P32563

PR
Gene name
VPH1
Protein name
V-type proton ATPase subunit a, vacuolar isoform
Names
V-ATPase a 1 subunit, V-ATPase 95 kDa subunit, Vacuolar pH protein 1, Vacuolar proton pump a subunit, Vacuolar proton translocating ATPase subunit a 1
Species
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
KEGG Pathway
sce:YOR270C
EC number
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

126-206 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

29 structures for P32563

Entry ID Method Resolution Chain Position Source
2JTW NMR - A 728-748 PDB
2NVJ NMR - A 721-745 PDB
2RPW NMR - X 728-748 PDB
3J9T EM 690 A b 1-840 PDB
3J9U EM 760 A b 1-840 PDB
3J9V EM 830 A b 1-840 PDB
5I1M EM 700 A V 383-840 PDB
5TJ5 EM 390 A A 400-829 PDB
5VOX EM 680 A b 1-840 PDB
5VOY EM 790 A b 1-840 PDB
5VOZ EM 760 A b 1-840 PDB
6C6L EM 350 A A 1-840 PDB
6HH0 NMR - A 728-748 PDB
6M0R EM 270 A A 3-827 PDB
6M0S EM 360 A A 3-827 PDB
6O7T EM 320 A a 1-840 PDB
6PE4 EM 310 A A 1-840 PDB
6PE5 EM 320 A A 1-840 PDB
7FDA EM 420 A Q 1-840 PDB
7FDB EM 480 A Q 1-840 PDB
7FDC EM 660 A Q 1-840 PDB
7TAO EM 320 A A 1-840 PDB
7TAP EM 280 A A 1-840 PDB
7TMR EM 350 A a 1-840 PDB
7TMS EM 380 A a 1-840 PDB
7TMT EM 380 A a 1-840 PDB
8EAS EM 260 A a 1-840 PDB
8EAU EM 310 A a 1-840 PDB
AF-P32563-F1 Predicted AlphaFoldDB

3 variants for P32563

Variant ID(s) Position Change Description Diseaes Association Provenance
s15-829910 222 V>I No SGRP
s15-828657 639 L>F No SGRP
s15-828479 699 V>L No SGRP

No associated diseases with P32563

1 regional properties for P32563

Type Name Position InterPro Accession
conserved_site Phosphorylase pyridoxal-phosphate attachment site 673 - 685 IPR035090

Functions

Description
EC Number
Subcellular Localization
  • Vacuole membrane ; Multi-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

6 GO annotations of cellular component

Name Definition
fungal-type vacuole A vacuole that has both lytic and storage functions. The fungal vacuole is a large, membrane-bounded organelle that functions as a reservoir for the storage of small molecules (including polyphosphate, amino acids, several divalent cations (e.g. calcium), other ions, and other small molecules) as well as being the primary compartment for degradation. It is an acidic compartment, containing an ensemble of acid hydrolases. At least in S. cerevisiae, there are indications that the morphology of the vacuole is variable and correlated with the cell cycle, with logarithmically growing cells having a multilobed, reticulated vacuole, while stationary phase cells contain a single large structure.
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.
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
vacuolar proton-transporting V-type ATPase complex A proton-transporting two-sector ATPase complex found in the vacuolar membrane, where it acts as a proton pump to mediate acidification of the vacuolar lumen.
vacuolar proton-transporting V-type ATPase, V0 domain The V0 domain of a proton-transporting V-type ATPase found in the vacuolar membrane.

3 GO annotations of molecular function

Name Definition
ATPase binding Binding to an ATPase, any enzyme that catalyzes the hydrolysis of ATP.
phosphatidylinositol-3,5-bisphosphate binding Binding to phosphatidylinositol-3,5-bisphosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 3' and 5' positions.
proton-transporting ATPase activity, rotational mechanism Enables the transfer of protons from one side of a membrane to the other according to the reaction: ATP + H2O + H+(in) = ADP + phosphate + H+(out), by a rotational mechanism.

6 GO annotations of biological process

Name Definition
cellular hyperosmotic response Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of detection of, or exposure to, a hyperosmotic environment, i.e. an environment with a higher concentration of solutes than the organism or cell.
cellular response to alkaline pH Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a pH stimulus with pH > 7. pH is a measure of the acidity or basicity of an aqueous solution.
polyphosphate metabolic process The chemical reactions and pathways involving a polyphosphate, the anion or salt of polyphosphoric acid.
protein-containing complex assembly The aggregation, arrangement and bonding together of a set of macromolecules to form a protein-containing complex.
proton transmembrane transport The directed movement of a proton across a membrane.
vacuolar acidification Any process that reduces the pH of the vacuole, measured by the concentration of the hydrogen ion.

