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 B6GX67

Entry ID Method Resolution Chain Position Source
AF-B6GX67-F1 Predicted AlphaFoldDB

No variants for B6GX67

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B6GX67

No associated diseases with B6GX67

2 regional properties for B6GX67

Type Name Position InterPro Accession
domain GB1/RHD3-type guanine nucleotide-binding (G) domain 66 - 320 IPR030386
domain Sey1/RHD3-like, three-helix bundle domain 383 - 821 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
MAERRPSGLE RSPTAPPVLS NGHFASIGAE GDASSYEHGV QVIDENKEFN PDLSKYLSLE
70 80 90 100 110 120
NVTPAGFNYH LISVFGSQST GKSTLLNHLF GTQFSVMSEL ERRQTTKGIW LSNNKKQGDA
130 140 150 160 170 180
GSAERMADNI LVMDVEGTDG RERGEDQDFE RKSALFALAT SEVLIVNIWE HQVGLYQGAN
190 200 210 220 230 240
MGLLKTVFEV NLQLFLKDKH TTHRSLLFFV IRDFIGTTPL KNLQKTLLED LSRLWDTISK
250 260 270 280 290 300
PAGLEKSTIH DYFDFQFYGL PHKGYQPDQF VTEANKLGLR FREGHRDPKR DALKGEFSEG
310 320 330 340 350 360
GVFLPEYHRR IPADGFSHYA EGIWDQIVNN KDLDLPTQQE LLAQFRCDEI LREVMIGFDE
370 380 390 400 410 420
AITAFEDKQA ESVRVGAPEV LGGLGVAMRA ARVKTLKSFE TEASRYHKGV YQRKSAELQG
430 440 450 460 470 480
KVDTRLKALF HGQLSAAHKS GIRDFSDSVS AAVKDGQKKG GSYDFAEIVA KETQSSLEKF
490 500 510 520 530 540
EEVAHSTLVD GASWSNCTQE LSLFKKELAE VSARLRRDEM RRLATRVERW VQSRLGESVG
550 560 570 580 590 600
LEFNALGSGR AGGGAPENGE KPTEKDFWDR IWNLFEETVL DAERRFTDRA SSFDASIDEV
610 620 630 640 650 660
DVGLWRLRRK SWGVLRAKIE EEMIEGNLLL KLRENFEDKF RYDEAGVPRI WRPTDDIEGI
670 680 690 700 710 720
YTRARESTLT VIPLLSRFRL ERTTAPPPLD RWIGHTPSTA TPADEEDLAP IGGVDEHEGK
730 740 750 760 770 780
SLEEEMTILS DAKRQELTVR FKKAADGVYV EAKRSAIGGM TQVPLYFYGL LLALGWNEIW
790 800 810 820 830 840
AVLRNPAYFI LLFAFAIGAY ITYQLNLWGP MLKMTEAASQ QALEEGKRRL REFLESSDTG
850 860 870
RQAIAMSAGE RAGSSGRKEE YEMSDMQKRA SNANDDLDDM