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 A2EI35

Entry ID Method Resolution Chain Position Source
AF-A2EI35-F1 Predicted AlphaFoldDB

No variants for A2EI35

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A2EI35

No associated diseases with A2EI35

3 regional properties for A2EI35

Type Name Position InterPro Accession
domain GB1/RHD3-type guanine nucleotide-binding (G) domain 28 - 245 IPR030386
domain Sey1/RHD3-like, three-helix bundle domain 314 - 596 IPR046758-1
domain Sey1/RHD3-like, three-helix bundle domain 599 - 691 IPR046758-2

Functions

Description
EC Number
Subcellular Localization
  • Endoplasmic reticulum membrane ; Multi-pass membrane protein
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.

No GO annotations of biological process

Name Definition
No GO annotations for biological process

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MEQIITGEGQ IVPDLDEHIT RSGIDQAGTD YHMVSIIGCQ SSGKSTLLNL LFGTKFETMN
70 80 90 100 110 120
EQKGRQQTTK GIHAARAVNG PILLFDVEGS DSRERGDSDA LFERKSSLFA LALSELLVIN
130 140 150 160 170 180
MWESDIGRYN AANIPMLKTV MEVNVQLFLA QSTSKSKILF VIRDSTIPNF DVIKFQINRD
190 200 210 220 230 240
MENIWAEITL PDSLKDKTIH DFFDFDFYAI HHMVIQRDIF DKDISALRQR FIDEKEENYL
250 260 270 280 290 300
FKEKSTKVVP GGGLSTYIRN LWEVINENKE LNIPSQKLML SRFKCEENAK AAYDQFKEKV
310 320 330 340 350 360
TKTILEPMAD ESVNLGDKFK SNAEEAIKAA NKFYHDNSWR YQQAAVEEFQ QKLSTDIGDL
370 380 390 400 410 420
LISYYIKHCN YYARQVMQEF TKFISGLPDS FEKGGKWAIE VQAKIDELSL RLDSTCRDSL
430 440 450 460 470 480
IEGYKWQFPS FKTIKAMDDA RKSYEEIMTK KLYKNIFAEE KIAFDDKASE LLMIADQNMW
490 500 510 520 530 540
ENLRKLIEAS AKVTDDRFME IIKTNVLNPK PQEGTLKRFQ RHALNIVKES ANYIMMKMKT
550 560 570 580 590 600
AFDRSFRYEK NGRPRVWTRR HNLNQIYEES RASGRKVLIL FTYCRLASPD DQTPNNPLNQ
610 620 630 640 650 660
VLIPVEKSQE IEEKFEKLII HAYEEARASV LASQNNEHIP PWAWFLFLFS CSDYILWWLS
670 680 690 700 710 720
NPLLFSLTVL FGGTYLVLNQ LGLWDTAVQK LLDIIKKKIV ELGATPDENN ETETNQTIPV
730 740 750 760 770 780
EESQITPPPP TETTTDDGPV MKRRVHRSKA QGLTKTESNV TFANVSNAND EQSLTKNNTE
790 800
DSLNTGSSSS GQRHRKRVRV GTLV