Q61789 · LAMA3_MOUSE

  • Protein
    Laminin subunit alpha-3
  • Gene
    Lama3
  • 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.
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 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 Componentadherens junction
Cellular Componentbasement membrane
Cellular Componentcollagen-containing extracellular matrix
Cellular Componentendoplasmic reticulum
Cellular Componentextracellular region
Cellular Componenthemidesmosome
Cellular Componentlaminin-3 complex
Cellular Componentlaminin-5 complex
Molecular Functionextracellular matrix structural constituent
Molecular Functionsignaling receptor binding
Biological Processanimal organ morphogenesis
Biological Processaxon guidance
Biological Processcell-cell adhesion
Biological Processendodermal cell differentiation
Biological Processhemidesmosome assembly
Biological Processregulation of cell adhesion
Biological Processregulation of cell migration
Biological Processregulation of embryonic development
Biological Processtissue development

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Laminin subunit alpha-3
  • Alternative names
    • Epiligrin subunit alpha
    • Kalinin subunit alpha
    • Laminin-5 subunit alpha
    • Laminin-6 subunit alpha
    • Laminin-7 subunit alpha
    • Nicein subunit alpha

Gene names

    • Name
      Lama3

Organism names

  • Taxonomic identifier
  • Strains
    • BALB/cJ
    • C57BL/6J
    • ICR
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q61789
  • Secondary accessions
    • E9PUR4
    • O08751
    • Q61788
    • Q61966
    • Q9JHQ7

Proteomes

Organism-specific databases

PTM/Processing

Features

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

TypeIDPosition(s)Description
Signal1-31
ChainPRO_000001705932-3330Laminin subunit alpha-3
Glycosylation139N-linked (GlcNAc...) asparagine
Disulfide bond296↔305
Disulfide bond298↔316
Disulfide bond318↔327
Disulfide bond330↔350
Disulfide bond353↔362
Disulfide bond355↔387
Disulfide bond390↔399
Disulfide bond402↔420
Disulfide bond423↔433
Disulfide bond425↔440
Disulfide bond442↔451
Glycosylation445N-linked (GlcNAc...) asparagine
Disulfide bond454↔464
Disulfide bond488↔500
Disulfide bond490↔506
Disulfide bond508↔517
Disulfide bond520↔530
Disulfide bond533↔545
Disulfide bond535↔552
Disulfide bond554↔563
Disulfide bond566↔583
Disulfide bond628↔642
Disulfide bond630↔649
Disulfide bond651↔660
Disulfide bond663↔678
Disulfide bond681↔693
Disulfide bond683↔700
Disulfide bond702↔711
Disulfide bond1309↔1316
Disulfide bond1311↔1323
Disulfide bond1325↔1334
Disulfide bond1337↔1350
Disulfide bond1353↔1368
Glycosylation1354N-linked (GlcNAc...) asparagine
Disulfide bond1355↔1375
Disulfide bond1377↔1386
Disulfide bond1389↔1399
Disulfide bond1402↔1414
Disulfide bond1404↔1421
Disulfide bond1423↔1432
Disulfide bond1435↔1450
Glycosylation1673N-linked (GlcNAc...) asparagine
Disulfide bond1684↔1693
Disulfide bond1686↔1700
Disulfide bond1703↔1712
Disulfide bond1715↔1728
Disulfide bond1731↔1743
Disulfide bond1733↔1752
Disulfide bond1754↔1763
Disulfide bond1766↔1781
Disulfide bond1819Interchain
Disulfide bond1822Interchain
Glycosylation2159N-linked (GlcNAc...) asparagine
Glycosylation2261N-linked (GlcNAc...) asparagine
Glycosylation2332N-linked (GlcNAc...) asparagine
Glycosylation2361N-linked (GlcNAc...) asparagine
Glycosylation2498N-linked (GlcNAc...) asparagine
Disulfide bond2557↔2587
Glycosylation2580N-linked (GlcNAc...) asparagine
Disulfide bond2733↔2756
Glycosylation2747N-linked (GlcNAc...) asparagine
Disulfide bond2891↔2923
Glycosylation3094N-linked (GlcNAc...) asparagine
Disulfide bond3124↔3147
Glycosylation3270N-linked (GlcNAc...) asparagine
Disulfide bond3299↔3327

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Basal membrane of the upper alimentary tract and urinary and nasal epithelia, salivary glands and teeth (both variants). Isoform A is predominantly expressed in skin, hair follicles and developing neurons of the trigeminal ganglion. Isoform B was found in bronchi, alveoli, stomach, intestinal crypts, whisker pads, CNS, telencephalic neuroectoderm, thalamus, Rathke pouch and periventricular subependymal germinal layer.

