P11046 · LAMB1_DROME
- ProteinLaminin subunit beta-1
- GeneLanB1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1788 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components (By similarity).
Required for Ndg localization to the basement membrane (PubMed:30260959).
Required for Ndg localization to the basement membrane (PubMed:30260959).
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-containing extracellular matrix | |
Cellular Component | extracellular region | |
Cellular Component | focal adhesion | |
Cellular Component | laminin complex | |
Biological Process | animal organ development | |
Biological Process | animal organ morphogenesis | |
Biological Process | axon guidance | |
Biological Process | basement membrane assembly | |
Biological Process | basement membrane organization | |
Biological Process | cardiac muscle cell development | |
Biological Process | cell adhesion mediated by integrin | |
Biological Process | cell migration | |
Biological Process | defense response to Gram-negative bacterium | |
Biological Process | embryonic heart tube morphogenesis | |
Biological Process | extracellular matrix organization | |
Biological Process | gonad development | |
Biological Process | imaginal disc-derived wing morphogenesis | |
Biological Process | positive regulation of innate immune response | |
Biological Process | substrate adhesion-dependent cell spreading | |
Biological Process | tissue development |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLaminin subunit beta-1
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionP11046
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Phenotypes & Variants
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-24 | |||||
Sequence: MLELRLIVVIVLALLSWQWDPVDS | ||||||
Chain | PRO_0000017073 | 25-1788 | Laminin subunit beta-1 | |||
Sequence: QRPPQHGRRDRPKYPPNKFIKTHPCERSSCYPATGNLLIGRENRLTASSTCGLHSPERFCILSHLQDKKCFLCDTREETKHDPYKNHRIGQIIYKTKPGTNIPTWWQSENGKENATIQLDLEAEFHFTHLIITFTTFRPAAMYIERSFDFGQTWHIYRYFAYDCKESFPGVPTVLENITDVMCTSRYSNVEPSRNGEVIFRVLPPNINVTDPYAEHVQNQLKMTNLRIQMTKLHKLGDNLLDSRLENEEKYYYGISNMVVRGSCSCYGHASQCLPLDPAFSQADNEDGMVHGRCECTHNTKGMNCEECEDFFNDLPWKPAFGKKTNACKKCECNDHAVSCHFDEAVFTASGFVSGGVCDNCLHNTRGQHCEECMPYFYRDPEQDITSERVCQPCDCDPQGSSDDGICDSLNELEEGAVAGACHCKAFVTGRRCNQCKDGYWNLQSDNPEGCEPCTCNPLGTLNNSGCVMRTGECKCKKYVTGKDCNQCMPETYGLSESPEGCSLCNCDAGGSYDNYCDVISGQCRCRPHMTGRSCSQPKQNYFIPLLPEVHEAEVVDECISYGANGNCSLVAETPDGSFTGIGFTRVPENSELVFTVGDIPRSMPYDAVIRYQSTSRGDWENAFITLVRPDQVDPEGGCGELAAATSSETRIPFSLPDRSRQVVALNEVCLEAGKVYKFRIYFERKRHDVDSPTATILVDSLTLIPRIDVTPIFQGSVLADIRKKDYEKYNCKSSLYDMNYKSDPKCQNLDNILSVFVHDGASMCNCNPTGSLSKVCESNGGYCQCKPNVVGRQCDQCAPGTYGFGPEGCKACDCNSIGSKDKYCDLITGQCQCVPNTYGRECNQCQPGYWNFPECRVCQCNGHAATCDPIQGTCIDCQDSTTGYSCDSCLDGYYGNPLFGSEIGCRPCRCPETVASGLAHADGCSLDTRNNNMLCHCQEGYSGSRCEICADNFFGNPDNGGTCSKCECSNNVDLYDTGNCDRQTGACLKCLYQTTGDHCELCKDGFFGDALQQNCQQCECDFLGTNNTIAHCDRFTGQCPCLPNVQGVRCDQCAENHWKIASGEGCESCNCDPIGALHEQCNSYTGQCQCKPGFGGRACNQCQAHYWGNPNEKCQPCECDQFGAADFQCDRETGNCVCHEGIGGYKCNECARGYIGQFPHCSPCGECFNNWDLILSALEDATTATILRAKEIKQVGATGAYTSEFSELDKKLQHIRNLLQNTSVSLVDIEKLDYETQSLRDQLQASHGRLSETEQNLDDIYNSLSLSGVELESLQNHSRLVQQLSKELKENGIQLQESNIEGALNLTRHAYERVSNLSTLKDEANELASNTDRNCKRVENLSNKIQAEADDLANNNKLIEDYRAELTSLTSQIPELNNQVCGKPGDPCDSLCGGAGCGHCGGFLSCEHGAKTHSEEALKVAKDAETAITSKKDQADQTIRALTQAKLNASEAYEKAKRGFEQSERYLNQTNANIKLAENLFIALNNFQENKTASPSESKELAQKTLDLDLKLEPEEIETLGDQINRAVSSLKNVEAIIYRTKPDLDRVNNLQSIANATKEKADKILDSANSVVESLAAADESQGKAKDAIQQANSNIELAGQDLEKIDEETYSAEAPANNTAQQVEKLAKKVQKLQNNIMKNDRDAKEITKEAGSVKLEAMRARGEANNLQSATSATNQTLTDRASRSENARERAKQLLQRASKLTVDTNAKLKDLNDLQTVYLNKNQQLLRLQAEIGPLNKELNEHLIHIKERGSHYRQCYT | ||||||
Glycosylation | 138 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 201 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 232 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 288↔297 | |||||
Sequence: CSCYGHASQC | ||||||
Disulfide bond | 290↔318 | |||||
Sequence: CYGHASQCLPLDPAFSQADNEDGMVHGRC | ||||||
Disulfide bond | 320↔329 | |||||
Sequence: CTHNTKGMNC | ||||||
Disulfide bond | 332↔352 | |||||
Sequence: CEDFFNDLPWKPAFGKKTNAC | ||||||
Disulfide bond | 355↔364 | |||||
Sequence: CECNDHAVSC | ||||||
Disulfide bond | 357↔382 | |||||
Sequence: CNDHAVSCHFDEAVFTASGFVSGGVC | ||||||
Disulfide bond | 385↔394 | |||||
Sequence: CLHNTRGQHC | ||||||
Disulfide bond | 397↔415 | |||||
Sequence: CMPYFYRDPEQDITSERVC | ||||||
Disulfide bond | 418↔431 | |||||
Sequence: CDCDPQGSSDDGIC | ||||||
Disulfide bond | 420↔446 | |||||
Sequence: CDPQGSSDDGICDSLNELEEGAVAGAC | ||||||
Disulfide bond | 448↔457 | |||||
Sequence: CKAFVTGRRC | ||||||
Disulfide bond | 460↔475 | |||||
Sequence: CKDGYWNLQSDNPEGC | ||||||
Disulfide bond | 478↔491 | |||||
Sequence: CTCNPLGTLNNSGC | ||||||
Disulfide bond | 480↔498 | |||||
Sequence: CNPLGTLNNSGCVMRTGEC | ||||||
Glycosylation | 487 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 500↔509 | |||||
Sequence: CKKYVTGKDC | ||||||
Disulfide bond | 512↔526 | |||||
Sequence: CMPETYGLSESPEGC | ||||||
Disulfide bond | 529↔541 | |||||
Sequence: CNCDAGGSYDNYC | ||||||
Disulfide bond | 531↔548 | |||||
Sequence: CDAGGSYDNYCDVISGQC | ||||||
Disulfide bond | 550↔559 | |||||
Sequence: CRPHMTGRSC | ||||||
Glycosylation | 591 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 789↔801 | |||||
Sequence: CNCNPTGSLSKVC | ||||||
Disulfide bond | 791↔808 | |||||
Sequence: CNPTGSLSKVCESNGGYC | ||||||
Disulfide bond | 810↔819 | |||||
Sequence: CKPNVVGRQC | ||||||
Disulfide bond | 822↔834 | |||||
Sequence: CAPGTYGFGPEGC | ||||||
Disulfide bond | 837↔849 | |||||
Sequence: CDCNSIGSKDKYC | ||||||
Disulfide bond | 839↔856 | |||||
Sequence: CNSIGSKDKYCDLITGQC | ||||||
Disulfide bond | 858↔867 | |||||
Sequence: CVPNTYGREC | ||||||
Disulfide bond | 870↔880 | |||||
