O95772 · STR3N_HUMAN
- ProteinSTARD3 N-terminal-like protein
- GeneSTARD3NL
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids234 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Tethering protein that creates contact site between the endoplasmic reticulum and late endosomes: localizes to late endosome membranes and contacts the endoplasmic reticulum via interaction with VAPA and VAPB (PubMed:24105263).
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 | cytosol | |
Cellular Component | endoplasmic reticulum-endosome membrane contact site | |
Cellular Component | endosome | |
Cellular Component | intracellular membrane-bounded organelle | |
Cellular Component | late endosome membrane | |
Cellular Component | lysosomal membrane | |
Cellular Component | membrane | |
Cellular Component | organelle membrane contact site | |
Molecular Function | cholesterol binding | |
Molecular Function | protein homodimerization activity | |
Biological Process | cholesterol transport | |
Biological Process | vesicle tethering to endoplasmic reticulum |
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameSTARD3 N-terminal-like protein
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO95772
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Late endosome membrane ; Multi-pass membrane protein
Note: Localizes to contact sites between the endoplasmic reticulum and late endosomes: associates with the endoplasmic reticulum membrane via interaction with VAPA, VAPB or MOSPD2.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-53 | Cytoplasmic | ||||
Sequence: MNHLPEDMENALTGSQSSHASLRNIHSINPTQLMARIESYEGREKKGISDVRR | ||||||
Transmembrane | 54-74 | Helical | ||||
Sequence: TFCLFVTFDLLFVTLLWIIEL | ||||||
Topological domain | 75-97 | Extracellular | ||||
Sequence: NVNGGIENTLEKEVMQYDYYSSY | ||||||
Transmembrane | 98-118 | Helical | ||||
Sequence: FDIFLLAVFRFKVLILAYAVC | ||||||
Topological domain | 119-122 | Cytoplasmic | ||||
Sequence: RLRH | ||||||
Transmembrane | 123-143 | Helical | ||||
Sequence: WWAIALTTAVTSAFLLAKVIL | ||||||
Topological domain | 144-150 | Extracellular | ||||
Sequence: SKLFSQG | ||||||
Transmembrane | 151-171 | Helical | ||||
Sequence: AFGYVLPIISFILAWIETWFL | ||||||
Topological domain | 172-234 | Cytoplasmic | ||||
Sequence: DFKVLPQEAEEENRLLIVQDASERAALIPGGLSDGQFYSPPESEAGSEEAEEKQDSEKPLLEL |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 209-234 | Loss of interaction with MOSPD2. | ||||
Sequence: Missing |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 258 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 modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue | 1 | UniProt | N-acetylmethionine | ||||
Sequence: M | |||||||
Chain | PRO_0000021666 | 1-234 | UniProt | STARD3 N-terminal-like protein | |||
Sequence: MNHLPEDMENALTGSQSSHASLRNIHSINPTQLMARIESYEGREKKGISDVRRTFCLFVTFDLLFVTLLWIIELNVNGGIENTLEKEVMQYDYYSSYFDIFLLAVFRFKVLILAYAVCRLRHWWAIALTTAVTSAFLLAKVILSKLFSQGAFGYVLPIISFILAWIETWFLDFKVLPQEAEEENRLLIVQDASERAALIPGGLSDGQFYSPPESEAGSEEAEEKQDSEKPLLEL | |||||||
Modified residue (large scale data) | 13 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 15 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 15 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 17 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 18 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 21 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 21 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 27 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 27 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 39 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 193 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 193 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 204 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 209 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 210 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 214 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 218 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 227 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Homodimer (PubMed:16709157).
Interacts (via the MENTAL domain) with STARD3NL (PubMed:16709157).
Interacts (via FFAT motif) with VAPA. Interacts (via FFAT motif) with VAPB (PubMed:24105263).
Interacts (via FFAT motif) with MOSPD2 (via MSP domain) (PubMed:29858488).
Interacts (via the MENTAL domain) with STARD3NL (PubMed:16709157).
Interacts (via FFAT motif) with VAPA. Interacts (via FFAT motif) with VAPB (PubMed:24105263).
Interacts (via FFAT motif) with MOSPD2 (via MSP domain) (PubMed:29858488).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O95772 | HCST Q9UBK5 | 3 | EBI-3916943, EBI-2801937 | |
BINARY | O95772 | MOSPD2 Q8NHP6 | 6 | EBI-3916943, EBI-2812848 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 48-218 | MENTAL | ||||
Sequence: ISDVRRTFCLFVTFDLLFVTLLWIIELNVNGGIENTLEKEVMQYDYYSSYFDIFLLAVFRFKVLILAYAVCRLRHWWAIALTTAVTSAFLLAKVILSKLFSQGAFGYVLPIISFILAWIETWFLDFKVLPQEAEEENRLLIVQDASERAALIPGGLSDGQFYSPPESEAGS | ||||||
Region | 200-234 | Disordered | ||||
Sequence: PGGLSDGQFYSPPESEAGSEEAEEKQDSEKPLLEL | ||||||
Motif | 208-213 | FFAT | ||||
Sequence: FYSPPE |
Domain
The FFAT motif mediates interaction with VAPA, VAPB and MOSPD2.
The MENTAL domain anchors the protein in endosome membranes and exposes the START domain in the cytosol (By similarity).
It binds cholesterol and mediates homotypic as well as heterotypic interactions between STARD3 and STARD3NL (PubMed:15718238, PubMed:16709157).
It binds cholesterol and mediates homotypic as well as heterotypic interactions between STARD3 and STARD3NL (PubMed:15718238, PubMed:16709157).
Sequence similarities
Belongs to the STARD3 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative initiation.
O95772-1
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.
- Name1
- Length234
- Mass (Da)26,655
- Last updated1999-05-01 v1
- ChecksumAFB7DAE381983FB0
O95772-2
- Name2
- Differences from canonical
- 1-7: Missing
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_018819 | 1-7 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ492267 EMBL· GenBank· DDBJ | CAD37353.1 EMBL· GenBank· DDBJ | mRNA | ||
AY358645 EMBL· GenBank· DDBJ | AAQ89008.1 EMBL· GenBank· DDBJ | mRNA | ||
AK315404 EMBL· GenBank· DDBJ | BAG37796.1 EMBL· GenBank· DDBJ | mRNA | ||
AC006033 EMBL· GenBank· DDBJ | AAS07552.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH236951 EMBL· GenBank· DDBJ | EAL23983.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471073 EMBL· GenBank· DDBJ | EAW94088.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC003074 EMBL· GenBank· DDBJ | AAH03074.1 EMBL· GenBank· DDBJ | mRNA | ||
BC005959 EMBL· GenBank· DDBJ | AAH05959.1 EMBL· GenBank· DDBJ | mRNA |