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 P53154

Entry ID Method Resolution Chain Position Source
AF-P53154-F1 Predicted AlphaFoldDB

6 variants for P53154

Variant ID(s) Position Change Description Diseaes Association Provenance
s07-352271 11 I>V No SGRP
s07-351952 117 R>H No SGRP
s07-351514 263 A>G No SGRP
s07-351290 338 H>Y No SGRP
s07-350710 531 I>S No SGRP
s07-350699 535 V>I No SGRP

No associated diseases with P53154

No regional properties for P53154

Type Name Position InterPro Accession
No domain, repeats, and functional sites for P53154

Functions

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

5 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.
mitochondrial membrane Either of the lipid bilayers that surround the mitochondrion and form the mitochondrial envelope.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

2 GO annotations of molecular function

Name Definition
acyltransferase activity Catalysis of the transfer of an acyl group from one compound (donor) to another (acceptor).
O-acyltransferase activity Catalysis of the transfer of an acyl group to an oxygen atom on the acceptor molecule.

3 GO annotations of biological process

Name Definition
glycerol catabolic process The chemical reactions and pathways resulting in the breakdown of glycerol, 1,2,3-propanetriol, a sweet, hygroscopic, viscous liquid, widely distributed in nature as a constituent of many lipids.
glycerol transmembrane transport The directed movement of glycerol across a membrane. Glycerol is 1,2,3-propanetriol, a sweet, hygroscopic, viscous liquid, widely distributed in nature as a constituent of many lipids.
GPI anchor biosynthetic process The chemical reactions and pathways resulting in the formation of a glycosylphosphatidylinositol (GPI) anchor that attaches some membrane proteins to the lipid bilayer of the cell membrane. The phosphatidylinositol group is linked via the C-6 hydroxyl residue of inositol to a carbohydrate chain which is itself linked to the protein via an ethanolamine phosphate group, its amino group forming an amide linkage with the C-terminal carboxyl of the protein. Some GPI anchors have variants on this canonical linkage.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q08929 GUP2 Membrane-bound O-acyltransferase GUP2 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
Q9HCP6 HHATL Protein-cysteine N-palmitoyltransferase HHAT-like protein Homo sapiens (Human) PR
10 20 30 40 50 60
MSLISILSPL ITSEGLDSRI KPSPKKDAST TTKPSLWKTT EFKFYYIAFL VVVPLMFYAG
70 80 90 100 110 120
LQASSPENPN YARYERLLSQ GWLFGRKVDN SDSQYRFFRD NFALLSVLML VHTSIKRIVL
130 140 150 160 170 180
YSTNITKLRF DLIFGLIFLV AAHGVNSIRI LAHMLILYAI AHVLKNFRRI ATISIWIYGI
190 200 210 220 230 240
STLFINDNFR AYPFGNICSF LSPLDHWYRG IIPRWDVFFN FTLLRVLSYN LDFLERWENL
250 260 270 280 290 300
QKKKSPSYES KEAKSAILLN ERARLTAAHP IQDYSLMNYI AYVTYTPLFI AGPIITFNDY
310 320 330 340 350 360
VYQSKHTLPS INFKFIFYYA VRFVIALLSM EFILHFLHVV AISKTKAWEN DTPFQISMIG
370 380 390 400 410 420
LFNLNIIWLK LLIPWRLFRL WALLDGIDTP ENMIRCVDNN YSSLAFWRAW HRSYNKWVVR
430 440 450 460 470 480
YIYIPLGGSK NRVLTSLAVF SFVAIWHDIE LKLLLWGWLI VLFLLPEIFA TQIFSHYTDA
490 500 510 520 530 540
VWYRHVCAVG AVFNIWVMMI ANLFGFCLGS DGTKKLLSDM FCTVSGFKFV ILASVSLFIA
550
VQIMFEIREE EKRHGIYLKC