Sequence: CQPGYWNFPEC | ||||||
Disulfide bond | 883↔892 | |||||
Sequence: CQCNGHAATC | ||||||
Disulfide bond | 885↔899 | |||||
Sequence: CNGHAATCDPIQGTC | ||||||
Disulfide bond | 902↔911 | |||||
Sequence: CQDSTTGYSC | ||||||
Disulfide bond | 914↔930 | |||||
Sequence: CLDGYYGNPLFGSEIGC | ||||||
Disulfide bond | 933↔949 | |||||
Sequence: CRCPETVASGLAHADGC | ||||||
Disulfide bond | 935↔960 | |||||
Sequence: CPETVASGLAHADGCSLDTRNNNMLC | ||||||
Disulfide bond | 962↔971 | |||||
Sequence: CQEGYSGSRC | ||||||
Disulfide bond | 974↔988 | |||||
Sequence: CADNFFGNPDNGGTC | ||||||
Disulfide bond | 991↔1005 | |||||
Sequence: CECSNNVDLYDTGNC | ||||||
Disulfide bond | 993↔1012 | |||||
Sequence: CSNNVDLYDTGNCDRQTGAC | ||||||
Disulfide bond | 1015↔1024 | |||||
Sequence: CLYQTTGDHC | ||||||
Disulfide bond | 1027↔1040 | |||||
Sequence: CKDGFFGDALQQNC | ||||||
Disulfide bond | 1043↔1057 | |||||
Sequence: CECDFLGTNNTIAHC | ||||||
Disulfide bond | 1045↔1064 | |||||
Sequence: CDFLGTNNTIAHCDRFTGQC | ||||||
Glycosylation | 1051 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1066↔1075 | |||||
Sequence: CLPNVQGVRC | ||||||
Disulfide bond | 1078↔1091 | |||||
Sequence: CAENHWKIASGEGC | ||||||
Disulfide bond | 1094↔1106 | |||||
Sequence: CNCDPIGALHEQC | ||||||
Disulfide bond | 1096↔1113 | |||||
Sequence: CDPIGALHEQCNSYTGQC | ||||||
Disulfide bond | 1115↔1124 | |||||
Sequence: CKPGFGGRAC | ||||||
Disulfide bond | 1127↔1139 | |||||
Sequence: CQAHYWGNPNEKC | ||||||
Disulfide bond | 1142↔1154 | |||||
Sequence: CECDQFGAADFQC | ||||||
Disulfide bond | 1144↔1161 | |||||
Sequence: CDQFGAADFQCDRETGNC | ||||||
Disulfide bond | 1163↔1172 | |||||
Sequence: CHEGIGGYKC | ||||||
Disulfide bond | 1175↔1186 | |||||
Sequence: CARGYIGQFPHC | ||||||
Disulfide bond | 1189 | Interchain | ||||
Sequence: C | ||||||
Disulfide bond | 1192 | Interchain | ||||
Sequence: C | ||||||
Glycosylation | 1246 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1301 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1330 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1341 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1473 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1493 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1515 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1581 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1644 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1703 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1786 | Interchain | ||||
Sequence: C |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Found in the basement membranes (major component).
Developmental stage
In the larva, expressed mainly by fat body adipocytes and blood cells and secreted in the basal membranes that surround the fat body, imaginal disks, tracheae, salivary glands, midgut, mature muscles and heart (at protein level).
