Protein detail
CO4A5
Collagen alpha-5(IV) chain
Protein symbol CO4A5 | UniProt ID | EVMP score 0.50 |
Frequency 1 | Transmembrane count | Protein classification |
EVMP score: annotation confidence score.
Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
Basic Information
Protein Names
Collagen alpha-5(IV) chain
Protein Function
- Predicted intracellular proteins
- Cancer-related genes:Candidate cancer biomarkers
- Predicted secreted proteins
- Human disease related genes:Congenital malformations:Other congenital malformations
- Disease related genes
- Human disease related genes:Reproductive system diseases:Reproductive system diseases
Ensembl
Entrez Gene Symbol
Frequency
1
EVMP Score
0.50
Fluorescence & Localization
Function & Pathway
Protein Function
- Predicted intracellular proteins
- Cancer-related genes:Candidate cancer biomarkers
- Predicted secreted proteins
- Human disease related genes:Congenital malformations:Other congenital malformations
- Disease related genes
- Human disease related genes:Reproductive system diseases:Reproductive system diseases
Cellular Component
Molecular Function
Biological Process
KEGG
- hsa04151 PI3K-Akt signaling pathway
- KEGG:hsa04382 Cornified envelope formation
- KEGG:hsa04510 Focal adhesion
- KEGG:hsa04512 ECM-receptor interaction
- KEGG:hsa04518 Integrin signaling
- KEGG:hsa04820 Cytoskeleton in muscle cells
- KEGG:hsa04926 Relaxin signaling pathway
- KEGG:hsa04933 AGE-RAGE signaling pathway in diabetic complications
- KEGG:hsa04974 Protein digestion and absorption
- KEGG:hsa05146 Amoebiasis
- KEGG:hsa05165 Human papillomavirus infection
- KEGG:hsa05200 Pathways in cancer
- KEGG:hsa05222 Small cell lung cancer
Reactome
- R-hsa-2214320 anchoring fibril formation
- R-hsa-2022090 assembly of collagen fibrils and other multimeric structures
- R-hsa-9638630 attachment of bacteria to epithelial cells
- R-hsa-9824439 bacterial infection pathways
- R-hsa-1650814 collagen biosynthesis and modifying enzymes
- R-hsa-8948216 collagen chain trimerization
- R-hsa-1442490 collagen degradation
- R-hsa-1474290 collagen formation
- R-hsa-2243919 crosslinking of collagen fibrils
- R-hsa-1474228 degradation of the extracellular matrix
- R-hsa-3000178 ecm proteoglycans
- R-hsa-1474244 extracellular matrix organization
- R-hsa-1566977 fibronectin matrix formation
- R-hsa-9640148 infection with enterobacteria
- R-hsa-5663205 infectious disease
- R-hsa-216083 integrin cell surface interactions
- R-hsa-3000157 laminin interactions
- R-hsa-419037 ncam1 interactions
- R-hsa-375165 ncam signaling for neurite out growth
- R-hsa-9675108 nervous system development
- R-hsa-3000171 non integrin membrane ecm interactions
- R-hsa-9010553 regulation of expression of slits and robos
- R-hsa-186797 signaling by pdgf
- R-hsa-9006934 signaling by receptor tyrosine kinases
- R-hsa-376176 signaling by robo receptors
Mediation Categories
Clinical-translation mediationReceptor-signaling mediation
Relations & Evidence
Enzyme-Mediated Modification
0 records.
Ligand-Receptor Signaling
20 records.
| Category | Parent | Database | Transmitter | Receiver | Secreted | Plasma Membrane (Transmembrane) | Plasma Membrane (Peripheral) |
|---|---|---|---|---|---|---|---|
| ecm | ecm | GO_Intercell | Yes | No | Yes | No | No |
| ecm | ecm | Ramilowski_location | Yes | No | Yes | No | No |
| basement membrane | ecm | Ramilowski_location | Yes | No | Yes | No | No |
| ecm | ecm | UniProt_location | Yes | No | Yes | No | No |
| ecm | ecm | OmniPath | Yes | No | Yes | No | No |
| extracellular | extracellular | LOCATE | No | No | Yes | No | No |
| extracellular | extracellular | OmniPath | No | No | Yes | No | No |
| intracellular | intracellular | GO_Intercell | No | No | Yes | No | No |
| intracellular | intracellular | OmniPath | No | No | Yes | No | No |
| cell_surface_ligand | cell_surface_ligand | CellChatDB | Yes | No | Yes | No | No |
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Regulatory Interaction Network
1 record.