16 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
O97681 ATP6V0A2 V-type proton ATPase 116 kDa subunit a 2 Bos taurus (Bovine) PR
Q29466 ATP6V0A1 V-type proton ATPase 116 kDa subunit a 1 Bos taurus (Bovine) PR
Q9I8D0 ATP6V0A1 V-type proton ATPase 116 kDa subunit a 1 Gallus gallus (Chicken) PR
Q9HBG4 ATP6V0A4 V-type proton ATPase 116 kDa subunit a 4 Homo sapiens (Human) PR
Q13488 TCIRG1 V-type proton ATPase 116 kDa subunit a 3 Homo sapiens (Human) PR
Q9Y487 ATP6V0A2 V-type proton ATPase 116 kDa subunit a 2 Homo sapiens (Human) PR
Q93050 ATP6V0A1 V-type proton ATPase 116 kDa subunit a 1 Homo sapiens (Human) PR
Q920R6 Atp6v0a4 V-type proton ATPase 116 kDa subunit a 4 Mus musculus (Mouse) PR
P15920 Atp6v0a2 V-type proton ATPase 116 kDa subunit a 2 Mus musculus (Mouse) PR
Q9Z1G4 Atp6v0a1 V-type proton ATPase 116 kDa subunit a 1 Mus musculus (Mouse) PR
P25286 Atp6v0a1 V-type proton ATPase 116 kDa subunit a 1 Rattus norvegicus (Rat) PR
P30628 unc-32 V-type proton ATPase 116 kDa subunit a 1 Caenorhabditis elegans PR
Q8RWZ7 VHA-a1 V-type proton ATPase subunit a1 Arabidopsis thaliana (Mouse-ear cress) PR
Q9SJT7 VHA-a2 V-type proton ATPase subunit a2 Arabidopsis thaliana (Mouse-ear cress) PR
Q8W4S4 VHA-a3 V-type proton ATPase subunit a3 Arabidopsis thaliana (Mouse-ear cress) PR
A1A5G6 atp6v0a1 V-type proton ATPase 116 kDa subunit a 1 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) PR
10 20 30 40 50 60
MAEKEEAIFR SAEMALVQFY IPQEISRDSA YTLGQLGLVQ FRDLNSKVRA FQRTFVNEIR
70 80 90 100 110 120
RLDNVERQYR YFYSLLKKHD IKLYEGDTDK YLDGSGELYV PPSGSVIDDY VRNASYLEER
130 140 150 160 170 180
LIQMEDATDQ IEVQKNDLEQ YRFILQSGDE FFLKGDNTDS TSYMDEDMID ANGENIAAAI
190 200 210 220 230 240
GASVNYVTGV IARDKVATLE QILWRVLRGN LFFKTVEIEQ PVYDVKTREY KHKNAFIVFS
250 260 270 280 290 300
HGDLIIKRIR KIAESLDANL YDVDSSNEGR SQQLAKVNKN LSDLYTVLKT TSTTLESELY
310 320 330 340 350 360
AIAKELDSWF QDVTREKAIF EILNKSNYDT NRKILIAEGW IPRDELATLQ ARLGEMIARL
370 380 390 400 410 420
GIDVPSIIQV LDTNHTPPTF HRTNKFTAGF QSICDCYGIA QYREINAGLP TIVTFPFMFA
430 440 450 460 470 480
IMFGDMGHGF LMTLAALSLV LNEKKINKMK RGEIFDMAFT GRYIILLMGV FSMYTGFLYN
490 500 510 520 530 540
DIFSKTMTIF KSGWKWPDHW KKGESITATS VGTYPIGLDW AWHGTENALL FSNSYKMKLS
550 560 570 580 590 600
ILMGFIHMTY SYFFSLANHL YFNSMIDIIG NFIPGLLFMQ GIFGYLSVCI VYKWAVDWVK
610 620 630 640 650 660
DGKPAPGLLN MLINMFLSPG TIDDELYPHQ AKVQVFLLLM ALVCIPWLLL VKPLHFKFTH
670 680 690 700 710 720
KKKSHEPLPS TEADASSEDL EAQQLISAMD ADDAEEEEVG SGSHGEDFGD IMIHQVIHTI
730 740 750 760 770 780
EFCLNCVSHT ASYLRLWALS LAHAQLSSVL WTMTIQIAFG FRGFVGVFMT VALFAMWFAL
790 800 810 820 830
TCAVLVLMEG TSAMLHSLRL HWVESMSKFF VGEGLPYEPF AFEYKDMEVA VASASSSASS