Q90584 · COHA1_CHICK
- ProteinCollagen alpha-1(XVII) chain
- GeneCOL17A1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1495 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
May play a role in the integrity of hemidesmosome and the attachment of basal keratinocytes to the underlying basement membrane.
The 120 kDa linear IgA disease antigen homolog is an anchoring filament component involved in dermal-epidermal cohesion.
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 trimer | |
Cellular Component | collagen-containing extracellular matrix | |
Cellular Component | extracellular space | |
Cellular Component | hemidesmosome | |
Cellular Component | membrane | |
Molecular Function | extracellular matrix structural constituent conferring tensile strength | |
Molecular Function | heparin binding | |
Biological Process | extracellular matrix organization |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCollagen alpha-1(XVII) chain
- Alternative names
- Cleaved into 1 chains
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Galloanserae > Galliformes > Phasianidae > Phasianinae > Gallus
Accessions
- Primary accessionQ90584
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Single-pass type II membrane protein
Note: Localized along the plasma membrane of the hemidesmosome.
120 kDa linear IgA disease antigen homolog
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-435 | Cytoplasmic | ||||
Sequence: MDSVTKKTRQDGSEVTERQGGSSSGLKTSSHTGGSGVEKRSYTHSSGYVTSSGSGRLNSSSSGYRQTQSPSSTLTKSPGSTFERKTYVNRHATYEGSSSANSSPEFPRKEFASASTRGRSQSRESEIRVRLQSASPSGRWTELDDVKRLLKGSRSASCSPTRSSSSTLPIPKKAVVETKMVTESSQSVSGTYDTTILNTTLPPYTWSSTLPAGSSLGGYHNSMGQSSSLINAMSHSTGSVFGVPNNLAPSSHALNTGLSTSSTVFGVQNNLSPSSSALNASAASAAYGMKNTSQTNTMNSTGVSASAGGTILSSQGDDFLHKDCKFLLLEKENAPAKKEMELLVMTKDSGKVFSASSTGLNGGSFAEDTLKKEKQGLSSYAADTGLKSDANGGLKSAPTRDKATYAEIQNGGAGGAIGSAPSWCPCGSCCSWWKW | ||||||
Transmembrane | 436-456 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: LLGLLLAWLLLLGLLFGLIAL | ||||||
Topological domain | 457-1495 | Extracellular | ||||
Sequence: AEEVRKLKSRVDNLEKINHSFLTVNQGNPYLEKDVSKVDFLHGVAPSSTFPFENEESVWLMVKSRLNKEIERGYFRGERGEPGMKGDMGLQGPKGDRGLPGVPGIPGPVGHQGPEGPKGQKGSMGDPGMEGPMGQRGREGLPGPRGEPGPPGFGEKGDRGAAGPPGPPGPPGSAGLKGPMGSPGPQGPPGPPGLQGFRGEAGLPGAKGEKGATGPPGPKGDQGEKGARGMTGEQGSRGIPGPPGEPGAKGPAGQAGRDGQPGERGEPGLMGMPGARGPPGPSGDTGEPGLTGPQGPPGLPGNPGRPGAKGEPGAPGKVISAEGSSTIALPGPPGPPGPIGPTGPPGVPGPVGPAGLPGQQGPRGEKGSAGEVVIETIKTEVSSLASQMLSDLQGRAGPPGPPGPPGESVQGLPGPRGPPGLPGPSGPPGRPGSSVSTSETFVSGPPGPPGPPGPKGDQGEPGPRGFTGEPGEPGLPGFSSHGGTVTMQGPPGPPGPPGPKGDAGVPGAPGIPGTSRGGSRQIQGPPGPPGPPGPPGPGGSSSQEIQQYVADYLKSDNVRHYLTGVQGPPGPPGPPGILTTADGKNFDFAELATRVMSYVTSSSDHYQSFASSVSTTSVLYQELLNMLQREEIRQYLVGPRGPPGPPGPGVDGMSLSLDYDELTRRFISYLTSSGMSIGLPGPPGPPGTPGISYSELTAYLRNSEFSGLVGPPGPAGPPGPPGIPGSSGISLEDISAYLQSVGYSSISGIQGPPGPPGPPGPPGFSGTGLLSYADITHSDEFRSELIQYLKSDEVRSYISGPPGPPGPRGPPGPKGDSGLVAGSMSSLYHDSLASERLHGGSIGAEGSHGGSLGASSSYGSSMSSSMSSYSASMGSDGSYGASVGSDGSFDGLLTAEESHRRSAGPGRSYSSSFTGSLDYNELARHVSENLQSRGILQDLMSYTGQGPPGPPGPPGPPGISRVFAAYGNVTEDLMDFFRTHGTVRGPPGEKGERGYPGPKGDPGPMGPPGRHGQRGPKGEKGEKGEQMYSGRRRRRSVGV |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000059409 | 1-1495 | Collagen alpha-1(XVII) chain | |||
Sequence: MDSVTKKTRQDGSEVTERQGGSSSGLKTSSHTGGSGVEKRSYTHSSGYVTSSGSGRLNSSSSGYRQTQSPSSTLTKSPGSTFERKTYVNRHATYEGSSSANSSPEFPRKEFASASTRGRSQSRESEIRVRLQSASPSGRWTELDDVKRLLKGSRSASCSPTRSSSSTLPIPKKAVVETKMVTESSQSVSGTYDTTILNTTLPPYTWSSTLPAGSSLGGYHNSMGQSSSLINAMSHSTGSVFGVPNNLAPSSHALNTGLSTSSTVFGVQNNLSPSSSALNASAASAAYGMKNTSQTNTMNSTGVSASAGGTILSSQGDDFLHKDCKFLLLEKENAPAKKEMELLVMTKDSGKVFSASSTGLNGGSFAEDTLKKEKQGLSSYAADTGLKSDANGGLKSAPTRDKATYAEIQNGGAGGAIGSAPSWCPCGSCCSWWKWLLGLLLAWLLLLGLLFGLIALAEEVRKLKSRVDNLEKINHSFLTVNQGNPYLEKDVSKVDFLHGVAPSSTFPFENEESVWLMVKSRLNKEIERGYFRGERGEPGMKGDMGLQGPKGDRGLPGVPGIPGPVGHQGPEGPKGQKGSMGDPGMEGPMGQRGREGLPGPRGEPGPPGFGEKGDRGAAGPPGPPGPPGSAGLKGPMGSPGPQGPPGPPGLQGFRGEAGLPGAKGEKGATGPPGPKGDQGEKGARGMTGEQGSRGIPGPPGEPGAKGPAGQAGRDGQPGERGEPGLMGMPGARGPPGPSGDTGEPGLTGPQGPPGLPGNPGRPGAKGEPGAPGKVISAEGSSTIALPGPPGPPGPIGPTGPPGVPGPVGPAGLPGQQGPRGEKGSAGEVVIETIKTEVSSLASQMLSDLQGRAGPPGPPGPPGESVQGLPGPRGPPGLPGPSGPPGRPGSSVSTSETFVSGPPGPPGPPGPKGDQGEPGPRGFTGEPGEPGLPGFSSHGGTVTMQGPPGPPGPPGPKGDAGVPGAPGIPGTSRGGSRQIQGPPGPPGPPGPPGPGGSSSQEIQQYVADYLKSDNVRHYLTGVQGPPGPPGPPGILTTADGKNFDFAELATRVMSYVTSSSDHYQSFASSVSTTSVLYQELLNMLQREEIRQYLVGPRGPPGPPGPGVDGMSLSLDYDELTRRFISYLTSSGMSIGLPGPPGPPGTPGISYSELTAYLRNSEFSGLVGPPGPAGPPGPPGIPGSSGISLEDISAYLQSVGYSSISGIQGPPGPPGPPGPPGFSGTGLLSYADITHSDEFRSELIQYLKSDEVRSYISGPPGPPGPRGPPGPKGDSGLVAGSMSSLYHDSLASERLHGGSIGAEGSHGGSLGASSSYGSSMSSSMSSYSASMGSDGSYGASVGSDGSFDGLLTAEESHRRSAGPGRSYSSSFTGSLDYNELARHVSENLQSRGILQDLMSYTGQGPPGPPGPPGPPGISRVFAAYGNVTEDLMDFFRTHGTVRGPPGEKGERGYPGPKGDPGPMGPPGRHGQRGPKGEKGEKGEQMYSGRRRRRSVGV | ||||||
Chain | PRO_0000342559 | 497-1495 | 120 kDa linear IgA disease antigen homolog | |||
