P42837

PR
Gene name
FIG4 (YNL325C, N0330)
Protein name
Polyphosphoinositide phosphatase
Names
Factor-induced gene 4 protein, Phosphatidylinositol 3,5-bisphosphate 5-phosphatase
Species
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
KEGG Pathway
sce:YNL325C
EC number
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-51 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for P42837

Entry ID Method Resolution Chain Position Source
AF-P42837-F1 Predicted AlphaFoldDB

9 variants for P42837

Variant ID(s) Position Change Description Diseaes Association Provenance
s14-31070 103 G>A No SGRP
s14-30977 134 G>A No SGRP
s14-30017 454 A>V No SGRP
s14-29555 608 R>K No SGRP
s14-29546 611 I>T No SGRP
s14-29514 622 V>I No SGRP
s14-29477 634 G>D No SGRP
s14-29319 687 L>V No SGRP
s14-28791 863 Q>K No SGRP

No associated diseases with P42837

3 regional properties for P42837

Type Name Position InterPro Accession
domain Fumarase C, C-terminal 452 - 504 IPR018951
conserved_site Fumarate lyase, conserved site 361 - 370 IPR020557
domain Fumarate lyase, N-terminal 55 - 386 IPR022761

Functions

Description
EC Number
Subcellular Localization
  • Vacuole membrane ; Peripheral membrane protein
  • Localized to the limiting membrane of the vacuole
  • Localization requires VAC14 and FAB1
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
extrinsic component of membrane The component of a membrane consisting of gene products and protein complexes that are loosely bound to one of its surfaces, but not integrated into the hydrophobic region.
fungal-type vacuole membrane The lipid bilayer surrounding a vacuole, the shape of which correlates with cell cycle phase. The membrane separates its contents from the cytoplasm of the cell. An example of this structure is found in Saccharomyces cerevisiae.
intracellular membrane-bounded organelle Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane.
nuclear periphery The portion of the nuclear lumen proximal to the inner nuclear membrane.
PAS complex A class III phosphatidylinositol 3-kinase complex that contains a phosphatidylinositol-3-phosphate 5-kinase subunit (Fab1p in yeast; PIKfyve in mammals), a kinase activator, and a phosphatase, and may also contain additional proteins; it is involved in regulating the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate. In mammals the complex is composed of PIKFYVE, FIG4 and VAC14. In yeast it is composed of Atg18p, Fig4p, Fab1p, Vac14p and Vac7p.

1 GO annotations of molecular function

Name Definition
phosphatidylinositol-3,5-bisphosphate 5-phosphatase activity Catalysis of the reaction: phosphatidylinositol-3,5-bisphosphate + H2O = phosphatidylinositol-3-phosphate + orthophosphate.

3 GO annotations of biological process

Name Definition
1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate metabolic process The chemical reactions and pathways involving 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate.
phosphatidylinositol dephosphorylation The process of removing one or more phosphate groups from a phosphatidylinositol.
regulation of phosphatidylinositol biosynthetic process Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of phosphatidylinositol.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q92562 FIG4 Polyphosphoinositide phosphatase Homo sapiens (Human) PR
Q91WF7 Fig4 Polyphosphoinositide phosphatase Mus musculus (Mouse) PR
10 20 30 40 50 60
MNNDAMEHTL GGGILTTSGS KQRKTSKFVM GKYTLYETKD RMYIVGSNKR ETMFRILEID
70 80 90 100 110 120
LTVPRGELTV LEDNVFFTRN EIMNVLASLE EATEDGLHKK ITGYGLLGFI KFTCWYYLIM
130 140 150 160 170 180
VTKYSQVAVI GGHGIYHIDG IDIIPITNNY KKPEKSSDEA RLLNIFKDLD LTKTFYFSYT
190 200 210 220 230 240
YDITNTLQTN ILREKLKAVD RCDITIPCGI TDYNEMFVWN NNLLSPIFAC IDTVFDWFQC
250 260 270 280 290 300
IIHGFIDQVN VSVLGKSIYI TLIARRSHHF AGARFLKRGV NNKGHVANEV ETEQIVTDMI
310 320 330 340 350 360
LTPFHQPGNG FFDSDRYTSF VQHRGSIPLY WTQDASNLTT KPPIRINVVD PFFSPAALHF
370 380 390 400 410 420
DNLFQRYGGG TIQILNLIKT KEKTPRETKL LWEFEQCIDY LNEFLPTLKK LDYTSWDMSR
430 440 450 460 470 480
ASKQDGQGVI EFLEKYAVNT VTTTGIFHNG PDFASTKIQE GICRSNCIDC LDRTNAAQFV
490 500 510 520 530 540
IGKRALGCQL KSLGIIDNSY LEYDSDIVNI LTELFHDLGD TIALQYGGSH LVNTMETYRK
550 560 570 580 590 600
INQWSSHSRD MIESIKRFYS NSFVDAQRQD AINLFLGHYS WREGFPSLWE MNTDFYLHNA
610 620 630 640 650 660
YSLNMPKRSY IHWWNDYNIK SVKELINEEL IATGNDVTRE KIIKNVRGYP GAFDNYWNEY
670 680 690 700 710 720
YLPRSVTWIR DLFAYNMNST RRYHNALSKQ DKAMSPFTSR KQSWLNNKLK MITSSKSLEK
730 740 750 760 770 780
AEGRVVETTD LDRDTSPKQE LELYEHYLHI ISDRSQKLEE KMNSFSYSKY PIFISHESSE
790 800 810 820 830 840
IPPMRKVIGE PLVDIAEDFT DVYDDDDDGD DENDEMTTEA LLIAPDHVSV DEKFYEKVLN
850 860 870
VDDYKPALDD YSAVIHIKPD NLQLYRDLCF SKDIQLDFQ