Q14050 · CO9A3_HUMAN
- ProteinCollagen alpha-3(IX) chain
- GeneCOL9A3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids684 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Structural component of hyaline cartilage and vitreous of the eye.
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 | collagen type IX trimer | |
Cellular Component | collagen-containing extracellular matrix | |
Cellular Component | endoplasmic reticulum lumen | |
Cellular Component | extracellular region | |
Cellular Component | extracellular space | |
Molecular Function | extracellular matrix structural constituent conferring tensile strength | |
Molecular Function | protein homodimerization activity | |
Biological Process | extracellular matrix organization |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCollagen alpha-3(IX) chain
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ14050
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Multiple epiphyseal dysplasia 3 (EDM3)
- Note
- DescriptionA generalized skeletal dysplasia associated with significant morbidity. Joint pain, joint deformity, waddling gait, and short stature are the main clinical signs and symptoms. Radiological examination of the skeleton shows delayed, irregular mineralization of the epiphyseal ossification centers and of the centers of the carpal and tarsal bones. Multiple epiphyseal dysplasia is broadly categorized into the more severe Fairbank and the milder Ribbing types. The Fairbank type is characterized by shortness of stature, short and stubby fingers, small epiphyses in several joints, including the knee, ankle, hand, and hip. The Ribbing type is confined predominantly to the hip joints and is characterized by hands that are normal and stature that is normal or near-normal.
- See alsoMIM:600969
Natural variants in EDM3
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_072736 | 35 | G>D | in EDM3; dbSNP:rs1390736361 |
Intervertebral disc disease (IDD)
- Note
- DescriptionA common musculo-skeletal disorder caused by degeneration of intervertebral disks of the lumbar spine. It results in low-back pain and unilateral leg pain.
- See alsoMIM:603932
Stickler syndrome 6 (STL6)
- Note
- DescriptionA form of Stickler syndrome, an inherited disorder that associates ocular signs with more or less complete forms of Pierre Robin sequence, bone disorders and sensorineural deafness. Ocular disorders may include juvenile cataract, myopia, strabismus, vitreoretinal or chorioretinal degeneration, retinal detachment, and chronic uveitis. Pierre Robin sequence includes an opening in the roof of the mouth (a cleft palate), a large tongue (macroglossia), and a small lower jaw (micrognathia). Bones are affected by slight platyspondyly and large, often defective epiphyses. Juvenile joint laxity is followed by early signs of arthrosis. The degree of hearing loss varies among affected individuals and may become more severe over time. STL6 is an autosomal recessive form characterized by early-onset progressive hearing loss and progressive myopia, with variable manifestation of facial dysmorphism and skeletal anomalies.
- See alsoMIM:620022
Natural variants in STL6
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_087540 | 90-684 | missing | in STL6 | |
VAR_087541 | 471-684 | missing | in STL6 | |
VAR_087542 | 577-684 | missing | in STL6 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_072736 | 35 | in EDM3; dbSNP:rs1390736361 | |||
Sequence: G → D | ||||||
Natural variant | VAR_087540 | 90-684 | in STL6 | |||
Sequence: Missing | ||||||
Natural variant | VAR_048808 | 94 | in dbSNP:rs35908728 | |||
Sequence: P → S | ||||||
Natural variant | VAR_026467 | 103 | in dbSNP:rs142639450 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_026468 | 103 | probable risk factor for intervertebral disk disease; dbSNP:rs61734651 | |||
Sequence: R → W | ||||||
Natural variant | VAR_026469 | 296 | in dbSNP:rs45628843 | |||
Sequence: P → L | ||||||
Natural variant | VAR_026470 | 402 | in dbSNP:rs373519549 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_026471 | 435 | in dbSNP:rs751557 | |||
Sequence: A → E | ||||||
Natural variant | VAR_087541 | 471-684 | in STL6 | |||
Sequence: Missing | ||||||
Natural variant | VAR_012660 | 563-565 | ||||
Sequence: Missing | ||||||
Natural variant | VAR_012661 | 564-566 | ||||
Sequence: Missing | ||||||
Natural variant | VAR_087542 | 577-684 | in STL6 | |||
Sequence: Missing |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,125 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-25 | |||||
Sequence: MAGPRACAPLLLLLLLGELLAAAGA | ||||||
Chain | PRO_0000005848 | 26-684 | Collagen alpha-3(IX) chain | |||
Sequence: QRVGLPGPPGPPGPPGKPGQDGIDGEAGPPGLPGPPGPKGAPGKPGKPGEAGLPGLPGVDGLTGRDGPPGPKGAPGERGSLGPPGPPGLGGKGLPGPPGEAGVSGPPGGIGLRGPPGPSGLPGLPGPPGPPGPPGHPGVLPEGATDLQCPSICPPGPPGPPGMPGFKGPTGYKGEQGEVGKDGEKGDPGPPGPAGLPGSVGLQGPRGLRGLPGPLGPPGDRGPIGFRGPPGIPGAPGKAGDRGERGPEGFRGPKGDLGRPGPKGTPGVAGPSGEPGMPGKDGQNGVPGLDGQKGEAGRNGAPGEKGPNGLPGLPGRAGSKGEKGERGRAGELGEAGPSGEPGVPGDAGMPGERGEAGHRGSAGALGPQGPPGAPGVRGFQGQKGSMGDPGLPGPQGLRGDVGDRGPGGAAGPKGDQGIAGSDGLPGDKGELGPSGLVGPKGESGSRGELGPKGTQGPNGTSGVQGVPGPPGPLGLQGVPGVPGITGKPGVPGKEASEQRIRELCGGMISEQIAQLAAHLRKPLAPGSIGRPGPAGPPGPPGPPGSIGHPGARGPPGYRGPTGELGDPGPRGNQGDRGDKGAAGAGLDGPEGDQGPQGPQGVPGTSKDGQDGAPGEPGPPGDPGLPGAIGAQGTPGICDTSACQGAVLGGVGEKSGSRSS | ||||||
Glycosylation | 483 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
Covalently linked to the telopeptides of type II collagen by lysine-derived cross-links.
Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Heterotrimer of an alpha 1(IX), an alpha 2(IX) and an alpha 3(IX) chain.
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 26-521 | Disordered | ||||
Sequence: QRVGLPGPPGPPGPPGKPGQDGIDGEAGPPGLPGPPGPKGAPGKPGKPGEAGLPGLPGVDGLTGRDGPPGPKGAPGERGSLGPPGPPGLGGKGLPGPPGEAGVSGPPGGIGLRGPPGPSGLPGLPGPPGPPGPPGHPGVLPEGATDLQCPSICPPGPPGPPGMPGFKGPTGYKGEQGEVGKDGEKGDPGPPGPAGLPGSVGLQGPRGLRGLPGPLGPPGDRGPIGFRGPPGIPGAPGKAGDRGERGPEGFRGPKGDLGRPGPKGTPGVAGPSGEPGMPGKDGQNGVPGLDGQKGEAGRNGAPGEKGPNGLPGLPGRAGSKGEKGERGRAGELGEAGPSGEPGVPGDAGMPGERGEAGHRGSAGALGPQGPPGAPGVRGFQGQKGSMGDPGLPGPQGLRGDVGDRGPGGAAGPKGDQGIAGSDGLPGDKGELGPSGLVGPKGESGSRGELGPKGTQGPNGTSGVQGVPGPPGPLGLQGVPGVPGITGKPGVPGKEAS | ||||||
Region | 29-519 | Triple-helical region 3 (COL3) | ||||
Sequence: GLPGPPGPPGPPGKPGQDGIDGEAGPPGLPGPPGPKGAPGKPGKPGEAGLPGLPGVDGLTGRDGPPGPKGAPGERGSLGPPGPPGLGGKGLPGPPGEAGVSGPPGGIGLRGPPGPSGLPGLPGPPGPPGPPGHPGVLPEGATDLQCPSICPPGPPGPPGMPGFKGPTGYKGEQGEVGKDGEKGDPGPPGPAGLPGSVGLQGPRGLRGLPGPLGPPGDRGPIGFRGPPGIPGAPGKAGDRGERGPEGFRGPKGDLGRPGPKGTPGVAGPSGEPGMPGKDGQNGVPGLDGQKGEAGRNGAPGEKGPNGLPGLPGRAGSKGEKGERGRAGELGEAGPSGEPGVPGDAGMPGERGEAGHRGSAGALGPQGPPGAPGVRGFQGQKGSMGDPGLPGPQGLRGDVGDRGPGGAAGPKGDQGIAGSDGLPGDKGELGPSGLVGPKGESGSRGELGPKGTQGPNGTSGVQGVPGPPGPLGLQGVPGVPGITGKPGVPGKE | ||||||
Compositional bias | 54-68 | Pro residues | ||||
Sequence: PPGLPGPPGPKGAPG | ||||||
Compositional bias | 143-163 | Pro residues | ||||
Sequence: PSGLPGLPGPPGPPGPPGHPG | ||||||
Compositional bias | 176-190 | Pro residues | ||||
Sequence: SICPPGPPGPPGMPG | ||||||
Motif | 423-425 | Cell attachment site | ||||
Sequence: RGD | ||||||
Region | 520-550 | Nonhelical region 3 (NC3) | ||||
Sequence: ASEQRIRELCGGMISEQIAQLAAHLRKPLAP | ||||||
Region | 548-665 | Disordered | ||||
Sequence: LAPGSIGRPGPAGPPGPPGPPGSIGHPGARGPPGYRGPTGELGDPGPRGNQGDRGDKGAAGAGLDGPEGDQGPQGPQGVPGTSKDGQDGAPGEPGPPGDPGLPGAIGAQGTPGICDTS | ||||||
Region | 551-630 | Triple-helical region 2 (COL2) | ||||
Sequence: GSIGRPGPAGPPGPPGPPGSIGHPGARGPPGYRGPTGELGDPGPRGNQGDRGDKGAAGAGLDGPEGDQGPQGPQGVPGTS | ||||||
Compositional bias | 554-574 | Pro residues | ||||
Sequence: GRPGPAGPPGPPGPPGSIGHP | ||||||
Motif | 601-603 | Cell attachment site | ||||
Sequence: RGD | ||||||
Region | 631-632 | Nonhelical region 2 (NC2) | ||||
Sequence: KD | ||||||
Region | 633-661 | Triple-helical region 1 (COL1) | ||||
Sequence: GQDGAPGEPGPPGDPGLPGAIGAQGTPGI | ||||||
Region | 662-684 | Nonhelical region 1 (NC1) | ||||
Sequence: CDTSACQGAVLGGVGEKSGSRSS |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length684
- Mass (Da)63,616
- Last updated2002-01-23 v2
- Checksum892F035CF6E06733
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q4VXW1 | Q4VXW1_HUMAN | COL9A3 | 191 |
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 18 | in Ref. 1; AAC41947 and 2; AAD47357 | ||||
Sequence: E → Q | ||||||
Sequence conflict | 39 | in Ref. 1; AAC41947 | ||||
Sequence: P → R | ||||||
Compositional bias | 54-68 | Pro residues | ||||
Sequence: PPGLPGPPGPKGAPG | ||||||
Compositional bias | 143-163 | Pro residues | ||||
Sequence: PSGLPGLPGPPGPPGPPGHPG | ||||||
Sequence conflict | 144 | in Ref. 1; AAC41947 | ||||
Sequence: S → P | ||||||
Compositional bias | 176-190 | Pro residues | ||||
Sequence: SICPPGPPGPPGMPG | ||||||
Sequence conflict | 524 | in Ref. 5; CAA62495 | ||||
Sequence: R → H | ||||||
Compositional bias | 554-574 | Pro residues | ||||
Sequence: GRPGPAGPPGPPGPPGSIGHP | ||||||
Sequence conflict | 576 | in Ref. 5; CAA62495 | ||||
Sequence: A → T |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L41162 EMBL· GenBank· DDBJ | AAC41947.1 EMBL· GenBank· DDBJ | mRNA | ||
AF026802 EMBL· GenBank· DDBJ | AAD47357.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF026801 EMBL· GenBank· DDBJ | AAD47357.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL035669 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC011705 EMBL· GenBank· DDBJ | AAH11705.1 EMBL· GenBank· DDBJ | mRNA | ||
X91013 EMBL· GenBank· DDBJ | CAA62495.1 EMBL· GenBank· DDBJ | mRNA |