P17140 · CO4A2_CAEEL
- ProteinCollagen alpha-2(IV) chain
- Genelet-2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1758 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Collagen type IV is specific for basement membranes (Probable). Together with fbl-1 and downstream of metalloprotease mig-17, recruits nidogen nid-1 to the gonad basement membrane thereby probably inducing basement membrane remodeling required for the directional migration of distal tip cells (PubMed:19104038).
Required to restrict presynaptic growth at the neuromuscular junctions in late larval stage and in adult motor neurons (PubMed:25080592).
Vital for embryonic development (PubMed:7691828, PubMed:8045258).
Required to restrict presynaptic growth at the neuromuscular junctions in late larval stage and in adult motor neurons (PubMed:25080592).
Vital for embryonic development (PubMed:7691828, PubMed:8045258).
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 | basement membrane | |
Cellular Component | collagen type IV trimer | |
Cellular Component | collagen-containing extracellular matrix | |
Cellular Component | extracellular space | |
Molecular Function | extracellular matrix structural constituent | |
Molecular Function | extracellular matrix structural constituent conferring tensile strength | |
Biological Process | cellular component organization | |
Biological Process | embryo development ending in birth or egg hatching | |
Biological Process | extracellular matrix organization | |
Biological Process | gonad morphogenesis | |
Biological Process | protein localization | |
Biological Process | regulation of distal tip cell migration |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCollagen alpha-2(IV) chain
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis
Accessions
- Primary accessionP17140
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 48 | In MN114; 73% lethal. | ||||
Sequence: G → E | ||||||
Mutagenesis | 366 | In MN126; 100% lethal. | ||||
Sequence: A → T | ||||||
Mutagenesis | 479 | In ju1166; suppresses the lethal phenotypes of the pxn-2 tm3464 mutant. | ||||
Sequence: E → K | ||||||
Mutagenesis | 570 | In MN109; 37% lethal. | ||||
Sequence: G → E | ||||||
Mutagenesis | 587 | In ju1180; suppresses the lethal phenotypes of the pxn-2 tm3464 mutant. | ||||
Sequence: P → L | ||||||
Mutagenesis | 588 | In MN103 and MN151; 96% lethal. | ||||
Sequence: G → R | ||||||
Mutagenesis | 597 | In MN152; 50% lethal. | ||||
Sequence: G → R | ||||||
Mutagenesis | 690 | In MN129; 100% lethal. | ||||
Sequence: G → E | ||||||
Mutagenesis | 690 | In MN101; 100% lethal. | ||||
Sequence: G → R | ||||||
Mutagenesis | 737 | In MN143; 100% lethal. | ||||
Sequence: G → E | ||||||
Mutagenesis | 877 | In g30; temperature-sensitive mutant. At the restrictive temperature, causes 90 percent lethality. At the permissive temperature of 16 degrees Celsius, causes the formation of ectopic presynaptic boutons on the ventral cord axons. | ||||
