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

3 structures for Q02725

Entry ID Method Resolution Chain Position Source
7YTJ EM 300 A E 1-835 PDB
8I6V EM 306 A D 1-835 PDB
AF-Q02725-F1 Predicted AlphaFoldDB

22 variants for Q02725

Variant ID(s) Position Change Description Diseaes Association Provenance
s16-516980 13 P>S No SGRP
s16-516901 39 S>N No SGRP
s16-516887 44 W>G No SGRP
s16-516778 80 D>G No SGRP
s16-516677 114 D>N No SGRP
s16-516310 236 V>A No SGRP
s16-516281 246 N>Y No SGRP
s16-516275 248 E>K No SGRP
s16-516256 254 Q>L No SGRP
s16-516189 276 Q>H No SGRP
s16-516170 283 S>T No SGRP
s16-515835 394 E>D No SGRP
s16-515714 435 I>V No SGRP
s16-515533 495 K>R No SGRP
s16-515509 503 Q>R No SGRP
s16-515493 508 E>D No SGRP
s16-515219 600 E>K No SGRP
s16-515194 608 N>S No SGRP
s16-515183 612 V>I No SGRP
s16-514988 677 P>S No SGRP
s16-514728 763 L>F No SGRP
s16-514726 764 T>I No SGRP

No associated diseases with Q02725

3 regional properties for Q02725

Type Name Position InterPro Accession
domain Domain of unknown function DUF202 698 - 763 IPR003807
domain SPX domain 1 - 145 IPR004331
domain VTC domain 205 - 536 IPR018966

Functions

Description
EC Number
Subcellular Localization
  • Vacuole membrane ; Multi-pass membrane protein
  • Cytoplasm, cell cortex
  • Endoplasmic reticulum membrane ; Multi-pass membrane protein
  • Cytoplasmic vesicle, autophagosome 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
autophagosome membrane The lipid bilayer surrounding an autophagosome, a double-membrane-bounded vesicle in which endogenous cellular material is sequestered.
endoplasmic reticulum The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
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 transporter chaperone complex A protein complex that contains four related proteins that have been implicated in several membrane-related processes, such as sorting of H+-translocating ATPases, endocytosis, ER-Golgi trafficking, vacuole fusion, vacuolar polyphosphate homeostasis and the microautophagic scission of vesicles into the vacuolar lumen. The complex is enriched at the vacuolar membrane, but also found in other cellular compartments, including the ER and the cell periphery. In Saccharomyces, the subunits are Vtc1p, Vtc2p, Vtc3p and Vtc4p.

2 GO annotations of molecular function

Name Definition
calmodulin binding Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states.
inositol hexakisphosphate binding Binding to inositol hexakisphosphate.

7 GO annotations of biological process

Name Definition
engulfment of target by autophagosome The membrane invagination process by which an autophagosomal membrane surrounds an object that will be degraded by macroautophagy.
inositol phosphate-mediated signaling A intracellular signal transduction in which the signal is transmitted within the cell via an inositol phosphate. Includes production of the inositol phosphate, and downstream effectors that further transmit the signal within the cell. Inositol phosphates are a group of mono- to poly-phosphorylated inositols, and include inositol monophosphate (IP), inositol trisphosphate (IP3), inositol pentakisphosphate (IP5) and inositol hexaphosphate (IP6).
lysosomal microautophagy The transfer of cytosolic components into the lysosomal compartment by direct invagination of the lysosomal membrane without prior sequestration into an autophagosome. The engulfing membranes fuse, resulting in the lysosomal delivery of the cargo wrapped in a single membrane derived from the invaginated lysosomal membrane. In S. cerevisiae, the vacuole is the lysosomal compartment.
polyphosphate biosynthetic process The chemical reactions and pathways resulting in the formation of a polyphosphate, the anion or salt of polyphosphoric acid.
polyphosphate metabolic process The chemical reactions and pathways involving a polyphosphate, the anion or salt of polyphosphoric acid.
vacuolar transport The directed movement of substances into, out of or within a vacuole.
vacuole fusion, non-autophagic The fusion of two vacuole membranes to form a single vacuole.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MLFGIKLAND VYPPWKDSYI DYERLKKLLK ESVIHDGRSS VDSWSERNES DFVEALDKEL
70 80 90 100 110 120
EKVYTFQISK YNAVLRKLDD LEENTKSAEK IQKINSEQFK NTLEECLDEA QRLDNFDRLN
130 140 150 160 170 180
FTGFIKIVKK HDKLHPNYPS VKSLLQVRLK ELPFNNSEEY SPLLYRISYL YEFLRSNYDH
190 200 210 220 230 240
PNTVSKSLAS TSKLSHFSNL EDASFKSYKF WVHDDNIMEV KARILRHLPA LVYASVPNEN
250 260 270 280 290 300
DDFVDNLESD VRVQPEARLN IGSKSNSLSS DGNSNQDVEI GKSKSVIFPQ SYDPTITTLY
310 320 330 340 350 360
FDNDFFDLYN NRLLKISGAP TLRLRWIGKL LDKPDIFLEK RTFTENTETG NSSFEEIRLQ
370 380 390 400 410 420
MKAKFINNFI FKNDPSYKNY LINQLRERGT QKEELEKLSR DFDNIQNFIV EEKLQPVLRA
430 440 450 460 470 480
TYNRTAFQIP GDQSIRVTID SNIMYIREDS LDKNRPIRNP ENWHRDDIDS NIPNPLRFLR
490 500 510 520 530 540
AGEYSKFPYS VMEIKVINQD NSQMPNYEWI KDLTNSHLVN EVPKFSLYLQ GVASLFGEDD
550 560 570 580 590 600
KYVNILPFWL PDLETDIRKN PQEAYEEEKK TLQKQKSIHD KLDNMRRLSK ISVPDGKTTE
610 620 630 640 650 660
RQGQKDQNTR HVIADLEDHE SSDEEGTALP KKSAVKKGKK FKTNAAFLKI LAGKNISENG
670 680 690 700 710 720
NDPYSDDTDS ASSFQLPPGV KKPVHLLKNA GPVKVEAKVW LANERTFNRW LSVTTLLSVL
730 740 750 760 770 780
TFSIYNSVQK AEFPQLADLL AYVYFFLTLF CGVWAYRTYL KRLTLIKGRS GKHLDAPVGP
790 800 810 820 830
ILVAVVLIVT LVVNFSVAFK EAARRERGLV NVSSQPSLPR TLKPIQDFIF NLVGE