Sigmar1
entrez
18391
canonical
uniprot
O55242
canonical
ensembl
ENSMUSG00000036078
resolver
ensp
ENSMUSP00000056027
resolver
ensp
ENSMUSP00000071492
resolver
ensp
ENSMUSP00000254526
resolver
ensp
ENSMUSP00000254527
resolver
ensp
ENSMUSP00000254530
resolver
ensp
ENSMUSP00000347886
resolver
ensp
ENSMUSP00000364958
resolver
genesymbol
Sigmar1
resolver
genesymbol_syn
Oprs1
resolver
uniprot
A2AMS0
resolver
uniprot
B7ZJH6
resolver
uniprot
B7ZJH7
resolver
uniprot
B7ZJH8
resolver
uniprot
B7ZJH9
resolver
uniprot
I4DCY6
resolver
uniprot
Q9JKU9
resolver
uniprot_entry
I4DCY6_MOUSE
resolver
uniprot_entry
SGMR1_MOUSE
resolver
uniprot_sec
A2AMS0
resolver
uniprot_sec
B7ZJH6
resolver
uniprot_sec
B7ZJH7
resolver
uniprot_sec
B7ZJH8
resolver
uniprot_sec
B7ZJH9
resolver
uniprot_sec
Q9JKU9
resolver
amino_acid_sequence
MPWAAGRRWAWITLILTIIAVLIQAAWLWLGTQNFVFSREEIAQLARQYAGLDHELAFSRLIVELRRLHPGHVLPDEELQWVFVNAGGWMGAMCILHASLSEYVLLFGTALGSHGHSGRYWAEISDTIISGTFHQWKEGTTKSEVFYPGETVVHGPGEATALEWGPNTWMVEYGRGVIPSTLFFALADTFFSTQDYLTLFYTLRAYARGLRLELTTYLFGQDS
uniprot
proteins
function
FUNCTION: Functions in lipid transport from the endoplasmic reticulum and is involved in a wide array of cellular functions probably through regulation of the biogenesis of lipid microdomains at the plasma membrane (PubMed:12730355). Involved in the regulation of different receptors it plays a role in BDNF signaling and EGF signaling. Also regulates ion channels like the potassium channel and could modulate neurotransmitter release. Plays a role in calcium signaling through modulation together with ANK2 of the ITP3R-dependent calcium efflux at the endoplasmic reticulum. Plays a role in several other cell functions including proliferation, survival and death. Originally identified for its ability to bind various psychoactive drugs it is involved in learning processes, memory and mood alteration (PubMed:11149946, PubMed:14622179, PubMed:15571673, PubMed:15777781, PubMed:23332758, PubMed:9425306, PubMed:9603192). Necessary for proper mitochondrial axonal transport in motor neurons, in particular the retrograde movement of mitochondria (PubMed:25678561). Plays a role in protecting cells against oxidative stress-induced cell death via its interaction with RNF112 (PubMed:26792191). {ECO:0000269|PubMed:11149946, ECO:0000269|PubMed:12730355, ECO:0000269|PubMed:14622179, ECO:0000269|PubMed:15571673, ECO:0000269|PubMed:15777781, ECO:0000269|PubMed:23332758, ECO:0000269|PubMed:25678561, ECO:0000269|PubMed:26792191, ECO:0000269|PubMed:9425306, ECO:0000269|PubMed:9603192}.
uniprot
proteins
mass_dalton
25250
uniprot
proteins
protein_family
ERG2 family
uniprot
proteins
pubmed
11149946
uniprot
proteins
pubmed
11207432
uniprot
proteins
pubmed
11476895
uniprot
proteins
pubmed
11687279
uniprot
proteins
pubmed
12730355
uniprot
proteins
pubmed
14622179
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15571673
uniprot
proteins
pubmed
15777781
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
20167253
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23332758
uniprot
proteins
pubmed
25678561
uniprot
proteins
pubmed
26792191
uniprot
proteins
pubmed
28350844
uniprot
proteins
pubmed
9425306
uniprot
proteins
pubmed
9603192
uniprot
proteins
sequence_length
223
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000250|UniProtKB:Q99720}. Nucleus outer membrane {ECO:0000250|UniProtKB:Q99720}. Nucleus envelope {ECO:0000269|PubMed:12730355}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q99720}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:12730355}. Membrane {ECO:0000250|UniProtKB:Q99720}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q99720}. Lipid droplet {ECO:0000269|PubMed:12730355}. Cell junction {ECO:0000250|UniProtKB:Q99720}. Cell membrane {ECO:0000250|UniProtKB:Q99720}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q99720}. Postsynaptic density membrane {ECO:0000269|PubMed:20167253}. Note=During interphase, detected at the inner and outer nuclear membrane and the endoplasmic reticulum. Detected on cytoplasmic vesicles during mitosis (By similarity). Targeted to lipid droplets, cholesterol and galactosylceramide-enriched domains of the endoplasmic reticulum (PubMed:12730355). Enriched at cell-cell communication regions, growth cone and postsynaptic structures. Localization is modulated by ligand-binding. In motor neurons it is enriched at cholinergic postsynaptic densities (PubMed:20167253). {ECO:0000250|UniProtKB:Q99720, ECO:0000269|PubMed:12730355, ECO:0000269|PubMed:20167253}.
uniprot
proteins
transmembrane_region
TRANSMEM 10..30; /note="Helical"; /evidence="ECO:0000250|UniProtKB:Q99720
uniprot
proteins