA Gallardo M., Luna R., Erdjument-Bromage H., Tempst P., Aguilera A.;
RT "Nab2p and the Thp1p-Sac3p complex functionally interact at the interface
RT between transcription and mRNA metabolism.";
RL J. Biol. Chem. 278:24225-24232(2003).
RN [8]
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 [9]
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 [10]
RP INTERACTION WITH SUS1.
RX PubMed=14718168; DOI=10.1016/s0092-8674(03)01025-0;
RA Rodriguez-Navarro S., Fischer T., Luo M.-J., Antunez O., Brettschneider S.,
RA Lechner J., Perez-Ortin J.E., Reed R., Hurt E.C.;
RT "Sus1, a functional component of the SAGA histone acetylase complex and the
RT nuclear pore-associated mRNA export machinery.";
RL Cell 116:75-86(2004).
RN [11]
RP INTERACTION WITH CDC31.
RX PubMed=15311284; DOI=10.1038/ncb1163;
RA Fischer T., Rodriguez-Navarro S., Pereira G., Racz A., Schiebel E.,
RA Hurt E.C.;
RT "Yeast centrin Cdc31 is linked to the nuclear mRNA export machinery.";
RL Nat. Cell Biol. 6:840-848(2004).
CC -!- FUNCTION: Component of the SAC3-THP1 complex, which functions in
CC transcription-coupled mRNA export from the nucleus to the cytoplasm.
CC SAC3-THP1 functions in docking export-competent ribonucleoprotein
CC particles (mRNPs) to the nuclear entrance of the nuclear pore complex
CC (nuclear basket), by association with components of the nuclear mRNA
CC export machinery (MEX67-MTR2 and SUB2) in the nucleoplasm and the
CC nucleoporin NUP1 at the nuclear basket. THP1 binds to RNA in vitro.
CC {ECO:0000269|PubMed:11139493, ECO:0000269|PubMed:12411502,
CC ECO:0000269|PubMed:12702719}.
CC -!- SUBUNIT: Heterodimer with THP1. The SAC3-THP1 complex interacts with
CC CDC31 and SUS1, and with the mRNA export factor MEX67-MTR2, the TREX
CC complex component SUB2, and the nucleoporin NUP1.
CC {ECO:0000269|PubMed:12411502, ECO:0000269|PubMed:14718168,
CC ECO:0000269|PubMed:15311284}.
CC -!- INTERACTION:
CC Q08231; P06704: CDC31; NbExp=4; IntAct=EBI-32097, EBI-4259;
CC Q08231; O94742: SEM1; NbExp=2; IntAct=EBI-32097, EBI-31337;
CC -!- SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000269|PubMed:12206772,
CC ECO:0000269|PubMed:12411502, ECO:0000269|PubMed:14562095}.
CC Note=Localizes to the nuclear pores.
CC -!- MISCELLANEOUS: Present with 1140 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z74814; CAA99082.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10711.1; -; Genomic_DNA.
DR PIR; S66765; S66765.
DR RefSeq; NP_014569.1; NM_001183327.1.
DR PDB; 3T5V; X-ray; 2.90 A; B/E=1-455.
DR PDB; 4TRQ; X-ray; 3.10 A; B/E=170-455.
DR PDB; 5G5P; EM; 5.30 A; B=1-455.
DR PDB; 5L3T; X-ray; 4.93 A; B=1-455.
DR PDB; 5UBP; X-ray; 2.30 A; B=1-455.
DR PDBsum; 3T5V; -.
DR PDBsum; 4TRQ; -.
DR PDBsum; 5G5P; -.
DR PDBsum; 5L3T; -.
DR PDBsum; 5UBP; -.
DR AlphaFoldDB; Q08231; -.
DR SMR; Q08231; -.
DR BioGRID; 34329; 171.
DR ComplexPortal; CPX-1686; TREX-2 transcription-export complex.
DR ComplexPortal; CPX-1687; Thp1-Sac3 complex.
DR DIP; DIP-5060N; -.
DR IntAct; Q08231; 6.
DR MINT; Q08231; -.
DR STRING; 4932.YOL072W; -.
DR TCDB; 3.A.22.1.1; the transcription-coupled trex/tap nuclear mrna export complex (trex) family.
DR MaxQB; Q08231; -.
DR PaxDb; Q08231; -.
DR PRIDE; Q08231; -.
DR EnsemblFungi; YOL072W_mRNA; YOL072W; YOL072W.
DR GeneID; 854082; -.
DR KEGG; sce:YOL072W; -.
DR SGD; S000005433; THP1.
DR VEuPathDB; FungiDB:YOL072W; -.
DR eggNOG; KOG2688; Eukaryota.
DR GeneTree; ENSGT00390000001101; -.
DR HOGENOM; CLU_048936_0_0_1; -.
DR InParanoid; Q08231; -.
DR OMA; PPVNERI; -.
DR BioCyc; YEAST:G3O-33477-MON; -.
