Q60675 · LAMA2_MOUSE

  • Protein
    Laminin subunit alpha-2
  • Gene
    Lama2
  • 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 Componentdendritic spine
Cellular Componentextracellular region
Cellular Componentneuromuscular junction
Cellular Componentprotein complex involved in cell-matrix adhesion
Cellular Componentsarcolemma
Cellular Componentsynaptic cleft
Molecular Functionextracellular matrix structural constituent
Molecular Functionsignaling receptor binding
Biological Processanimal organ morphogenesis
Biological Processaxon guidance
Biological Processcell adhesion
Biological Processpositive regulation of cell adhesion
Biological Processpositive regulation of integrin-mediated signaling pathway
Biological Processpositive regulation of muscle cell differentiation
Biological Processpositive regulation of synaptic transmission, cholinergic
Biological Processregulation of basement membrane organization
Biological Processregulation of cell migration
Biological Processregulation of embryonic development
Biological ProcessSchwann cell differentiation
Biological Processtissue development

Keywords

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Laminin subunit alpha-2
  • Alternative names
    • Laminin M chain
    • Laminin-12 subunit alpha
    • Laminin-2 subunit alpha
    • Laminin-4 subunit alpha
    • Merosin heavy chain

Gene names

    • Name
      Lama2

Organism names

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

Accessions

  • Primary accession
    Q60675
  • Secondary accessions
    • F8VQ43
    • Q05003
    • Q64061

Proteomes

Organism-specific databases

Phenotypes & Variants

Involvement in disease

  • Defects in Lama2 are a cause of murine muscular dystrophy (dy2J)

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 135 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

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

TypeIDPosition(s)Description
Signal1-19
ChainPRO_000001705720-3118Laminin subunit alpha-2
Glycosylation51N-linked (GlcNAc...) asparagine
Glycosylation85N-linked (GlcNAc...) asparagine
Disulfide bond283↔292
Disulfide bond285↔303
Glycosylation299N-linked (GlcNAc...) asparagine
Disulfide bond305↔314
Disulfide bond317↔337
Disulfide bond340↔349
Disulfide bond342↔374
Glycosylation359N-linked (GlcNAc...) asparagine
Glycosylation376N-linked (GlcNAc...) asparagine
Disulfide bond377↔386
Disulfide bond389↔407
Disulfide bond410↔422
Disulfide bond412↔438
Disulfide bond440↔449
Disulfide bond452↔462
Disulfide bond465↔478
Glycosylation466N-linked (GlcNAc...) asparagine
Disulfide bond467↔482
Disulfide bond484↔493
Disulfide bond496↔511
Glycosylation742N-linked (GlcNAc...) asparagine
Disulfide bond753↔762
Disulfide bond755↔769
Disulfide bond772↔781
Disulfide bond784↔800
Disulfide bond803↔818
Disulfide bond805↔828
Disulfide bond831↔840
Disulfide bond843↔858
Disulfide bond861↔875
Disulfide bond863↔882
Disulfide bond885↔894
Disulfide bond897↔911
Disulfide bond914↔926
Disulfide bond916↔933
Glycosylation919N-linked (GlcNAc...) asparagine
Disulfide bond935↔944
Disulfide bond947↔960
Disulfide bond963↔975
Disulfide bond965↔981
Disulfide bond983↔992
Disulfide bond995↔1007
Disulfide bond1010↔1019
Disulfide bond1012↔1026
Disulfide bond1028↔1037
Glycosylation1031N-linked (GlcNAc...) asparagine
Disulfide bond1040↔1053
Disulfide bond1056↔1068
Glycosylation1057N-linked (GlcNAc...) asparagine
Disulfide bond1058↔1075
Disulfide bond1077↔1086
Disulfide bond1089↔1099
Disulfide bond1102↔1114
Disulfide bond1104↔1130
Disulfide bond1132↔1141
Disulfide bond1144↔1159
Disulfide bond1378↔1387
Disulfide bond1416↔1425
Disulfide bond1418↔1432
Disulfide bond1435↔1444
Disulfide bond1447↔1462
Disulfide bond1465↔1480
Disulfide bond1467↔1490
Disulfide bond1493↔1502
Disulfide bond1505↔1520
Disulfide bond1523↔1535
Disulfide bond1525↔1542
Disulfide bond1544↔1553
Disulfide bond1556↔1567
Disulfide bond1570Interchain
Disulfide bond1574Interchain
Glycosylation1593N-linked (GlcNAc...) asparagine
Glycosylation1610N-linked (GlcNAc...) asparagine
Glycosylation1696N-linked (GlcNAc...) asparagine
Glycosylation1806N-linked (GlcNAc...) asparagine
Glycosylation1897N-linked (GlcNAc...) asparagine
Glycosylation1912N-linked (GlcNAc...) asparagine
Glycosylation1916N-linked (GlcNAc...) asparagine
Glycosylation2013N-linked (GlcNAc...) asparagine
Glycosylation2024N-linked (GlcNAc...) asparagine
Glycosylation2041N-linked (GlcNAc...) asparagine
Glycosylation2122N-linked (GlcNAc...) asparagine
Glycosylation2236N-linked (GlcNAc...) asparagine
Disulfide bond2298↔2324
Glycosylation2356N-linked (GlcNAc...) asparagine
Glycosylation2431N-linked (GlcNAc...) asparagine
Glycosylation2474N-linked (GlcNAc...) asparagine
Disulfide bond2491↔2517
Glycosylation2547N-linked (GlcNAc...) asparagine
Glycosylation2554N-linked (GlcNAc...) asparagine
Glycosylation2644N-linked (GlcNAc...) asparagine
Disulfide bond2679↔2706
Glycosylation2889N-linked (GlcNAc...) asparagine
Disulfide bond2905↔2930
Disulfide bond3083↔3115

