TTI1_SCHPO
ID TTI1_SCHPO Reviewed; 1098 AA.
AC O94600;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=TEL2-interacting protein 1;
GN Name=tti1; ORFNames=SPCC622.13c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP IDENTIFICATION IN THE TORC1 AND TORC2 COMPLEXES, INTERACTION WITH TEL2, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18076573; DOI=10.1111/j.1365-2443.2007.01141.x;
RA Hayashi T., Hatanaka M., Nagao K., Nakaseko Y., Kanoh J., Kokubu A.,
RA Ebe M., Yanagida M.;
RT "Rapamycin sensitivity of the Schizosaccharomyces pombe tor2 mutant and
RT organization of two highly phosphorylated TOR complexes by specific and
RT common subunits.";
RL Genes Cells 12:1357-1370(2007).
CC -!- FUNCTION: Component of the TORC1 and TORC2 complexes required for the
CC regulation of the cellular respons to changes in available nutrients.
CC -!- SUBUNIT: Component of the TORC1 complex composed of at least mip1,
CC orb5, tel2, toc1, toc89, tor2, tti1 and wat1. Component of the TORC2
CC complex composed of at least bit61, orb5, sin1, ste20, tel2, tor1, tti1
CC and wat1. Interacts with tel2. {ECO:0000269|PubMed:18076573}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the tti1 family. {ECO:0000305}.
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DR EMBL; CU329672; CAA21869.1; -; Genomic_DNA.
DR PIR; T41493; T41493.
DR RefSeq; NP_588185.1; NM_001023175.2.
DR AlphaFoldDB; O94600; -.
DR BioGRID; 276043; 6.
DR IntAct; O94600; 4.
DR MINT; O94600; -.
DR STRING; 4896.SPCC622.13c.1; -.
DR iPTMnet; O94600; -.
DR MaxQB; O94600; -.
DR PaxDb; O94600; -.
DR PRIDE; O94600; -.
DR EnsemblFungi; SPCC622.13c.1; SPCC622.13c.1:pep; SPCC622.13c.
DR GeneID; 2539480; -.
DR KEGG; spo:SPCC622.13c; -.
DR PomBase; SPCC622.13c; tti1.
DR VEuPathDB; FungiDB:SPCC622.13c; -.
DR eggNOG; KOG4524; Eukaryota.
DR HOGENOM; CLU_005544_0_0_1; -.
DR InParanoid; O94600; -.
DR OMA; GAHTCQV; -.
DR PhylomeDB; O94600; -.
DR PRO; PR:O94600; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0070209; C:ASTRA complex; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0110078; C:TTT complex; IDA:PomBase.
DR GO; GO:0006338; P:chromatin remodeling; IPI:PomBase.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR016441; Tti1.
DR PIRSF; PIRSF005250; UCP005250; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome.
FT CHAIN 1..1098
FT /note="TEL2-interacting protein 1"
FT /id="PRO_0000353822"
FT REGION 768..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1098 AA; 124765 MW; 7F77BB2666EC0F94 CRC64;
MSHIQSIFAQ IRDPFRKLSF YSLPLSSETS SVDSNGLKNS LKDAYFGLEK ALTNTDADLP
LNLCDYIFFP IVPVLKSWYR VPSTGVEYAI QCVNLLYKHG WREAHNEMLT MQLLLMLLNI
ADGWKSPSET VEQDFRVREI TFETLENVIT DFKPNFHDKR QYLLFARALS SALDIIPNKN
SSRRLQFASL CCVQKLICPK QYRLPTEFLT TFLPGIVSGL TKGLAPNGTC QYFKNVCISL
NILGDTVVKA ISDDNTKDLP DEKDASSNSH FFGPTKRTKS WKRATCQQLS NAVKAILHLR
SSQNLHVQDA LFDFCFILFR DCLDSLKDCR IHLLESMLKL INKKENPKLR DYGMNKLVSL
IESFNNITME SVLTECLNDW STTWSSVSTF ASEDNKLEEL NRLKSLLSIS SHLPKTLQLM
EPLLDGILSQ LVPKSSGIDS NSQKLLTSST SNEYIHGEFF GGNEMERTTQ EIVTSFAKAP
NVKYVMQSLL SKATSATNEN SVRAFWAFMV LLKSDVETVD SLEMYIDSLE QYSFEVLQQL
SQLNVFTKAS LEDKQKKEKY NLLCVRSCIA IDSISWISSL QGVKFRSKLM AYFYPLLEHL
AFASPYVSSF AEACIQAIAT NCNYSTPAEL LRENIDYVVN SVALKLNTLD VSPQLPIVMA
YVIKNDDGGC IRYIGDVVDA IFGILDAYHG YARLTEGLLG ILYAIIKQES INGEEKKLIV
GVEEDAMNED KNKPCKKIRE FVQLLLENPN YPLPKDDHEL EDMIHDEQQE TKSGHEQFRE
HAMKEKEKKG KENENMGETT VDHENINSNV MDEQGEKQKD DVVDMVRKIT EKAQLFLSHE
QITIRVEMLK LLSYGSNVLA KEPNTFYPAI NTFWPLVVIQ LDTDNELLVE CALETIYQVC
ALADDFMTSR IRQDLLPRLE TLCQRWHLFN VARTYSSEHR LQRAMLKVTS ACVANKLSIV
VYLKLMGITA PIIRAITHMS QKYAGDESLV EETWNAFSKQ NPDAVYYERE VRGSQMIDTF
STELLIPGKQ RVQRTYRRTH EVLEPVGAKT SETVFNDLLG QQGSGKTETQ EEPLPSLDNL
LHLNQPKKGA KKPLISII