MIP1_SCHPO
ID MIP1_SCHPO Reviewed; 1313 AA.
AC P87141;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 161.
DE RecName: Full=Target of rapamycin complex 1 subunit mip1 {ECO:0000305|PubMed:18076573};
DE Short=TORC1 subunit mip1;
GN Name=mip1 {ECO:0000303|PubMed:10648609};
GN ORFNames=SPAC57A7.11 {ECO:0000312|PomBase:SPAC57A7.11};
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 [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10648609; DOI=10.1128/mcb.20.4.1234-1242.2000;
RA Shinozaki-Yabana S., Watanabe Y., Yamamoto M.;
RT "Novel WD-repeat protein Mip1p facilitates function of the meiotic
RT regulator Mei2p in fission yeast.";
RL Mol. Cell. Biol. 20:1234-1242(2000).
RN [2]
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 [3]
RP FUNCTION, AND INTERACTION WITH TOR2.
RX PubMed=17046992; DOI=10.1242/jcs.03241;
RA Alvarez B., Moreno S.;
RT "Fission yeast Tor2 promotes cell growth and represses cell
RT differentiation.";
RL J. Cell Sci. 119:4475-4485(2006).
RN [4]
RP IDENTIFICATION IN THE TORC1 COMPLEX, PHOSPHORYLATION AT SER-834 AND
RP SER-882, AND 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).
RN [5]
RP FUNCTION, AND INTERACTION WITH TOR2.
RX PubMed=17261596; DOI=10.1128/mcb.01039-06;
RA Matsuo T., Otsubo Y., Urano J., Tamanoi F., Yamamoto M.;
RT "Loss of the TOR kinase Tor2 mimics nitrogen starvation and activates the
RT sexual development pathway in fission yeast.";
RL Mol. Cell. Biol. 27:3154-3164(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-837, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Component of TORC1, which regulates multiple cellular
CC processes to control cell growth in response to environmental signals.
CC Tor2 is essential for growth. Nutrient limitation and environmental
CC stress signals cause inactivation of TORC1. Active TORC1 positively
CC controls cell growth and ribosome biogenesis by regulating ribosomal
CC protein gene expression. TORC1 negatively controls G1 cell-cycle
CC arrest, sexual development and amino acid uptake. Represses mating,
CC meiosis and sporulation efficiency by interfering with the functions of
CC the transcription factor ste11 and the meiosis-promoting RNA-binding
CC protein mei2. {ECO:0000269|PubMed:10648609,
CC ECO:0000269|PubMed:17046992, ECO:0000269|PubMed:17261596}.
CC -!- SUBUNIT: The target of rapamycin complex 1 (TORC1) is composed of at
CC least mip1, pop3/wat1, tco89, toc1 and tor2.
CC {ECO:0000269|PubMed:17046992, ECO:0000269|PubMed:17261596,
CC ECO:0000269|PubMed:18076573}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10648609,
CC ECO:0000269|PubMed:18076573}.
CC -!- SIMILARITY: Belongs to the WD repeat RAPTOR family. {ECO:0000305}.
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DR EMBL; AB032552; BAA84585.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB08769.1; -; Genomic_DNA.
DR PIR; T38943; T38943.
DR RefSeq; NP_593370.1; NM_001018802.2.
DR AlphaFoldDB; P87141; -.
DR SMR; P87141; -.
DR BioGRID; 278868; 8.
DR IntAct; P87141; 1.
DR STRING; 4896.SPAC57A7.11.1; -.
DR iPTMnet; P87141; -.
DR MaxQB; P87141; -.
DR PaxDb; P87141; -.
DR PRIDE; P87141; -.
DR EnsemblFungi; SPAC57A7.11.1; SPAC57A7.11.1:pep; SPAC57A7.11.
DR GeneID; 2542404; -.
DR KEGG; spo:SPAC57A7.11; -.
DR PomBase; SPAC57A7.11; mip1.
DR VEuPathDB; FungiDB:SPAC57A7.11; -.
DR eggNOG; KOG1517; Eukaryota.
DR HOGENOM; CLU_001136_0_2_1; -.
DR InParanoid; P87141; -.
DR OMA; QWSCLCL; -.
DR PhylomeDB; P87141; -.
DR Reactome; R-SPO-3371571; HSF1-dependent transactivation.
DR Reactome; R-SPO-9639288; Amino acids regulate mTORC1.
DR PRO; PR:P87141; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:PomBase.
DR GO; GO:0031931; C:TORC1 complex; IDA:PomBase.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IBA:GO_Central.
DR GO; GO:0009267; P:cellular response to starvation; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030307; P:positive regulation of cell growth; IBA:GO_Central.
