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PIB2_YEAST
ID   PIB2_YEAST              Reviewed;         635 AA.
AC   P53191; D6VUB4; E9P8Z2;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 155.
DE   RecName: Full=Glutamine sensor PIB2 {ECO:0000303|PubMed:34535752};
DE   AltName: Full=Phosphatidylinositol 3-phosphate-binding protein 2 {ECO:0000305};
GN   Name=PIB2 {ECO:0000312|SGD:S000002991};
GN   OrderedLocusNames=YGL023C {ECO:0000312|SGD:S000002991};
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=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(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   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-124; SER-165;
RP   SER-174 AND SER-300, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46; SER-53; THR-56; SER-73;
RP   SER-113; SER-165; SER-300; SER-309 AND SER-381, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
RN   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, DOMAIN FYVE-TYPE, DISRUPTION PHENOTYPE, AND
RP   MUTAGENESIS OF 621-SER--PHE-635.
RX   PubMed=26510498; DOI=10.1091/mbc.e15-08-0581;
RA   Kim A., Cunningham K.W.;
RT   "A LAPF/phafin1-like protein regulates TORC1 and lysosomal membrane
RT   permeabilization in response to endoplasmic reticulum membrane stress.";
RL   Mol. Biol. Cell 26:4631-4645(2015).
RN   [9]
RP   FUNCTION, SUBUNIT, INTERACTION WITH TOR1, AND DISRUPTION PHENOTYPE.
RX   PubMed=28483912; DOI=10.1128/mcb.00075-17;
RA   Tanigawa M., Maeda T.;
RT   "An In Vitro TORC1 Kinase Assay That Recapitulates the Gtr-Independent
RT   Glutamine-Responsive TORC1 Activation Mechanism on Yeast Vacuoles.";
RL   Mol. Cell. Biol. 37:e00075-e00075(2017).
RN   [10]
RP   FUNCTION, ACTIVITY REGULATION, SUBUNIT, INTERACTION WITH TOR1; KOG1; TCO89;
RP   LST8 AND TOR2, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION,
RP   DOMAIN FYVE-TYPE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF PRO-337;
RP   ARG-475; CYS-522 AND 621-SER--PHE-635.
RX   PubMed=29698392; DOI=10.1371/journal.pgen.1007334;
RA   Ukai H., Araki Y., Kira S., Oikawa Y., May A.I., Noda T.;
RT   "Gtr/Ego-independent TORC1 activation is achieved through a glutamine-
RT   sensitive interaction with Pib2 on the vacuolar membrane.";
RL   PLoS Genet. 14:e1007334-e1007334(2018).
RN   [11]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=32801125; DOI=10.1242/jcs.245555;
RA   Uemura S., Mochizuki T., Amemiya K., Kurosaka G., Yazawa M., Nakamoto K.,
RA   Ishikawa Y., Izawa S., Abe F.;
RT   "Amino acid homeostatic control by TORC1 in Saccharomyces cerevisiae under
RT   high hydrostatic pressure.";
RL   J. Cell Sci. 133:jcs245555-jcs245555(2020).
RN   [12]
RP   FUNCTION, ACTIVITY REGULATION, SUBUNIT, INTERACTION WITH TOR1, DISRUPTION
RP   PHENOTYPE, AND MUTAGENESIS OF PRO-337; LEU-340; ARG-341 AND VAL-626.
RX   PubMed=34535752; DOI=10.1038/s42003-021-02625-w;
RA   Tanigawa M., Yamamoto K., Nagatoishi S., Nagata K., Noshiro D., Noda N.N.,
RA   Tsumoto K., Maeda T.;
RT   "A glutamine sensor that directly activates TORC1.";
RL   Commun. Biol. 4:1093-1093(2021).
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 (PubMed:34535752, PubMed:29698392,
CC       PubMed:28483912, PubMed:26510498, PubMed:32801125). May play a role in
CC       repressing NPR1 activity independently of TORC1 signaling (By
CC       similarity). {ECO:0000250|UniProtKB:A0A8H4C2S2,
CC       ECO:0000269|PubMed:26510498, ECO:0000269|PubMed:28483912,
CC       ECO:0000269|PubMed:29698392, ECO:0000269|PubMed:32801125,
CC       ECO:0000269|PubMed:34535752}.
CC   -!- ACTIVITY REGULATION: Activated by glutamine (PubMed:34535752,
CC       PubMed:29698392). May also be activated by cysteine (PubMed:34535752).
CC       {ECO:0000269|PubMed:29698392, ECO:0000269|PubMed:34535752}.
CC   -!- SUBUNIT: Interacts with the TORC1 complex when activated by glutamine
CC       or cysteine (PubMed:34535752, PubMed:29698392, PubMed:28483912).
CC       Interacts with TOR1; glutamine enhances the interaction
CC       (PubMed:34535752, PubMed:29698392, PubMed:28483912). Interacts with
CC       KOG1; glutamine enhances the interaction (PubMed:29698392). Interacts
CC       with TCO89 (PubMed:29698392). Interacts with LST8; glutamine enhances
CC       the interaction (PubMed:29698392). Interacts with TOR2; glutamine
CC       enhances the interaction (PubMed:29698392).
CC       {ECO:0000269|PubMed:28483912, ECO:0000269|PubMed:29698392,
CC       ECO:0000269|PubMed:34535752}.
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:26510498, ECO:0000269|PubMed:29698392}; Peripheral
CC       membrane protein {ECO:0000269|PubMed:14562095}.
CC   -!- DOMAIN: The FYVE-type zinc finger domain contributes to vacuolar
CC       localization. {ECO:0000269|PubMed:26510498,
CC       ECO:0000269|PubMed:29698392}.
CC   -!- DISRUPTION PHENOTYPE: Abnormal activation of TORC1 signaling in
CC       nitrogen-replete conditions (glutamine nitrogen source), and during
CC       high hydrostatic pressure (mechanical stress) (PubMed:29698392,
CC       PubMed:28483912, PubMed:32801125). Increases cellular levels of
CC       glutamine and alanine during high hydrostatic pressure (mechanical
CC       stress) (PubMed:32801125). Sensitive to rapamycin (TORC1 signaling-
CC       inhibitor), caffeine, and high hydrostatic pressure (mechanical stress)
CC       (PubMed:29698392, PubMed:34535752, PubMed:26510498, PubMed:32801125).
CC       Resistance to tunicamycin (endoplasmic reticulum stressor) administered
CC       together with FK506 (calcineurin inhibitor) (PubMed:26510498).
CC       Localization of TORC1 to vacuoles is normal (PubMed:28483912).
CC       Simultaneous disruption of GTR1 results in TOR1 mislocalization and
CC       loss of TORC1 activity and viability (PubMed:29698392). Simultaneous
CC       disruption of EGO1 results in loss of viability (PubMed:29698392).
CC       {ECO:0000269|PubMed:26510498, ECO:0000269|PubMed:28483912,
CC       ECO:0000269|PubMed:29698392, ECO:0000269|PubMed:32801125,
CC       ECO:0000269|PubMed:34535752}.
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DR   EMBL; Z72545; CAA96724.1; -; Genomic_DNA.
DR   EMBL; Z72544; CAA96723.1; -; Genomic_DNA.
DR   EMBL; AY692918; AAT92937.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08075.1; -; Genomic_DNA.
DR   PIR; S64025; S64025.
DR   RefSeq; NP_011492.3; NM_001180888.3.
DR   AlphaFoldDB; P53191; -.
DR   SMR; P53191; -.
DR   BioGRID; 33223; 315.
DR   DIP; DIP-6378N; -.
DR   IntAct; P53191; 8.
DR   MINT; P53191; -.
DR   STRING; 4932.YGL023C; -.
DR   iPTMnet; P53191; -.
DR   MaxQB; P53191; -.
DR   PaxDb; P53191; -.
DR   PRIDE; P53191; -.
DR   EnsemblFungi; YGL023C_mRNA; YGL023C; YGL023C.
DR   GeneID; 852861; -.
DR   KEGG; sce:YGL023C; -.
DR   SGD; S000002991; PIB2.
DR   VEuPathDB; FungiDB:YGL023C; -.
DR   eggNOG; KOG1729; Eukaryota.
DR   HOGENOM; CLU_020649_0_0_1; -.
DR   InParanoid; P53191; -.
DR   OMA; RHWLYLD; -.
DR   BioCyc; YEAST:G3O-30542-MON; -.
DR   PRO; PR:P53191; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P53191; protein.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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..635
FT                   /note="Glutamine sensor PIB2"
FT                   /id="PRO_0000058425"
FT   ZN_FING         452..527
FT                   /note="FYVE-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   REGION          1..164
FT                   /note="May play a role in attenuating TORC1 signaling"
FT                   /evidence="ECO:0000250|UniProtKB:A0A8H4C2S2"
FT   REGION          1..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          123..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          224..254
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          304..440
FT                   /note="Required for interaction with TORC1"
FT                   /evidence="ECO:0000269|PubMed:34535752"
FT   REGION          534..557
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          570..623
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          620..635
FT                   /note="May be required for TORC1 activation"
FT                   /evidence="ECO:0000269|PubMed:34535752"
FT   COMPBIAS        10..47
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..110
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        159..181
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        236..254
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        584..598
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         458
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         461
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         474
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         477
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         482
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         485
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         519
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         522
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   MOD_RES         46
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         53
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         56
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         73
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         113
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         124
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         148
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
FT   MOD_RES         165
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         174
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         300
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         309
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         381
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MUTAGEN         337
FT                   /note="P->A: Mildly decreases interaction with and
FT                   activation of TOR1 in response to glutamine. Sensitive to
FT                   rapamycin."
FT                   /evidence="ECO:0000269|PubMed:34535752"
FT   MUTAGEN         337
FT                   /note="P->S: Decreases interaction with and activation of
FT                   TOR1."
FT                   /evidence="ECO:0000269|PubMed:29698392"
FT   MUTAGEN         340
FT                   /note="L->A: Decreases interaction with and activation of
FT                   TOR1 in response to glutamine. Sensitive to rapamycin."
FT                   /evidence="ECO:0000269|PubMed:34535752"
FT   MUTAGEN         341
FT                   /note="R->A: Abolishes interaction with and activation of
FT                   TOR1 in response to glutamine. Sensitive to rapamycin."
FT                   /evidence="ECO:0000269|PubMed:34535752"
FT   MUTAGEN         475
FT                   /note="R->A: Decreases localization to the vacuolar
FT                   membrane and results in rapamycin sensitivity; when
FT                   associated with S-522."
FT                   /evidence="ECO:0000269|PubMed:29698392"
FT   MUTAGEN         522
FT                   /note="C->S: Decreases localization to the vacuolar
FT                   membrane and results in rapamycin sensitivity; when
FT                   associated with A-475."
FT                   /evidence="ECO:0000269|PubMed:29698392"
FT   MUTAGEN         621..635
FT                   /note="Missing: Abnormal TORC1 activation in glutamine-
FT                   replete conditions. Sensitive to caffeine. Resistance to
FT                   tunicamycin (endoplasmic reticulum stressor) administered
FT                   together with FK506 (calcineurin inhibitor)."
FT                   /evidence="ECO:0000269|PubMed:26510498,
FT                   ECO:0000269|PubMed:29698392"
FT   MUTAGEN         626
FT                   /note="V->A: Increases activity in presence of glutamine."
FT                   /evidence="ECO:0000269|PubMed:34535752"
FT   CONFLICT        152
FT                   /note="E -> G (in Ref. 3; AAT92937)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   635 AA;  70617 MW;  512E9B873E6E0164 CRC64;
     MTALHSVSKT PAIKEEEEDG DERDGRGVPL GPRNHDYRGR KGDEESGADT VTSPITFEKK
     KIAPRASTHS EQSILSSISL KSMVNQHRQQ QLQQESSTGA GTGFVDRKQQ IQSPAMVSIL
     RKNSAEENVR SSHSSKLGEG QIDGRKASAS KEIGKTLPFT DDQRSNPELD PTNSVVDVSR
     GKNTKSKTVF NELEDDADDD DEVRQKNLTT QALRKLSSFK MNASSNLRLS KENKAKESSS
     SSTSSVSSSS TSKVENIVDK LTTTNSSSMS QLRFGNTNVI IDSVNHAAKP PHQQMLRKPS
     LEFLPQPASS TNLNFNSNKH KSNVRQISNP KKPLYIPAVL RKVSETNITN DDLLNATLSS
     YYKKASNLEH GFNPSKSQSA SVQNANNLRI ISSQSSVQSN TSSILESYKN KISSYLFPNS
     IPNSDRINLI PTISNRNSAR VNPPTKDHWI PDSKRNSCRY CHKPFTLWER KHHCRHCGDI
     FCQDHLRHWL YLDSQANFIM INELNNGGIN GGGTLCKICD DCLVEYENLS TTNHNANTNE
     DNINVEEGED DDNDNRKKLR NYYKNRQMNA LFRPKKGGSS QEHATVDRDT TTPIQVKSND
     EEADNENTGG EQEEGNDVLG SVIGSVPANW NWSSF
 
 
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