Q16787 · LAMA3_HUMAN
- ProteinLaminin subunit alpha-3
- GeneLAMA3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids3333 (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.
Laminin-5 is thought to be involved in 1 cell adhesion via integrin alpha-3/beta-1 in focal adhesion and integrin alpha-6/beta-4 in hemidesmosomes, 2 signal transduction via tyrosine phosphorylation of pp125-FAK and p80, 3 differentiation of keratinocytes.
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 | adherens junction | |
Cellular Component | basement membrane | |
Cellular Component | collagen-containing extracellular matrix | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | extracellular exosome | |
Cellular Component | extracellular region | |
Cellular Component | hemidesmosome | |
Cellular Component | laminin-3 complex | |
Cellular Component | laminin-5 complex | |
Molecular Function | signaling receptor binding | |
Molecular Function | structural molecule activity | |
Biological Process | cell-cell adhesion | |
Biological Process | endodermal cell differentiation | |
Biological Process | epidermis development | |
Biological Process | hemidesmosome assembly | |
Biological Process | regulation of cell adhesion | |
Biological Process | regulation of cell migration | |
Biological Process | regulation of embryonic development |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLaminin subunit alpha-3
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ16787
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Major component.
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Epidermolysis bullosa, junctional 2A, intermediate (JEB2A)
- Note
- DescriptionA form of epidermolysis bullosa, a genodermatosis characterized by recurrent blistering, fragility of the skin and mucosal epithelia, and erosions caused by minor mechanical trauma. JEB2A is an autosomal recessive, intermediate form in which blistering lesions occur between the epidermis and the dermis at the lamina lucida level of the basement membrane zone. In intermediate forms of junctional epidermolysis bullosa, blistering does not lead to the formation of chronic granulation tissue and does not affect the lifespan of affected individuals. Nail dystrophy and dental enamel defects are present. Scarring or non-scarring alopecia and diffuse hair loss may occur.
- See alsoMIM:619783
Epidermolysis bullosa, junctional 2B, severe (JEB2B)
- Note
- DescriptionA form of epidermolysis bullosa, a genodermatosis characterized by recurrent blistering, fragility of the skin and mucosal epithelia, and erosions caused by minor mechanical trauma. JEB2B is an autosomal recessive form in which blistering lesions occur between the epidermis and the dermis at the lamina lucida level of the basement membrane zone. It belongs to the severe spectrum of junctional epidermolysis bullosa (previously known as generalized severe or Herlitz type), characterized by onset of blistering over large regions of the body at birth or in early infancy. Blistering also affects the mucous membranes, such as the moist lining of the mouth and digestive tract, which can make it difficult to eat and digest food. The extensive blistering leads to scarring and the formation of red, bumpy patches called granulation tissue. Other complications can include fusion of the fingers and toes, abnormalities of the fingernails and toenails, joint deformities, dental enamel defects, and alopecia. Severe, junctional forms are associated with death in the first 6 to 24 months of life.
- See alsoMIM:619784
Natural variants in JEB2B
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_086401 | 2270-3333 | missing | in JEB2B |
Epidermolysis bullosa, junctional 2C, laryngoonychocutaneous (JEB2C)
- Note
- DescriptionA form of epidermolysis bullosa, a genodermatosis characterized by recurrent blistering, fragility of the skin and mucosal epithelia, and erosions caused by minor mechanical trauma. JEB2C is an autosomal recessive, severe form in which blistering lesions occur between the epidermis and the dermis at the lamina lucida level of the basement membrane zone. JEB2C manifestations appear in early infancy and include hoarse cry, skin ulceration, nail dystrophy with recurrent loss of toenails and fingernails, and conjunctival scarring. Some patients have amelogenesis imperfecta. Death in childhood is common.
