Q9HBJ8 · CLTRN_HUMAN
- ProteinCollectrin
- GeneCLTRN
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids222 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 125-126 | Cleavage by BACE2 | ||||
Sequence: FL |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | brush border membrane | |
Cellular Component | cytoplasm | |
Cellular Component | extracellular exosome | |
Cellular Component | plasma membrane | |
Molecular Function | protein homodimerization activity | |
Biological Process | calcium-ion regulated exocytosis | |
Biological Process | insulin secretion involved in cellular response to glucose stimulus | |
Biological Process | positive regulation of amino acid transport | |
Biological Process | positive regulation of L-proline import across plasma membrane | |
Biological Process | regulation of transmembrane transporter activity | |
Biological Process | SNARE complex assembly |
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameCollectrin
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9HBJ8
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
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).
Colocalizes with SLC6A19 in the early proximal S1 tubule (By similarity).
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 15-141 | Extracellular | ||||
Sequence: ELCQPGAENAFKVRLSIRTALGDKAYAWDTNEEYLFKAMVAFSMRKVPNREATEISHVLLCNVTQRVSFWFVVTDPSKNHTLPAVEVQSAIRMNKNRINNAFFLNDQTLEFLKIPSTLAPPMDPSVP | ||||||
Transmembrane | 142-162 | Helical | ||||
Sequence: IWIIIFGVIFCIIIVAIALLI | ||||||
Topological domain | 163-222 | Cytoplasmic | ||||
Sequence: LSGIWQRRRKNKEPSEVDDAEDKCENMITIENGIPSDPLDMKGGHINDAFMTEDERLTPL |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 75 | Increased dimerization leading to hyperoligomerized. Abolishes processing by BACE2. Abolishes localization to the cell membrane. | ||||
Sequence: C → A | ||||||
Mutagenesis | 76 | Loss of localization to the cell membrane. Abolishes processing by BACE2. Loss of localization to the cell membrane; when associated with I-93. | ||||
Sequence: N → I | ||||||
Mutagenesis | 93 | Loss of localization to the cell membrane. Abolishes processing by BACE2. Loss of localization to the cell membrane; when associated with I-76. | ||||
Sequence: N → I | ||||||
Mutagenesis | 115-119 | Increases processing by BACE2. Decreases of protein abundance. | ||||
Sequence: AFFLN → GGGGG, AAAAA, or TYYLR | ||||||
Mutagenesis | 123-128 | Does not affet processing by BACE2. | ||||
Sequence: LEFLKI → NTYGKR | ||||||
Mutagenesis | 152 | Does not affect dimerization. Does not affect cell membrane localization. Abolishes dimerization; when associated with A-186. | ||||
Sequence: C → A | ||||||
Mutagenesis | 186 | Abolishes dimerization. Does not affect cell membrane localization. Does not affect processing by BACE2. Abolishes dimerization; when associated with A-152. | ||||
Sequence: C → A |
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.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-14 | |||||
Sequence: MLWLLFFLVTAIHA | ||||||
Chain | PRO_0000245867 | 15-222 | Collectrin | |||
Sequence: ELCQPGAENAFKVRLSIRTALGDKAYAWDTNEEYLFKAMVAFSMRKVPNREATEISHVLLCNVTQRVSFWFVVTDPSKNHTLPAVEVQSAIRMNKNRINNAFFLNDQTLEFLKIPSTLAPPMDPSVPIWIIIFGVIFCIIIVAIALLILSGIWQRRRKNKEPSEVDDAEDKCENMITIENGIPSDPLDMKGGHINDAFMTEDERLTPL | ||||||
Glycosylation | 76 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 93 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 214 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 220 | Phosphothreonine | ||||
Sequence: T |
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).
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
- PTM
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).
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
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9HBJ8 | OLFM4 Q6UX06 | 3 | EBI-3924906, EBI-2804156 | |
BINARY | Q9HBJ8 | SMCO4 Q9NRQ5 | 3 | EBI-3924906, EBI-8640191 | |
BINARY | Q9HBJ8 | UBE2J1 Q9Y385 | 3 | EBI-3924906, EBI-988826 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 21-222 | Collectrin-like | ||||
Sequence: AENAFKVRLSIRTALGDKAYAWDTNEEYLFKAMVAFSMRKVPNREATEISHVLLCNVTQRVSFWFVVTDPSKNHTLPAVEVQSAIRMNKNRINNAFFLNDQTLEFLKIPSTLAPPMDPSVPIWIIIFGVIFCIIIVAIALLILSGIWQRRRKNKEPSEVDDAEDKCENMITIENGIPSDPLDMKGGHINDAFMTEDERLTPL |
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
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length222
- Mass (Da)25,235
- Last updated2001-03-01 v1
- Checksum52C0ED522134ED05
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A3B3ITM8 | A0A3B3ITM8_HUMAN | CLTRN | 170 |
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |