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 C5FJT2

Entry ID Method Resolution Chain Position Source
AF-C5FJT2-F1 Predicted AlphaFoldDB

No variants for C5FJT2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for C5FJT2

No associated diseases with C5FJT2

2 regional properties for C5FJT2

Type Name Position InterPro Accession
domain GB1/RHD3-type guanine nucleotide-binding (G) domain 48 - 301 IPR030386
domain Sey1/RHD3-like, three-helix bundle domain 364 - 802 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
MASNGHFSSV GDVDGGNYQH GVQVVDGDKE FNPNLSKYLA HENVTPAGFN YHLISVFGSQ
70 80 90 100 110 120
STGKSTLLNT LFKTDFSVMS ETERRQTTKG IWLSKNKRTA SNEKEKMADN VLVMDVEGTD
130 140 150 160 170 180
GRERGEDQDF ERKSALFALA TSEVLIVNIW EHQVGLYQGA NMGLLKTVFE VNLQLFLKDT
190 200 210 220 230 240
KSTPRSLLFF VIRDFVGTTP LENLRNTLMQ DLQRIWMSLS KPEGTENSTI EDYFDFEFAG
250 260 270 280 290 300
LPHKSFQPEK FASEVDKLST RFRDGHRDPS STSAKGTAVE GGVFLPEYHR RIPADGFAVY
310 320 330 340 350 360
AEGIWDQIVN NKDLDLPTQQ ELLAQFRCDE IAREVLILFD ETIGPFEVQQ AEGVRSGIPL
370 380 390 400 410 420
ILGSLGVAMR AARGKTMTSF ETEASRYHKR VFMTKKSELE EKIDTRLKAL FSGQLSAAHK
430 440 450 460 470 480
SGVTQFSEAV SAAVKAGQKK GASYDFAEIV TRERKLAIEK FENEASTTMV EGAPWSDYKQ
490 500 510 520 530 540
ELSLFQKDLE KISSQLRKDE MRRLATRVER WVRSRLGDSI DLEFNALGSG RGGSRAPENG
550 560 570 580 590 600
DKPSEKTIWD RIWSLFVNTV LDAERRFTER ARSFDASLEE VDVGLWRLRR KSWGVLRSKI
610 620 630 640 650 660
EEEMMEGNIL HKLRENFEDK FRYDDVGVPR IWRPTDDIEG IYTTARESTL SLIPLLARFR
670 680 690 700 710 720
LNETSAPPPL DKWVGHMPSS ASAADEEDLA PIGGVDEDDG KSLEEEMTML SEAKRQDLTV
730 740 750 760 770 780
RFKKAADGVY VEAKRSAIGG ITQVPLYFYG LLLALGWNEI IAVLRNPIYF IFLLLIGVGA
790 800 810 820 830 840
YVTFRLNLWG PMINMAEAAS RQAVEEGKRR LREFLESSDS GRQAMAMSGR NARGTEEYEM
850 860
SSNLKSKGRR TDTSDDDNDD DL