- See alsoMIM:245660
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_050078 | 796 | in dbSNP:rs17187262 | |||
Sequence: T → N | ||||||
Natural variant | VAR_050079 | 1206 | in dbSNP:rs12457323 | |||
Sequence: V → A | ||||||
Natural variant | VAR_050080 | 1208 | in dbSNP:rs17202961 | |||
Sequence: P → T | ||||||
Natural variant | VAR_059444 | 1774 | in dbSNP:rs958631 | |||
Sequence: F → L | ||||||
Natural variant | VAR_086401 | 2270-3333 | in JEB2B | |||
Sequence: Missing | ||||||
Natural variant | VAR_047374 | 2702 | in dbSNP:rs9952370 | |||
Sequence: T → A | ||||||
Natural variant | VAR_047375 | 2815 | in dbSNP:rs1154232 | |||
Sequence: N → K | ||||||
Natural variant | VAR_059445 | 2834 | in dbSNP:rs1154233 | |||
Sequence: G → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 3,827 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-35 | |||||
Sequence: MAAAARPRGRALGPVLPPTPLLLLVLRVLPACGAT | ||||||
Chain | PRO_0000017058 | 36-3333 | Laminin subunit alpha-3 | |||
Sequence: ARDPGAAAGLSLHPTYFNLAEAARIWATATCGERGPGEGRPQPELYCKLVGGPTAPGSGHTIQGQFCDYCNSEDPRKAHPVTNAIDGSERWWQSPPLSSGTQYNRVNLTLDLGQLFHVAYILIKFANSPRPDLWVLERSVDFGSTYSPWQYFAHSKVDCLKEFGREANMAVTRDDDVLCVTEYSRIVPLENGEVVVSLINGRPGAKNFTFSHTLREFTKATNIRLRFLRTNTLLGHLISKAQRDPTVTRRYYYSIKDISIGGQCVCNGHAEVCNINNPEKLFRCECQHHTCGETCDRCCTGYNQRRWRPAAWEQSHECEACNCHGHASNCYYDPDVERQQASLNTQGIYAGGGVCINCQHNTAGVNCEQCAKGYYRPYGVPVDAPDGCIPCSCDPEHADGCEQGSGRCHCKPNFHGDNCEKCAIGYYNFPFCLRIPIFPVSTPSSEDPVAGDIKGCDCNLEGVLPEICDAHGRCLCRPGVEGPRCDTCRSGFYSFPICQACWCSALGSYQMPCSSVTGQCECRPGVTGQRCDRCLSGAYDFPHCQGSSSACDPAGTINSNLGYCQCKLHVEGPTCSRCKLLYWNLDKENPSGCSECKCHKAGTVSGTGECRQGDGDCHCKSHVGGDSCDTCEDGYFALEKSNYFGCQGCQCDIGGALSSMCSGPSGVCQCREHVVGKVCQRPENNYYFPDLHHMKYEIEDGSTPNGRDLRFGFDPLAFPEFSWRGYAQMTSVQNDVRITLNVGKSSGSLFRVILRYVNPGTEAVSGHITIYPSWGAAQSKEIIFLPSKEPAFVTVPGNGFADPFSITPGIWVACIKAEGVLLDYLVLLPRDYYEASVLQLPVTEPCAYAGPPQENCLLYQHLPVTRFPCTLACEARHFLLDGEPRPVAVRQPTPAHPVMVDLSGREVELHLRLRIPQVGHYVVVVEYSTEAAQLFVVDVNVKSSGSVLAGQVNIYSCNYSVLCRSAVIDHMSRIAMYELLADADIQLKGHMARFLLHQVCIIPIEEFSAEYVRPQVHCIASYGRFVNQSATCVSLAHETPPTALILDVLSGRPFPHLPQQSSPSVDVLPGVTLKAPQNQVTLRGRVPHLGRYVFVIHFYQAAHPTFPAQVSVDGGWPRAGSFHASFCPHVLGCRDQVIAEGQIEFDISEPEVAATVKVPEGKSLVLVRVLVVPAENYDYQILHKKSMDKSLEFITNCGKNSFYLDPQTASRFCKNSARSLVAFYHKGALPCECHPTGATGPHCSPEGGQCPCQPNVIGRQCTRCATGHYGFPRCKPCSCGRRLCEEMTGQCRCPPRTVRPQCEVCETHSFSFHPMAGCEGCNCSRRGTIEAAMPECDRDSGQCRCKPRITGRQCDRCASGFYRFPECVPCNCNRDGTEPGVCDPGTGACLCKENVEGTECNVCREGSFHLDPANLKGCTSCFCFGVNNQCHSSHKRRTKFVDMLGWHLETADRVDIPVSFNPGSNSMVADLQELPATIHSASWVAPTSYLGDKVSSYGGYLTYQAKSFGLPGDMVLLEKKPDVQLTGQHMSIIYEETNTPRPDRLHHGRVHVVEGNFRHASSRAPVSREELMTVLSRLADVRIQGLYFTETQRLTLSEVGLEEASDTGSGRIALAVEICACPPAYAGDSCQGCSPGYYRDHKGLYTGRCVPCNCNGHSNQCQDGSGICVNCQHNTAGEHCERCQEGYYGNAVHGSCRACPCPHTNSFATGCVVNGGDVRCSCKAGYTGTQCERCAPGYFGNPQKFGGSCQPCSCNSNGQLGSCHPLTGDCINQEPKDSSPAEECDDCDSCVMTLLNDLATMGEQLRLVKSQLQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVKIKNVIRNVHILLKQISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRNFGKHLREAEADKRESQLLLNRIRTWQKTHQGENNGLANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNASGDELVRCAVDAATAYENILNAIKAAEDAANRAASASESALQTVIKEDLPRKAKTLSSNSDKLLNEAKMTQKKLKQEVSPALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQRGDIDAMISSAKSMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQNEDFKKALTDADNSVNKLTNKLPDLWRKIESINQQLLPLGNISDNMDRIRELIQQARDAASKVAVPMRFNGKSGVEVRLPNDLEDLKGYTSLSLFLQRPNSRENGGTENMFVMYLGNKDASRDYIGMAVVDGQLTCVYNLGDREAELQVDQILTKSETKEAVMDRVKFQRIYQFARLNYTKGATSSKPETPGVYDMDGRNSNTLLNLDPENVVFYVGGYPPDFKLPSRLSFPPYKGCIELDDLNENVLSLYNFKKTFNLNTTEVEPCRRRKEESDKNYFEGTGYARVPTQPHAPIPTFGQTIQTTVDRGLLFFAENGDRFISLNIEDGKLMVRYKLNSELPKERGVGDAINNGRDHSIQIKIGKLQKRMWINVDVQNTIIDGEVFDFSTYYLGGIPIAIRERFNISTPAFRGCMKNLKKTSGVVRLNDTVGVTKKCSEDWKLVRSASFSRGGQLSFTDLGLPPTDHLQASFGFQTFQPSGILLDHQTWTRNLQVTLEDGYIELSTSDSGGPIFKSPQTYMDGLLHYVSVISDNSGLRLLIDDQLLRNSKRLKHISSSRQSLRLGGSNFEGCISNVFVQRLSLSPEVLDLTSNSLKRDVSLGGCSLNKPPFLMLLKGSTRFNKTKTFRINQLLQDTPVASPRSVKVWQDACSPLPKTQANHGALQFGDIPTSHLLFKLPQELLKPRSQFAVDMQTTSSRGLVFHTGTKNSFMALYLSKGRLVFALGTDGKKLRIKSKEKCNDGKWHTVVFGHDGEKGRLVVDGLRAREGSLPGNSTISIRAPVYLGSPPSGKPKSLPTNSFVGCLKNFQLDSKPLYTPSSSFGVSSCLGGPLEKGIYFSEEGGHVVLAHSVLLGPEFKLVFSIRPRSLTGILIHIGSQPGKHLCVYLEAGKVTASMDSGAGGTSTSVTPKQSLCDGQWHSVAVTIKQHILHLELDTDSSYTAGQIPFPPASTQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIHVNHIPVPVTEALEVQGPVSLNGCPDQ | ||||||
Glycosylation | 142 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 242 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 299↔308 | |||||
Sequence: CVCNGHAEVC | ||||||
Disulfide bond | 301↔319 | |||||
Sequence: CNGHAEVCNINNPEKLFRC | ||||||
Disulfide bond | 321↔330 | |||||
Sequence: CQHHTCGETC | ||||||
Disulfide bond | 333↔353 | |||||
Sequence: CCTGYNQRRWRPAAWEQSHEC | ||||||
Disulfide bond | 356↔365 | |||||
Sequence: CNCHGHASNC | ||||||
Disulfide bond | 358↔390 | |||||
Sequence: CHGHASNCYYDPDVERQQASLNTQGIYAGGGVC | ||||||
Disulfide bond | 393↔402 | |||||
Sequence: CQHNTAGVNC | ||||||
Disulfide bond | 405↔423 | |||||
Sequence: CAKGYYRPYGVPVDAPDGC | ||||||
Disulfide bond | 426↔436 | |||||
Sequence: CSCDPEHADGC | ||||||
Disulfide bond | 428↔443 | |||||
Sequence: CDPEHADGCEQGSGRC | ||||||
Disulfide bond | 445↔454 | |||||
Sequence: CKPNFHGDNC | ||||||
Disulfide bond | 457↔467 | |||||
Sequence: CAIGYYNFPFC | ||||||
Disulfide bond | 491↔503 | |||||
Sequence: CDCNLEGVLPEIC | ||||||
Disulfide bond | 493↔509 | |||||
Sequence: CNLEGVLPEICDAHGRC | ||||||
Disulfide bond | 511↔520 | |||||
Sequence: CRPGVEGPRC | ||||||
Disulfide bond | 523↔533 | |||||
Sequence: CRSGFYSFPIC | ||||||
Disulfide bond | 536↔548 | |||||
Sequence: CWCSALGSYQMPC | ||||||
Disulfide bond | 538↔555 | |||||
Sequence: CSALGSYQMPCSSVTGQC | ||||||
Disulfide bond | 557↔566 | |||||
Sequence: CRPGVTGQRC | ||||||
Disulfide bond | 569↔586 | |||||
Sequence: CLSGAYDFPHCQGSSSAC | ||||||
Disulfide bond | 601↔610 | |||||
Sequence: CKLHVEGPTC | ||||||
Disulfide bond | 613↔628 | |||||
Sequence: CKLLYWNLDKENPSGC | ||||||
Disulfide bond | 631↔645 | |||||
Sequence: CKCHKAGTVSGTGEC | ||||||
Disulfide bond | 633↔652 | |||||
Sequence: CHKAGTVSGTGECRQGDGDC | ||||||
Disulfide bond | 654↔663 | |||||