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. 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

Structure

3D structure databases

Family & Domains

Features

Showing features for domain, region, coiled coil, motif.

TypeIDPosition(s)Description
Domain40-295Laminin N-terminal
Region295-725Domain V
Domain296-350Laminin EGF-like 1
Domain353-420Laminin EGF-like 2
Domain423-464Laminin EGF-like 3
Domain488-530Laminin EGF-like 4
Domain533-576Laminin EGF-like 5
Domain582-625Laminin EGF-like 6
Domain628-678Laminin EGF-like 7
Domain681-725Laminin EGF-like 8
Region793-1262Domain IV 1 (domain IV B)
Region1263-1462Domain III B
Domain1309-1352Laminin EGF-like 9
Domain1353-1401Laminin EGF-like 10
Domain1402-1452Laminin EGF-like 11
Domain1453-1462Laminin EGF-like 12; first part
Domain1466-1650Laminin IV type A
Domain1651-1683Laminin EGF-like 12; second part
Region1651-1818Domain III A
Domain1684-1730Laminin EGF-like 13
Domain1731-1783Laminin EGF-like 14
Domain1784-1818Laminin EGF-like 15; truncated
Region1819-2385Domain II and I
Coiled coil1851-1980
Coiled coil2012-2057
Coiled coil2088-2165
Coiled coil2211-2238
Motif2274-2276Cell attachment site
Coiled coil2318-2383
Domain2386-2587Laminin G-like 1
Domain2594-2756Laminin G-like 2
Domain2763-2923Laminin G-like 3
Domain2983-3147Laminin G-like 4
Domain3154-3327Laminin G-like 5

Domain

The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.
Domains IV and G are globular.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.

This entry describes 2 isoforms produced by Alternative splicing.

Q61789-1

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.

Download
  • Length
    3,330
  • Mass (Da)
    366,227
  • Last updated
    2013-10-16 v4
  • Checksum
    993EB20BACDD6C59
MAVALGRAPRSLPLLLTLLLLLLLRMSPSWSVVGQDHPMSSRSLHPPYFNLAQAARIWATATCGERDPEVSRPRPELFCKLVGGPAAQGSGHTIQGQFCDYCNSEDSRKAHPASHAIDGSERWWQSPPLSSGTQYNQVNLTLDLGQLFHVAYILIKFANSPRPDLWILERSVDFGSTYSPWQYFAHSRRDCVEQFGQEANMAITQDDQMLCVTEYSRIVPLENGEIVVSLINGRPGAKKFAFSDTLREFTKATNIRLRFLRTNTLLGHLISKAERDPTVTRRYYYSIKDISVGGRCVCNGHAEACSADNPEKQFRCECQHHTCGDTCNRCCAGYNQRRWQPAGQEQHNECEACNCHGHAVDCYYDPDVEHQQASLNSKGVYAGGGVCINCQHNTAGVNCEKCAKGYFRPHGVPVDALHGCIPCSCDPERADDCDQGSGHCHCKPNFSGDYCETCADGYYNFPFCLRIPVFPNYTPSPEDPVAGNIKGCDCNLEGVLPEICDDRGRCLCRPGVEGPQCDSCRSGSYSFPICQACQCSTIGSYPVPCDPGNGQCDCLPGITGRQCDRCLSGAYDFPYCQGSGSVCHPAGTLDSSLGYCQCKQHVASPTCSVCKPLYWNLAKENPRGCSECQCHEAGTLSGIGECGQEDGDCSCKAHVTGDACDTCEDGFFSLEKSNYFGCQGCQCDIGGALTTMCSGPSGVCQCREHVEGKQCQRPENNYYFPDLHHMKYEVEDGTGPNGRNLRFGFDPLVFPEFSWRGYAPMTSVQNEVRVRLSVRQSSLSLFRIVLRYISPGTEAISGRITLYSSQGDSDALQSRKITFPPSKEPAFVTVPGNGFAGPFSITPGTWIACIQVEGVLLDYLVLLPRDYYEAFTLQVPVTEPCAHTGSPQDNCLLYQHLPLTAFSCTLACEARHFLLDGELRPLAMRQPTPTHPAMVDLSGREVELQLRLRVPQVGHYVVLLEYATEVEQLFVVDVNLKSSGSALAGQVNIYSCKYSIPCRSVVIDSLSRTAVHELLADADIQLKAHMAHFLLYHICIIPAEEFSTEYLRPQVHCIASYRQHANPSASCVSLAHETPPTASILDATSRGLFSALPHEPSSPADGVTLKAPQSQVTLKGLIPHLGRHVFVIHFYQAEHPGFPTEVIVNGGRQWSGSFLASFCPHLLGCRDQVISDGQVEFDISEAEVAVTVKIPDGKSLTLVRVLVVPAENYDYQILHKTTVDKSSEFISSCGGDSFYIDPQAASGFCKNSARSLVAFYHNGAIPCECDPAGTAGHHCSPEGGQCPCRPNVIGRQCSRCATGYYGFPYCKPCNCGRRLCEEVTGKCLCPPHTVRPQCEVCEMNSFNFHPVAGCDVCNCSRKGTIEAAVSECDRDSGQCRCKPRVTGQQCDKCAPGFYQFPECVPCSCNRDGTEPSVCDPETGACMCKENVEGPQCQLCREGSFYLDPTNPKGCTKCFCFGVNTDCQSSHKQRAKFVDMMGWRLETADGVDVPVSFNPGSNSMVADLQELPPSVHSASWVAPPSYLGDKVSSYGGYLTYHAKSFGLPGDMVLLGKQPDVQLTGQHMSLIHKEPSDPRPDRLHHGRVQVIEGNFRHEGSSAPVSREELMTVLSRLERLHIRGLHFTETQRLTLGEVGLEEASDTGSGPRAHLVEMCACPPDYTGDSCQGCRPGYYWDNKSLPVGRCVPCNCNGHSNRCQDGSGICINCQHNTAGEHCERCQAGHYGNAIHGSCRVCPCPHTNSFATGCAVDGGAVRCACKPGYTGTQCERCAPGYFGNPQKFGGSCQPCNCNSNGQLGPCDPLTGDCVNQEPKDGSPAEECDDCDSCVMTLLNDLASMGEELRLVKSKLQGLSVSTGALEQIRHMETQAKDLRNQLLGFRSATSSHGSKMDDLEKELSHLNREFETLQEKAQVNSRKAQTLYNNIDQTIQSAKELDMKIKNIVQNVHILLKQMARPGGEGTDLPVGDWSRELAEAQRMMRDLRSRDFKKHLQEAEAEKMEAQLLLHRIRTWLESHQVENNGLLKNIRDSLNDYEDKLQDLRSILQEAAAQAKQATGINHENEGVLGAIQRQMKEMDSLKNDFTKYLATADSSLLQTNNLLQQMDKSQKEYESLAAALNGARQELSDRVRELSRSGGKAPLVVEAEKHAQSLQELAKQLEEIKRNTSGDELVRCAVDAATAYENILNAIRAAEDAASKATSASKSAFQTVIKEDLPKRAKTLSSDSEELLNEAKMTQKRLQQVSPALNSLQQTLKTVSVQKDLLDANLTVARDDLHGIQRGDIDSVVIGAKSMVREANGITSEVLDGLNPIQTDLGRIKDSYESARREDFSKALVDANNSVKKLTRKLPDLFIKIESINQQLLPLGNISDNVDRIRELIQQARDAANKVAIPMRFNGKSGVEVRLPNDLEDLKGYTSLSLFLQRPDLRENGGTEDMFVMYLGNKDASKDYIGMAVVDGQLTCVYNLGDREAEVQIDQVLTESESQEAVMDRVKFQRIYQFAKLNYTKEATSTKPKAPGVYDMESASSNTLLNLDPENAVFYVGGYPPGFELPRRLRFPPYKGCIELDDLNENVLSLYNFKTTFNLNTTEVEPCRRRKEESDKNYFEGTGYARIPTQPNAPFPNFMQTIQTTVDRGLLFFAENQDNFISLNIEDGNLMVKYKLNSEPPKEKGIRDTINNGRDHMILISIGKSQKRMLINMNKHSIIIEGEIFDFSTYYLGGIPIAIRERFNISTPAFQGCMKNLKKTSGVVRLNDTVGVTKKCSEDWKLVRTASFSRGGQMSFTNLDVPSLDRFQLSFGFQTFQPSGTLLNHQTRTSSLLVTLEDGHIALSTRDSSSPIFKSPGTYMDGLLHHVSVISDTSGLRLLIDDQVLRRNQRLASFSNAQQSLSMGGGYFEGCISNVFVQRMSQSPEVLDMASKSTKRDAFLGGCSLNKPPFLMLFKSPKGFNKARSFNVNQLLQDAPQAARSIEAWQDGKSCLPPLNTKATHRALQFGDSPTSHLLFKLPQELLKPRLQFSLDIQTTSSRGLVFHTGTRDSFVALYLSEGHVIFALGAGGKKLRLRSKERYHDGKWHSVVFGLSGRKVHLVVDGLRAQEGSLPGNSTISPREQVYLGLSPSRKSKSLPQHSFVGCLRNFQLDSKPLDSPSARSGVSPCLGGSLEKGIYFSQGGGHVVLANSVSLEPALTLTLSIRPRSLTGVLIHIASQSGEHLSVYMEAGKVTTSMNSEAGGTVTSITPKRSLCDGQWHSVTVSIKQHTLHLELDTDNSYTAGQLSFPPNSTRGSLHIGGVPDKLKMLTLPVWNSFFGCLKNIQVNHIPVPITEATDVQGSVSLNGCPDH