Sequence: LHGVAPSSTFPFENEESVWLMVKSRLNKEIERGYFRGERGEPGMKGDMGLQGPKGDRGLPGVPGIPGPVGHQGPEGPKGQKGSMGDPGMEGPMGQRGREGLPGPRGEPGPPGFGEKGDRGAAGPPGPPGPPGSAGLKGPMGSPGPQGPPGPPGLQGFRGEAGLPGAKGEKGATGPPGPKGDQGEKGARGMTGEQGSRGIPGPPGEPGAKGPAGQAGRDGQPGERGEPGLMGMPGARGPPGPSGDTGEPGLTGPQGPPGLPGNPGRPGAKGEPGAPGKVISAEGSSTIALPGPPGPPGPIGPTGPPGVPGPVGPAGLPGQQGPRGEKGSAGEVVIETIKTEVSSLASQMLSDLQGRAGPPGPPGPPGESVQGLPGPRGPPGLPGPSGPPGRPGSSVSTSETFVSGPPGPPGPPGPKGDQGEPGPRGFTGEPGEPGLPGFSSHGGTVTMQGPPGPPGPPGPKGDAGVPGAPGIPGTSRGGSRQIQGPPGPPGPPGPPGPGGSSSQEIQQYVADYLKSDNVRHYLTGVQGPPGPPGPPGILTTADGKNFDFAELATRVMSYVTSSSDHYQSFASSVSTTSVLYQELLNMLQREEIRQYLVGPRGPPGPPGPGVDGMSLSLDYDELTRRFISYLTSSGMSIGLPGPPGPPGTPGISYSELTAYLRNSEFSGLVGPPGPAGPPGPPGIPGSSGISLEDISAYLQSVGYSSISGIQGPPGPPGPPGPPGFSGTGLLSYADITHSDEFRSELIQYLKSDEVRSYISGPPGPPGPRGPPGPKGDSGLVAGSMSSLYHDSLASERLHGGSIGAEGSHGGSLGASSSYGSSMSSSMSSYSASMGSDGSYGASVGSDGSFDGLLTAEESHRRSAGPGRSYSSSFTGSLDYNELARHVSENLQSRGILQDLMSYTGQGPPGPPGPPGPPGISRVFAAYGNVTEDLMDFFRTHGTVRGPPGEKGERGYPGPKGDPGPMGPPGRHGQRGPKGEKGEKGEQMYSGRRRRRSVGV | ||||||
Glycosylation | 1424 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
The intracellular/endo domain is disulfide-linked.
Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
The ectodomain is shedded from the surface of keratinocytes resulting in a 120-kDa soluble form, also named as 120 kDa linear IgA disease antigen homolog. The shedding is mediated by membrane-bound metalloproteases (By similarity).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-138 | Disordered | ||||
Sequence: MDSVTKKTRQDGSEVTERQGGSSSGLKTSSHTGGSGVEKRSYTHSSGYVTSSGSGRLNSSSSGYRQTQSPSSTLTKSPGSTFERKTYVNRHATYEGSSSANSSPEFPRKEFASASTRGRSQSRESEIRVRLQSASPSG | ||||||
Region | 1-535 | Nonhelical region (NC16) | ||||
Sequence: MDSVTKKTRQDGSEVTERQGGSSSGLKTSSHTGGSGVEKRSYTHSSGYVTSSGSGRLNSSSSGYRQTQSPSSTLTKSPGSTFERKTYVNRHATYEGSSSANSSPEFPRKEFASASTRGRSQSRESEIRVRLQSASPSGRWTELDDVKRLLKGSRSASCSPTRSSSSTLPIPKKAVVETKMVTESSQSVSGTYDTTILNTTLPPYTWSSTLPAGSSLGGYHNSMGQSSSLINAMSHSTGSVFGVPNNLAPSSHALNTGLSTSSTVFGVQNNLSPSSSALNASAASAAYGMKNTSQTNTMNSTGVSASAGGTILSSQGDDFLHKDCKFLLLEKENAPAKKEMELLVMTKDSGKVFSASSTGLNGGSFAEDTLKKEKQGLSSYAADTGLKSDANGGLKSAPTRDKATYAEIQNGGAGGAIGSAPSWCPCGSCCSWWKWLLGLLLAWLLLLGLLFGLIALAEEVRKLKSRVDNLEKINHSFLTVNQGNPYLEKDVSKVDFLHGVAPSSTFPFENEESVWLMVKSRLNKEIERGYFRGER | ||||||
Compositional bias | 15-120 | Polar residues | ||||
Sequence: VTERQGGSSSGLKTSSHTGGSGVEKRSYTHSSGYVTSSGSGRLNSSSSGYRQTQSPSSTLTKSPGSTFERKTYVNRHATYEGSSSANSSPEFPRKEFASASTRGRS | ||||||
Region | 532-824 | Disordered | ||||
