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 P32476

Entry ID Method Resolution Chain Position Source
AF-P32476-F1 Predicted AlphaFoldDB

7 variants for P32476

Variant ID(s) Position Change Description Diseaes Association Provenance
s07-847926 168 T>I No SGRP
s07-847759 224 V>F No SGRP
s07-847732 233 G>C No SGRP
251 L>F strain: A2-M8; confers resistance to the allylamine antifungal terbinafine [UniProt] No
s07-847635 265 P>R No SGRP
s07-847354 359 I>V No SGRP
s07-847307 374 L>F No SGRP

No associated diseases with P32476

1 regional properties for P32476

Type Name Position InterPro Accession
conserved_site SsrA-binding protein, conserved site 30 - 42 IPR020081

Functions

Description
EC Number
Subcellular Localization
  • Microsome membrane ; Multi-pass membrane protein
  • Endoplasmic reticulum membrane ; Multi-pass membrane protein
  • Lipid droplet
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
endoplasmic reticulum The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
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.
lipid droplet An intracellular non-membrane-bounded organelle comprising a matrix of coalesced lipids surrounded by a phospholipid monolayer. May include associated proteins.

2 GO annotations of molecular function

Name Definition
flavin adenine dinucleotide binding Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.
squalene monooxygenase activity Catalysis of the reaction: H(+) + NADPH + O(2) + squalene = (S)-2,3-epoxysqualene + H(2)O + NADP(+).

2 GO annotations of biological process

Name Definition
ergosterol biosynthetic process The chemical reactions and pathways resulting in the formation of ergosterol, (22E)-ergosta-5,7,22-trien-3-beta-ol, a sterol found in ergot, yeast and moulds.
sterol biosynthetic process The chemical reactions and pathways resulting in the formation of sterols, steroids with one or more hydroxyl groups and a hydrocarbon side-chain in the molecule.

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q14534 SQLE Squalene monooxygenase Homo sapiens (Human) PR
P52019 Sqle Squalene monooxygenase Mus musculus (Mouse) PR
P52020 Sqle Squalene monooxygenase Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MSAVNVAPEL INADNTITYD AIVIGAGVIG PCVATGLARK GKKVLIVERD WAMPDRIVGE
70 80 90 100 110 120
LMQPGGVRAL RSLGMIQSIN NIEAYPVTGY TVFFNGEQVD IPYPYKADIP KVEKLKDLVK
130 140 150 160 170 180
DGNDKVLEDS TIHIKDYEDD ERERGVAFVH GRFLNNLRNI TAQEPNVTRV QGNCIEILKD
190 200 210 220 230 240
EKNEVVGAKV DIDGRGKVEF KAHLTFICDG IFSRFRKELH PDHVPTVGSS FVGMSLFNAK
250 260 270 280 290 300
NPAPMHGHVI LGSDHMPILV YQISPEETRI LCAYNSPKVP ADIKSWMIKD VQPFIPKSLR
310 320 330 340 350 360
PSFDEAVSQG KFRAMPNSYL PARQNDVTGM CVIGDALNMR HPLTGGGMTV GLHDVVLLIK
370 380 390 400 410 420
KIGDLDFSDR EKVLDELLDY HFERKSYDSV INVLSVALYS LFAADSDNLK ALQKGCFKYF
430 440 450 460 470 480
QRGGDCVNKP VEFLSGVLPK PLQLTRVFFA VAFYTIYLNM EERGFLGLPM ALLEGIMILI
490
TAIRVFTPFL FGELIG