Sequence: CKSHVGGDSC | ||||||
Disulfide bond | 666↔681 | |||||
Sequence: CEDGYFALEKSNYFGC | ||||||
Disulfide bond | 684↔696 | |||||
Sequence: CQCDIGGALSSMC | ||||||
Disulfide bond | 686↔703 | |||||
Sequence: CDIGGALSSMCSGPSGVC | ||||||
Disulfide bond | 705↔714 | |||||
Sequence: CREHVVGKVC | ||||||
Disulfide bond | 1266↔1278 | |||||
Sequence: CECHPTGATGPHC | ||||||
Disulfide bond | 1268↔1285 | |||||
Sequence: CHPTGATGPHCSPEGGQC | ||||||
Disulfide bond | 1287↔1296 | |||||
Sequence: CQPNVIGRQC | ||||||
Disulfide bond | 1299↔1309 | |||||
Sequence: CATGHYGFPRC | ||||||
Disulfide bond | 1312↔1319 | |||||
Sequence: CSCGRRLC | ||||||
Disulfide bond | 1314↔1326 | |||||
Sequence: CGRRLCEEMTGQC | ||||||
Disulfide bond | 1328↔1337 | |||||
Sequence: CPPRTVRPQC | ||||||
Disulfide bond | 1340↔1353 | |||||
Sequence: CETHSFSFHPMAGC | ||||||
Disulfide bond | 1356↔1371 | |||||
Sequence: CNCSRRGTIEAAMPEC | ||||||
Disulfide bond | 1358↔1378 | |||||
Sequence: CSRRGTIEAAMPECDRDSGQC | ||||||
Disulfide bond | 1380↔1389 | |||||
Sequence: CKPRITGRQC | ||||||
Disulfide bond | 1392↔1402 | |||||
Sequence: CASGFYRFPEC | ||||||
Disulfide bond | 1405↔1417 | |||||
Sequence: CNCNRDGTEPGVC | ||||||
Disulfide bond | 1407↔1424 | |||||
Sequence: CNRDGTEPGVCDPGTGAC | ||||||
Disulfide bond | 1426↔1435 | |||||
Sequence: CKENVEGTEC | ||||||
Disulfide bond | 1438↔1453 | |||||
Sequence: CREGSFHLDPANLKGC | ||||||
Disulfide bond | 1687↔1696 | |||||
Sequence: CNCNGHSNQC | ||||||
Disulfide bond | 1689↔1703 | |||||
Sequence: CNGHSNQCQDGSGIC | ||||||
Disulfide bond | 1706↔1715 | |||||
Sequence: CQHNTAGEHC | ||||||
Disulfide bond | 1718↔1731 | |||||
Sequence: CQEGYYGNAVHGSC | ||||||
Disulfide bond | 1734↔1746 | |||||
Sequence: CPCPHTNSFATGC | ||||||
Disulfide bond | 1736↔1755 | |||||
Sequence: CPHTNSFATGCVVNGGDVRC | ||||||
Disulfide bond | 1757↔1766 | |||||
Sequence: CKAGYTGTQC | ||||||
Disulfide bond | 1769↔1784 | |||||
Sequence: CAPGYFGNPQKFGGSC | ||||||
Disulfide bond | 1822 | Interchain | ||||
Sequence: C | ||||||
Disulfide bond | 1825 | Interchain | ||||
Sequence: C | ||||||
Glycosylation | 2365 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2502 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2561↔2591 | |||||
Sequence: CIELDDLNENVLSLYNFKKTFNLNTTEVEPC | ||||||
Glycosylation | 2584 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 2737↔2760 | |||||
Sequence: CMKNLKKTSGVVRLNDTVGVTKKC | ||||||
Disulfide bond | 2895↔2927 | |||||
Sequence: CISNVFVQRLSLSPEVLDLTSNSLKRDVSLGGC | ||||||
Disulfide bond | 3127↔3150 | |||||
Sequence: CLKNFQLDSKPLYTPSSSFGVSSC | ||||||
Disulfide bond | 3302↔3330 | |||||
Sequence: CLRNIHVNHIPVPVTEALEVQGPVSLNGC |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Skin; respiratory, urinary, and digestive epithelia and in other specialized tissues with prominent secretory or protective functions. Epithelial basement membrane, and epithelial cell tongue that migrates into a wound bed. A differential and focal expression of the subunit alpha-3 is observed in the CNS.
