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   27-MAR-2024, entry version 164.
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   EMDB; EMD-10713; -.
DR   EMDB; EMD-4214; -.
DR   SMR; P34078; -.
DR   BioGRID; 33993; 183.
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; 4932-YKL143W; -.
DR   PeptideAtlas; P34078; -.
DR   EnsemblFungi; YKL143W_mRNA; YKL143W; YKL143W.
DR   GeneID; 853714; -.
DR   KEGG; sce:YKL143W; -.
DR   AGR; SGD:S000001626; -.
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; TAQHFTL; -.
DR   OrthoDB; 325133at2759; -.
DR   BioCyc; YEAST:G3O-31918-MONOMER; -.
DR   Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   BioGRID-ORCS; 853714; 4 hits in 10 CRISPR screens.
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; NAS: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; LOW-TEMPERATURE VIABILITY PROTEIN LTV1-RELATED; 1.
DR   PANTHER; PTHR21531:SF0; PROTEIN LTV1 HOMOLOG; 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
//