PIB2_YEASX
ID PIB2_YEASX Reviewed; 635 AA.
AC A0A8H4C2S2;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2022, sequence version 1.
DT 03-AUG-2022, entry version 3.
DE RecName: Full=Glutamine sensor PIB2 {ECO:0000250|UniProtKB:P53191};
DE AltName: Full=Phosphatidylinositol 3-phosphate-binding protein 2 {ECO:0000250|UniProtKB:P53191};
GN Name=PIB2 {ECO:0000250|UniProtKB:P53191};
GN ORFNames=GI527_G0002398 {ECO:0000312|EMBL:KAF1908241.1};
OS Saccharomyces cerevisiae (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=4932 {ECO:0000312|EMBL:KAF1908241.1, ECO:0000312|Proteomes:UP000470054};
RN [1] {ECO:0000312|Proteomes:UP000470054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=INSC1005 {ECO:0000312|Proteomes:UP000470054};
RA Fiddes I.T., Church D.M.;
RT "Inscripta technologies.";
RL Submitted (JAN-2020) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 200060 / W303 {ECO:0000303|PubMed:28993463};
RX PubMed=28993463; DOI=10.1242/jcs.207910;
RA Varlakhanova N.V., Mihalevic M.J., Bernstein K.A., Ford M.G.J.;
RT "Pib2 and the EGO complex are both required for activation of TORC1.";
RL J. Cell Sci. 130:3878-3890(2017).
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:28993463). May play a role in repressing
CC NPR1 activity independently of TORC1 signaling (PubMed:28993463).
CC {ECO:0000269|PubMed:28993463}.
CC -!- ACTIVITY REGULATION: Activated by glutamine (By similarity). May also
CC be activated by cysteine (By similarity).
CC {ECO:0000250|UniProtKB:P53191}.
CC -!- SUBUNIT: Interacts with the TORC1 complex when activated by glutamine
CC or cysteine (By similarity). Interacts with TOR1; glutamine enhances
CC the interaction (By similarity). Interacts with KOG1; glutamine
CC enhances the interaction (By similarity). Interacts with TCO89 (By
CC similarity). Interacts with LST8; glutamine enhances the interaction
CC (By similarity). Interacts with TOR2; glutamine enhances the
CC interaction (By similarity). {ECO:0000250|UniProtKB:P53191}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250|UniProtKB:P53191};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P53191}.
CC -!- DOMAIN: The FYVE-type zinc finger domain contributes to vacuolar
CC localization. {ECO:0000250|UniProtKB:P53191}.
CC -!- DISRUPTION PHENOTYPE: Abnormal activation of TORC1 in nitrogen-replete
CC conditions (glutamine or leucine nitrogen source) (PubMed:28993463).
CC Abnormal TORC1-reactivation following inactivaton by rapamycin (TORC1
CC signaling-inhibitor) (PubMed:28993463). Sensitive to rapamycin (TORC1
CC signaling-inhibitor) (PubMed:28993463). Abnormal localization of TOR1
CC to vacuoles (PubMed:28993463). Localization of GTR1 and GTR2 to
CC vacuoles is normal (PubMed:28993463). Macroautophagy appears normal
CC (PubMed:28993463). {ECO:0000269|PubMed:28993463}.
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DR EMBL; JAAEAL010000004; KAF1908241.1; -; Genomic_DNA.
DR SMR; A0A8H4C2S2; -.
DR Proteomes; UP000470054; Unassembled WGS sequence.
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 3: Inferred from homology;
KW Membrane; Metal-binding; Phosphoprotein; Transducer; Vacuole; Zinc;
KW Zinc-finger.
FT CHAIN 1..635
FT /note="Glutamine sensor PIB2"
FT /id="PRO_0000456199"
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:0000269|PubMed:28993463"
FT REGION 304..440
FT /note="Required for interaction with TORC1"
FT /evidence="ECO:0000250|UniProtKB:P53191"
FT REGION 620..635
FT /note="May be required for TORC1 activation"
FT /evidence="ECO:0000250|UniProtKB:P53191"
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:0000250|UniProtKB:P53191"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53191"
FT MOD_RES 56
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P53191"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53191"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53191"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53191"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53191"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53191"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53191"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53191"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53191"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53191"
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
