TUS1_YEAST
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 03-AUG-2022, entry version 164.
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; 419.
DR DIP; DIP-4635N; -.
DR IntAct; Q06412; 5.
DR MINT; Q06412; -.
DR STRING; 4932.YLR425W; -.
DR iPTMnet; Q06412; -.
DR MaxQB; Q06412; -.
DR PaxDb; Q06412; -.
DR PRIDE; Q06412; -.
DR EnsemblFungi; YLR425W_mRNA; YLR425W; YLR425W.
DR GeneID; 851145; -.
DR KEGG; sce:YLR425W; -.
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; LLPCYSF; -.
DR BioCyc; YEAST:G3O-32485-MON; -.
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; -; 1.
DR Gene3D; 2.30.29.30; -; 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 Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; SSF48065; 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