Keywords

Proteomic databases

PTM databases

Expression

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-2 is a subunit of laminin-2 (laminin-211 or merosin), laminin-4 (laminin-221 or S-merosin) and laminin-12 (laminin-213). Interacts with FBLN1, FBLN2 and NID2.

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain, region, coiled coil.

TypeIDPosition(s)Description
Domain31-282Laminin N-terminal
Domain283-339Laminin EGF-like 1
Domain340-409Laminin EGF-like 2
Domain410-464Laminin EGF-like 3
Domain465-513Laminin EGF-like 4
Domain514-523Laminin EGF-like 5; first part
Domain527-719Laminin IV type A 1
Domain720-752Laminin EGF-like 5; second part
Domain753-802Laminin EGF-like 6
Domain803-860Laminin EGF-like 7
Domain861-913Laminin EGF-like 8
Domain914-962Laminin EGF-like 9
Domain963-1009Laminin EGF-like 10
Domain1010-1055Laminin EGF-like 11
Domain1056-1101Laminin EGF-like 12
Domain1102-1161Laminin EGF-like 13
Domain1162-1171Laminin EGF-like 14; first part
Domain1172-1375Laminin IV type A 2
Domain1376-1415Laminin EGF-like 14; second part
Domain1416-1464Laminin EGF-like 15
Domain1465-1522Laminin EGF-like 16
Domain1523-1569Laminin EGF-like 17
Region1570-2140Domain II and I
Coiled coil1662-1863
Coiled coil1923-2146
Domain2141-2324Laminin G-like 1
Domain2336-2517Laminin G-like 2
Domain2522-2706Laminin G-like 3
Domain2759-2930Laminin G-like 4
Domain2929-3115Laminin 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 VI, IV and G 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
    3,118
  • Mass (Da)
    343,815
  • Last updated
    2013-10-16 v2
  • Checksum
    CCD31C71B1E0DFD4
