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 Q2GUT7

Entry ID Method Resolution Chain Position Source
AF-Q2GUT7-F1 Predicted AlphaFoldDB

No variants for Q2GUT7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q2GUT7

No associated diseases with Q2GUT7

2 regional properties for Q2GUT7

Type Name Position InterPro Accession
domain GB1/RHD3-type guanine nucleotide-binding (G) domain 47 - 283 IPR030386
domain Sey1/RHD3-like, three-helix bundle domain 359 - 797 IPR046758

Functions

Description
EC Number
Subcellular Localization
  • Endoplasmic reticulum membrane ; Multi-pass membrane protein
  • Enriched in the cortical ER
  • Concentrated in punctae along the ER tubules
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
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.

2 GO annotations of molecular function

Name Definition
GTP binding Binding to GTP, guanosine triphosphate.
GTPase activity Catalysis of the reaction: GTP + H2O = GDP + H+ + phosphate.

1 GO annotations of biological process

Name Definition
endoplasmic reticulum organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the endoplasmic reticulum.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MNGHFAAVGN GPTAQQYEHG IQVIDEDKAF NTNLNDYLGE TRVAEAGFNY HLISVFGSQS
70 80 90 100 110 120
TGKSTLLNHL FKTEFSVMSE SARRQTTKGI WMSKNKRAGA NGDAATMADN ILVMDVEGTD
130 140 150 160 170 180
GRERGEDQDF ERKSALFALA TSEVLIVNIW EHQIGLYQGA NMGLLKTVFE VNLQLFLKDR
190 200 210 220 230 240
QSQTRSLLFF VIRDHVGNTP LANLRDTLVQ DLTKIWSTLS KPQGLEDSKI EDYFDFAFAA
250 260 270 280 290 300
LPHKILQPEK FLEEADKLST RFTTGHRSAK DQEFVGGVFL PEYHRRIPAD GLSVYAEGVW
310 320 330 340 350 360
DQIVNNKDLD LPTQQELLAQ FRCDEISREV FVGFDSVIVP LEEQQAEATR LGKATVLPDL
370 380 390 400 410 420
GVTGAGTREK CVKAFETQAS RYHKGVYSVK RGELESKIDA RLKALYQTQL SAAHKSGVAA
430 440 450 460 470 480
FSDAVTNAVK AGQKAGGYEF AEIVDKQKKK TLEFFKKEAQ SLLIQGVAWT NFKPQYRLFE
490 500 510 520 530 540
KELDEVSARL RKEEMRRLAI RVERWVKSRL GDSIGVEFNK LGSGRGGSGA PENGEKPATE
550 560 570 580 590 600
KDLWDRIWNT FSGIIREAET RFADRAKSFE ASPEEVEVGL WRLRRKSWVA LREKIEEEMM
610 620 630 640 650 660
ESNILMKLRE NFEDKFRYDE EGVPRIWRPT DDIEGIYTRA RESTLGLIPL LARFRLAETY
670 680 690 700 710 720
APPDLPTFVG PQPAGAEPED EEDLAPIGGV DEEEGKSLEE EMTVLSESKR QDLVVRFKKM
730 740 750 760 770 780
ADGVYVEAKR SAIGGITQVP LYFYIVLLIF GWNEIVMVLR NPMLFMLLLV MGGGTYVAYT
790 800 810 820 830 840
LNLLGPMMQM ANAASNQAVE IGKEKLRDFL ENNQTMRQAI AMPPRSQDNG IGMDRLDSRG
850
KKAQEVEEDD DI