Sequence: RGERGEPGMKGDMGLQGPKGDRGLPGVPGIPGPVGHQGPEGPKGQKGSMGDPGMEGPMGQRGREGLPGPRGEPGPPGFGEKGDRGAAGPPGPPGPPGSAGLKGPMGSPGPQGPPGPPGLQGFRGEAGLPGAKGEKGATGPPGPKGDQGEKGARGMTGEQGSRGIPGPPGEPGAKGPAGQAGRDGQPGERGEPGLMGMPGARGPPGPSGDTGEPGLTGPQGPPGLPGNPGRPGAKGEPGAPGKVISAEGSSTIALPGPPGPPGPIGPTGPPGVPGPVGPAGLPGQQGPRGEKGS | ||||||
Region | 536-1482 | Triple-helical region | ||||
Sequence: GEPGMKGDMGLQGPKGDRGLPGVPGIPGPVGHQGPEGPKGQKGSMGDPGMEGPMGQRGREGLPGPRGEPGPPGFGEKGDRGAAGPPGPPGPPGSAGLKGPMGSPGPQGPPGPPGLQGFRGEAGLPGAKGEKGATGPPGPKGDQGEKGARGMTGEQGSRGIPGPPGEPGAKGPAGQAGRDGQPGERGEPGLMGMPGARGPPGPSGDTGEPGLTGPQGPPGLPGNPGRPGAKGEPGAPGKVISAEGSSTIALPGPPGPPGPIGPTGPPGVPGPVGPAGLPGQQGPRGEKGSAGEVVIETIKTEVSSLASQMLSDLQGRAGPPGPPGPPGESVQGLPGPRGPPGLPGPSGPPGRPGSSVSTSETFVSGPPGPPGPPGPKGDQGEPGPRGFTGEPGEPGLPGFSSHGGTVTMQGPPGPPGPPGPKGDAGVPGAPGIPGTSRGGSRQIQGPPGPPGPPGPPGPGGSSSQEIQQYVADYLKSDNVRHYLTGVQGPPGPPGPPGILTTADGKNFDFAELATRVMSYVTSSSDHYQSFASSVSTTSVLYQELLNMLQREEIRQYLVGPRGPPGPPGPGVDGMSLSLDYDELTRRFISYLTSSGMSIGLPGPPGPPGTPGISYSELTAYLRNSEFSGLVGPPGPAGPPGPPGIPGSSGISLEDISAYLQSVGYSSISGIQGPPGPPGPPGPPGFSGTGLLSYADITHSDEFRSELIQYLKSDEVRSYISGPPGPPGPRGPPGPKGDSGLVAGSMSSLYHDSLASERLHGGSIGAEGSHGGSLGASSSYGSSMSSSMSSYSASMGSDGSYGASVGSDGSFDGLLTAEESHRRSAGPGRSYSSSFTGSLDYNELARHVSENLQSRGILQDLMSYTGQGPPGPPGPPGPPGISRVFAAYGNVTEDLMDFFRTHGTVRGPPGEKGERGYPGPKGDPGPMGPPGRHGQRGPKGEKGEKGEQ | ||||||
Compositional bias | 785-808 | Pro residues | ||||
Sequence: LPGPPGPPGPIGPTGPPGVPGPVG | ||||||
Region | 847-999 | Disordered | ||||
Sequence: DLQGRAGPPGPPGPPGESVQGLPGPRGPPGLPGPSGPPGRPGSSVSTSETFVSGPPGPPGPPGPKGDQGEPGPRGFTGEPGEPGLPGFSSHGGTVTMQGPPGPPGPPGPKGDAGVPGAPGIPGTSRGGSRQIQGPPGPPGPPGPPGPGGSSSQ | ||||||
Compositional bias | 853-885 | Pro residues | ||||
Sequence: GPPGPPGPPGESVQGLPGPRGPPGLPGPSGPPG | ||||||
Compositional bias | 900-914 | Pro residues | ||||
Sequence: GPPGPPGPPGPKGDQ | ||||||
Compositional bias | 945-959 | Pro residues | ||||
Sequence: GPPGPPGPPGPKGDA | ||||||
Compositional bias | 980-994 | Pro residues | ||||
Sequence: GPPGPPGPPGPPGPG | ||||||
Region | 1160-1185 | Disordered | ||||
Sequence: EFSGLVGPPGPAGPPGPPGIPGSSGI | ||||||
Region | 1201-1226 | Disordered | ||||
Sequence: SISGIQGPPGPPGPPGPPGFSGTGLL | ||||||
Region | 1251-1278 | Disordered | ||||
Sequence: RSYISGPPGPPGPRGPPGPKGDSGLVAG | ||||||
Region | 1295-1336 | Disordered | ||||
Sequence: GGSIGAEGSHGGSLGASSSYGSSMSSSMSSYSASMGSDGSYG | ||||||
Compositional bias | 1306-1336 | Polar residues | ||||
