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 Q32LT9

Entry ID Method Resolution Chain Position Source
AF-Q32LT9-F1 Predicted AlphaFoldDB

No variants for Q32LT9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q32LT9

No associated diseases with Q32LT9

3 regional properties for Q32LT9

Type Name Position InterPro Accession
domain Phospholipid/glycerol acyltransferase 266 - 397 IPR002123
domain GPAT/DHAPAT, acyltransferase domain 249 - 452 IPR041728
domain GPAT/DHAPAT, C-terminal domain 405 - 768 IPR045520

Functions

Description
EC Number 3.5.1.14 In linear amides
Subcellular Localization
  • Secreted
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
extracellular space That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid.

5 GO annotations of molecular function

Name Definition
aminoacylase activity Catalysis of the reaction: an N-acyl-L-amino acid + H2O = a carboxylate + an L-amino acid.
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides Catalysis of the hydrolysis of any non-peptide carbon-nitrogen bond in a linear amide.
lyase activity Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring.
metal ion binding Binding to a metal ion.
peptidase activity Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid.

11 GO annotations of biological process

Name Definition
adaptive thermogenesis The regulated production of heat in response to short term environmental changes, such as stress, diet or reduced temperature.
amide biosynthetic process The chemical reactions and pathways resulting in the formation of an amide, any derivative of an oxoacid in which an acidic hydroxy group has been replaced by an amino or substituted amino group.
cellular amide catabolic process The chemical reactions and pathways resulting in the breakdown of an amide, any derivative of an oxoacid in which an acidic hydroxy group has been replaced by an amino or substituted amino group.
cellular amino acid metabolic process The chemical reactions and pathways involving amino acids, carboxylic acids containing one or more amino groups, as carried out by individual cells.
cellular lipid metabolic process The chemical reactions and pathways involving lipids, as carried out by individual cells.
energy homeostasis Any process involved in the balance between food intake (energy input) and energy expenditure.
fatty acid metabolic process The chemical reactions and pathways involving fatty acids, aliphatic monocarboxylic acids liberated from naturally occurring fats and oils by hydrolysis.
nitrogen compound metabolic process The chemical reactions and pathways involving organic or inorganic compounds that contain nitrogen.
proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
regulation of oxidative phosphorylation uncoupler activity Any process that modulates the frequency, rate or extent of oxidative phosphorylation uncoupler activity.
respiratory electron transport chain A process in which a series of electron carriers operate together to transfer electrons from donors such as NADH and FADH2 to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKTKFTKKTV LKFFGILFAI LLLSVLILFS VVIGRTFTFK VNRELGQWEN TSTIYPYLSP
70 80 90 100 110 120
EQREKLLDNF KVAVQIPTVS FSESDQNITA LQEFDLLLRR VFPKVFSSSL VRHEVVGNYS
130 140 150 160 170 180
HLFTVVGADA GLEPYMLLAH IDVVPANEAG GWDAPPFSAQ EIDGFIYGRG TIDNKQSVMG
190 200 210 220 230 240
ILQALEYLLE RGYTPRRTFY IGLGHDEEIN GEEGAVKIVN LLKSRGVKLL YVLDEGLTIM
250 260 270 280 290 300
DGVVDGLNEP AALIGVSEKG QTTVKLSVST PPGHSSMPPR ESSIGILASA VARLEKNRMP
310 320 330 340 350 360
NLFGHGPERA TFEHLAHKFG WSYRMIMSNL WLFSSLLSSV LEGQPDTNAF VRTTTAVTMF
370 380 390 400 410 420
NSGVKINVMP AHAEAFVNFR IHSSQTVQGV LNRIESTVSD KRVKVEFING FDPLPIGSYE
430 440 450 460 470 480
DDTFGYQIIK KSVQDIFPQV TVTPGICVAN TDSRHYTQLS PDIYRFAPSW YKPGDSARFH
490 500 510
GVNERISIQN YEEIVLFYFQ LMQNSDVRNL PTLRS