TUNAR_HUMAN
ID TUNAR_HUMAN Reviewed; 48 AA.
AC A0A1B0GTB2; A0A1B0GUV0;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2017, sequence version 2.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=Protein TUNAR {ECO:0000305};
DE Short=pTUNAR {ECO:0000250|UniProtKB:A0A1B0GQX2};
DE AltName: Full=Beta cell and neural cell-regulin {ECO:0000303|PubMed:34513312};
DE Short=BNLN {ECO:0000303|PubMed:34513312};
DE AltName: Full=TCL1 upstream neural differentiation-associated RNA {ECO:0000312|HGNC:HGNC:44088};
GN Name=TUNAR {ECO:0000312|HGNC:HGNC:44088};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000312|Proteomes:UP000005640};
RN [1] {ECO:0000312|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [2] {ECO:0000312|EMBL:EAW81624.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH ATP2A3, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=34513312; DOI=10.1016/j.omtn.2021.06.027;
RA Li M., Shao F., Qian Q., Yu W., Zhang Z., Chen B., Su D., Guo Y.,
RA Phan A.V., Song L.S., Stephens S.B., Sebag J., Imai Y., Yang L., Cao H.;
RT "A putative long noncoding RNA-encoded micropeptide maintains cellular
RT homeostasis in pancreatic beta cells.";
RL Mol. Ther. Nucleic Acids 26:307-320(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 (By similarity). 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 (By similarity). In
CC pancreatic beta cells, lowers Ca(2+) levels in the endoplasmic
CC reticulum and enhances glucose-stimulated insulin secretion
CC (PubMed:34513312). {ECO:0000250|UniProtKB:A0A1B0GQX2,
CC ECO:0000269|PubMed:34513312}.
CC -!- SUBUNIT: Interacts with ATPase ATP2A2/SERCA2 (By similarity). Interacts
CC with ATPase ATP2A3/SERCA3; the interaction occurs at low levels in low
CC glucose conditions and is increased by high glucose levels
CC (PubMed:34513312). {ECO:0000250|UniProtKB:A0A1B0GQX2,
CC ECO:0000269|PubMed:34513312}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:34513312}; Single-pass membrane protein
CC {ECO:0000255}. Extracellular vesicle membrane
CC {ECO:0000250|UniProtKB:A0A1B0GQX2}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in pancreatic islets where it is
CC enriched in the insulin-producing beta cells.
CC {ECO:0000269|PubMed:34513312}.
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DR EMBL; AL133167; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471061; EAW81624.1; -; Genomic_DNA.
DR BioMuta; TUNAR; -.
DR Ensembl; ENST00000503525.2; ENSP00000489624.2; ENSG00000250366.4.
DR Ensembl; ENST00000504119.1; ENSP00000498192.1; ENSG00000250366.4.
DR Ensembl; ENST00000554321.1; ENSP00000490254.2; ENSG00000250366.4.
DR Ensembl; ENST00000687554.1; ENSP00000510004.1; ENSG00000250366.4.
DR GeneCards; TUNAR; -.
DR HGNC; HGNC:44088; TUNAR.
DR OpenTargets; ENSG00000250366; -.
DR VEuPathDB; HostDB:ENSG00000250366; -.
DR GeneTree; ENSGT01020000230938; -.
DR OMA; VLTKMVI; -.
DR ChiTaRS; TUNAR; human.
DR Proteomes; UP000005640; Chromosome 14.
DR Bgee; ENSG00000250366; Expressed in putamen and 90 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; IDA:UniProtKB.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; ISS:UniProtKB.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IDA:UniProtKB.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Neurogenesis; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..48
FT /note="Protein TUNAR"
FT /id="PRO_0000455681"
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; 5360 MW; 59BE2C36EE0E0E57 CRC64;
MVITSENDED RGGQEKESKE ESVLAMLGII GTILNLIVII FVYIYTTL