Sequence: G → R | ||||||
Mutagenesis | 904 | In E1470; 94% lethal. | ||||
Sequence: G → R | ||||||
Mutagenesis | 1003 | In MN139; 20% lethal. | ||||
Sequence: G → E | ||||||
Mutagenesis | 1125 | In g25; temperature-sensitive mutant. At the restrictive temperature of 25 degrees Celsius, causes 96 percent embryonic lethality. At the permissive temperature of 22.5 degrees Celsius, partially restores normal distal tip cell migration in a mig-17 (k174) mutant background. | ||||
Sequence: G → D | ||||||
Mutagenesis | 1152 | In MN147; 7% lethal. | ||||
Sequence: G → D | ||||||
Mutagenesis | 1286 | In g37 and b246; 9% lethal. Moderate reduction in basement membrane localization associated with a moderate accumulation in muscle cell cytoplasm. At the restrictive temperature of 25 degrees Celsius, causes a reduction of nid-1 recruitment to the gonad basement membrane. At the permissive temperature of 22.5 degrees Celsius, partially restores normal distal tip cell migration in a mig-17 (k174) mutant background. | ||||
Sequence: G → D | ||||||
Mutagenesis | 1465 | In k196; temperature-sensitive mutant. At the restrictive temperature of 25 degrees Celsius, causes 85 percent larval lethality. Slight reduction in basement membrane localization associated with a slight intracellular accumulation in muscle and distal tip cells (DTC). In a mig-17 (k174) mutant background, restores normal DTC migration and nid-1 basement membrane localization. | ||||
Sequence: G → R | ||||||
Mutagenesis | 1610 | In k193; temperature-sensitive mutant. At both the restrictive and permissive temperatures, causes 16-20 percent embryonic lethality. Slight reduction in basement membrane localization associated with a slight intracellular accumulation in muscle and distal tip cells (DTC). In a mig-17 (k174) mutant background, restores normal DTC migration and nid-1 basement membrane localization. Enhances the lethality of the pxn-2 mutant (ju432). | ||||
Sequence: S → L |
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-26 | |||||
Sequence: MKQRAALGPVLRLAILALLAVSYVQS | ||||||
Chain | PRO_0000005829 | 27-1758 | Collagen alpha-2(IV) chain | |||
Sequence: QATCRDCSNRGCFCVGEKGSMGAPGPQGPPGTQGIRGFPGPEGLAGPKGLKGAQGPPGPVGIKGDRGAVGVPGFPGNDGGNGRPGEPGPPGAPGWDGCNGTDGAPGIPGRPGPPGMPGFPGPPGMDGLKGEPAIGYAGAPGEKGDGGMPGMPGLPGPSGRDGYPGEKGDRGDTGNAGPRGPPGEAGSPGNPGIGSIGPKGDPGDLGSVGPPGPPGPREFTGSGSIVGPRGNPGEKGDKGEPGEGGQRGYPGNGGLSGQPGLPGMKGEKGLSGPAGPRGKEGRPGNAGPPGFKGDRGLDGLGGIPGLPGQKGEAGYPGRDGPKGNSGPPGPPGGGTFNDGAPGPPGLPGRPGNPGPPGTDGYPGAPGPAGPIGNTGGPGLPGYPGNEGLPGPKGDKGDGGIPGAPGVSGPSGIPGLPGPKGEPGYRGTPGQSIPGLPGKDGKPGLDGAPGRKGENGLPGVRGPPGDSLNGLPGAPGQRGAPGPNGYDGRDGVNGLPGAPGTKGDRGGTCSACAPGTKGEKGLPGYSGQPGPQGDRGLPGMPGPVGDAGDDGLPGPAGRPGSPGPPGQDGFPGLPGQKGEPTQLTLRPGPPGYPGLKGENGFPGQPGVDGLPGPSGPVGPPGAPGYPGEKGDAGLPGLSGKPGQDGLPGLPGNKGEAGYGQPGQPGFPGAKGDGGLPGLPGTPGLQGMPGEPAPENQVNPAPPGQPGLPGLPGTKGEGGYPGRPGEVGQPGFPGLPGMKGDSGLPGPPGLPGHPGVPGDKGFGGVPGLPGIPGPKGDVGNPGLPGLNGQKGEPGVGVPGQPGSPGFPGLKGDAGLPGLPGTPGLEGQRGFPGAPGLKGGDGLPGLSGQPGYPGEKGDAGLPGVPGREGSPGFPGQDGLPGVPGMKGEDGLPGLPGVTGLKGDLGAPGQSGAPGLPGAPGYPGMKGNAGIPGVPGFKGDGGLPGLPGLNGPKGEPGVPGMPGTPGMKGNGGLPGLPGRDGLSGVPGMKGDRGFNGLPGEKGEAGPAARDGQKGDAGLPGQPGLRGPQGPSGLPGVPGFKGETGLPGYGQPGQPGEKGLPGIPGKAGRQGAPGSPGQDGLPGFPGMKGESGYPGQDGLPGRDGLPGVPGQKGDLGQSGQPGLSGAPGLDGQPGVPGIRGDKGQGGLPGIPGDRGMDGYPGQKGENGYPGQPGLPGLGGEKGFAGTPGFPGLKGSPGYPGQDGLPGIPGLKGDSGFPGQPGQEGLPGLSGEKGMGGLPGMPGQPGQSIAGPVGPPGAPGLQGKDGFPGLPGQKGESGLSGLPGAPGLKGESGMPGFPGAKGDLGANGIPGKRGEDGLPGVPGRDGQPGIPGLKGEVGGAGLPGQPGFPGIPGLKGEGGLPGFPGAKGEAGFPGTPGVPGYAGEKGDGGLPGLPGRDGLPGADGPVGPPGPSGPQNLVEPGEKGLPGLPGAPGLRGEKGMPGLDGPPGNDGPPGLPGQRGNDGYPGAPGLSGEKGMGGLPGFPGLDGQPGGPGAPGLPGAPGAAGPAYRDGFVLVKHSQTTEVPRCPEGQTKLWDGYSLLYIEGNEKSHNQDLGHAGSCLQRFSTMPFLFCDFNNVCNYASRNEKSYWLSTSEAIPMMPVNEREIEPYISRCAVCEAPANTIAVHSQTIQIPNCPAGWSSLWIGYSFAMHTGAGAEGGGQSPSSPGSCLEDFRATPFIECNGARGSCHYFANKFSFWLTTIDNDSEFKVPESQTLKSGNLRTRVSRCQVCVKSTDGRH | ||||||
Glycosylation | 248 | O-linked (Xyl...) (glycosaminoglycan) serine | ||||
Sequence: S | ||||||
Disulfide bond | 1546↔1635 | |||||
Sequence: CPEGQTKLWDGYSLLYIEGNEKSHNQDLGHAGSCLQRFSTMPFLFCDFNNVCNYASRNEKSYWLSTSEAIPMMPVNEREIEPYISRCAVC | ||||||
Disulfide bond | 1579↔1632 | |||||
Sequence: CLQRFSTMPFLFCDFNNVCNYASRNEKSYWLSTSEAIPMMPVNEREIEPYISRC | ||||||
Disulfide bond | 1591↔1597 | |||||
Sequence: CDFNNVC | ||||||
Disulfide bond | 1654↔1750 | |||||
Sequence: CPAGWSSLWIGYSFAMHTGAGAEGGGQSPSSPGSCLEDFRATPFIECNGARGSCHYFANKFSFWLTTIDNDSEFKVPESQTLKSGNLRTRVSRCQVC | ||||||
Disulfide bond | 1688↔1747 | |||||
Sequence: CLEDFRATPFIECNGARGSCHYFANKFSFWLTTIDNDSEFKVPESQTLKSGNLRTRVSRC | ||||||
Disulfide bond | 1700↔1707 | |||||
Sequence: CNGARGSC |
Post-translational modification
Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
Type IV collagens contain numerous cysteine residues which are involved in inter- and intramolecular disulfide bonding. 12 of these, located in the NC1 domain, are conserved in all known type IV collagens.
The trimeric structure of the NC1 domains is stabilized by covalent bonds between Lys and Met residues.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Localizes to the basement membrane between distal tip cells and the germline. Localizes to the intestinal basement membrane.
Developmental stage
Alternatively spliced, in part by RNA-binding protein asd-2, to produce isoforms which are expressed at different developmental stages (PubMed:18230701).
Isoform a: Predominantly expressed in embryos (PubMed:18230701, PubMed:7691828).
Isoform b: Predominantly expressed in larvae and adults (PubMed:18230701, PubMed:7691828).
Isoform a: Predominantly expressed in embryos (PubMed:18230701, PubMed:7691828).
Isoform b: Predominantly expressed in larvae and adults (PubMed:18230701, PubMed:7691828).
