Q9HBJ8 · CLTRN_HUMAN

  • Protein
    Collectrin
  • Gene
    CLTRN
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Plays an important role in amino acid transport by acting as binding partner of amino acid transporters SLC6A18 and SLC6A19, regulating their trafficking on the cell surface and their amino acid transporter activity (By similarity).
May also play a role in trafficking of amino acid transporters SLC3A1 and SLC7A9 to the renal cortical cell membrane (By similarity).
Regulator of SNARE complex function (PubMed:16330323).
Stimulator of beta cell replication (PubMed:16330323).

Features

Showing features for site.

122220406080100120140160180200220
TypeIDPosition(s)Description
Site125-126Cleavage by BACE2

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 Componentbrush border membrane
Cellular Componentcytoplasm
Cellular Componentextracellular exosome
Cellular Componentplasma membrane
Molecular Functionprotein homodimerization activity
Biological Processcalcium-ion regulated exocytosis
Biological Processinsulin secretion involved in cellular response to glucose stimulus
Biological Processpositive regulation of amino acid transport
Biological Processpositive regulation of L-proline import across plasma membrane
Biological Processregulation of transmembrane transporter activity
Biological ProcessSNARE complex assembly

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Collectrin
  • Alternative names
    • Transmembrane protein 27

Gene names

    • Name
      CLTRN
    • Synonyms
      TMEM27
    • ORF names
      UNQ679/PRO1312

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q9HBJ8
  • Secondary accessions
    • B2R9M1
    • Q6UW07

Proteomes

Organism-specific databases

Subcellular Location

Cell membrane
; Single-pass type I membrane protein
Note: Localizes to the brush border membranes of cells in the proximal tubules of kidney (By similarity).
Colocalizes with SLC6A19 in the early proximal S1 tubule (By similarity).

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain15-141Extracellular
Transmembrane142-162Helical
Topological domain163-222Cytoplasmic

Keywords

Disease & Variants

Involvement in disease

  • An interstitial deletion on chromosome Xp22.2 encompassing CLTRN and a deletion spanning CLTRN exons 1 to 3 have been found in two individuals with a neuropsychiatric disorder characterized by autistic features, anxiety, depression, compulsions, motor tics, and neutral aminoaciduria. Plasma amino acids were normal in both patients

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis75Increased dimerization leading to hyperoligomerized. Abolishes processing by BACE2. Abolishes localization to the cell membrane.
Mutagenesis76Loss of localization to the cell membrane. Abolishes processing by BACE2. Loss of localization to the cell membrane; when associated with I-93.
Mutagenesis93Loss of localization to the cell membrane. Abolishes processing by BACE2. Loss of localization to the cell membrane; when associated with I-76.
Mutagenesis115-119Increases processing by BACE2. Decreases of protein abundance.
Mutagenesis123-128Does not affet processing by BACE2.
Mutagenesis152Does not affect dimerization. Does not affect cell membrane localization. Abolishes dimerization; when associated with A-186.
Mutagenesis186Abolishes dimerization. Does not affect cell membrane localization. Does not affect processing by BACE2. Abolishes dimerization; when associated with A-152.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 200 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for signal, chain, glycosylation, modified residue.

TypeIDPosition(s)Description
Signal1-14
ChainPRO_000024586715-222Collectrin
Glycosylation76N-linked (GlcNAc...) asparagine
Glycosylation93N-linked (GlcNAc...) asparagine
Modified residue214Phosphothreonine
Modified residue220Phosphothreonine

Post-translational modification

Glycosylated. Glycosylation is required for plasma membrane localization and for its cleavage by BACE2.
Proteolytically processed in pancreatic beta cells by BACE2 leading to the generation and extracellular release of soluble CLTRN, and a corresponding cell-associated C-terminal fragment which is later cleaved by gamma-secretase. This shedding process inactivates CLTRN (By similarity).
Three cleavage sites have been identified for BACE2, two clustered sites after Phe-116 and Leu-118 and a more membrane proximal site at Phe-125; the preferred BACE2 cleavage site seems to be between Phe-125 and Leu-126, Phe-116 and Leu-118 act as alternative sites (PubMed:21907142, PubMed:22628310).

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Kidney; collecting ducts. Pancreas; beta cells of islets.

Gene expression databases

Organism-specific databases

Interaction

Subunit

Monomer (PubMed:22628310).
Homodimer; dimerization prevents CLTRN cleavage by BACE2 (PubMed:22628310).
Interacts with SLC6A18; this interaction regulates the trafficking of SLC6A18 to the cell membrane and its amino acid transporter activity (By similarity).
Interacts with SLC6A19; this interaction regulates the trafficking of SLC6A19 to the cell membrane and its amino acid transporter activity (By similarity).
Interacts with SNAPIN (PubMed:16330323).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q9HBJ8OLFM4 Q6UX063EBI-3924906, EBI-2804156
BINARY Q9HBJ8SMCO4 Q9NRQ53EBI-3924906, EBI-8640191
BINARY Q9HBJ8UBE2J1 Q9Y3853EBI-3924906, EBI-988826
View interactors in UniProtKB
View CPX-8191 in Complex Portal

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain21-222Collectrin-like

Domain

The cleavage site containing the double Phe-Phe motif acts as negative regulator of shedding by BACE2.

Sequence similarities

Belongs to the CLTRN family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    222
  • Mass (Da)
    25,235
  • Last updated
    2001-03-01 v1
  • Checksum
    52C0ED522134ED05
MLWLLFFLVTAIHAELCQPGAENAFKVRLSIRTALGDKAYAWDTNEEYLFKAMVAFSMRKVPNREATEISHVLLCNVTQRVSFWFVVTDPSKNHTLPAVEVQSAIRMNKNRINNAFFLNDQTLEFLKIPSTLAPPMDPSVPIWIIIFGVIFCIIIVAIALLILSGIWQRRRKNKEPSEVDDAEDKCENMITIENGIPSDPLDMKGGHINDAFMTEDERLTPL

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A3B3ITM8A0A3B3ITM8_HUMANCLTRN170

Sequence caution

The sequence AAQ89419.1 differs from that shown. Reason: Frameshift

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF229179
EMBL· GenBank· DDBJ
AAG09466.1
EMBL· GenBank· DDBJ
mRNA
AY359060
EMBL· GenBank· DDBJ
AAQ89419.1
EMBL· GenBank· DDBJ
mRNA Frameshift
AK313835
EMBL· GenBank· DDBJ
BAG36568.1
EMBL· GenBank· DDBJ
mRNA
AC003669
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AC112497
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CH471074
EMBL· GenBank· DDBJ
EAW98894.1
EMBL· GenBank· DDBJ
Genomic DNA
BC014317
EMBL· GenBank· DDBJ
AAH14317.1
EMBL· GenBank· DDBJ
mRNA
BC015099
EMBL· GenBank· DDBJ
AAH15099.1
EMBL· GenBank· DDBJ
mRNA
BC050606
EMBL· GenBank· DDBJ
AAH50606.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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