ID   TUS1_YEAST              Reviewed;        1307 AA.
AC   Q06412; D6VZ61;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 171.
DE   RecName: Full=Rho1 guanine nucleotide exchange factor TUS1;
DE   AltName: Full=TOR unique function suppressor protein 1;
GN   Name=TUS1; Synonyms=SOP10; OrderedLocusNames=YLR425W;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
RN   [2]
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   [3]
RP   FUNCTION, AND INTERACTION WITH RHO1.
RX   PubMed=11839800; DOI=10.1128/mcb.22.5.1329-1339.2002;
RA   Schmelzle T., Helliwell S.B., Hall M.N.;
RT   "Yeast protein kinases and the RHO1 exchange factor TUS1 are novel
RT   components of the cell integrity pathway in yeast.";
RL   Mol. Cell. Biol. 22:1329-1339(2002).
RN   [4]
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).
CC   -!- FUNCTION: Guanine nucleotide-exchange factor (GEF) for RHO1 that
CC       stimulates the exchange of RHO1 GDP-bound form into GTP-bound form.
CC       Required for signaling of cell wall defects to RHO1.
CC       {ECO:0000269|PubMed:11839800}.
CC   -!- SUBUNIT: Interacts with RHO1. {ECO:0000269|PubMed:11839800}.
CC   -!- INTERACTION:
CC       Q06412; P40073: SHO1; NbExp=3; IntAct=EBI-37117, EBI-18140;
CC   -!- DOMAIN: The DH domain mediates interaction with RHO1.
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DR   EMBL; U20939; AAB67506.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09727.1; -; Genomic_DNA.
DR   PIR; S53412; S53412.
DR   RefSeq; NP_013529.3; NM_001182313.3.
DR   AlphaFoldDB; Q06412; -.
DR   BioGRID; 31685; 425.
DR   DIP; DIP-4635N; -.
DR   IntAct; Q06412; 5.
DR   MINT; Q06412; -.
DR   STRING; 4932.YLR425W; -.
DR   iPTMnet; Q06412; -.
DR   MaxQB; Q06412; -.
DR   PaxDb; 4932-YLR425W; -.
DR   PeptideAtlas; Q06412; -.
DR   EnsemblFungi; YLR425W_mRNA; YLR425W; YLR425W.
DR   GeneID; 851145; -.
DR   KEGG; sce:YLR425W; -.
DR   AGR; SGD:S000004417; -.
DR   SGD; S000004417; TUS1.
DR   VEuPathDB; FungiDB:YLR425W; -.
DR   eggNOG; KOG4305; Eukaryota.
DR   GeneTree; ENSGT00940000163420; -.
DR   HOGENOM; CLU_002884_0_0_1; -.
DR   InParanoid; Q06412; -.
DR   OMA; HEIITWE; -.
DR   OrthoDB; 2044425at2759; -.
DR   BioCyc; YEAST:G3O-32485-MONOMER; -.
DR   BioGRID-ORCS; 851145; 0 hits in 10 CRISPR screens.
DR   PRO; PR:Q06412; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; Q06412; Protein.
DR   GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR   GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:SGD.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IMP:SGD.
DR   GO; GO:1903501; P:positive regulation of mitotic actomyosin contractile ring assembly; IMP:SGD.
DR   GO; GO:0007165; P:signal transduction; IMP:SGD.
DR   CDD; cd00160; RhoGEF; 1.
DR   Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR001180; CNH_dom.
DR   InterPro; IPR035899; DBL_dom_sf.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR46572; RHO1 GDP-GTP EXCHANGE PROTEIN 1-RELATED; 1.
DR   PANTHER; PTHR46572:SF1; RHO1 GUANINE NUCLEOTIDE EXCHANGE FACTOR TUS1; 1.
DR   Pfam; PF00780; CNH; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00036; CNH; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50219; CNH; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Guanine-nucleotide releasing factor; Reference proteome.
FT   CHAIN           1..1307
FT                   /note="Rho1 guanine nucleotide exchange factor TUS1"
FT                   /id="PRO_0000080979"
FT   DOMAIN          467..657
FT                   /note="DH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT   DOMAIN          715..877
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          938..1279
FT                   /note="CNH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00795"
FT   REGION          1..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          164..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          219..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          780..802
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..95
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        119..142
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..181
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1307 AA;  149113 MW;  561574AB58FFBC54 CRC64;
     MYRYNRSSPF ERTPEKRVSR QESQRKSIEL PKLPPLNTRN SFLDDSDNGT DNISIGWTPI
     SDTQQFQSPV PQAFTFTSKH SARGNGTSSS ESTPKSTKYV KERRPPPPPP LLYSTESIRI
     DSPMVSPSSQ SRERSPNKLS FIGNSEERHH MEYISNHSRI LKSPFANGFS PNSPKSPRDS
     SKQQAHFSDE SDLRCHEREK ALPPIPFTTT LLLSPFDDED SEFFTKPPPP LSTSRNVSGN
     SRVSEALESV YSDSDYTFNN SNARQSSFNS LLGAKPLELA PSITAPTQPF SIQSIDEHKL
     YQCDNVYKLS AIYEWILKVY FEWFNECVFT KIDLFQIVQL LLEFQMPTNF DQDTIDSNVD
     NIMASFISQK AVRFDIINDE EVAVVVGGLD ITGVFTELLP CYSFIDNTYG STNSLICYSN
     VCTHGQSSGF RKEIKLSEII NKSVGLWTEY WHLTPDDLAE INPREVQRQS FIFDLIILEE
     RSLNMATAAV EIYGKRFDKS LLPDEPEFKA LAFDIFEPLI QLHTEFLLTP IFWKLKTRGK
     FIDGVGKIYS KWCGEAKNIY LNYAKAMATV HEIIMWEKKN KTKFVTWLKE IDNSVEITRS
     KMYHDVIFFG GFFKSLQNMP VTLRSILKNT DPSMEDYEYL KIVIKEVEKL NFEVNQVHGL
     AIDHRKLVRF SKQLVLSTNS SNATSYVNVG GSTNANDDDA IQDKLALGLT YPERKLVLSG
     TVYKKRDLWL DPTPVYIALL DNCLLITEEI SKGETQKYKL IERPIPIDYL SLEKRKIPGT
     SKQPLRNYSQ KEHKSPMHNF STPINSMRPL LKSSGNHMST AYGDRKTSNT EISNANPNTD
     EFSFKIRNTA TGESFKFFTE SAEVLNQWID AIMESFKRNA ENHDLNAFEF TVLSSEFAYF
     DKDAPVNLPV APEGSEIDVA LKAYAQKANK DSCSWSKTTR ILCCEDVKFE GRIYLFVATT
     DGIYVKYRDD YGSGFVKILE LNDVKRMEAN VKLGLLFVLD NRKLCYFNIS TVVSRYLAQG
     NTLDENCIVG TVIRDKVRFF KIADDFGNSK HLFFERKGKI VILTPEFDQL TNQVKYFKFY
     KEYKLPSSSN NILNNEIEDI AIFRKSFAVC TKKTVILYQD SFEDNGIVLP SFLNDKDMMA
     HLRHPHLNSL PFKSATDSKK RPSIESLTEE AKKDIATCKA IPVNFFQISQ SSFFALVYDE
     AVVKINCYGE MSDWRKDILL LDFCCTGASF HGNHLILVGD NLIQIYDLKN VEQNLGELVP
     VQIIKGKKIK LASSERREKT ILVLSHPNIL NRQLLVACNP VAMADHQ
//