DR GO; GO:0031139; P:positive regulation of conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0010506; P:regulation of autophagy; IBA:GO_Central.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR GO; GO:0031929; P:TOR signaling; IBA:GO_Central.
DR GO; GO:0038202; P:TORC1 signaling; EXP:PomBase.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR004083; Raptor.
DR InterPro; IPR029347; Raptor_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR12848; PTHR12848; 1.
DR Pfam; PF14538; Raptor_N; 1.
DR SMART; SM01302; Raptor_N; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Meiosis; Phosphoprotein; Reference proteome; Repeat;
KW Sporulation; WD repeat.
FT CHAIN 1..1313
FT /note="Target of rapamycin complex 1 subunit mip1"
FT /id="PRO_0000051078"
FT REPEAT 986..1029
FT /note="WD 1"
FT REPEAT 1033..1074
FT /note="WD 2"
FT REPEAT 1087..1126
FT /note="WD 3"
FT REPEAT 1130..1170
FT /note="WD 4"
FT REPEAT 1176..1216
FT /note="WD 5"
FT REPEAT 1219..1259
FT /note="WD 6"
FT REPEAT 1268..1308
FT /note="WD 7"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 834
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18076573"
FT MOD_RES 837
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517,
FT ECO:0000305|PubMed:18076573"
FT MOD_RES 882
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18076573"
SQ SEQUENCE 1313 AA; 148534 MW; C71B663B0171E7A4 CRC64;
MNDRISEVSG SSRARRSVLS YGTTETGSDR YTENSNIATE NGVDTASSMI DGIQSGFPQP
RHGFEEEYNN AEYINMLEQV FYMYYTDKRH RGVISKKNAE PTETIHDWRM RERLKTVSAA
LLVCLNIGVD PPDVIKPNPA AKYECWIDPF SLPASKALEA IGKNLQQQYE TLSMRTRYRH
YLDPAIEEVK KLCIGQRRNA KEERILFHYN GHGVPMPTAS GEIWVFNKNY TQYIPVSLYD
LQSWLGAPCI YVYDCSAAGN IIVNFNRFAE QRDKEALRIA KQNPNVLAMP SHTSCIQLAA
CGPKETLPMN PDLPADLFTS CLTSPIEISV RWYVLQNPFP NKLNLNMLLK IPGRLQDRRT
PLGELNWIFT AITDTIAWNV FPKHLFRRLF RQDLMVAALF RNFLLAERIM LVHSCHPQSS
PELPPTHDHP MWNSWDLAID NCLSQLPDML DAESKGIAYE YKHSTFFSEQ LTAFEVWLSQ
GLISRKPPDQ LPLVLQVLLS QVHRLRALIL LSKFLDLGVW AVDLALSIGI FPYVLKLLQS
PAIELKPVLV FIWARILAVD DSCQADLLKD NGYGYFVQIL NPNSSIFPSS NISEHRAMCA
FILSVFCRGF PQGQLACLNP QVLSHCLSHL NSPDSLLRQW ACLCISQLWE NYSEAKWSGT
RDNAHVKLAE IIVDSVPEVR ASVLTAFTTF LGFPEKTEEV VAVETYIAIA ALAALSDASP
LVRHELVIFL SHFVVNYKKQ LMVVAYESSL ADILEKKNHN SISASTIYET VWQAVLVLAA
DPSIEISLAA EAIINYVYQS MLNSELRESF LAFLLQHLPA LHKASLSKDT DTNSVTSDPK
PHPFVPSVSE NKILNRSFSL TRSLKGLALS LAGSDRASEL LSLNGENKPA ESNLNHLTSA
KVPGPPAFNE LEYQSELDMP LTSYLFDWSR KYFTEPQMRP NEDDEPGSIC YNQRLWRRNR
NEKLIYRTRP LAEYSTNGRW NQQLMTFNNT IAPRKLMFHQ FEDQLITLGD KDIIQVWDWR
RNRCLNSFKT SASATTNVTD MQLLNEDDVA LLMTGSSDGT IKLYRDYENE KVELVTSWNS
LSDLVFGDRN ASLLMSWQQN CGHLLVAGDV RVIRIWDASK EICYANLPVR SSNSITSLTS
DLVGCNIIVA GFSDGVLRVY DKRLPARDSL TDVWKEHSSE IVNVEMQSSG MRELISASSD
GEVKLWDIRM NHSLQTFSTD NSGLTSLTVH SHAPVYATGS SNQSIKIWDT LGQNINTFRE
NPRFLNQPKP SSLMCLKFHP HHLLLACGDN TDSRVNLYSC TKNEIHTDSP NEF
