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 B3LJJ8

Entry ID Method Resolution Chain Position Source
AF-B3LJJ8-F1 Predicted AlphaFoldDB

No variants for B3LJJ8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B3LJJ8

No associated diseases with B3LJJ8

2 regional properties for B3LJJ8

Type Name Position InterPro Accession
domain GB1/RHD3-type guanine nucleotide-binding (G) domain 34 - 263 IPR030386
domain Sey1/RHD3-like, three-helix bundle domain 331 - 740 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
MADRSAIQLI DEEKEFHQSA LQYFQQCIGN RDVGLDYHVI SVFGSQSSGK STLLNVLFNT
70 80 90 100 110 120
NFDTMDAQVK RQQTTKGIWL AHTKQVNTTI EIDNDRPDIF VLDVEGSDGS ERGEDQDFER
130 140 150 160 170 180
KAALFAIAVS EVLIVNMWEQ QIGLYQGNNM ALLKTVFEVN LSLFGKNDND HKVLLLFVIR
190 200 210 220 230 240
DHVGVTPLSS LSDSVTRELE KIWTELSKPA GCEGSSLYDY FDLKFVGLAH KLLQEDKFTQ
250 260 270 280 290 300
DVKKLGDSFV MKGTENYYFK PQYHHRLPLD GWTMYAENCW DQIERNKDLD LPTQQILVAR
310 320 330 340 350 360
FKTEEISNEA LEEFISKYDE SIAPLKGNLG SLTSQLVKLK EECLTKYDEQ ASRYARNVYM
370 380 390 400 410 420
EKREALNTNL NSHISGTINE FLESLMEKLW DDLKLEVSSR DKATTSFVES VAAGKSKIEK
430 440 450 460 470 480
EFNESMETFK KLGLLISNEE ITCKFSDDIE ERIKQLRDAE LKAKIGRIKK NLVPELKDHV
490 500 510 520 530 540
IHLLSHPSKK VWDDIMNDFE STIKDNISAY QVEKDKYDFK IGLSESENAK IYKNIRILAW
550 560 570 580 590 600
RTLDTTVHDY LKIDTIVSIL RDRFEDVFRY DAEGSPRLWK TEEEIDGTFR VAKEHALEVF
610 620 630 640 650 660
EVLSLAVTSD NVEIIPDVPM AEEESGEDNE IYRDNEGVFH SRRFAHILTE LQKENVLDQF
670 680 690 700 710 720
RRQINITVLD SKRSIITTRT HIPPWIYVLL AVLGWNEFVA VIRNPLFVTL TLILGATFFV
730 740 750 760 770
IHKFGLWGPV VNVVQSAVGE TRTAIKDKLR QFVVEDHEVK ESFEMKDFSK NEQKEK