Sequence: GSLGASSSYGSSMSSSMSSYSASMGSDGSYG | ||||||
Region | 1396-1416 | Disordered | ||||
Sequence: MSYTGQGPPGPPGPPGPPGIS | ||||||
Region | 1435-1495 | Disordered | ||||
Sequence: THGTVRGPPGEKGERGYPGPKGDPGPMGPPGRHGQRGPKGEKGEKGEQMYSGRRRRRSVGV | ||||||
Compositional bias | 1469-1488 | Basic and acidic residues | ||||
Sequence: QRGPKGEKGEKGEQMYSGRR | ||||||
Region | 1483-1495 | Nonhelical region (NC1) | ||||
Sequence: MYSGRRRRRSVGV |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,495
- Mass (Da)151,204
- Last updated2008-07-01 v2
- ChecksumBE8D8BE3A02BCC0F
Sequence caution
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 15-120 | Polar residues | ||||
Sequence: VTERQGGSSSGLKTSSHTGGSGVEKRSYTHSSGYVTSSGSGRLNSSSSGYRQTQSPSSTLTKSPGSTFERKTYVNRHATYEGSSSANSSPEFPRKEFASASTRGRS | ||||||
Sequence conflict | 384 | in Ref. 2; AAA48703 | ||||
Sequence: T → P | ||||||
Sequence conflict | 617 | in Ref. 2; AAA48703 | ||||
Sequence: A → P | ||||||
Sequence conflict | 684 | in Ref. 2; AAA48703 | ||||
Sequence: R → H | ||||||
Sequence conflict | 728 | in Ref. 2; AAA48703 | ||||
Sequence: M → I | ||||||
Compositional bias | 785-808 | Pro residues | ||||
Sequence: LPGPPGPPGPIGPTGPPGVPGPVG | ||||||
Sequence conflict | 826 | in Ref. 2; AAA48703 | ||||
Sequence: G → V | ||||||
Compositional bias | 853-885 | Pro residues | ||||
Sequence: GPPGPPGPPGESVQGLPGPRGPPGLPGPSGPPG | ||||||
Compositional bias | 900-914 | Pro residues | ||||
Sequence: GPPGPPGPPGPKGDQ | ||||||
Compositional bias | 945-959 | Pro residues | ||||
Sequence: GPPGPPGPPGPKGDA | ||||||
Compositional bias | 980-994 | Pro residues | ||||
Sequence: GPPGPPGPPGPPGPG | ||||||
Sequence conflict | 1185 | in Ref. 2; AAA48703 | ||||
Sequence: I → T | ||||||
Sequence conflict | 1260 | in Ref. 2; AAA48703 | ||||
Sequence: P → S | ||||||
Sequence conflict | 1264 | in Ref. 2; AAA48703 | ||||
Sequence: R → P | ||||||
Compositional bias | 1306-1336 | Polar residues | ||||
Sequence: GSLGASSSYGSSMSSSMSSYSASMGSDGSYG | ||||||
Sequence conflict | 1311 | in Ref. 2; AAA48703 | ||||
Sequence: S → T | ||||||
Sequence conflict | 1463 | in Ref. 2; AAA48703 | ||||
Sequence: Missing | ||||||
Sequence conflict | 1469 | in Ref. 2; AAA48703 | ||||
Sequence: Missing | ||||||
Compositional bias | 1469-1488 | Basic and acidic residues | ||||
Sequence: QRGPKGEKGEKGEQMYSGRR |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M60172 EMBL· GenBank· DDBJ | AAA48703.1 EMBL· GenBank· DDBJ | mRNA | Frameshift |