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 27-42 | 7S domain | ||||
Sequence: QATCRDCSNRGCFCVG | ||||||
Region | 42-1527 | Triple-helical region | ||||
Sequence: GEKGSMGAPGPQGPPGTQGIRGFPGPEGLAGPKGLKGAQGPPGPVGIKGDRGAVGVPGFPGNDGGNGRPGEPGPPGAPGWDGCNGTDGAPGIPGRPGPPGMPGFPGPPGMDGLKGEPAIGYAGAPGEKGDGGMPGMPGLPGPSGRDGYPGEKGDRGDTGNAGPRGPPGEAGSPGNPGIGSIGPKGDPGDLGSVGPPGPPGPREFTGSGSIVGPRGNPGEKGDKGEPGEGGQRGYPGNGGLSGQPGLPGMKGEKGLSGPAGPRGKEGRPGNAGPPGFKGDRGLDGLGGIPGLPGQKGEAGYPGRDGPKGNSGPPGPPGGGTFNDGAPGPPGLPGRPGNPGPPGTDGYPGAPGPAGPIGNTGGPGLPGYPGNEGLPGPKGDKGDGGIPGAPGVSGPSGIPGLPGPKGEPGYRGTPGQSIPGLPGKDGKPGLDGAPGRKGENGLPGVRGPPGDSLNGLPGAPGQRGAPGPNGYDGRDGVNGLPGAPGTKGDRGGTCSACAPGTKGEKGLPGYSGQPGPQGDRGLPGMPGPVGDAGDDGLPGPAGRPGSPGPPGQDGFPGLPGQKGEPTQLTLRPGPPGYPGLKGENGFPGQPGVDGLPGPSGPVGPPGAPGYPGEKGDAGLPGLSGKPGQDGLPGLPGNKGEAGYGQPGQPGFPGAKGDGGLPGLPGTPGLQGMPGEPAPENQVNPAPPGQPGLPGLPGTKGEGGYPGRPGEVGQPGFPGLPGMKGDSGLPGPPGLPGHPGVPGDKGFGGVPGLPGIPGPKGDVGNPGLPGLNGQKGEPGVGVPGQPGSPGFPGLKGDAGLPGLPGTPGLEGQRGFPGAPGLKGGDGLPGLSGQPGYPGEKGDAGLPGVPGREGSPGFPGQDGLPGVPGMKGEDGLPGLPGVTGLKGDLGAPGQSGAPGLPGAPGYPGMKGNAGIPGVPGFKGDGGLPGLPGLNGPKGEPGVPGMPGTPGMKGNGGLPGLPGRDGLSGVPGMKGDRGFNGLPGEKGEAGPAARDGQKGDAGLPGQPGLRGPQGPSGLPGVPGFKGETGLPGYGQPGQPGEKGLPGIPGKAGRQGAPGSPGQDGLPGFPGMKGESGYPGQDGLPGRDGLPGVPGQKGDLGQSGQPGLSGAPGLDGQPGVPGIRGDKGQGGLPGIPGDRGMDGYPGQKGENGYPGQPGLPGLGGEKGFAGTPGFPGLKGSPGYPGQDGLPGIPGLKGDSGFPGQPGQEGLPGLSGEKGMGGLPGMPGQPGQSIAGPVGPPGAPGLQGKDGFPGLPGQKGESGLSGLPGAPGLKGESGMPGFPGAKGDLGANGIPGKRGEDGLPGVPGRDGQPGIPGLKGEVGGAGLPGQPGFPGIPGLKGEGGLPGFPGAKGEAGFPGTPGVPGYAGEKGDGGLPGLPGRDGLPGADGPVGPPGPSGPQNLVEPGEKGLPGLPGAPGLRGEKGMPGLDGPPGNDGPPGLPGQRGNDGYPGAPGLSGEKGMGGLPGFPGLDGQPGGPGAPGLPGAPGAAGPA | ||||||
Region | 47-943 | Disordered | ||||
Sequence: MGAPGPQGPPGTQGIRGFPGPEGLAGPKGLKGAQGPPGPVGIKGDRGAVGVPGFPGNDGGNGRPGEPGPPGAPGWDGCNGTDGAPGIPGRPGPPGMPGFPGPPGMDGLKGEPAIGYAGAPGEKGDGGMPGMPGLPGPSGRDGYPGEKGDRGDTGNAGPRGPPGEAGSPGNPGIGSIGPKGDPGDLGSVGPPGPPGPREFTGSGSIVGPRGNPGEKGDKGEPGEGGQRGYPGNGGLSGQPGLPGMKGEKGLSGPAGPRGKEGRPGNAGPPGFKGDRGLDGLGGIPGLPGQKGEAGYPGRDGPKGNSGPPGPPGGGTFNDGAPGPPGLPGRPGNPGPPGTDGYPGAPGPAGPIGNTGGPGLPGYPGNEGLPGPKGDKGDGGIPGAPGVSGPSGIPGLPGPKGEPGYRGTPGQSIPGLPGKDGKPGLDGAPGRKGENGLPGVRGPPGDSLNGLPGAPGQRGAPGPNGYDGRDGVNGLPGAPGTKGDRGGTCSACAPGTKGEKGLPGYSGQPGPQGDRGLPGMPGPVGDAGDDGLPGPAGRPGSPGPPGQDGFPGLPGQKGEPTQLTLRPGPPGYPGLKGENGFPGQPGVDGLPGPSGPVGPPGAPGYPGEKGDAGLPGLSGKPGQDGLPGLPGNKGEAGYGQPGQPGFPGAKGDGGLPGLPGTPGLQGMPGEPAPENQVNPAPPGQPGLPGLPGTKGEGGYPGRPGEVGQPGFPGLPGMKGDSGLPGPPGLPGHPGVPGDKGFGGVPGLPGIPGPKGDVGNPGLPGLNGQKGEPGVGVPGQPGSPGFPGLKGDAGLPGLPGTPGLEGQRGFPGAPGLKGGDGLPGLSGQPGYPGEKGDAGLPGVPGREGSPGFPGQDGLPGVPGMKGEDGLPGLPGVTGLKGDLGAPGQSGAPGLPGAPG | ||||||
Compositional bias | 133-147 | Pro residues | ||||
Sequence: IPGRPGPPGMPGFPG | ||||||
Compositional bias | 369-389 | Pro residues | ||||
Sequence: PPGLPGRPGNPGPPGTDGYPG | ||||||
Compositional bias | 719-733 | Pro residues | ||||
