TSC1_SCHPO
ID TSC1_SCHPO Reviewed; 899 AA.
AC Q09778;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Tuberous sclerosis 1 protein homolog;
GN Name=tsc1; ORFNames=SPAC22F3.13;
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 FUNCTION, AND INTERACTION WITH TSC2.
RX PubMed=12136010; DOI=10.1093/genetics/161.3.1053;
RA Matsumoto S., Bandyopadhyay A., Kwiatkowski D.J., Maitra U., Matsumoto T.;
RT "Role of the Tsc1-Tsc2 complex in signaling and transport across the cell
RT membrane in the fission yeast Schizosaccharomyces pombe.";
RL Genetics 161:1053-1063(2002).
RN [3]
RP FUNCTION.
RX PubMed=14718525; DOI=10.1074/jbc.m313874200;
RA van Slegtenhorst M., Carr E., Stoyanova R., Kruger W.D., Henske E.P.;
RT "Tsc1+ and tsc2+ regulate arginine uptake and metabolism in
RT Schizosaccharomyces pombe.";
RL J. Biol. Chem. 279:12706-12713(2004).
RN [4]
RP FUNCTION.
RX PubMed=16624901; DOI=10.1534/genetics.106.056895;
RA Nakase Y., Fukuda K., Chikashige Y., Tsutsumi C., Morita D., Kawamoto S.,
RA Ohnuki M., Hiraoka Y., Matsumoto T.;
RT "A defect in protein farnesylation suppresses a loss of Schizosaccharomyces
RT pombe tsc2+, a homolog of the human gene predisposing to tuberous sclerosis
RT complex.";
RL Genetics 173:569-578(2006).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Together with tsc2, required for uptake of various amino
CC acids from the environment and for proper conjugation. Involved in
CC induction of gene expression of permeases and genes required for
CC meiosis upon nitrogen starvation. May act as a GTPase-activating
CC protein (GAP) for the small GTPase rhb1. {ECO:0000269|PubMed:12136010,
CC ECO:0000269|PubMed:14718525, ECO:0000269|PubMed:16624901}.
CC -!- SUBUNIT: Interacts with tsc2. {ECO:0000269|PubMed:12136010}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
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DR EMBL; CU329670; CAA91078.1; -; Genomic_DNA.
DR PIR; S62428; S62428.
DR RefSeq; NP_593028.1; NM_001018427.2.
DR PDB; 4KK0; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J=1-431.
DR PDB; 4KK1; X-ray; 3.30 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=1-431.
DR PDBsum; 4KK0; -.
DR PDBsum; 4KK1; -.
DR AlphaFoldDB; Q09778; -.
DR SMR; Q09778; -.
DR BioGRID; 278359; 89.
DR IntAct; Q09778; 1.
DR STRING; 4896.SPAC22F3.13.1; -.
DR iPTMnet; Q09778; -.
DR MaxQB; Q09778; -.
DR PaxDb; Q09778; -.
DR PRIDE; Q09778; -.
DR DNASU; 2541869; -.
DR EnsemblFungi; SPAC22F3.13.1; SPAC22F3.13.1:pep; SPAC22F3.13.
DR GeneID; 2541869; -.
DR KEGG; spo:SPAC22F3.13; -.
DR PomBase; SPAC22F3.13; tsc1.
DR VEuPathDB; FungiDB:SPAC22F3.13; -.
DR eggNOG; ENOG502R01W; Eukaryota.
DR HOGENOM; CLU_314266_0_0_1; -.
DR InParanoid; Q09778; -.
DR OMA; AYERRIM; -.
DR PhylomeDB; Q09778; -.
DR Reactome; R-SPO-165181; Inhibition of TSC complex formation by PKB.
DR Reactome; R-SPO-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR Reactome; R-SPO-5628897; TP53 Regulates Metabolic Genes.
DR PRO; PR:Q09778; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0033596; C:TSC1-TSC2 complex; IPI:PomBase.
DR GO; GO:0005096; F:GTPase activator activity; NAS:PomBase.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IMP:PomBase.
DR GO; GO:0032007; P:negative regulation of TOR signaling; IBA:GO_Central.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IMP:PomBase.
DR GO; GO:1905589; P:positive regulation of L-arginine import across plasma membrane; IMP:PomBase.
DR GO; GO:1905626; P:positive regulation of L-methionine import across plasma membrane; IMP:PomBase.
DR GO; GO:1905534; P:positive regulation of leucine import across plasma membrane; IMP:PomBase.
DR GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR007483; Hamartin.
DR PANTHER; PTHR15154; PTHR15154; 1.
DR Pfam; PF04388; Hamartin; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; Reference proteome.