Induction
Laminin-5 is up-regulated in wound sites of human skin.
Gene expression databases
Organism-specific 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. Alpha-3 is a subunit of laminin-5 (laminin-332 or epiligrin/kalinin/nicein), laminin-6 (laminin-311 or K-laminin) and laminin-7 (laminin-321 or KS-laminin).
Protein-protein interaction databases
Miscellaneous
Family & Domains
Features
Showing features for domain, region, coiled coil, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 43-298 | Laminin N-terminal | ||||
Sequence: AGLSLHPTYFNLAEAARIWATATCGERGPGEGRPQPELYCKLVGGPTAPGSGHTIQGQFCDYCNSEDPRKAHPVTNAIDGSERWWQSPPLSSGTQYNRVNLTLDLGQLFHVAYILIKFANSPRPDLWVLERSVDFGSTYSPWQYFAHSKVDCLKEFGREANMAVTRDDDVLCVTEYSRIVPLENGEVVVSLINGRPGAKNFTFSHTLREFTKATNIRLRFLRTNTLLGHLISKAQRDPTVTRRYYYSIKDISIGGQ | ||||||
Region | 298-728 | Domain V | ||||
Sequence: QCVCNGHAEVCNINNPEKLFRCECQHHTCGETCDRCCTGYNQRRWRPAAWEQSHECEACNCHGHASNCYYDPDVERQQASLNTQGIYAGGGVCINCQHNTAGVNCEQCAKGYYRPYGVPVDAPDGCIPCSCDPEHADGCEQGSGRCHCKPNFHGDNCEKCAIGYYNFPFCLRIPIFPVSTPSSEDPVAGDIKGCDCNLEGVLPEICDAHGRCLCRPGVEGPRCDTCRSGFYSFPICQACWCSALGSYQMPCSSVTGQCECRPGVTGQRCDRCLSGAYDFPHCQGSSSACDPAGTINSNLGYCQCKLHVEGPTCSRCKLLYWNLDKENPSGCSECKCHKAGTVSGTGECRQGDGDCHCKSHVGGDSCDTCEDGYFALEKSNYFGCQGCQCDIGGALSSMCSGPSGVCQCREHVVGKVCQRPENNYYFPDLHH | ||||||
Domain | 299-355 | Laminin EGF-like 1 | ||||
Sequence: CVCNGHAEVCNINNPEKLFRCECQHHTCGETCDRCCTGYNQRRWRPAAWEQSHECEA | ||||||
Domain | 356-425 | Laminin EGF-like 2 | ||||
Sequence: CNCHGHASNCYYDPDVERQQASLNTQGIYAGGGVCINCQHNTAGVNCEQCAKGYYRPYGVPVDAPDGCIP | ||||||
Domain | 426-469 | Laminin EGF-like 3 | ||||
Sequence: CSCDPEHADGCEQGSGRCHCKPNFHGDNCEKCAIGYYNFPFCLR | ||||||
Domain | 491-535 | Laminin EGF-like 4 | ||||
Sequence: CDCNLEGVLPEICDAHGRCLCRPGVEGPRCDTCRSGFYSFPICQA | ||||||
Domain | 536-588 | Laminin EGF-like 5 | ||||
Sequence: CWCSALGSYQMPCSSVTGQCECRPGVTGQRCDRCLSGAYDFPHCQGSSSACDP | ||||||
Domain | 590-630 | Laminin EGF-like 6 | ||||
Sequence: GTINSNLGYCQCKLHVEGPTCSRCKLLYWNLDKENPSGCSE | ||||||
Domain | 631-683 | Laminin EGF-like 7 | ||||
Sequence: CKCHKAGTVSGTGECRQGDGDCHCKSHVGGDSCDTCEDGYFALEKSNYFGCQG | ||||||
Domain | 684-728 | Laminin EGF-like 8 | ||||
Sequence: CQCDIGGALSSMCSGPSGVCQCREHVVGKVCQRPENNYYFPDLHH | ||||||
Region | 796-1265 | Domain IV 1 (domain IV B) | ||||
