Q9D7W4 · TSN17_MOUSE

  • Protein
    Tetraspanin-17
  • Gene
    Tspan17
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

Function

function

Part of TspanC8 subgroup, composed of 6 members that interact with the transmembrane metalloprotease ADAM10. This interaction is required for ADAM10 exit from the endoplasmic reticulum and for enzymatic maturation and trafficking to the cell surface as well as substrate specificity. Different TspanC8/ADAM10 complexes have distinct substrates (PubMed:23035126, PubMed:26668317).
Seems to regulate VE-cadherin expression in endothelial cells probably through interaction with ADAM10, promoting leukocyte transmigration (By similarity).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentplasma membrane
Molecular Functionenzyme binding
Biological Processprotein maturation
Biological Processregulation of membrane protein ectodomain proteolysis

Names & Taxonomy

Protein names

  • Recommended name
    Tetraspanin-17
  • Short names
    Tspan-17
  • Alternative names
    • F-box only protein 23
    • Tetraspan protein SB134
    • Transmembrane 4 superfamily member 17

Gene names

    • Name
      Tspan17
    • Synonyms
      Fbxo23, Tm4sf17

Organism names

  • Taxonomic identifier
  • Strain
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q9D7W4
  • Secondary accessions
    • Q91VI6

Proteomes

Organism-specific databases

Subcellular Location

Cell membrane
; Multi-pass membrane protein

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-19Cytoplasmic
Transmembrane20-40Helical
Topological domain41-63Extracellular
Transmembrane64-84Helical
Topological domain85-94Cytoplasmic
Transmembrane95-115Helical
Topological domain116-234Extracellular
Transmembrane235-255Helical
Topological domain256-270Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for chain, glycosylation, disulfide bond.

TypeIDPosition(s)Description
ChainPRO_00002192661-270Tetraspanin-17
Glycosylation51N-linked (GlcNAc...) asparagine
Disulfide bond155↔223
Disulfide bond156↔188
Glycosylation171N-linked (GlcNAc...) asparagine
Disulfide bond172↔182
Disulfide bond189↔202

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Interacts with ADAM10; the interaction influences ADAM10 substrate specificity, endocytosis and turnover.

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Sequence similarities

Belongs to the tetraspanin (TM4SF) family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    270
  • Mass (Da)
    30,126
  • Last updated
    2001-06-01 v1
  • Checksum
    220FF195C1EA42C1
MPGKHQQFQDPEVGCCGKYFLFGFNIVFWVLGALFLAIGLWAWGEKGVLSNISALTDLGGLDPVWLFVVVGGVMSVLGFAGCIGALRENTFLLKFFSVFLGLIFFLELAAGILAFVFKDWIRDQLNLFINNNVKAYRDDLDLQNLIDFAQEYWSCCGARGPNDWNLNIYFNCTDLNPSRERCGVPFSCCVRDPAEDVLNTQCGYDIRLKLELEQEGSIYTKGCVGQFEKWLQDNLIVVAGVLVGIALLQIFGLCLAQNLVSDIKAVKANW

Computationally mapped potential isoform sequences

There are 8 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
E9QAJ5E9QAJ5_MOUSETspan17152
Q3TLW9Q3TLW9_MOUSETspan17285
E9PWC3E9PWC3_MOUSETspan17193
F6R550F6R550_MOUSETspan17192
F7CRB7F7CRB7_MOUSETspan17145
E9QN85E9QN85_MOUSETspan17273
Q3TAQ3Q3TAQ3_MOUSETspan17270
F6VW20F6VW20_MOUSETspan17187

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict215in Ref. 2; AAH10346

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AK008761
EMBL· GenBank· DDBJ
BAB25880.1
EMBL· GenBank· DDBJ
mRNA
BC010346
EMBL· GenBank· DDBJ
AAH10346.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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