PIB2_SCHPO
ID PIB2_SCHPO Reviewed; 293 AA.
AC Q9Y7M3;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Glutamine sensor pib2 {ECO:0000250|UniProtKB:P53191};
GN Name=pib2 {ECO:0000312|PomBase:SPBC9B6.03};
GN ORFNames=SPBC9B6.03 {ECO:0000312|PomBase:SPBC9B6.03};
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 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).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, 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: Functions as an intracellular glutamine sensor that directly
CC activates the TORC1 signaling pathway, to promote cell growth when
CC glutamine is available. {ECO:0000250|UniProtKB:P53191}.
CC -!- ACTIVITY REGULATION: Activated by glutamine.
CC {ECO:0000250|UniProtKB:P53191}.
CC -!- SUBUNIT: Interacts with the TORC1 complex when activated by glutamine
CC or cysteine. {ECO:0000250|UniProtKB:P53191}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:16823372};
CC Peripheral membrane protein {ECO:0000269|PubMed:16823372}.
CC -!- DOMAIN: The FYVE-type zinc finger domain contributes to vacuolar
CC localization. {ECO:0000250|UniProtKB:P53191}.
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DR EMBL; CU329671; CAB42364.1; -; Genomic_DNA.
DR PIR; T40784; T40784.
DR RefSeq; NP_595745.1; NM_001021645.2.
DR AlphaFoldDB; Q9Y7M3; -.
DR SMR; Q9Y7M3; -.
DR BioGRID; 276741; 41.
DR STRING; 4896.SPBC9B6.03.1; -.
DR iPTMnet; Q9Y7M3; -.
DR MaxQB; Q9Y7M3; -.
DR PaxDb; Q9Y7M3; -.
DR PRIDE; Q9Y7M3; -.
DR EnsemblFungi; SPBC9B6.03.1; SPBC9B6.03.1:pep; SPBC9B6.03.
DR GeneID; 2540208; -.
DR KEGG; spo:SPBC9B6.03; -.
DR PomBase; SPBC9B6.03; pib2.
DR VEuPathDB; FungiDB:SPBC9B6.03; -.
DR eggNOG; KOG1729; Eukaryota.
DR HOGENOM; CLU_987501_0_0_1; -.
DR InParanoid; Q9Y7M3; -.
DR OMA; DNWVWST; -.
DR PhylomeDB; Q9Y7M3; -.
DR PRO; PR:Q9Y7M3; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:PomBase.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISM:PomBase.
DR GO; GO:0016197; P:endosomal transport; ISS:PomBase.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF01363; FYVE; 1.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 1: Evidence at protein level;
KW Membrane; Metal-binding; Phosphoprotein; Reference proteome; Transducer;
KW Vacuole; Zinc; Zinc-finger.
FT CHAIN 1..293
FT /note="Glutamine sensor pib2"
FT /id="PRO_0000357025"
FT ZN_FING 156..220
FT /note="FYVE-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 38..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 215
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 293 AA; 32053 MW; C8D8AD33B137F1D6 CRC64;
MTTVHQLSGH GPLSRLNIYS GASPYTQRVR PSYELIEAPT RQATNGTGSV SGSPNSSSNS
TPANQGSLPS HTNPQLYSSI TRKERPELFR SYSGNPRLSK PYASSKLAAS SRTASYQAMS
YSVSPTSTNS SVATSLNYQS SRETGISKDH WKPDSDVSVC SFPSCSVRFG LFDRRHHCRR
CGDIFCALHC DRNIPLTMDV KFCLAGSLYR SCVSCFYEYL KWKQSIDLAS SNDITVIEST
IAPQQATTHP PSQPKNAVSV PIPKMDSTDS KGELPSESLV LGTVPDNWVW STF
