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 Q5R6L8

Entry ID Method Resolution Chain Position Source
AF-Q5R6L8-F1 Predicted AlphaFoldDB

No variants for Q5R6L8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5R6L8

No associated diseases with Q5R6L8

1 regional properties for Q5R6L8

Type Name Position InterPro Accession
domain PI4-kinase, N-terminal 1 - 167 IPR045495

Functions

Description
EC Number
Subcellular Localization
  • Endoplasmic reticulum membrane ; Single-pass type I membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
GPI-anchor transamidase complex An enzyme complex which in humans and yeast consists of at least five proteins; for example, the complex contains GAA1, GPI8, PIG-S, PIG-U, and PIG-T in human, and Gaa1p, Gab1p, Gpi8p, Gpi16p, and Gpi17p in yeast. Catalyzes the posttranslational attachment of the carboxy-terminus of a precursor protein to a GPI-anchor.

1 GO annotations of molecular function

Name Definition
GPI-anchor transamidase activity Catalysis of the formation of the linkage between a protein and a glycosylphosphatidylinositol anchor. The reaction probably occurs by subjecting a peptide bond to nucleophilic attack by the amino group of ethanolamine-GPI, transferring the protein from a signal peptide to the GPI anchor.

2 GO annotations of biological process

Name Definition
attachment of GPI anchor to protein A transamidation reaction that results in the cleavage of the polypeptide chain and the concomitant transfer of the GPI anchor to the newly formed carboxy-terminal amino acid of the anchored protein. The cleaved C-terminal contains the C-terminal GPI signal sequence of the newly synthesized polypeptide chain.
proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAVTDSLSRA ASTLAAVLLL SFGSVAASHI EDQAEQFFRS GHTNNWAVLV CTSRFWFNYR
70 80 90 100 110 120
HVANTLSVYR SVKRLGIPDS HIVLMLADDM ACNPRNPKPA TVFSHKNMEL NVYGDDVEVD
130 140 150 160 170 180
YRSYEVTVEN FLRVLTGRIP PSTPRSKRLL SDDRSNILIY MTGHGGNGFL KFQDSEEITN
190 200 210 220 230 240
IELADAFEQM WQKRRYNELL FIIDTCQGAS MYERFYSPNI MALASSQVGE DSLSHQPDPA
250 260 270 280 290 300
IGVHLMDRYT FYVLEFLEEI NPASQTNMND LFQVCPKSLC VSTPGHRTDL FQRDPKNVLI
310 320 330 340 350 360
TDFFGSVRKV EITTETIKLQ QDSEIMESSY KEDQMDEELM EPLKYAEQLP VAQIIHQKPK
370 380 390
LKDWHPPGGF ILGLWALIIM VFFKTYGIKH MKFIF