P15800 · LAMB2_RAT

  • Protein
    Laminin subunit beta-2
  • Gene
    Lamb2
  • 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 Componentlaminin complex
Cellular Componentlaminin-3 complex
Cellular Componentneuromuscular junction
Cellular Componentsynapse
Cellular Componentsynaptic cleft
Molecular Functionintegrin binding
Molecular Functionstructural constituent of synapse-associated extracellular matrix
Biological Processanimal organ morphogenesis
Biological Processastrocyte development
Biological Processaxon extension involved in regeneration
Biological Processaxon guidance
Biological Processbasement membrane assembly
Biological Processcell migration
Biological Processcell morphogenesis
Biological Processmetanephric glomerular basement membrane development
Biological Processmetanephric podocyte development
Biological Processneuromuscular junction development
Biological Processneuron projection development
Biological Processretina development in camera-type eye
Biological ProcessSchwann cell development
Biological Processsubstrate adhesion-dependent cell spreading
Biological Processsynapse organization
Biological Processtissue development
Biological Processvisual perception

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Laminin subunit beta-2
  • Alternative names
    • Laminin chain B3
    • Laminin-11 subunit beta
    • Laminin-14 subunit beta
    • Laminin-15 subunit beta
    • Laminin-3 subunit beta

Gene names

    • Name
      Lamb2

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus

Accessions

  • Primary accession
    P15800

Proteomes

Organism-specific databases

PTM/Processing

Features

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

TypeIDPosition(s)Description
Signal1-35
ChainPRO_000001707036-1801Laminin subunit beta-2
Glycosylation251N-linked (GlcNAc...) asparagine
Disulfide bond286↔295
Disulfide bond288↔313
Disulfide bond315↔324
Disulfide bond327↔347
Disulfide bond350↔359
Disulfide bond352↔377
Glycosylation371N-linked (GlcNAc...) asparagine
Disulfide bond380↔389
Disulfide bond392↔410
Disulfide bond413↔426
Disulfide bond415↔441
Disulfide bond443↔452
Disulfide bond455↔470
Disulfide bond473↔487
Disulfide bond475↔494
Disulfide bond496↔505
Disulfide bond508↔522
Disulfide bond525↔537
Disulfide bond527↔544
Disulfide bond546↔555
Disulfide bond786↔798
Disulfide bond788↔805
Disulfide bond807↔816
Disulfide bond819↔831
Disulfide bond834↔846
Disulfide bond836↔853
Disulfide bond855↔864
Disulfide bond867↔877
Disulfide bond880↔889
Disulfide bond882↔896
Disulfide bond899↔908
Disulfide bond911↔927
Disulfide bond930↔946
Disulfide bond932↔957
Disulfide bond959↔968
Disulfide bond971↔986
Disulfide bond989↔1003
Disulfide bond991↔1010
Disulfide bond1013↔1022
Disulfide bond1025↔1038
Disulfide bond1041↔1061
Disulfide bond1043↔1068
Disulfide bond1070↔1079
Disulfide bond1082↔1095
Glycosylation1088N-linked (GlcNAc...) asparagine
Disulfide bond1098↔1110
Disulfide bond1100↔1117
Disulfide bond1119↔1128
Disulfide bond1131↔1143
Disulfide bond1146↔1158
Disulfide bond1148↔1165
Disulfide bond1167↔1176
Disulfide bond1179↔1190
Disulfide bond1193Interchain
Disulfide bond1196Interchain
Glycosylation1252N-linked (GlcNAc...) asparagine
Glycosylation1311N-linked (GlcNAc...) asparagine
Glycosylation1351N-linked (GlcNAc...) asparagine
Glycosylation1502N-linked (GlcNAc...) asparagine
Modified residue1535Phosphoserine
Disulfide bond1800Interchain

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Found in the basement membranes (major component). S-laminin is concentrated in the synaptic cleft of the neuromuscular junction.

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-2 is a subunit of laminin-3 (laminin-121 or S-laminin), laminin-4 (laminin-221 or S-merosin), laminin-7 (laminin-321 or KS-laminin), laminin-9 (laminin-421), laminin-11 (laminin-521), laminin-14 (laminin-423) and laminin-15 (laminin-523).

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region, coiled coil.

TypeIDPosition(s)Description
Domain46-285Laminin N-terminal
Domain286-349Laminin EGF-like 1
Domain350-412Laminin EGF-like 2
Domain413-472Laminin EGF-like 3
Domain473-524Laminin EGF-like 4
Domain525-555Laminin EGF-like 5; truncated
Domain564-780Laminin IV type B
Domain786-833Laminin EGF-like 6
Domain834-879Laminin EGF-like 7
Domain880-929Laminin EGF-like 8
Domain930-988Laminin EGF-like 9
Domain989-1040Laminin EGF-like 10
Domain1041-1097Laminin EGF-like 11
Domain1098-1145Laminin EGF-like 12
Domain1146-1192Laminin EGF-like 13
Region1193-1412Domain II
Coiled coil1259-1306
Region1413-1445Domain alpha
Region1446-1801Domain I
Coiled coil1475-1529
Coiled coil1576-1793
Region1684-1703Disordered

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    1,801
  • Mass (Da)
    196,474
  • Last updated
    1990-04-01 v1
  • Checksum
    97AEF32F8F31FA75
MEWASGKPGRGRQGQPVPWELRLGLLLSVLAATLAQVPSLDVPGCSRGSCYPATGDLLVGRADRLTASSTCGLHSPQPYCIVSHLQDEKKCFLCDSRRPFSARDNPNSHRIQNVVTSFAPQRRTAWWQSENGVPMVTIQLDLEAEFHFTHLIMTFKTFRPAAMLVERSADFGRTWRVYRYFSYDCGADFPGIPLAPPRRWDDVVCESRYSEIEPSTEGEVIYRVLDPAIPIPDPYSSRIQNLLKITNLRVNLTRLHTLGDNLLDPRREIREKYYYALYELVIRGNCFCYGHASQCAPAPGAPAHAEGMVHGACICKHNTRGLNCEQCQDFYQDLPWHPAEDGHTHACRKCECNGHSHSCHFDMAVYLASGNVSGGVCDGCQHNTAGRHCELCRPFFYRDPTKDMRDPAACRPCDCDPMGSQDGGRCDSHDDPVLGLVSGQCRCKEHVVGTRCQQCRDGFFGLSASNPRGCQRCQCNSRGTVPGGTPCDSSSGTCFCKRLVTGDGCDRCLPGHWGLSHDLLGCRPCDCDVGGALDPQCDEATGQCPCRPHMIGRRCEQVQPGYFRPFLDHLTWEAEGAHGQVLEVVERLVTNRETPSWTGVGFVRLREGQEVEFLVTSLPRAMDYDLLLRWEPQVPEQWAELELVVQRPGPVSAHSPCGHVLPRDDRIQGMLHPNTRVLVFPRPVCLEPGLSYKLKLKLTGTGGRAHPETPYSGSGILIDSLVLQPHVLMLEMFSGGDAAALERRTTFERYRCHEEGLMPSKTPLSEACVPLLISASSLVYNGALPCQCDPQGSLSSECNPHGGQCRCKPGVVGRRCDACATGYYGFGPAGCQACQCSPDGALSALCEGTSGQCLCRTGAFGLRCDHCQRGQWGFPNCRPCVCNGRADECDAHTGACLGCRDYTGGEHCERCIAGFHGDPRLPYGGQCRPCPCPEGPGSQRHFATSCHRDGYSQQIVCHCRAGYTGLRCEACAPGHFGDPSKPGGRCQLCECSGNIDPTDPGACDPHTGQCLRCLHHTEGPHCGHCKPGFHGQAARQSCHRCTCNLLGTDPQRCPSTDLCHCDPSTGQCPCLPHVQGLSCDRCAPNFWNFTSGRGCQPCACHPSRARGPTCNEFTGQCHCHAGFGGRTCSECQELHWGDPGLQCRACDCDPRGIDKPQCHRSTGHCSCRPGVSGVRCDQCARGFSGVFPACHPCHACFGDWDRVVQDLAARTRRLEQWAQELQQTGVLGAFESSFLNLQGKLGMVQAIVAARNTSAASTAKLVEATEGLRHEIGKTTERLTQLEAELTDVQDENFNANHALSGLERDGLALNLTLRQLDQHLDILKHSNFLGAYDSIRHAHSQSTEAERRANASTFAIPSPVSNSADTRRRAEVLMGAQRENFNRQHLANQQALGRLSTHTHTLSLTGVNELVCGAPGDAPCATSPCGGAGCRDEDGQPRCGGLGCSGAAATADLALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIEMVATRVLDISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQIYNTCQ

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
M0R6K0M0R6K0_RATLamb21801
Q5M7W9Q5M7W9_RATLamb21593

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X16563
EMBL· GenBank· DDBJ
CAA34561.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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