Gene expression databases
Interaction
Subunit
Laminin is a complex glycoprotein, consisting of three different polypeptide chains (alpha, beta, gamma), which are bound to each other by disulfide bonds into a cross-shaped molecule comprising one long and three short arms with globules at each end.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain, motif, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 23-43 | Disordered | ||||
Sequence: DSQRPPQHGRRDRPKYPPNKF | ||||||
Compositional bias | 26-41 | Basic and acidic residues | ||||
Sequence: RPPQHGRRDRPKYPPN | ||||||
Domain | 50-287 | Laminin N-terminal | ||||
Sequence: ERSSCYPATGNLLIGRENRLTASSTCGLHSPERFCILSHLQDKKCFLCDTREETKHDPYKNHRIGQIIYKTKPGTNIPTWWQSENGKENATIQLDLEAEFHFTHLIITFTTFRPAAMYIERSFDFGQTWHIYRYFAYDCKESFPGVPTVLENITDVMCTSRYSNVEPSRNGEVIFRVLPPNINVTDPYAEHVQNQLKMTNLRIQMTKLHKLGDNLLDSRLENEEKYYYGISNMVVRGS | ||||||
Domain | 288-354 | Laminin EGF-like 1 | ||||
Sequence: CSCYGHASQCLPLDPAFSQADNEDGMVHGRCECTHNTKGMNCEECEDFFNDLPWKPAFGKKTNACKK | ||||||
Domain | 355-417 | Laminin EGF-like 2 | ||||
Sequence: CECNDHAVSCHFDEAVFTASGFVSGGVCDNCLHNTRGQHCEECMPYFYRDPEQDITSERVCQP | ||||||
Domain | 418-477 | Laminin EGF-like 3 | ||||
Sequence: CDCDPQGSSDDGICDSLNELEEGAVAGACHCKAFVTGRRCNQCKDGYWNLQSDNPEGCEP | ||||||
Domain | 478-528 | Laminin EGF-like 4 | ||||
Sequence: CTCNPLGTLNNSGCVMRTGECKCKKYVTGKDCNQCMPETYGLSESPEGCSL | ||||||
Domain | 529-559 | Laminin EGF-like 5; truncated | ||||
Sequence: CNCDAGGSYDNYCDVISGQCRCRPHMTGRSC | ||||||
Domain | 567-783 | Laminin IV type B | ||||
Sequence: FIPLLPEVHEAEVVDECISYGANGNCSLVAETPDGSFTGIGFTRVPENSELVFTVGDIPRSMPYDAVIRYQSTSRGDWENAFITLVRPDQVDPEGGCGELAAATSSETRIPFSLPDRSRQVVALNEVCLEAGKVYKFRIYFERKRHDVDSPTATILVDSLTLIPRIDVTPIFQGSVLADIRKKDYEKYNCKSSLYDMNYKSDPKCQNLDNILSVFVH | ||||||
Motif | 641-643 | Cell attachment site | ||||
Sequence: RGD | ||||||
Domain | 789-836 | Laminin EGF-like 6 | ||||
Sequence: CNCNPTGSLSKVCESNGGYCQCKPNVVGRQCDQCAPGTYGFGPEGCKA | ||||||
Domain | 837-882 | Laminin EGF-like 7 | ||||
Sequence: CDCNSIGSKDKYCDLITGQCQCVPNTYGRECNQCQPGYWNFPECRV | ||||||
Domain | 883-932 | Laminin EGF-like 8 | ||||
Sequence: CQCNGHAATCDPIQGTCIDCQDSTTGYSCDSCLDGYYGNPLFGSEIGCRP | ||||||
Domain | 933-990 | Laminin EGF-like 9 | ||||
Sequence: CRCPETVASGLAHADGCSLDTRNNNMLCHCQEGYSGSRCEICADNFFGNPDNGGTCSK | ||||||
Domain | 991-1042 | Laminin EGF-like 10 | ||||
Sequence: CECSNNVDLYDTGNCDRQTGACLKCLYQTTGDHCELCKDGFFGDALQQNCQQ | ||||||
Domain | 1043-1093 | Laminin EGF-like 11 | ||||
Sequence: CECDFLGTNNTIAHCDRFTGQCPCLPNVQGVRCDQCAENHWKIASGEGCES | ||||||
Domain | 1094-1141 | Laminin EGF-like 12 | ||||
Sequence: CNCDPIGALHEQCNSYTGQCQCKPGFGGRACNQCQAHYWGNPNEKCQP | ||||||
Domain | 1142-1188 | Laminin EGF-like 13 | ||||
Sequence: CECDQFGAADFQCDRETGNCVCHEGIGGYKCNECARGYIGQFPHCSP | ||||||
Region | 1189-1405 | Domain II | ||||
Sequence: CGECFNNWDLILSALEDATTATILRAKEIKQVGATGAYTSEFSELDKKLQHIRNLLQNTSVSLVDIEKLDYETQSLRDQLQASHGRLSETEQNLDDIYNSLSLSGVELESLQNHSRLVQQLSKELKENGIQLQESNIEGALNLTRHAYERVSNLSTLKDEANELASNTDRNCKRVENLSNKIQAEADDLANNNKLIEDYRAELTSLTSQIPELNNQV | ||||||
