LTV1_YEAST
ID LTV1_YEAST Reviewed; 463 AA.
AC P34078; D6VX53;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Protein LTV1;
DE AltName: Full=Low-temperature viability protein 1;
GN Name=LTV1; OrderedLocusNames=YKL143W; ORFNames=YKL2;
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=1574929; DOI=10.1002/yea.320080309;
RA Abraham P.R., Mulder A., Van'T Riet J., Planta R.J., Raue H.A.;
RT "Molecular cloning and physical analysis of an 8.2 kb segment of chromosome
RT XI of Saccharomyces cerevisiae reveals five tightly linked genes.";
RL Yeast 8:227-238(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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 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 FUNCTION.
RX PubMed=15611164; DOI=10.1534/genetics.104.032656;
RA Loar J.W., Seiser R.M., Sundberg A.E., Sagerson H.J., Ilias N.,
RA Zobel-Thropp P., Craig E.A., Lycan D.E.;
RT "Genetic and biochemical interactions among Yar1, Ltv1 and Rps3 define
RT novel links between environmental stress and ribosome biogenesis in
RT Saccharomyces cerevisiae.";
RL Genetics 168:1877-1889(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH THE PRE-40S RIBOSOME,
RP AND PHOSPHORYLATION.
RX PubMed=16738661; DOI=10.1038/nature04840;
RA Schaefer T., Maco B., Petfalski E., Tollervey D., Boettcher B., Aebi U.,
RA Hurt E.;
RT "Hrr25-dependent phosphorylation state regulates organization of the pre-
RT 40S subunit.";
RL Nature 441:651-655(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE GSE COMPLEX, AND
RP INTERACTION WITH GTR1.
RX PubMed=16732272; DOI=10.1038/ncb1419;
RA Gao M., Kaiser C.A.;
RT "A conserved GTPase-containing complex is required for intracellular
RT sorting of the general amino-acid permease in yeast.";
RL Nat. Cell Biol. 8:657-667(2006).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, NUCLEAR EXPORT SIGNAL, AND INTERACTION WITH
RP CRM1.
RX PubMed=16888326; DOI=10.1534/genetics.106.062117;
RA Seiser R.M., Sundberg A.E., Wollam B.J., Zobel-Thropp P., Baldwin K.,
RA Spector M.D., Lycan D.E.;
RT "Ltv1 is required for efficient nuclear export of the ribosomal small
RT subunit in Saccharomyces cerevisiae.";
RL Genetics 174:679-691(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303, AND IDENTIFICATION BY
RP 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-288; SER-293; SER-299 AND
RP SER-303, AND 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).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Involved in protein transport. Non-ribosomal factor required
CC for efficient nuclear export of the ribosomal 40S subunit. Component of
CC the GSE complex, a GTPase complex required for intracellular sorting of
CC GAP1 out of the endosome. {ECO:0000269|PubMed:15611164,
CC ECO:0000269|PubMed:16888326}.
CC -!- SUBUNIT: Associates with the pre-40S ribosomal subunit. Component of
CC the GSE complex composed of GTR1, GTR2, SLM4, MEH1 and LTV1. Interacts
CC directly with GTR1. Interacts with CRM1. {ECO:0000269|PubMed:16732272,
CC ECO:0000269|PubMed:16738661, ECO:0000269|PubMed:16888326}.
CC -!- INTERACTION:
CC P34078; P40160: RIO2; NbExp=4; IntAct=EBI-10248, EBI-29124;
CC P34078; P05750: RPS3; NbExp=2; IntAct=EBI-10248, EBI-16140;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles between the
CC nucleus and the cytoplasm.
CC -!- PTM: Phosphorylated, leading to its dissociation from the 40S pre-40S
CC ribosome. {ECO:0000269|PubMed:16738661}.
CC -!- MISCELLANEOUS: Present with 589 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the LTV1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA80955.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z25464; CAA80955.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z28143; CAA81984.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09019.1; -; Genomic_DNA.
DR PIR; S37972; S37972.
DR RefSeq; NP_012779.1; NM_001179709.1.
DR PDB; 5WWO; X-ray; 2.40 A; C=333-463.
DR PDB; 6FAI; EM; 3.40 A; j=1-463.
DR PDB; 6Y7C; EM; 3.80 A; j=1-463.
DR PDBsum; 5WWO; -.
DR PDBsum; 6FAI; -.
DR PDBsum; 6Y7C; -.
DR AlphaFoldDB; P34078; -.
DR SMR; P34078; -.
DR BioGRID; 33993; 177.
DR ComplexPortal; CPX-1604; Small ribosomal subunit processome, variant 1.
DR ComplexPortal; CPX-1607; Small ribosomal subunit processome, variant 2.
DR ComplexPortal; CPX-1608; Small ribosomal subunit processome, variant 3.
DR ComplexPortal; CPX-3233; GSE complex.
DR DIP; DIP-2801N; -.
DR IntAct; P34078; 12.
DR MINT; P34078; -.
DR STRING; 4932.YKL143W; -.
DR iPTMnet; P34078; -.
DR MaxQB; P34078; -.
DR PaxDb; P34078; -.
DR PRIDE; P34078; -.
DR EnsemblFungi; YKL143W_mRNA; YKL143W; YKL143W.
DR GeneID; 853714; -.
DR KEGG; sce:YKL143W; -.
DR SGD; S000001626; LTV1.
DR VEuPathDB; FungiDB:YKL143W; -.
DR eggNOG; KOG2637; Eukaryota.
DR GeneTree; ENSGT00390000002789; -.
DR HOGENOM; CLU_028555_1_0_1; -.
DR InParanoid; P34078; -.
DR OMA; QYDYMQH; -.
DR BioCyc; YEAST:G3O-31918-MON; -.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:P34078; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P34078; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005770; C:late endosome; IDA:ComplexPortal.
DR GO; GO:0031902; C:late endosome membrane; IDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0030688; C:preribosome, small subunit precursor; IDA:GO_Central.
DR GO; GO:0071986; C:Ragulator complex; IDA:SGD.
DR GO; GO:0032040; C:small-subunit processome; IPI:ComplexPortal.
DR GO; GO:1904669; P:ATP export; IMP:SGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
DR GO; GO:0032456; P:endocytic recycling; IDA:ComplexPortal.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IC:ComplexPortal.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006970; P:response to osmotic stress; IMP:SGD.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IMP:SGD.
DR GO; GO:0000056; P:ribosomal small subunit export from nucleus; IMP:SGD.
DR InterPro; IPR007307; Ltv1.
DR PANTHER; PTHR21531; PTHR21531; 1.
DR Pfam; PF04180; LTV; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Coiled coil; Cytoplasm; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..463
FT /note="Protein LTV1"
FT /id="PRO_0000084522"
FT REGION 37..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 355..462
FT /evidence="ECO:0000255"
FT MOTIF 168..179
FT /note="Nuclear export signal"
FT COMPBIAS 46..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..455
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT HELIX 361..369
FT /evidence="ECO:0007829|PDB:5WWO"
FT HELIX 371..382
FT /evidence="ECO:0007829|PDB:5WWO"
FT HELIX 388..390
FT /evidence="ECO:0007829|PDB:5WWO"
FT HELIX 395..402
FT /evidence="ECO:0007829|PDB:5WWO"
SQ SEQUENCE 463 AA; 53390 MW; F432C239B3B0A68A CRC64;
MSKKFSSKNS QRYVVVHRPH DDPSFYDTDA SAHVLVPVSN PNKTSPEADL RKKDVSSTKP
KGRRAHVGEA ALYGINFDDS EYDYTQHLKP IGLDPENSIF IASKGNEQKV EKKNIEDLFI
EPKYRRDEIE KDDALPVFQR GMAKPEYLLH QQDTTDEIRG FKPDMNPALR EVLEALEDEA
YVVNDDVVVE DISKKTQLQG DNYGEEEKED DIFAQLLGSG EAKDEDEFED EFDEWDIDNV
ENFEDENYVK EMAQFDNIEN LEDLENIDYQ ADVRRFQKDN SILEKHNSDD EFSNAGLDSV
NPSEEEDVLG ELPSIQDKSK TGKKKRKSRQ KKGAMSDVSG FSMSSSAIAR TETMTVLDDQ
YDQIINGYEN YEEELEEDEE QNYQPFDMSA ERSDFESMLD DFLDNYELES GGRKLAKKDK
EIERLKEAAD EVSKGKLSQR RNRERQEKKK LEKVTNTLSS LKF
