Sigmar1
entrez
29336
canonical
uniprot
Q9R0C9
canonical
ensembl
ENSRNOG00000014604
resolver
ensembl
ENSRNOG00055017128
resolver
ensembl
ENSRNOG00060004218
resolver
ensembl
ENSRNOG00065004820
resolver
ensp
ENSRNOP00000019795
resolver
genesymbol
Sigmar1
resolver
genesymbol_syn
Oprs1
resolver
uniprot
Q9R1J7
resolver
uniprot
Q9Z2W2
resolver
uniprot_entry
SGMR1_RAT
resolver
uniprot_sec
Q9R1J7
resolver
uniprot_sec
Q9Z2W2
resolver
amino_acid_sequence
MPWAVGRRWAWITLFLTIVAVLIQAVWLWLGTQSFVFQREEIAQLARQYAGLDHELAFSRLIVELRRLHPGHVLPDEELQWVFVNAGGWMGAMCLLHASLSEYVLLFGTALGSHGHSGRYWAEISDTIISGTFHQWREGTTKSEVYYPGETVVHGPGEATAVEWGPNTWMVEYGRGVIPSTLAFALSDTIFSTQDFLTLFYTLRAYARGLRLELTTYLFGQDP
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. 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. Necessary for proper mitochondrial axonal transport in motor neurons, in particular the retrograde movement of mitochondria. Plays a role in protecting cells against oxidative stress-induced cell death via its interaction with RNF112 (By similarity). {ECO:0000250|UniProtKB:O55242, ECO:0000269|PubMed:11861817, ECO:0000269|PubMed:11988171, ECO:0000269|PubMed:15170821, ECO:0000269|PubMed:15466698, ECO:0000269|PubMed:16522641, ECO:0000269|PubMed:9489711}.
uniprot
proteins
mass_dalton
25270
uniprot
proteins
protein_family
ERG2 family
uniprot
proteins
pubmed
10771347
uniprot
proteins
pubmed
11149946
uniprot
proteins
pubmed
11687279
uniprot
proteins
pubmed
11861817
uniprot
proteins
pubmed
11988171
uniprot
proteins
pubmed
12535781
uniprot
proteins
pubmed
15064136
uniprot
proteins
pubmed
15170821
uniprot
proteins
pubmed
15466698
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16522641
uniprot
proteins
pubmed
9489711
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:0000250|UniProtKB:Q99720}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q99720}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:15466698}. Membrane {ECO:0000250|UniProtKB:Q99720}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q99720}. Lipid droplet {ECO:0000269|PubMed:15466698}. Cell junction {ECO:0000250|UniProtKB:Q99720}. Cell membrane {ECO:0000250|UniProtKB:Q99720}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q99720}. Postsynaptic density membrane {ECO:0000250|UniProtKB:Q99720}. 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:15466698). 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 (By similarity). {ECO:0000250|UniProtKB:O55242, ECO:0000250|UniProtKB:Q99720, ECO:0000269|PubMed:15466698}.
uniprot
proteins
transmembrane_region
TRANSMEM 10..30; /note="Helical"; /evidence="ECO:0000250|UniProtKB:Q99720
uniprot
proteins