TOR2X_HUMAN
ID TOR2X_HUMAN Reviewed; 242 AA.
AC Q8N2E6;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 133.
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; ORFNames=HEMBA1005096, PSEC0218;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Embryo;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP FUNCTION OF SALUSINS, TISSUE SPECIFICITY, AMIDATION AT LYS-241, AND
RP SUBCELLULAR LOCATION.
RX PubMed=12910263; DOI=10.1038/nm913;
RA Shichiri M., Ishimaru S., Ota T., Nishikawa T., Isogai T., Hirata Y.;
RT "Salusins: newly identified bioactive peptides with hemodynamic and
RT mitogenic activities.";
RL Nat. Med. 9:1166-1172(2003).
CC -!- FUNCTION: Salusins -alpha and -beta may be endocrine and/or paracrine
CC factors able to increase intracellular calcium concentrations and
CC induce cell mitogenesis. Salusins may also be potent hypotensive
CC peptides. {ECO:0000269|PubMed:12910263}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12910263}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=4;
CC IsoId=Q8N2E6-1; Sequence=Displayed;
CC Name=1;
CC IsoId=Q5JU69-1; Sequence=External;
CC Name=2;
CC IsoId=Q5JU69-2; Sequence=External;
CC Name=3;
CC IsoId=Q5JU69-5; Sequence=External;
CC -!- TISSUE SPECIFICITY: Isoform 4 is ubiquitously expressed, with high
CC level in vascular endothelial cells and vascular smooth muscle cells.
CC {ECO:0000269|PubMed:12910263}.
CC -!- PTM: Amidation of salusin-alpha(29-Gly) by peptidylglycine alpha-
CC amidating monooxygenase, PAM, converts Lys-241-Gly-242 to Lys-241-NH2
CC and gives raise to salusin-alpha. {ECO:0000269|PubMed:12910263}.
CC -!- MISCELLANEOUS: [Isoform 4]: Salusins -alpha and -beta peptides are
CC derived from isoform 4.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. Torsin subfamily.
CC {ECO:0000305}.
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DR EMBL; AK075520; BAC11667.1; -; mRNA.
DR EMBL; AL162426; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS48024.1; -. [Q8N2E6-1]
DR RefSeq; NP_001127902.1; NM_001134430.2. [Q8N2E6-1]
DR AlphaFoldDB; Q8N2E6; -.
DR SMR; Q8N2E6; -.
DR BioGRID; 118167; 31.
DR GlyConnect; 1644; 2 N-Linked glycans (1 site).
DR PhosphoSitePlus; Q8N2E6; -.
DR BioMuta; TOR2A; -.
DR DMDM; 74750929; -.
DR EPD; Q8N2E6; -.
DR jPOST; Q8N2E6; -.
DR MassIVE; Q8N2E6; -.
DR MaxQB; Q8N2E6; -.
DR PeptideAtlas; Q8N2E6; -.
DR PRIDE; Q8N2E6; -.
DR ProteomicsDB; 71686; -. [Q8N2E6-1]
DR Antibodypedia; 30786; 144 antibodies from 22 providers.
DR DNASU; 27433; -.
DR Ensembl; ENST00000336067.10; ENSP00000338317.6; ENSG00000160404.18. [Q8N2E6-1]
DR GeneID; 27433; -.
DR UCSC; uc004brt.5; human. [Q8N2E6-1]
DR CTD; 27433; -.
DR DisGeNET; 27433; -.
DR GeneCards; TOR2A; -.
DR HGNC; HGNC:11996; TOR2A.
DR HPA; ENSG00000160404; Low tissue specificity.
DR MIM; 608052; gene.
DR neXtProt; NX_Q8N2E6; -.
DR OpenTargets; ENSG00000160404; -.
DR PharmGKB; PA36677; -.
DR VEuPathDB; HostDB:ENSG00000160404; -.
DR GeneTree; ENSGT00950000182888; -.
DR HOGENOM; CLU_1199501_0_0_1; -.
DR PathwayCommons; Q8N2E6; -.
DR SignaLink; Q8N2E6; -.
DR BioGRID-ORCS; 27433; 167 hits in 1088 CRISPR screens.
DR ChiTaRS; TOR2A; human.
DR GenomeRNAi; 27433; -.
DR Pharos; Q8N2E6; Tbio.
DR Proteomes; UP000005640; Chromosome 9.
DR Bgee; ENSG00000160404; Expressed in oocyte and 108 other tissues.
DR ExpressionAtlas; Q8N2E6; baseline and differential.
DR Genevisible; Q8N2E6; HS.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IC:UniProtKB.
DR GO; GO:0031640; P:killing of cells of another organism; IMP:UniProtKB.
DR GO; GO:0051673; P:membrane disruption in another organism; IDA:UniProtKB.
DR GO; GO:1904427; P:positive regulation of calcium ion transmembrane transport; IDA:UniProtKB.
DR GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; IDA:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0030103; P:vasopressin secretion; IDA:UniProtKB.
DR GO; GO:0030104; P:water homeostasis; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Alternative splicing; Amidation; ATP-binding;
KW Cleavage on pair of basic residues; Glycoprotein; Hormone;
KW Nucleotide-binding; Reference proteome; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..242
FT /note="Prosalusin"
FT /id="PRO_0000228825"
FT PROPEP 27..189
FT /evidence="ECO:0000255"
FT /id="PRO_0000228826"
FT PEPTIDE 192..211
FT /note="Salusin-beta"
FT /id="PRO_0000228827"
FT PEPTIDE 214..241
FT /note="Salusin-alpha"
FT /id="PRO_0000228828"
FT REGION 210..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 93..100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 241
FT /note="Lysine amide"
FT /evidence="ECO:0000269|PubMed:12910263"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 242 AA; 26262 MW; 8118353CE5A0D628 CRC64;
MAAATRGCRP WGSLLGLLGL VSAAAAAWDL ASLRCTLGAF CECDFRPDLP GLECDLAQHL
AGQHLAKALV VKALKAFVRD PAPTKPLVLS LHGWTGTGKS YVSSLLAHYL FQGGLRSPRV
HHFSPVLHFP HPSHIERYKK DLKSWVQGNL TACGRSLFLF DEMDKMPPGL MEVLRPFLGS
SWVVYGTNYR KAIFIFIRWL LKLGHHGRAP PRRSGALPPA PAAPRPALRA QRAGPAGPGA
KG