DR PRO; PR:Q08231; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08231; protein.
DR GO; GO:0005635; C:nuclear envelope; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0070390; C:transcription export complex 2; IDA:SGD.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:SGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:0000282; P:cellular bud site selection; HMP:SGD.
DR GO; GO:0031124; P:mRNA 3'-end processing; IMP:SGD.
DR GO; GO:0006406; P:mRNA export from nucleus; IMP:SGD.
DR GO; GO:0071028; P:nuclear mRNA surveillance; IMP:SGD.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0000973; P:post-transcriptional tethering of RNA polymerase II gene DNA at nuclear periphery; IMP:SGD.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IMP:SGD.
DR GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IMP:SGD.
DR InterPro; IPR045114; Csn12-like.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR040114; Thp1-like.
DR PANTHER; PTHR12732; PTHR12732; 1.
DR PANTHER; PTHR12732:SF5; PTHR12732:SF5; 1.
DR Pfam; PF01399; PCI; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; mRNA transport; Nucleus; Reference proteome; Transport.
FT CHAIN 1..455
FT /note="Nuclear mRNA export protein THP1"
FT /id="PRO_0000270618"
FT DOMAIN 220..431
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT HELIX 3..12
FT /evidence="ECO:0007829|PDB:5UBP"
FT HELIX 23..37
FT /evidence="ECO:0007829|PDB:5UBP"
FT HELIX 42..51
FT /evidence="ECO:0007829|PDB:5UBP"
FT HELIX 59..74
FT /evidence="ECO:0007829|PDB:5UBP"
FT HELIX 80..96
FT /evidence="ECO:0007829|PDB:5UBP"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:3T5V"
FT HELIX 106..128
FT /evidence="ECO:0007829|PDB:5UBP"
FT HELIX 131..134
FT /evidence="ECO:0007829|PDB:5UBP"
FT HELIX 140..155
FT /evidence="ECO:0007829|PDB:5UBP"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:5UBP"
FT HELIX 175..188
FT /evidence="ECO:0007829|PDB:5UBP"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:5UBP"
FT HELIX 195..205
FT /evidence="ECO:0007829|PDB:5UBP"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:5UBP"
FT HELIX 216..232
FT /evidence="ECO:0007829|PDB:5UBP"
FT HELIX 236..251
FT /evidence="ECO:0007829|PDB:5UBP"
FT HELIX 258..277
FT /evidence="ECO:0007829|PDB:5UBP"
FT HELIX 285..290
FT /evidence="ECO:0007829|PDB:5UBP"
FT HELIX 293..308
FT /evidence="ECO:0007829|PDB:5UBP"
FT HELIX 311..320
FT /evidence="ECO:0007829|PDB:5UBP"
FT HELIX 322..327
FT /evidence="ECO:0007829|PDB:5UBP"
FT HELIX 331..354
FT /evidence="ECO:0007829|PDB:5UBP"
FT TURN 355..358
FT /evidence="ECO:0007829|PDB:5UBP"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:5UBP"
FT HELIX 365..376
FT /evidence="ECO:0007829|PDB:5UBP"
FT TURN 390..392
FT /evidence="ECO:0007829|PDB:5UBP"
FT HELIX 397..399
FT /evidence="ECO:0007829|PDB:4TRQ"
FT HELIX 400..409
FT /evidence="ECO:0007829|PDB:5UBP"
FT STRAND 416..418
FT /evidence="ECO:0007829|PDB:5UBP"
FT TURN 419..422
FT /evidence="ECO:0007829|PDB:5UBP"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:5UBP"
FT HELIX 432..435
FT /evidence="ECO:0007829|PDB:5UBP"
FT HELIX 439..446
FT /evidence="ECO:0007829|PDB:5UBP"
SQ SEQUENCE 455 AA; 52678 MW; 7026F1F6FCC73FFA CRC64;
MDMANQLLDE LAHGNFSHLT LNLSQNGREI AILQKQLTGF DDKQLETFVE QHPAMPNDTR
FKIMCTSFLN YARDVDPWSA WSSSDLIFEF YQCLINCLIN DNAPHIEMLI PVATRETEFI
INLAGKLDSF HLQLHTRSHQ FLSHISSILS RLFNSIKPPR GNASSTNIPG KQRILLYLVN
KLNNIYFRIE SPQLCSNIFK NFQPKSMLAH FNEYQLDQQI EYRYLLGRYY LLNSQVHNAF
VQFNEAFQSL LNLPLTNQAI TRNGTRILNY MIPTGLILGK MVKWGPLRPF LSQETIDNWS
VLYKHVRYGN IQGVSLWLRQ NERHLCARQL LIVLLEKLPM VTYRNLIKTV IKSWTTEWGQ
NKLPYSLIER VLQLSIGPTF EDPGAQEITI YNGIHSPKNV ENVLVTLINL GLLRANCFPQ
LQLCVVKKTT MIQEIVPPVN ERITKMFPAH SHVLW