Coiled coil | 1255-1405 | |||||
Sequence: EKLDYETQSLRDQLQASHGRLSETEQNLDDIYNSLSLSGVELESLQNHSRLVQQLSKELKENGIQLQESNIEGALNLTRHAYERVSNLSTLKDEANELASNTDRNCKRVENLSNKIQAEADDLANNNKLIEDYRAELTSLTSQIPELNNQV | ||||||
Region | 1406-1432 | Domain alpha | ||||
Sequence: CGKPGDPCDSLCGGAGCGHCGGFLSCE | ||||||
Region | 1433-1788 | Domain I | ||||
Sequence: HGAKTHSEEALKVAKDAETAITSKKDQADQTIRALTQAKLNASEAYEKAKRGFEQSERYLNQTNANIKLAENLFIALNNFQENKTASPSESKELAQKTLDLDLKLEPEEIETLGDQINRAVSSLKNVEAIIYRTKPDLDRVNNLQSIANATKEKADKILDSANSVVESLAAADESQGKAKDAIQQANSNIELAGQDLEKIDEETYSAEAPANNTAQQVEKLAKKVQKLQNNIMKNDRDAKEITKEAGSVKLEAMRARGEANNLQSATSATNQTLTDRASRSENARERAKQLLQRASKLTVDTNAKLKDLNDLQTVYLNKNQQLLRLQAEIGPLNKELNEHLIHIKERGSHYRQCYT | ||||||
Coiled coil | 1453-1505 | |||||
Sequence: ITSKKDQADQTIRALTQAKLNASEAYEKAKRGFEQSERYLNQTNANIKLAENL | ||||||
Coiled coil | 1540-1561 | |||||
Sequence: EEIETLGDQINRAVSSLKNVEA | ||||||
Coiled coil | 1608-1762 | |||||
Sequence: QGKAKDAIQQANSNIELAGQDLEKIDEETYSAEAPANNTAQQVEKLAKKVQKLQNNIMKNDRDAKEITKEAGSVKLEAMRARGEANNLQSATSATNQTLTDRASRSENARERAKQLLQRASKLTVDTNAKLKDLNDLQTVYLNKNQQLLRLQAEI | ||||||
Region | 1690-1719 | Disordered | ||||
Sequence: GEANNLQSATSATNQTLTDRASRSENARER | ||||||
Compositional bias | 1692-1710 | Polar residues | ||||
Sequence: ANNLQSATSATNQTLTDRA |
Domain
The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.
Domains VI and IV are globular.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length1,788
- Mass (Da)198,333
- Last updated2007-11-13 v4
- Checksum7CB99C9608452085
Sequence caution
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 12 | in Ref. 1; AAD19752 and 2; AAA28663 | ||||
Sequence: L → LAL | ||||||
Compositional bias | 26-41 | Basic and acidic residues | ||||
Sequence: RPPQHGRRDRPKYPPN | ||||||
Sequence conflict | 666 | in Ref. 1; AAD19752 | ||||
Sequence: L → H | ||||||
Sequence conflict | 724-725 | in Ref. 2; AAA28663 | ||||
Sequence: DS → VT | ||||||
Sequence conflict | 766-767 | in Ref. 1; AAD19752 and 2; AAA28663 | ||||
Sequence: KS → NA | ||||||
Sequence conflict | 939 | in Ref. 5; AAT94451 | ||||
Sequence: V → I | ||||||
Sequence conflict | 946-947 | in Ref. 1; AAD19752 and 2; AAA28663 | ||||
Sequence: Missing | ||||||
Sequence conflict | 1356-1373 | in Ref. 1; AAD19752 and 2; AAA28663 | ||||
Sequence: TDRNCKRVENLSNKIQAE → SDRIAREWKICLIRFRPN | ||||||
Compositional bias | 1692-1710 | Polar residues | ||||
Sequence: ANNLQSATSATNQTLTDRA |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M95811 EMBL· GenBank· DDBJ | AAD19752.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M19525 EMBL· GenBank· DDBJ | AAA28663.1 EMBL· GenBank· DDBJ | mRNA | ||
AE014134 EMBL· GenBank· DDBJ | AAF52563.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014134 EMBL· GenBank· DDBJ | AAN10647.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT015222 EMBL· GenBank· DDBJ | AAT94451.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AY095001 EMBL· GenBank· DDBJ | AAM11329.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |