ID   TOR2X_BOVIN             Reviewed;         242 AA.
AC   P0C7W1;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Prosalusin;
DE   AltName: Full=Torsin family 2 member A;
DE   AltName: Full=Torsin-2A;
DE   Contains:
DE     RecName: Full=Salusin-alpha;
DE   Contains:
DE     RecName: Full=Salusin-beta;
DE   Flags: Precursor;
GN   Name=TOR2A;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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=2;
CC       Name=2; Synonyms=Prosalusin;
CC         IsoId=P0C7W1-1; Sequence=Displayed;
CC       Name=1;
CC         IsoId=A4FUH1-1; Sequence=External;
CC   -!- MISCELLANEOUS: [Isoform 2]: Salusin-beta peptide is derived from
CC       isoform 2.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family. Torsin subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AAFC03079547; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_005213359.1; XM_005213302.3. [P0C7W1-1]
DR   AlphaFoldDB; P0C7W1; -.
DR   SMR; P0C7W1; -.
DR   GeneID; 534311; -.
DR   CTD; 27433; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IBA:GO_Central.
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   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010448; Torsin.
DR   PANTHER; PTHR10760; PTHR10760; 1.
DR   Pfam; PF06309; Torsin; 1.
DR   SUPFAM; SSF52540; SSF52540; 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..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..242
FT                   /note="Prosalusin"
FT                   /id="PRO_0000345611"
FT   PROPEP          27..189
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000345610"
FT   PEPTIDE         192..211
FT                   /note="Salusin-beta"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000345612"
FT   PEPTIDE         214..241
FT                   /note="Salusin-alpha"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000345613"
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   242 AA;  26421 MW;  0D928F30C55DA32E CRC64;
     MAAATRSCRP WGSLLGLIWL VSAAAASWDL SSLRCNFGSF CECDFQPDFQ GLECDLAQHL
     AGQHLARSLV VKALKAFLQD PAPTKPLVLS LHGWTGTGKS YVSSLLAHYL FRDGLRSPHV
     HHFSPVIHFP HPSHLERYKK DLKSWVQGNL TVCSRSLFLF DEMDKLAPGL IEVLRPFLGS
     SWVVYGTNYR KAIFIFIRWL LALGHHGRAS PGRSGALPAT PAAPRAALCA QRAGPSGPGA
     QG