Sequence: TEAVSGHITIYPSWGAAQSKEIIFLPSKEPAFVTVPGNGFADPFSITPGIWVACIKAEGVLLDYLVLLPRDYYEASVLQLPVTEPCAYAGPPQENCLLYQHLPVTRFPCTLACEARHFLLDGEPRPVAVRQPTPAHPVMVDLSGREVELHLRLRIPQVGHYVVVVEYSTEAAQLFVVDVNVKSSGSVLAGQVNIYSCNYSVLCRSAVIDHMSRIAMYELLADADIQLKGHMARFLLHQVCIIPIEEFSAEYVRPQVHCIASYGRFVNQSATCVSLAHETPPTALILDVLSGRPFPHLPQQSSPSVDVLPGVTLKAPQNQVTLRGRVPHLGRYVFVIHFYQAAHPTFPAQVSVDGGWPRAGSFHASFCPHVLGCRDQVIAEGQIEFDISEPEVAATVKVPEGKSLVLVRVLVVPAENYDYQILHKKSMDKSLEFITNCGKNSFYLDPQTASRFCKNSARSLVAFYHKGALP | ||||||
Domain | 1266-1311 | Laminin EGF-like 9 | ||||
Sequence: CECHPTGATGPHCSPEGGQCPCQPNVIGRQCTRCATGHYGFPRCKP | ||||||
Region | 1266-1465 | Domain III B | ||||
Sequence: CECHPTGATGPHCSPEGGQCPCQPNVIGRQCTRCATGHYGFPRCKPCSCGRRLCEEMTGQCRCPPRTVRPQCEVCETHSFSFHPMAGCEGCNCSRRGTIEAAMPECDRDSGQCRCKPRITGRQCDRCASGFYRFPECVPCNCNRDGTEPGVCDPGTGACLCKENVEGTECNVCREGSFHLDPANLKGCTSCFCFGVNNQC | ||||||
Domain | 1312-1355 | Laminin EGF-like 10 | ||||
Sequence: CSCGRRLCEEMTGQCRCPPRTVRPQCEVCETHSFSFHPMAGCEG | ||||||
Domain | 1356-1404 | Laminin EGF-like 11 | ||||
Sequence: CNCSRRGTIEAAMPECDRDSGQCRCKPRITGRQCDRCASGFYRFPECVP | ||||||
Domain | 1405-1455 | Laminin EGF-like 12 | ||||
Sequence: CNCNRDGTEPGVCDPGTGACLCKENVEGTECNVCREGSFHLDPANLKGCTS | ||||||
Domain | 1476-1653 | Laminin IV type A | ||||
Sequence: VDMLGWHLETADRVDIPVSFNPGSNSMVADLQELPATIHSASWVAPTSYLGDKVSSYGGYLTYQAKSFGLPGDMVLLEKKPDVQLTGQHMSIIYEETNTPRPDRLHHGRVHVVEGNFRHASSRAPVSREELMTVLSRLADVRIQGLYFTETQRLTLSEVGLEEASDTGSGRIALAVEI | ||||||
Region | 1654-1821 | Domain III A | ||||
Sequence: CACPPAYAGDSCQGCSPGYYRDHKGLYTGRCVPCNCNGHSNQCQDGSGICVNCQHNTAGEHCERCQEGYYGNAVHGSCRACPCPHTNSFATGCVVNGGDVRCSCKAGYTGTQCERCAPGYFGNPQKFGGSCQPCSCNSNGQLGSCHPLTGDCINQEPKDSSPAEECDD | ||||||
Domain | 1687-1733 | Laminin EGF-like 13 | ||||
Sequence: CNCNGHSNQCQDGSGICVNCQHNTAGEHCERCQEGYYGNAVHGSCRA | ||||||
Domain | 1734-1786 | Laminin EGF-like 14 | ||||
Sequence: CPCPHTNSFATGCVVNGGDVRCSCKAGYTGTQCERCAPGYFGNPQKFGGSCQP | ||||||
Domain | 1787-1821 | Laminin EGF-like 15; truncated | ||||
Sequence: CSCNSNGQLGSCHPLTGDCINQEPKDSSPAEECDD | ||||||
Region | 1822-2389 | Domain II and I | ||||
Sequence: CDSCVMTLLNDLATMGEQLRLVKSQLQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVKIKNVIRNVHILLKQISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRNFGKHLREAEADKRESQLLLNRIRTWQKTHQGENNGLANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNASGDELVRCAVDAATAYENILNAIKAAEDAANRAASASESALQTVIKEDLPRKAKTLSSNSDKLLNEAKMTQKKLKQEVSPALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQRGDIDAMISSAKSMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQNEDFKKALTDADNSVNKLTNKLPDLWRKIESINQQLLPLGNISDNMDRIRELIQQARDAASKVAV | ||||||
Coiled coil | 1852-1941 | |||||
Sequence: ASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVKIKNVI | ||||||
Coiled coil | 1987-2169 | |||||
Sequence: KHLREAEADKRESQLLLNRIRTWQKTHQGENNGLANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNASGDELV | ||||||
Motif | 2278-2280 | Cell attachment site | ||||
Sequence: RGD | ||||||
Coiled coil | 2322-2388 | |||||
Sequence: RTQNEDFKKALTDADNSVNKLTNKLPDLWRKIESINQQLLPLGNISDNMDRIRELIQQARDAASKVA | ||||||
Domain | 2390-2591 | Laminin G-like 1 | ||||
Sequence: PMRFNGKSGVEVRLPNDLEDLKGYTSLSLFLQRPNSRENGGTENMFVMYLGNKDASRDYIGMAVVDGQLTCVYNLGDREAELQVDQILTKSETKEAVMDRVKFQRIYQFARLNYTKGATSSKPETPGVYDMDGRNSNTLLNLDPENVVFYVGGYPPDFKLPSRLSFPPYKGCIELDDLNENVLSLYNFKKTFNLNTTEVEPC | ||||||
Domain | 2598-2760 | Laminin G-like 2 | ||||
Sequence: SDKNYFEGTGYARVPTQPHAPIPTFGQTIQTTVDRGLLFFAENGDRFISLNIEDGKLMVRYKLNSELPKERGVGDAINNGRDHSIQIKIGKLQKRMWINVDVQNTIIDGEVFDFSTYYLGGIPIAIRERFNISTPAFRGCMKNLKKTSGVVRLNDTVGVTKKC | ||||||
Domain | 2767-2927 | Laminin G-like 3 | ||||
Sequence: VRSASFSRGGQLSFTDLGLPPTDHLQASFGFQTFQPSGILLDHQTWTRNLQVTLEDGYIELSTSDSGGPIFKSPQTYMDGLLHYVSVISDNSGLRLLIDDQLLRNSKRLKHISSSRQSLRLGGSNFEGCISNVFVQRLSLSPEVLDLTSNSLKRDVSLGGC | ||||||
Domain | 2986-3150 | Laminin G-like 4 | ||||
Sequence: ALQFGDIPTSHLLFKLPQELLKPRSQFAVDMQTTSSRGLVFHTGTKNSFMALYLSKGRLVFALGTDGKKLRIKSKEKCNDGKWHTVVFGHDGEKGRLVVDGLRAREGSLPGNSTISIRAPVYLGSPPSGKPKSLPTNSFVGCLKNFQLDSKPLYTPSSSFGVSSC | ||||||
Domain | 3157-3330 | Laminin G-like 5 | ||||
Sequence: KGIYFSEEGGHVVLAHSVLLGPEFKLVFSIRPRSLTGILIHIGSQPGKHLCVYLEAGKVTASMDSGAGGTSTSVTPKQSLCDGQWHSVAVTIKQHILHLELDTDSSYTAGQIPFPPASTQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIHVNHIPVPVTEALEVQGPVSLNGC |
Domain
The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.
Domain G is globular.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 4 isoforms produced by Alternative splicing.
Q16787-2
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.
- Name2
- SynonymsB
- Length3,333
- Mass (Da)366,619
- Last updated2022-02-23 v3
- Checksum6F99AF4D4B99FCB0
Q16787-1
- Name1
- SynonymsA
- Differences from canonical
- 1-1620: Missing
- 1621-1665: LYFTETQRLTLSEVGLEEASDTGSGRIALAVEICACPPAYAGDSC → MPPAVRRSACSMGWLWIFGAALGQCLGYSSQQQRVPFLQPPGQSQLQASYVEFRPS
Q16787-3
- Name3
- Differences from canonical
- 1946-2002: ILLKQISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRNFGKHLREAEADKRESQLL → M
Q16787-4
- Name4
- Differences from canonical
- 1-1609: Missing
- 1610-1665: LSRLADVRIQGLYFTETQRLTLSEVGLEEASDTGSGRIALAVEICACPPAYAGDSC → MPPAVRRSACSMGWLWIFGAALGQCLGYSSQQQRVPFLQPPGQSQLQASYVEFRPS
- 1946-2002: ILLKQISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRNFGKHLREAEADKRESQLL → M
Computationally mapped potential isoform sequences
There are 10 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A075B783 | A0A075B783_HUMAN | LAMA3 | 576 | ||
K7EIP4 | K7EIP4_HUMAN | LAMA3 | 1147 | ||
A0A0A0MSA0 | A0A0A0MSA0_HUMAN | LAMA3 | 3277 | ||
A0A0A0MTS5 | A0A0A0MTS5_HUMAN | LAMA3 | 1668 | ||
A0A0A6YYF2 | A0A0A6YYF2_HUMAN | LAMA3 | 1724 | ||
A0A3B3ITG1 | A0A3B3ITG1_HUMAN | LAMA3 | 2198 | ||
K7EMU9 | K7EMU9_HUMAN | LAMA3 | 37 | ||
K7EPP3 | K7EPP3_HUMAN | LAMA3 | 94 | ||
K7EQ42 | K7EQ42_HUMAN | LAMA3 | 59 | ||
K7ERM0 | K7ERM0_HUMAN | LAMA3 | 134 |
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_047079 | 1-1609 | in isoform 4 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_035738 | 1-1620 | in isoform 1 | |||
Sequence: Missing | ||||||
Sequence conflict | 1544 | in Ref. 5; CAA59429 and 6; CAA59325 | ||||
Sequence: G → A | ||||||
Alternative sequence | VSP_047080 | 1610-1665 | in isoform 4 | |||
Sequence: LSRLADVRIQGLYFTETQRLTLSEVGLEEASDTGSGRIALAVEICACPPAYAGDSC → MPPAVRRSACSMGWLWIFGAALGQCLGYSSQQQRVPFLQPPGQSQLQASYVEFRPS | ||||||
Alternative sequence | VSP_035739 | 1621-1665 | in isoform 1 | |||
Sequence: LYFTETQRLTLSEVGLEEASDTGSGRIALAVEICACPPAYAGDSC → MPPAVRRSACSMGWLWIFGAALGQCLGYSSQQQRVPFLQPPGQSQLQASYVEFRPS | ||||||
Sequence conflict | 1743-1745 | in Ref. 5; CAA59428/CAA59429 | ||||
Sequence: ATG → GMC | ||||||
Alternative sequence | VSP_043487 | 1946-2002 | in isoform 3 and isoform 4 | |||
Sequence: ILLKQISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRNFGKHLREAEADKRESQLL → M | ||||||
Sequence conflict | 2101 | in Ref. 5; CAA59428/CAA59429 | ||||
Sequence: M → K | ||||||
Sequence conflict | 2374 | in Ref. 5; CAA59428/CAA59429 | ||||
Sequence: R → L | ||||||
Sequence conflict | 2589 | in Ref. 5; CAA59428/CAA59429 | ||||
Sequence: E → Q | ||||||
Sequence conflict | 2672 | in Ref. 5; CAA59428/CAA59429 | ||||
Sequence: D → A | ||||||
Sequence conflict | 2804 | in Ref. 5; CAA59428/CAA59429 | ||||
Sequence: G → A |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY327114 EMBL· GenBank· DDBJ | AAQ72569.1 EMBL· GenBank· DDBJ | mRNA | ||
AY327115 EMBL· GenBank· DDBJ | AAQ72570.1 EMBL· GenBank· DDBJ | mRNA | ||
AY327116 EMBL· GenBank· DDBJ | AAQ72571.1 EMBL· GenBank· DDBJ | mRNA | ||
AB107369 EMBL· GenBank· DDBJ | BAD13428.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
EF444992 EMBL· GenBank· DDBJ | ACA06011.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC010754 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC067796 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC090366 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
X85107 EMBL· GenBank· DDBJ | CAA59428.1 EMBL· GenBank· DDBJ | mRNA | ||
X85108 EMBL· GenBank· DDBJ | CAA59429.1 EMBL· GenBank· DDBJ | mRNA | ||
X84900 EMBL· GenBank· DDBJ | CAA59325.1 EMBL· GenBank· DDBJ | mRNA | ||
L34155 EMBL· GenBank· DDBJ | AAA59483.1 EMBL· GenBank· DDBJ | mRNA |