Q9ULV4 · COR1C_HUMAN
- ProteinCoronin-1C
- GeneCORO1C
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids474 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Plays a role in directed cell migration by regulating the activation and subcellular location of RAC1 (PubMed:25074804, PubMed:25925950).
Increases the presence of activated RAC1 at the leading edge of migrating cells (PubMed:25074804, PubMed:25925950).
Required for normal organization of the cytoskeleton, including the actin cytoskeleton, microtubules and the vimentin intermediate filaments (By similarity).
Plays a role in endoplasmic reticulum-associated endosome fission: localizes to endosome membrane tubules and promotes recruitment of TMCC1, leading to recruitment of the endoplasmic reticulum to endosome tubules for fission (PubMed:30220460).
Endosome membrane fission of early and late endosomes is essential to separate regions destined for lysosomal degradation from carriers to be recycled to the plasma membrane (PubMed:30220460).
Required for normal cell proliferation, cell migration, and normal formation of lamellipodia (By similarity).
Required for normal distribution of mitochondria within cells (By similarity).
Increases the presence of activated RAC1 at the leading edge of migrating cells (PubMed:25074804, PubMed:25925950).
Required for normal organization of the cytoskeleton, including the actin cytoskeleton, microtubules and the vimentin intermediate filaments (By similarity).
Plays a role in endoplasmic reticulum-associated endosome fission: localizes to endosome membrane tubules and promotes recruitment of TMCC1, leading to recruitment of the endoplasmic reticulum to endosome tubules for fission (PubMed:30220460).
Endosome membrane fission of early and late endosomes is essential to separate regions destined for lysosomal degradation from carriers to be recycled to the plasma membrane (PubMed:30220460).
Required for normal cell proliferation, cell migration, and normal formation of lamellipodia (By similarity).
Required for normal distribution of mitochondria within cells (By similarity).
Isoform 3
Involved in myogenic differentiation.
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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Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCoronin-1C
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9ULV4
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Note: All isoforms colocalize with the actin cytoskeleton in the cytosol, and especially in the cell cortex (PubMed:10828594, PubMed:19651142, PubMed:25074804).
Colocalizes with F-actin at the leading edge of lamellipodia. Partially colocalizes with microtubules and vimentin intermediate filaments (PubMed:10828594, PubMed:19651142, PubMed:25074804).
Localizes to endosome membrane tubules/buds (PubMed:30220460).
Colocalizes with F-actin at the leading edge of lamellipodia. Partially colocalizes with microtubules and vimentin intermediate filaments (PubMed:10828594, PubMed:19651142, PubMed:25074804).
Localizes to endosome membrane tubules/buds (PubMed:30220460).
Isoform 3
Cell membrane ; Peripheral membrane protein
Note: Colocalizes with the thin filaments of the sarcomere and with the postsynaptic area and the junctional sarcoplasm of motor end plates. Colocalizes with the actin cytoskeleton in the cytosol, and especially in the cell cortex.
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 446 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 chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000050926 | 1-474 | UniProt | Coronin-1C | |||
Sequence: MRRVVRQSKFRHVFGQAVKNDQCYDDIRVSRVTWDSSFCAVNPRFVAIIIEASGGGAFLVLPLHKTGRIDKSYPTVCGHTGPVLDIDWCPHNDQVIASGSEDCTVMVWQIPENGLTLSLTEPVVILEGHSKRVGIVAWHPTARNVLLSAGCDNAIIIWNVGTGEALINLDDMHSDMIYNVSWNRNGSLICTASKDKKVRVIDPRKQEIVAEKEKAHEGARPMRAIFLADGNVFTTGFSRMSERQLALWNPKNMQEPIALHEMDTSNGVLLPFYDPDTSIIYLCGKGDSSIRYFEITDESPYVHYLNTFSSKEPQRGMGYMPKRGLDVNKCEIARFFKLHERKCEPIIMTVPRKSDLFQDDLYPDTAGPEAALEAEEWFEGKNADPILISLKHGYIPGKNRDLKVVKKNILDSKPTANKKCDLISIPKKTTDTASVQNEAKLDEILKEIKSIKDTICNQDERISKLEQQMAKIAA | |||||||
Modified residue (large scale data) | 187 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 299 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 301 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 415 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 430 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 434 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 446 | UniProt | N6-acetyllysine | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Tissue specificity
Ubiquitous.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Binds F-actin (PubMed:12377779, PubMed:22364218).
