TUNAR_MOUSE
ID TUNAR_MOUSE Reviewed; 48 AA.
AC A0A1B0GQX2;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2017, sequence version 2.
DT 03-AUG-2022, entry version 24.
DE RecName: Full=Protein TUNAR {ECO:0000305};
DE Short=pTUNAR {ECO:0000303|PubMed:35036403};
DE AltName: Full=Beta cell and neural cell-regulin {ECO:0000250|UniProtKB:A0A1B0GTB2};
DE Short=BNLN {ECO:0000250|UniProtKB:A0A1B0GTB2};
DE AltName: Full=Tcl1 upstream neural differentiation-associated RNA {ECO:0000312|MGI:MGI:1917202};
GN Name=Tunar {ECO:0000312|MGI:MGI:1917202};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000312|Proteomes:UP000000589};
RN [1] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0000305}
RP FUNCTION, INTERACTION WITH ATP2A2, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=35036403; DOI=10.3389/fcell.2021.747667;
RA Senis E., Esgleas M., Najas S., Jimenez-Sabado V., Bertani C.,
RA Gimenez-Alejandre M., Escriche A., Ruiz-Orera J., Hergueta-Redondo M.,
RA Jimenez M., Giralt A., Nuciforo P., Alba M.M., Peinado H., Del Toro D.,
RA Hove-Madsen L., Goetz M., Abad M.;
RT "TUNAR lncRNA Encodes a Microprotein that Regulates Neural Differentiation
RT and Neurite Formation by Modulating Calcium Dynamics.";
RL Front. Cell Dev. Biol. 9:747667-747667(2021).
CC -!- FUNCTION: In neurons, plays a role in the regulation of intracellular
CC Ca(2+), possibly by acting as an activator of ATP2A2/SERCA2, thus
CC increasing the efficiency with which Ca(2+) is removed from the
CC cytoplasm (PubMed:35036403). Inhibits differentiation of embryonic stem
CC cells into neurons and inhibits neurite outgrowth, likely as a result
CC of its role in intracellular Ca(2+) regulation (PubMed:35036403). In
CC pancreatic beta cells, lowers Ca(2+) levels in the endoplasmic
CC reticulum and enhances glucose-stimulated insulin secretion (By
CC similarity). {ECO:0000250|UniProtKB:A0A1B0GTB2,
CC ECO:0000269|PubMed:35036403}.
CC -!- SUBUNIT: Interacts with ATPase ATP2A2/SERCA2 (PubMed:35036403).
CC Interacts with ATPase ATP2A3/SERCA3; the interaction occurs at low
CC levels in low glucose conditions and is increased by high glucose
CC levels (By similarity). {ECO:0000250|UniProtKB:A0A1B0GTB2,
CC ECO:0000269|PubMed:35036403}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:35036403}; Single-pass membrane protein
CC {ECO:0000255}. Extracellular vesicle membrane
CC {ECO:0000269|PubMed:35036403}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: In the adult, expressed in Purkinje cells in the
CC cerebellum, in motor neurons and interneurons in the spinal cord and in
CC neurons of the cortex, hippocampus and thalamus (at protein level)
CC (PubMed:35036403). Also detected in the developing cortex, hippocampus
CC and thalamus at embryonic day E15.5 (at protein level)
CC (PubMed:35036403). {ECO:0000269|PubMed:35036403}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A1B0GQX2; -.
DR SMR; A0A1B0GQX2; -.
DR Ensembl; ENSMUST00000180458; ENSMUSP00000147361; ENSMUSG00000097929.
DR Ensembl; ENSMUST00000180503; ENSMUSP00000147289; ENSMUSG00000097929.
DR MGI; MGI:1917202; Tunar.
DR VEuPathDB; HostDB:ENSMUSG00000097929; -.
DR GeneTree; ENSGT01020000230647; -.
DR ChiTaRS; Tunar; mouse.
DR Proteomes; UP000000589; Chromosome 12.
DR Bgee; ENSMUSG00000097929; Expressed in lumbar subsegment of spinal cord and 74 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0051117; F:ATPase binding; IPI:UniProtKB.
DR GO; GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; ISS:UniProtKB.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:UniProtKB.
DR GO; GO:0048812; P:neuron projection morphogenesis; IMP:UniProtKB.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; ISS:UniProtKB.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IMP:UniProtKB.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..48
FT /note="Protein TUNAR"
FT /id="PRO_0000455682"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 48 AA; 5288 MW; 59BE2E9464240E57 CRC64;
MVITSGNDED RGGQEKESKE ESVLAMLGII GTILNLIVII FVYIYTTL