| Source Protein Symbol | Source UniProt ID | Target Protein Symbol | Target UniProt ID | Is Directed | Is Stimulation | Is Inhibition | Database | References |
|---|---|---|---|---|---|---|---|---|
| CO4A5 | P29400 | COMPLEX:P05556_P56199 | Yes | Yes | No | CellPhoneDBICELLNETSIGNOR | ICELLNET:15147720ICELLNET:21421911ICELLNET:16988024SIGNOR:35267698ICELLNET:26857815 |
Protein Complex Composition
14 records.
| Component Name | Component Gene Symbols | Component UniProt ID | Stoichiometry | Database | Database IDs | References |
|---|---|---|---|---|---|---|
| COL4A3COL4A4COL4A5COL4A6MRPS2SERPINE2 | P07093P29400P53420Q01955Q14031Q9Y399 | 1:1:1:1:1:1 | NetworkBlastCompleat | Compleat:HC8536 | ||
| COL4A2COL4A5EEF1AKMT2HADHBSDF4SMN1 | P08572P29400P55084Q16637Q5JPI9Q9BRK5 | 1:1:1:1:1:1 | NetworkBlastCompleat | Compleat:HC4947 | ||
| COL4A5COL8A2 | P25067P29400 | 0:0 | hu.MAP | |||
| COL4A5EEF1AKMT2HADHBTIMM13TIMM8B | P29400P55084Q5JPI9Q9Y5J9Q9Y5L4 | 1:1:1:1:1 | NetworkBlastCompleat | Compleat:HC5990 |
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Sequence, Structure & Domains
Sequences
Length
1,685
Mass
161,044
Sequence
MKLRGVSLAAGLFLLALSLWGQPAEAAACYGCSPGSKCDCSGIKGEKGERGFPGLEGHPGLPGFPGPEGPPGPRGQKGDDGIPGPPGPKGIRGPPGLPGFPGTPGLPGMPGHDGAPGPQGIPGCNGTKGERGFPGSPGFPGLQGPPGPPGIPGMKGEPGSIIMSSLPGPKGNPGYPGPPGIQGLPGPTGIPGPIGPPGPPGLMGPPGPPGLPGPKGNMGLNFQGPKGEKGEQGLQGPPGPPGQISEQKRPIDVEFQKGDQGLPGDRGPPGPPGIRGPPGPPGGEKGEKGEQGEPGKRGKPGKDGENGQPGIPGLPGDPGYPGEPGRDGEKGQKGDTGPPGPPGLVIPRPGTGITIGEKGNIGLPGLPGEKGERGFPGIQGPPGLPGPPGAAVMGPPGPPGFPGERGQKGDEGPPGISIPGPPGLDGQPGAPGLPGPPGPAGPHIPPSDEICEPGPPGPPGSPGDKGLQGEQGVKGDKGDTCFNCIGTGISGPPGQPGLPGLPGPPGSLGFPGQKGEKGQAGATGPKGLPGIPGAPGAPGFPGSKGEPGDILTFPGMKGDKGELGSPGAPGLPGLPGTPGQDGLPGLPGPKGEPGGITFKGERGPPGNPGLPGLPGNIGPMGPPGFGPPGPVGEKGIQGVAGNPGQPGIPGPKGDPGQTITQPGKPGLPGNPGRDGDVGLPGDPGLPGQPGLPGIPGSKGEPGIPGIGLPGPPGPKGFPGIPGPPGAPGTPGRIGLEGPPGPPGFPGPKGEPGFALPGPPGPPGLPGFKGALGPKGDRGFPGPPGPPGRTGLDGLPGPKGDVGPNGQPGPMGPPGLPGIGVQGPPGPPGIPGPIGQPGLHGIPGEKGDPGPPGLDVPGPPGERGSPGIPGAPGPIGPPGSPGLPGKAGASGFPGTKGEMGMMGPPGPPGPLGIPGRSGVPGLKGDDGLQGQPGLPGPTGEKGSKGEPGLPGPPGPMDPNLLGSKGEKGEPGLPGIPGVSGPKGYQGLPGDPGQPGLSGQPGLPGPPGPKGNPGLPGQPGLIGPPGLKGTIGDMGFPGPQGVEGPPGPSGVPGQPGSPGLPGQKGDKGDPGISSIGLPGLPGPKGEPGLPGYPGNPGIKGSVGDPGLPGLPGTPGAKGQPGLPGFPGTPGPPGPKGISGPPGNPGLPGEPGPVGGGGHPGQPGPPGEKGKPGQDGIPGPAGQKGEPGQPGFGNPGPPGLPGLSGQKGDGGLPGIPGNPGLPGPKGEPGFHGFPGVQGPPGPPGSPGPALEGPKGNPGPQGPPGRPGLPGPEGPPGLPGNGGIKGEKGNPGQPGLPGLPGLKGDQGPPGLQGNPGRPGLNGMKGDPGLPGVPGFPGMKGPSGVPGSAGPEGEPGLIGPPGPPGLPGPSGQSIIIKGDAGPPGIPGQPGLKGLPGPQGPQGLPGPTGPPGDPGRNGLPGFDGAGGRKGDPGLPGQPGTRGLDGPPGPDGLQGPPGPPGTSSVAHGFLITRHSQTTDAPQCPQGTLQVYEGFSLLYVQGNKRAHGQDLGTAGSCLRRFSTMPFMFCNINNVCNFASRNDYSYWLSTPEPMPMSMQPLKGQSIQPFISRCAVCEAPAVVIAVHSQTIQIPHCPQGWDSLWIGYSFMMHTSAGAEGSGQALASPGSCLEEFRSAPFIECHGRGTCNYYANSYSFWLATVDVSDMFSKPQSETLKAGDLRTRISRCQVCMKRT
Alternative Products
Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P29400-1; Sequence=Displayed; Name=2; IsoId=P29400-2; Sequence=VSP_001173
Alternative Sequence
1264; G -> GPTGFQG (in isoform 2)
3D Structural Models
Turn
1523..1525
Helix
1506..1508; 1554..1560; 1605..1607; 1617..1619; 1654..1656; 1668..1670; 1672..1674
Beta Strand
1461..1467; 1469..1472; 1481..1494; 1497..1500; 1509..1512; 1518..1521; 1527..1530; 1535..1540; 1563..1571; 1573..1577; 1579..1582; 1590..1603; 1609..1611; 1620..1623; 1629..1633; 1636..1639; 1645..1650; 1657..1659; 1664..1666; 1677..1683
3D Structure
X-ray crystallography (2)
Domain & Motif Annotations
Compositional Bias
52..61; Low complexity; 62..73; Pro residues; 188..212; Pro residues; 214..225; Low complexity; 246..257; Basic and acidic residues; 266..281; Pro residues; 284..305; Basic and acidic residues; 324..333; Basic and acidic residues; 413..430; Low complexity; 431..445; Pro residues; 493..505; Pro residues; 620..630; Pro residues; 709..727; Pro residues; 788..797; Low complexity; 848..859; Pro residues; 868..880; Pro residues; 882..901; Low complexity; 912..931; Low complexity; 983..999; Low complexity; 1010..1026; Low complexity; 1111..1120; Low complexity; 1139..1148; Pro residues; 1149..1158; Gly residues; 1202..1211; Gly residues; 1234..1243; Pro residues; 1256..1274; Pro residues; 1295..1308; Low complexity; 1353..1362; Pro residues
Domain (CC)
Alpha chains of type IV collagen have a non-collagenous domain (NC1) at their C-terminus, frequent interruptions of the G-X-Y repeats in the long central triple-helical domain (which may cause flexibility in the triple helix), and a short N-terminal triple-helical 7S domain.
Domain (FT)
1461..1685; Collagen IV NC1
Region
27..41; Nonhelical region (NC2); 42..1456; Triple-helical region; 49..1459; Disordered
Protein Families
Type IV collagen family
Sequence Similarities
Belongs to the type IV collagen family.