TOR2X_RAT
ID TOR2X_RAT Reviewed; 231 AA.
AC P0C7W2;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 62.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18344632; DOI=10.1291/hypres.30.1255;
RA Suzuki N., Shichiri M., Akashi T., Sato K., Sakurada M., Hirono Y.,
RA Yoshimoto T., Koyama T., Hirata Y.;
RT "Systemic distribution of salusin expression in the rat.";
RL Hypertens. Res. 30:1255-1262(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
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:0000269|PubMed:18344632}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2;
CC IsoId=P0C7W2-1; Sequence=Displayed;
CC Name=1;
CC IsoId=Q6AYR4-1; Sequence=External;
CC -!- TISSUE SPECIFICITY: Isoform 2 is ubiquitously expressed.
CC {ECO:0000269|PubMed:18344632}.
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}.
CC -!- CAUTION: Salusin-beta detected systemically according to
CC PubMed:18344632 represents the putative rat salusin consisting of 40
CC amino acid residues or a shorter fragment produced by an unknown
CC processing mechanism. No salusin-alpha homolog is detected in rat
CC tissues. {ECO:0000305}.
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DR EMBL; AABR03024382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P0C7W2; -.
DR SMR; P0C7W2; -.
DR UCSC; RGD:1359111; rat. [P0C7W2-1]
DR RGD; 1359111; Tor2a.
DR VEuPathDB; HostDB:ENSRNOG00000022514; -.
DR HOGENOM; CLU_1199501_0_0_1; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000022514; Expressed in pancreas and 20 other tissues.
DR ExpressionAtlas; P0C7W2; baseline and differential.
DR Genevisible; P0C7W2; RN.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; ISO:RGD.
DR GO; GO:0005576; C:extracellular region; ISO:RGD.
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; ISO:RGD.
DR GO; GO:1904427; P:positive regulation of calcium ion transmembrane transport; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
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 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Glycoprotein; Hormone;
KW Nucleotide-binding; Reference proteome; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..231
FT /note="Prosalusin"
FT /id="PRO_0000345618"
FT PROPEP 28..189
FT /evidence="ECO:0000255"
FT /id="PRO_0000345617"
FT PEPTIDE 192..231
FT /note="Salusin-beta"
FT /id="PRO_0000345619"
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; 25127 MW; 31AB9C7D2DC63814 CRC64;
MAVARHGCPP WGSILGLLVL ALAAAAAWDV SFLRCSLGSF CECDFWPDLP GLECDLARHL
AGQHLAKALV VKSLKAFVQD PAPSKPLVLS LHGWTGTGKS YVSSLLAQYL FRGGLRSPHV
HHFSPIIHFP HPSHTEQYKN ELKSWVQGNL TACGRSLFLF DEMDKLPPGL MEVLKPFLGP
SWVVYGTNYR KAIFIFIRWL LAVWHHGGAA AGCCGPLPPP PAASCAPLCA Q
