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 C4R432

Entry ID Method Resolution Chain Position Source
AF-C4R432-F1 Predicted AlphaFoldDB

No variants for C4R432

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for C4R432

No associated diseases with C4R432

2 regional properties for C4R432

Type Name Position InterPro Accession
domain GB1/RHD3-type guanine nucleotide-binding (G) domain 40 - 266 IPR030386
domain Sey1/RHD3-like, three-helix bundle domain 333 - 748 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
MTDLEVSAIQ VIDENKVFNS LLVDYMKQFY SQNNSSDDKG LNYHIVSVFG SQSTGKSTLL
70 80 90 100 110 120
NHLFHTKFDV MDESQRQQTT KGIWLAHANH ISSSNESGDF ANNTKNVFVM DVEGTDGRER
130 140 150 160 170 180
GEDQDFERKA ALFALSTSEI LIINIWEHQV GLYQGANLGL LRTVFEVNLS LFAKNKQRCL
190 200 210 220 230 240
LLFVIRDHVG NTSLESLSDV LTLDLQNIWS QLNKPQGTEG FELDDFFDLK FVALAHKLLQ
250 260 270 280 290 300
PDKFIEDISV LGDKFISEDQ LFNEGYHRAI PIDGWSMYAE QVWEQIETNQ DLDLPTQQIL
310 320 330 340 350 360
VARFRCDEIS SQVYESFHEQ FVKSNWDDLS FTEIGNSLKE LRQNAVQQYD ILAGRYSESV
370 380 390 400 410 420
YLQRKKLLVQ KVDLSILEVY TSVLQKLIRQ SRDLYLKQIE SSLTKKEAGI IFYQVLDNAE
430 440 450 460 470 480
RESLKYFNEN TSLISFVDVD DSEARSYDPS PKLRELEEEL SNLRTELVNK EQENIKTKIP
490 500 510 520 530 540
RKFKSHFKLI VQDELSNIKP SSWEELLDQF RQVSEKLLAK YKSPDSNYDF HLGLSKEKNK
550 560 570 580 590 600
ELHEQVLIKF WIKFKEILND FVTETNVLRL LVSKFEDEFR YDEEGLPVVW KNSAEIDVKF
610 620 630 640 650 660
AKARNSALDL LPLFSLAHTA EGEILPDYDI AHDEAEAESD NEEDDGFKES HKFAHLLSAR
670 680 690 700 710 720
DQDAIRNKFK KQTDALYVET KRSVINSKTE VPLYIYALLL VLGWNEFMII LRNPLLITLL
730 740 750 760 770 780
LIGLTGLYLG YKTKLLGPIV QVVQAMIQEL QDQAKNKLRD VLVSEPEAPS QVRIGKEVDA
TKDED