Sequence: ENQVNPAPPGQPGLP | ||||||
Region | 955-1304 | Disordered | ||||
Sequence: GVPGFKGDGGLPGLPGLNGPKGEPGVPGMPGTPGMKGNGGLPGLPGRDGLSGVPGMKGDRGFNGLPGEKGEAGPAARDGQKGDAGLPGQPGLRGPQGPSGLPGVPGFKGETGLPGYGQPGQPGEKGLPGIPGKAGRQGAPGSPGQDGLPGFPGMKGESGYPGQDGLPGRDGLPGVPGQKGDLGQSGQPGLSGAPGLDGQPGVPGIRGDKGQGGLPGIPGDRGMDGYPGQKGENGYPGQPGLPGLGGEKGFAGTPGFPGLKGSPGYPGQDGLPGIPGLKGDSGFPGQPGQEGLPGLSGEKGMGGLPGMPGQPGQSIAGPVGPPGAPGLQGKDGFPGLPGQKGESGLSGLPG | ||||||
Region | 1316-1339 | Disordered | ||||
Sequence: GFPGAKGDLGANGIPGKRGEDGLP | ||||||
Region | 1367-1525 | Disordered | ||||
Sequence: GFPGIPGLKGEGGLPGFPGAKGEAGFPGTPGVPGYAGEKGDGGLPGLPGRDGLPGADGPVGPPGPSGPQNLVEPGEKGLPGLPGAPGLRGEKGMPGLDGPPGNDGPPGLPGQRGNDGYPGAPGLSGEKGMGGLPGFPGLDGQPGGPGAPGLPGAPGAAG | ||||||
Domain | 1531-1754 | Collagen IV NC1 | ||||
Sequence: GFVLVKHSQTTEVPRCPEGQTKLWDGYSLLYIEGNEKSHNQDLGHAGSCLQRFSTMPFLFCDFNNVCNYASRNEKSYWLSTSEAIPMMPVNEREIEPYISRCAVCEAPANTIAVHSQTIQIPNCPAGWSSLWIGYSFAMHTGAGAEGGGQSPSSPGSCLEDFRATPFIECNGARGSCHYFANKFSFWLTTIDNDSEFKVPESQTLKSGNLRTRVSRCQVCVKST |
Domain
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.
Sequence similarities
Belongs to the type IV collagen family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing. Exons 9 and 10 are mutually exclusive splicing exons. There is alternative usage of either exon 9 (isoform a) or exon 10 (isoform b).
P17140-1
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.
- Namea
- SynonymsI
- Length1,758
- Mass (Da)167,751
- Last updated1994-10-01 v2
- Checksum97EE3F3DBB2D2AC5
P17140-2
- Nameb
- SynonymsII
- Differences from canonical
- 229-264: GDLGSVGPPGPPGPREFTGSGSIVGPRGNPGEKGDK → GDIGAMGPAGPPGPIASTMSKGTIIGPKGDLGEKGEK
Sequence caution
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 133-147 | Pro residues | ||||
Sequence: IPGRPGPPGMPGFPG | ||||||
Alternative sequence | VSP_001160 | 229-264 | in isoform b | |||
Sequence: GDLGSVGPPGPPGPREFTGSGSIVGPRGNPGEKGDK → GDIGAMGPAGPPGPIASTMSKGTIIGPKGDLGEKGEK | ||||||
Compositional bias | 369-389 | Pro residues | ||||
Sequence: PPGLPGRPGNPGPPGTDGYPG | ||||||
Compositional bias | 719-733 | Pro residues | ||||
Sequence: ENQVNPAPPGQPGLP | ||||||
Sequence conflict | 1604 | in Ref. 2; CCD68907/CCD68906 | ||||
Sequence: E → D | ||||||
Sequence conflict | 1682 | in Ref. 2; CCD68907/CCD68906 | ||||
Sequence: P → L |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Z22964 EMBL· GenBank· DDBJ | CAA80536.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z22964 EMBL· GenBank· DDBJ | CAA80537.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U22327 EMBL· GenBank· DDBJ | AAA64312.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
BX284606 EMBL· GenBank· DDBJ | CCD68907.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BX284606 EMBL· GenBank· DDBJ | CCD68906.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
J05066 EMBL· GenBank· DDBJ | AAA27989.1 EMBL· GenBank· DDBJ | Genomic DNA |