Q61789-2

  • Name
    A
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1-1619: Missing
    • 1620-1662: FTETQRLTLGEVGLEEASDTGSGPRAHLVEMCACPPDYTGDSC → MLPAVRWSAWSTGWLWIFGAALGQCLGYGSEQQRVAFLQRPSQNHLQASYMELRPS

Sequence caution

The sequence CAA58837.1 differs from that shown. Reason: Frameshift

Features

Showing features for alternative sequence, sequence conflict.

TypeIDPosition(s)Description
Alternative sequenceVSP_0030381-1619in isoform A
Sequence conflict982in Ref. 1; CAA58837
Sequence conflict1150in Ref. 1; CAA58837
Sequence conflict1224in Ref. 1; CAA58837
Sequence conflict1272in Ref. 1; CAA58837
Sequence conflict1291in Ref. 1; CAA58837
Sequence conflict1398in Ref. 1; CAA58837
Sequence conflict1466in Ref. 1; CAA58837
Sequence conflict1479in Ref. 1; CAA58837
Sequence conflict1488in Ref. 1; CAA58837
Sequence conflict1527-1528in Ref. 1; CAA58837
Sequence conflict1608in Ref. 1; CAA58837
Alternative sequenceVSP_0030391620-1662in isoform A
Sequence conflict1983-1984in Ref. 1; CAA58836/CAA58837 and 6; AAA68091
Sequence conflict1987in Ref. 1; CAA58836/CAA58837 and 6; AAA68091
Sequence conflict2463in Ref. 1; CAA58836/CAA58837 and 6; AAA68091
Sequence conflict2488in Ref. 1; CAA58836/CAA58837 and 6; AAA68091
Sequence conflict2617-2620in Ref. 1; CAA58836/CAA58837
Sequence conflict2724-2725in Ref. 1; CAA58836/CAA58837
Sequence conflict3257in Ref. 1; CAA58836/CAA58837

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X84013
EMBL· GenBank· DDBJ
CAA58836.1
EMBL· GenBank· DDBJ
mRNA
X84014
EMBL· GenBank· DDBJ
CAA58837.1
EMBL· GenBank· DDBJ
mRNA Frameshift
AC102131
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AC102248
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AC139027
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AC157909
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AJ293592
EMBL· GenBank· DDBJ
CAB99254.2
EMBL· GenBank· DDBJ
mRNA
U88353
EMBL· GenBank· DDBJ
AAC53179.1
EMBL· GenBank· DDBJ
mRNA
L20478
EMBL· GenBank· DDBJ
AAA68091.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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