ID TOR2X_MOUSE Reviewed; 231 AA. AC P0C7W3; DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot. DT 22-JUL-2008, sequence version 1. DT 03-MAY-2023, entry version 73. DE RecName: Full=Prosalusin; DE AltName: Full=Torsin family 2 member A; DE AltName: Full=Torsin-2A; DE Contains: DE RecName: Full=Salusin-beta; DE Flags: Precursor; GN Name=Tor2a; 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; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; 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] RP REGION. RX PubMed=16697365; DOI=10.1016/j.ejphar.2006.03.064; RA Wang Z., Takahashi T., Saito Y., Nagasaki H., Ly N.K., Nothacker H.-P., RA Reinscheid R.K., Yang J., Chang J.K., Shichiri M., Civelli O.; RT "Salusin beta is a surrogate ligand of the mas-like G protein-coupled RT receptor MrgA1."; RL Eur. J. Pharmacol. 539:145-150(2006). CC -!- FUNCTION: Salusin may be a endocrine and/or paracrine factor able to CC increase intracellular calcium concentrations and induce cell CC mitogenesis. Salusin may also be a potent hypotensive peptide (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=3; CC IsoId=P0C7W3-1; Sequence=Displayed; CC Name=1; CC IsoId=Q8R1J9-1; Sequence=External; CC Name=2; CC IsoId=Q8R1J9-2; Sequence=External; CC -!- MISCELLANEOUS: [Isoform 3]: Salusin-beta peptide is derived from CC isoform 3. CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. Torsin subfamily. CC {ECO:0000305}. 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 EMBL; AL772271; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; P0C7W3; -. DR SMR; P0C7W3; -. DR GlyCosmos; P0C7W3; 1 site, No reported glycans. DR PhosphoSitePlus; P0C7W3; -. DR PeptideAtlas; P0C7W3; -. DR ProteomicsDB; 260652; -. [P0C7W3-1] DR MGI; MGI:1353596; Tor2a. DR ChiTaRS; Tor2a; mouse. DR Proteomes; UP000000589; Unplaced. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:MGI. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0005635; C:nuclear envelope; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW. DR GO; GO:0042802; F:identical protein binding; IPI:MGI. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR010448; Torsin. DR PANTHER; PTHR10760; TORSIN; 1. DR PANTHER; PTHR10760:SF4; TORSIN-2A; 1. DR Pfam; PF06309; Torsin; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. PE 3: Inferred from homology; KW Alternative splicing; ATP-binding; Cleavage on pair of basic residues; KW Glycoprotein; Hormone; Nucleotide-binding; Reference proteome; Secreted; KW Signal. FT SIGNAL 1..27 FT /evidence="ECO:0000255" FT CHAIN 28..231 FT /note="Prosalusin" FT /id="PRO_0000345614" FT PROPEP 28..189 FT /evidence="ECO:0000255" FT /id="PRO_0000345615" FT PEPTIDE 192..231 FT /note="Salusin-beta" FT /evidence="ECO:0000250" FT /id="PRO_0000345616" FT REGION 192..211 FT /note="Partial activation of MRGPRA1" FT BINDING 93..100 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255" FT CARBOHYD 149 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" SQ SEQUENCE 231 AA; 25377 MW; 56DC8F6C09F5EFC5 CRC64; MAVARHGYRP WGSILGLLGL ALAAAAAWDV ASLRCTFGSF CECDFWPDLP GLECDLAQHL AGQHLAKALV VKSLKAFVQD PAPSKPLVLS LHGWTGTGKS YVSSLLAQHL FRDGLRSPHV HHFSPIIHFP HPSRTEQYKK ELKSWVQGNL TACGRSLFLF DEMDKLPPGL MEVLQPFLGP SWVVYGTNYR KAIFIFIRWL LAVWHHGGAP AGRCGALPPA PAASRAPLRT Q //