Interacts with RCC2 (PubMed:25074804).
Interacts preferentially with nucleotide-free and GDP-bound RAC1 (PubMed:25074804).
Interacts with VIM (via head domain) (By similarity).
Isoform 1 and isoform 2 appear as homotrimers, while isoform 3 seems to exist as monomers (PubMed:19651142).
Interacts with MICAL2; this interaction recruits MICAL2 to the actin filaments (PubMed:34106209).
Interacts with RCC2 (PubMed:25074804).
Interacts preferentially with nucleotide-free and GDP-bound RAC1 (PubMed:25074804).
Interacts with VIM (via head domain) (By similarity).
Isoform 1 and isoform 2 appear as homotrimers, while isoform 3 seems to exist as monomers (PubMed:19651142).
Interacts with MICAL2; this interaction recruits MICAL2 to the actin filaments (PubMed:34106209).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9ULV4 | CORO1B Q9BR76 | 7 | EBI-351384, EBI-351152 | |
BINARY | Q9ULV4 | LRRK2 Q5S007 | 3 | EBI-351384, EBI-5323863 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for repeat, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 25-70 | WD 1 | ||||
Sequence: DDIRVSRVTWDSSFCAVNPRFVAIIIEASGGGAFLVLPLHKTGRID | ||||||
Repeat | 78-118 | WD 2 | ||||
Sequence: GHTGPVLDIDWCPHNDQVIASGSEDCTVMVWQIPENGLTLS | ||||||
Repeat | 128-168 | WD 3 | ||||
Sequence: GHSKRVGIVAWHPTARNVLLSAGCDNAIIIWNVGTGEALIN | ||||||
Repeat | 172-202 | WD 4 | ||||
Sequence: MHSDMIYNVSWNRNGSLICTASKDKKVRVID | ||||||
Repeat | 215-249 | WD 5 | ||||
Sequence: AHEGARPMRAIFLADGNVFTTGFSRMSERQLALWN | ||||||
Repeat | 263-303 | WD 6 | ||||
Sequence: DTSNGVLLPFYDPDTSIIYLCGKGDSSIRYFEITDESPYVH | ||||||
Coiled coil | 436-474 | |||||
Sequence: QNEAKLDEILKEIKSIKDTICNQDERISKLEQQMAKIAA |
Domain
The C-terminal coiled-coil domain is essential for cortical membrane localization and oligomerization.
Sequence similarities
Belongs to the WD repeat coronin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q9ULV4-1
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
- Length474
- Mass (Da)53,249
- Last updated2000-05-01 v1
- ChecksumC7256797C514BB53
Q9ULV4-2
- Name2
- SynonymsCRN2i2
- Differences from canonical
- 1-1: M → MRWKDTM
Q9ULV4-3
- Name3
- SynonymsCRN2i3
- NoteExclusively expressed in well-differentiated myoblasts as well as in mature skeletal muscle.
- Differences from canonical
- 1-1: M → MYGPGSQLGKSGNNSWAKERGCSIACQGSLTSARLHAPSIGERPLSHMRWKDTM
Computationally mapped potential isoform sequences
There are 9 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB030656 EMBL· GenBank· DDBJ | BAA83077.1 EMBL· GenBank· DDBJ | mRNA | ||
AM849477 EMBL· GenBank· DDBJ | CAO94662.1 EMBL· GenBank· DDBJ | mRNA | ||
AM849478 EMBL· GenBank· DDBJ | CAO94663.1 EMBL· GenBank· DDBJ | mRNA | ||
AK096363 EMBL· GenBank· DDBJ | BAG53274.1 EMBL· GenBank· DDBJ | mRNA | ||
AL162070 EMBL· GenBank· DDBJ | CAB82406.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AC007569 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471054 EMBL· GenBank· DDBJ | EAW97826.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC002342 EMBL· GenBank· DDBJ | AAH02342.1 EMBL· GenBank· DDBJ | mRNA |