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Q8N2E6 (TOR2X_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Prosalusin
Alternative name(s):
Torsin family 2 member A
Torsin-2A

Cleaved into the following 2 chains:

  1. Salusin-alpha
  2. Salusin-beta
Gene names
Name:TOR2A
ORF Names:HEMBA1005096, PSEC0218
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length242 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Salusins -alpha and -beta may be endocrine and/or paracrine factors able to increase intracellular calcium concentrations and induce cell mitogenesis. Salusins may also be potent hypotensive peptides. Ref.3

Subcellular location

Secreted Ref.3.

Tissue specificity

Isoform 4 is ubiquitously expressed, with high level in vascular endothelial cells and vascular smooth muscle cells. Ref.3

Post-translational modification

Amidation of salusin-alpha(29-Gly) by peptidylglycine alpha-amidating monooxygenase, PAM, converts Lys-241-Gly-242 to Lys-241-NH2 and gives raise to salusin-alpha.

Sequence similarities

Belongs to the ClpA/ClpB family. Torsin subfamily.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
   DomainSignal
   LigandATP-binding
Nucleotide-binding
   Molecular functionHormone
   PTMAmidation
Cleavage on pair of basic residues
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchaperone mediated protein folding requiring cofactor

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 4 (identifier: Q8N2E6-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: Salusins -alpha and -beta peptides are derived from isoform 4.
Isoform 1 (identifier: Q5JU69-1)

The sequence of this isoform can be found in the external entry Q5JU69.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Isoform 2 (identifier: Q5JU69-2)

The sequence of this isoform can be found in the external entry Q5JU69.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q5JU69-5)

The sequence of this isoform can be found in the external entry Q5JU69.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Chain27 – 242216Prosalusin
PRO_0000228825
Propeptide27 – 189163 Potential
PRO_0000228826
Peptide192 – 21120Salusin-beta
PRO_0000228827
Peptide214 – 24128Salusin-alpha
PRO_0000228828

Regions

Nucleotide binding93 – 1008ATP Potential

Amino acid modifications

Modified residue2411Lysine amide Ref.3
Glycosylation1491N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Isoform 4 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 8118353CE5A0D628

FASTA24226,262
        10         20         30         40         50         60 
MAAATRGCRP WGSLLGLLGL VSAAAAAWDL ASLRCTLGAF CECDFRPDLP GLECDLAQHL 

        70         80         90        100        110        120 
AGQHLAKALV VKALKAFVRD PAPTKPLVLS LHGWTGTGKS YVSSLLAHYL FQGGLRSPRV 

       130        140        150        160        170        180 
HHFSPVLHFP HPSHIERYKK DLKSWVQGNL TACGRSLFLF DEMDKMPPGL MEVLRPFLGS 

       190        200        210        220        230        240 
SWVVYGTNYR KAIFIFIRWL LKLGHHGRAP PRRSGALPPA PAAPRPALRA QRAGPAGPGA 


KG 

« Hide

Isoform 1 [UniParc].

See Q5JU69.

Isoform 2 [UniParc].

See Q5JU69.

Isoform 3 [UniParc].

See Q5JU69.

References

« Hide 'large scale' references
[1]"Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y. expand/collapse author list , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Embryo.
[2]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Salusins: newly identified bioactive peptides with hemodynamic and mitogenic activities."
Shichiri M., Ishimaru S., Ota T., Nishikawa T., Isogai T., Hirata Y.
Nat. Med. 9:1166-1172(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF SALUSINS, TISSUE SPECIFICITY, AMIDATION AT LYS-241, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK075520 mRNA. Translation: BAC11667.1.
AL162426 Genomic DNA. Translation: CAI41185.1.
RefSeqNP_001127902.1. NM_001134430.2.
UniGeneHs.444106.

3D structure databases

ProteinModelPortalQ8N2E6.
SMRQ8N2E6. Positions 47-202.
ModBaseSearch...
MobiDBSearch...

Polymorphism databases

DMDM74750929.

Proteomic databases

PRIDEQ8N2E6.

Protocols and materials databases

DNASU27433.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000336067; ENSP00000338317; ENSG00000160404. [Q8N2E6-1]
GeneID27433.
KEGGhsa:27433.
UCSCuc004brt.4. human. [Q8N2E6-1]

Organism-specific databases

CTD27433.
GeneCardsGC09M130493.
HGNCHGNC:11996. TOR2A.
MIM608052. gene.
neXtProtNX_Q8N2E6.
PharmGKBPA36677.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHOG000115770.
HOVERGENHBG094082.
OrthoDBEOG7TF791.

Gene expression databases

ArrayExpressQ8N2E6.
BgeeQ8N2E6.
CleanExHS_TOR2A.
GenevestigatorQ8N2E6.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR010448. Torsin.
[Graphical view]
PANTHERPTHR10760. PTHR10760. 1 hit.
PfamPF06309. Torsin. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
ProtoNetSearch...

Other

GenomeRNAi27433.
NextBio50475.
SOURCESearch...

Entry information

Entry nameTOR2X_HUMAN
AccessionPrimary (citable) accession number: Q8N2E6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: October 1, 2002
Last modified: April 16, 2014
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM