Q61087 · LAMB3_MOUSE

  • Protein
    Laminin subunit beta-3
  • Gene
    Lamb3
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentbasement membrane
Cellular Componentcollagen-containing extracellular matrix
Cellular Componentextracellular region
Cellular Componentlaminin complex
Cellular Componentlaminin-5 complex
Molecular Functionprotein-containing complex binding
Biological Processanimal organ morphogenesis
Biological Processaxon guidance
Biological Processbasement membrane assembly
Biological Processbrown fat cell differentiation
Biological Processcell migration
Biological Processendodermal cell differentiation
Biological Processsubstrate adhesion-dependent cell spreading
Biological Processtissue development

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Laminin subunit beta-3
  • Alternative names
    • Epiligrin subunit bata
    • Kalinin B1 chain
    • Kalinin subunit beta
    • Laminin-5 subunit beta
    • Nicein subunit beta

Gene names

    • Name
      Lamb3

Organism names

  • Taxonomic identifier
  • Strains
    • FVB/NJ
    • FVB/N
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q61087
  • Secondary accessions
    • Q91V90

Proteomes

Organism-specific databases

PTM/Processing

Features

Showing features for signal, chain, glycosylation, disulfide bond.

TypeIDPosition(s)Description
Signal1-17
ChainPRO_000001707218-1168Laminin subunit beta-3
Glycosylation220N-linked (GlcNAc...) asparagine
Disulfide bond250↔259
Disulfide bond252↔276
Disulfide bond278↔287
Disulfide bond290↔310
Disulfide bond313↔322
Disulfide bond315↔340
Disulfide bond343↔352
Disulfide bond355↔373
Disulfide bond376↔389
Disulfide bond378↔396
Disulfide bond398↔407
Disulfide bond410↔425
Disulfide bond428↔441
Disulfide bond430↔448
Disulfide bond450↔459
Disulfide bond462↔475
Disulfide bond478↔490
Disulfide bond480↔497
Disulfide bond499↔508
Disulfide bond516↔528
Disulfide bond531↔543
Disulfide bond533↔550
Disulfide bond552↔561
Disulfide bond564↔575
Disulfide bond578Interchain
Disulfide bond581Interchain
Glycosylation601N-linked (GlcNAc...) asparagine
Glycosylation806N-linked (GlcNAc...) asparagine
Disulfide bond1167Interchain

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Found in the basement membranes (major component).

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. Beta-3 is a subunit of laminin-5 (laminin-332 or epiligrin/kalinin/nicein). Interacts with ECM1 (By similarity).

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain, region, compositional bias, coiled coil.

TypeIDPosition(s)Description
Domain22-249Laminin N-terminal
Domain250-312Laminin EGF-like 1
Domain313-375Laminin EGF-like 2
Domain376-427Laminin EGF-like 3
Domain428-477Laminin EGF-like 4
Domain478-530Laminin EGF-like 5
Domain531-577Laminin EGF-like 6
Region576-781Domain II
Compositional bias723-737Polar residues
Region723-760Disordered
Coiled coil732-754
Region782-812Domain alpha
Region813-1168Domain I
Coiled coil827-879
Coiled coil944-1129

Domain

The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.
Domain VI is globular.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    1,168
  • Mass (Da)
    128,900
  • Last updated
    2011-07-27 v2
  • Checksum
    66EB2BE1AA232215
MTAFFLLWLALPGFLCAQQACSRGACYPPVGDLLIGRTQLLRASSTCGLTKPETYCTQYGQWQMKCCKCDSRLPRNYNSHRVENVASSSGPMRWWQSQNDVSPVSLQLDLDKRMQLQDIMMDFKGLTPAGMLIERSSDFGKTWRVYQYLATDCASTFPQVHQGQPKNWQDVRCRPLSQRPNGHLTGGKVQLNLMDLASAIPASQSKKIQELGDITNLRVNFTKLAPVPQRGSYPPSAYFAVSQLRLQGSCFCHGHADRCAPNPGGSTTAVQVNNVCVCQHNTAGPNCDRCAPFYNNRPWRPAEGQDTHECQRCDCNGHSETCHFDPAVFAASQGTNGGVCDNCRDHTEGKNCERCQLHYFRNRRPSAPIHETCIPCECDPDGAVQGAPCDRLTGQCVCKEYVQGERCDLCKPGFTGLTFANPKGCHACDCSILGARKDMPCEEETGRCLCLPNVVGPKCDQCAPSHWKLASGLGCEPCACDPRNSLSSQCNQFTGQCPCREGFGGLTCSSAAIRQCPDQTYGHVATGCRACDCDFRGTEGPGCDKASGRCLCRPGFTGPRCDQCQRGHCDRYPVCVACHSCFQAYDTDLQEQARRLHSLRNATEGLWTGTGLEDHGLASRLLDAKSKIEQIRQILEGTSVTEQDVAQVANGILSIRRTLQGLPLDLPLEEEMESFSGDLGNLDRSFSRLLLMYRSKKEQFEKLSSEDPSGAFRMLTMAYEQSSRAAQQVSDSSSLLSQLRDSRREAEGLERQAGGGGTGGAQLMALRLEMASLPDLTPTINKLCGRSRQTACTPGDCPGELCPQDNGTACGSHCRGALPRAKGAFHMAGRVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVSTSRLLMEEDVQRTRLLIQQVRGFLTDPDTDAATIQQVSEAVLALWLPTDSATVLRKMKEIQAIAARLPNVDSVLSQTKQDIARARRLQAEAEQARSRAHAVEGQVDDVVGNLRQGTVALQEAQDTMQGTGRSLRLIQERVGEVQQVLVPAERLVKGMKEQMSGFWARMKELRRQAQEEQAQAMQARQLAEGASQQAMNAQEGFKRLKQKYTELKDRLGQSPVLGEQGNRILSIKMEAEELFGETMEMMDKMKDMESELLRGSQAIMLRSADLSGLEKRVEQIRSYINGRVLYYATCK

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A0A6YVX1A0A0A6YVX1_MOUSELamb3244

Features

Showing features for sequence conflict, compositional bias.

TypeIDPosition(s)Description
Sequence conflict34in Ref. 1; AAA85255
Sequence conflict271in Ref. 1; AAA85255
Sequence conflict284in Ref. 1; AAA85255
Sequence conflict320in Ref. 1; AAA85255
Sequence conflict354in Ref. 1; AAA85255
Sequence conflict361in Ref. 1; AAA85255
Sequence conflict420in Ref. 1; AAA85255
Sequence conflict525in Ref. 1; AAA85255
Sequence conflict542in Ref. 1; AAA85255
Sequence conflict646in Ref. 1; AAA85255
Compositional bias723-737Polar residues
Sequence conflict1079in Ref. 1; AAA85255
Sequence conflict1115in Ref. 1; AAA85255

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U43298
EMBL· GenBank· DDBJ
AAA85255.1
EMBL· GenBank· DDBJ
mRNA
AK155769
EMBL· GenBank· DDBJ
BAE33428.1
EMBL· GenBank· DDBJ
mRNA
CH466555
EMBL· GenBank· DDBJ
EDL12945.1
EMBL· GenBank· DDBJ
Genomic DNA
CH466555
EMBL· GenBank· DDBJ
EDL12946.1
EMBL· GenBank· DDBJ
Genomic DNA
BC008516
EMBL· GenBank· DDBJ
AAH08516.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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