FT CHAIN 1..899
FT /note="Tuberous sclerosis 1 protein homolog"
FT /id="PRO_0000065653"
FT REGION 874..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 540..706
FT /evidence="ECO:0000255"
FT COILED 737..847
FT /evidence="ECO:0000255"
FT COMPBIAS 885..899
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 2..14
FT /evidence="ECO:0007829|PDB:4KK0"
FT HELIX 26..38
FT /evidence="ECO:0007829|PDB:4KK0"
FT HELIX 44..60
FT /evidence="ECO:0007829|PDB:4KK0"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:4KK0"
FT HELIX 66..79
FT /evidence="ECO:0007829|PDB:4KK0"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:4KK0"
FT HELIX 87..96
FT /evidence="ECO:0007829|PDB:4KK0"
FT HELIX 98..103
FT /evidence="ECO:0007829|PDB:4KK0"
FT HELIX 109..123
FT /evidence="ECO:0007829|PDB:4KK0"
FT TURN 128..131
FT /evidence="ECO:0007829|PDB:4KK0"
FT HELIX 135..154
FT /evidence="ECO:0007829|PDB:4KK0"
FT HELIX 165..185
FT /evidence="ECO:0007829|PDB:4KK0"
FT HELIX 187..198
FT /evidence="ECO:0007829|PDB:4KK0"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:4KK0"
FT HELIX 204..216
FT /evidence="ECO:0007829|PDB:4KK0"
FT HELIX 222..228
FT /evidence="ECO:0007829|PDB:4KK0"
FT HELIX 230..240
FT /evidence="ECO:0007829|PDB:4KK0"
FT HELIX 244..258
FT /evidence="ECO:0007829|PDB:4KK0"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:4KK0"
FT TURN 264..268
FT /evidence="ECO:0007829|PDB:4KK0"
FT HELIX 269..280
FT /evidence="ECO:0007829|PDB:4KK0"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:4KK0"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:4KK0"
FT HELIX 339..349
FT /evidence="ECO:0007829|PDB:4KK0"
FT HELIX 351..357
FT /evidence="ECO:0007829|PDB:4KK0"
FT HELIX 361..366
FT /evidence="ECO:0007829|PDB:4KK0"
FT TURN 367..369
FT /evidence="ECO:0007829|PDB:4KK0"
FT HELIX 378..389
FT /evidence="ECO:0007829|PDB:4KK0"
FT HELIX 396..399
FT /evidence="ECO:0007829|PDB:4KK0"
FT HELIX 403..407
FT /evidence="ECO:0007829|PDB:4KK0"
FT HELIX 412..427
FT /evidence="ECO:0007829|PDB:4KK0"
SQ SEQUENCE 899 AA; 103435 MW; 03D7E9CC8866ECAB CRC64;
MPLQSLVKAL WNVLHEEESE GYPDLTELIA EVESYQQRYP KQNPTNSQKI RHILDEIYEK
TPFNNTRRRI LWLAVLKTVI PLLILDRQAV GEWWDQIFFP FLNSPTQLKP VFSDLKSILF
YILIFHDEDE WGGDLRRECA EETITRLVDL YVSKAIENLG DVESQEQRNQ TIECLVNVLV
HYGIQRPKEL SSCFCHHFLN PPTRIPILSV MVEVIRRQGP RLYEIPQTGF YDLVLKCAEF
DTSPILLSYA LSFILMILSH ICNSLDDSLY RLFCIYLRFS MIDPTSGFPS STASGNWEVF
HDFMSTYAST TTSQTDSSYN DVHDIVGSSQ PDYLESLDYS QLFSILYALY PINFLEFLRD
PKLYASKHNF QIRYSFNQEL LSTKSDGLLG RHLAHSNFLK YTAETELTDK SRWTRLDSIA
VVALCNSLNA VGIAESVMDP FGGKLPTTYE ETSSATGLLA YPNESHDIAS EPFSISWPQN
PSISGSVHSA TTFDKAQLSN TEDSYDNISH GTSYSEGVSS IHMVKGERGS NNLELTSESL
SSTNDTIRRL QRDLLFLQNE LRFEKFVRQQ HLQNIGKLHR EHILDMAVES ERQKLLLTNK
RYKAQIELLN SEIDKHRSES QAALNRRVKW ENDFNNKIKA LREEKKAWKS EESELKSSIE
SLISQLESIR NSQIDIAFSK NQLELKLQLY ETKLKEYEQH LSCVNISKKQ VSSSSDTSFG
NTKMDSSMIL SNSEAVSDEQ ERELIESEKH RMKLESENLH LQANIELLKK DLEAINVVYE
AKIFDLEKRL SSEANAPELH NPVNLNYDAQ LSKISEIKEN YDELLTRYRE LEGKFLESQA
EVEELKNFQK PLVDTGSSIH SSPGLQQSKF IIRNDSLHPK VGPPRRQSTD TSRSTFRQY
