Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for P43562

Entry ID Method Resolution Chain Position Source
AF-P43562-F1 Predicted AlphaFoldDB

9 variants for P43562

Variant ID(s) Position Change Description Diseaes Association Provenance
s06-51479 44 P>S No SGRP
s06-51603 85 C>Y No SGRP
s06-51925 192 I>M No SGRP
s06-52024 225 E>D No SGRP
s06-52550 401 I>V No SGRP
s06-52716 456 T>K No SGRP
s06-52770 474 W>L No SGRP
s06-52838 497 G>S No SGRP
s06-52925 526 L>V No SGRP

No associated diseases with P43562

2 regional properties for P43562

Type Name Position InterPro Accession
conserved_site Sugar transporter, conserved site 127 - 152 IPR005829
domain Major facilitator superfamily domain 28 - 479 IPR020846

Functions

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

4 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.
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.
prospore membrane The prospore membrane is a double-membraned structure that extends from the cytoplasmic face of the spindle pole bodies to encompass the spindle pole bodies and the four nuclear lobes that are formed during meiosis. It helps isolate the meiotic nuclei from the cytoplasm during spore formation and serves as a foundation for the formation of the spore walls. An example of this component is found in Schizosaccharomyces pombe.

2 GO annotations of molecular function

Name Definition
myo-inositol:proton symporter activity Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: myo-inositol(out) + H+(out) = myo-inositol(in) + H+(in).
transmembrane transporter activity Enables the transfer of a substance, usually a specific substance or a group of related substances, from one side of a membrane to the other.

2 GO annotations of biological process

Name Definition
myo-inositol import across plasma membrane The directed movement of myo-inositol from outside of a cell, across the plasma membrane and into the cytosol.
transmembrane transport The process in which a solute is transported across a lipid bilayer, from one side of a membrane to the other.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P30605 ITR1 Myo-inositol transporter 1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
P30606 ITR2 Myo-inositol transporter 2 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
10 20 30 40 50 60
MTAMKAIVWR LPKMPKIKIT KTYEVTKITA ILTLVGFIMG LEVPSLATFL TNKTFNEYFK
70 80 90 100 110 120
YPTPLQQGLL MGSTPLGGIM GCFICCIMND RFSRIYQFQS GIIIWNIVTL LNFCIWDILG
130 140 150 160 170 180
LLICRMIKGM ILGNFSILVA SYANEVIPRG KRGSTMSYIQ LCLTIGILVM HYLCIALSLW
190 200 210 220 230 240
DSHFAFRIAW CIGIIPGLLF WMASYALPES YHWLVLHGKM SEAQEIQHNL AKKFNESQPR
250 260 270 280 290 300
DAVPEMSKIE LAGDFWIGVN DLDFSKKLPR GSFKPLILGM TLQLLVQFSG INIILGYITY
310 320 330 340 350 360
ICEIVGLEGN VKLFTSSIPY FINMVLSLLP ITFIDYTSRK LITLLGGFPI SGLLITIGAL
370 380 390 400 410 420
FVKYGQDTKP IDGNRSLVWS IGENPFVGGW ILTLCFLIVG IFAMSLSSIP WVYTNEMLPS
430 440 450 460 470 480
RVKVKGFAIC VTFGWLGNFI LTFLCPVMIE RLKGTTFIIF GSLTFLISLS VLIWFPETKG
490 500 510 520 530
MSIEDIDKFF EFESKEGTNL HGEKGIKTPD SNSNGGSTRS SQEGQLHKPI KLKSDEEMII