MPAATAGILLLLLLGTLEGSQTQRRQSQAHQQRGLFPAVLNLASNALITTNATCGEKGPEMYCKLVEHVPGQPVRNPQCRICNQNSSNPYQRHPITNAIDGKNTWWQSPSIKNGVEYHYVTITLDLQQVFQIAYVIVKAANSPRPGNWILERSLDDVEYKPWQYHAVTDTECLTLYNIYPRTGPPSYAKDDEVICTSFYSKIHPLENGEIHISLINGRPSADDPSPELLEFTSARYIRLRFQRIRTLNADLMMFAHKDPREIDPIVTRRYYYSVKDISVGGMCICYGHARACPLDPATNKSRCECEHNTCGESCDRCCPGFHQKPWRAGTFLTKSECEACNCHGKAEECYYDETVASRNLSLNIHGKYIGGGVCINCTHNTAGINCETCVDGFFRPKGVSPNYPRPCQPCHCDPTGSLSEVCVKDEKYAQRGLKPGSCHCKTGFGGVNCDRCVRGYHGYPDCQPCNCSGLGSTNEDPCVGPCSCKENVEGEDCSRCKSGFFNLQEDNQKGCEECFCSGVSNRCQSSYWTYGNIQDMRGWYLTDLSGRIRMAPQLDNPDSPQQISISNSEARKSLLDGYYWSAPPPYLGNRLPAVGGQLSFTISYDLEEEEDDTEKILQLMIIFEGNDLRISTAYKEVYLEPSEEHIEEVSLKEEAFTIHGTNLPVTRKDFMIVLTNLERVLMQITYNLGMDAIFRLSSVNLESAVPYPTDRRIATDVEVCQCPPGYSGSSCETCWPRHRRVNGTIFGGICEPCQCFAHAEACDDITGECLNCKDHTGGPYCNECLPGFYGDPTRGSPEDCQPCACPLNIPSNNFSPTCHLDRSLGLICDECPIGYTGPRCERCAEGYFGQPSIPGGSCQPCQCNDNLDYSIPGSCDSLSGSCLICKPGTTGRYCELCADGYFGDAVNAKNCQPCRCNINGSFSEICHTRTGQCECRPNVQGRHCDECKPETFGLQLGRGCLPCNCNSFGSKSFDCEASGQCWCQPGVAGKKCDRCAHGYFNFQEGGCIACDCSHLGNNCDPKTGQCICPPNTTGEKCSECLPNTWGHSIVTGCKVCNCSTVGSLASQCNVNTGQCSCHPKFSGMKCSECSRGHWNYPLCTLCDCFLPGTDATTCDLETRKCSCSDQTGQCSCKVNVEGVHCDRCRPGKFGLDAKNPLGCSSCYCFGVTSQCSEAKGLIRTWVTLSDEQTILPLVDEALQHTTTKGIAFQKPEIVAKMDEVRQELHLEPFYWKLPQQFEGKKLMAYGGKLKYAIYFEARDETGFATYKPQVIIRGGTPTHARIITRHMAAPLIGQLTRHEIEMTEKEWKYYGDDPRISRTVTREDFLDILYDIHYILIKATYGNVVRQSRISEISMEVAEPGHVLAGSPPAHLIERCDCPPGYSGLSCETCAPGFYRLRSEPGGRTPGPTLGTCVPCQCNGHSSQCDPETSVCQNCQHHTAGDFCERCALGYYGIVRGLPNDCQPCACPLISPSNNFSPSCVLEGLEDYRCTACPRGYEGQYCERCAPGYTGSPSSPGGSCQECECDPYGSLPVPCDRVTGLCTCRPGATGRKCDGCEHWHAREGAECVFCGDECTGLLLGDLARLEQMTMNINLTGPLPAPYKILYGLENTTQELKHLLSPQRAPERLIQLAEGNVNTLVMETNELLTRATKVTADGEQTGQDAERTNSRAESLEEFIKGLVQDAEAINEKAVQLNETLGNQDKTAERNLEELQKEIDRMLKELRSKDLQTQKEVAEDELVAAEGLLKRVNKLFGEPRAQNEDMEKDLQQKLAEYKNKLDDAWDLLREATDKTRDANRLSAANQKNMTILETKKEAIEGSKRQIENTLKEGNDILDEANRLLGEINSVIDYVDDIKTKLPPMSEELSDKIDDLAQEIKDRRLAEKVFQAESHAAQLNDSSAVLDGILDEAKNISFNATAAFRAYSNIKDYIDEAEKVAREAKELAQGATKLATSPQGLLKEDAKGSLQKSFRILNEAKKLANDVKGNHNDLNDLKTRLETADLRNSGLLGALNDTMDKLSAITNDTAAKLQAVKEKAREANDTAKAVLAQVKDLHQNLDGLKQNYNKLADSVAKTNAVVKDPSKNKIIADAGTSVRNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIKVSVSSGGDCVRTYRPEIKKGSYNNIVVHVKTAVADNLLFYLGSAKFIDFLAIEMRKGKVSFLWDVGSGVGRVEYPDLTIDDSYWYRIEASRTGRNGSISVRALDGPKASMVPSTYHSVSPPGYTILDVDANAMLFVGGLTGKIKKADAVRVITFTGCMGETYFDNKPIGLWNFREKEGDCKGCTVSPQVEDSEGTIQFDGEGYALVSRPIRWYPNISTVMFKFRTFSSSALLMYLATRDLKDFMSVELSDGHVKVSYDLGSGMTSVVSNQNHNDGKWKAFTLSRIQKQANISIVDIDSNQEENVATSSSGNNFGLDLKADDKIYFGGLPTLRNLSMKARPEVNVKKYSGCLKDIEISRTPYNILSSPDYVGVTKGCSLENVYTVSFPKPGFVELAAVSIDVGTEINLSFSTRNESGIILLGSGGTLTPPRRKRRQTTQAYYAIFLNKGRLEVHLSSGTRTMRKIVIKPEPNLFHDGREHSVHVERTRGIFTVQIDEDRRHMQNLTEEQPIEVKKLFVGGAPPEFQPSPLRNIPAFQGCVWNLVINSIPMDFAQPIAFKNADIGRCTYQKPREDESEAVPAEVIVQPQPVPTPAFPFPAPTMVHGPCVAESEPALLTGSKQFGLSRNSHIAIAFDDTKVKNRLTIELEVRTEAESGLLFYMARINHADFATVQLRNGFPYFSYDLGSGDTSTMIPTKINDGQWHKIKIVRVKQEGILYVDDASSQTISPKKADILDVVGILYVGGLPINYTTRRIGPVTYSLDGCVRNLHMEQAPVDLDQPTSSFHVGTCFANAESGTYFDGTGFAKAVGGFKVGLDLLVEFEFRTTRPTGVLLGVSSQKMDGMGIEMIDEKLMFHVDNGAGRFTAIYDAGIPGHMCNGQWHKVTAKKIKNRLELVVDGNQVDAQSPNSASTSADTNDPVFVGGFPGGLNQFGLTTNIRFRGCIRSLKLTKGTGKPLEVNFAKALELRGVQPVSCPTT

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A1W2P7N3A0A1W2P7N3_MOUSELama21127
A0A5F8MPG7A0A5F8MPG7_MOUSELama2256
A0A087WRP2A0A087WRP2_MOUSELama21349

Sequence caution

The sequence AAC52165.1 differs from that shown. Reason: Frameshift

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict616in Ref. 1; AAC52165
Sequence conflict646in Ref. 1; AAC52165
Sequence conflict678-682in Ref. 1; AAC52165
Sequence conflict704in Ref. 1; AAC52165
Sequence conflict853in Ref. 1; AAC52165
Sequence conflict908in Ref. 1; AAC52165
Sequence conflict917in Ref. 1; AAC52165
Sequence conflict925in Ref. 1; AAC52165
Sequence conflict1694in Ref. 1; AAC52165
Sequence conflict1840in Ref. 1; AAC52165
Sequence conflict2205in Ref. 1; AAC52165
Sequence conflict2214-2215in Ref. 1; AAC52165
Sequence conflict2523in Ref. 1; AAC52165
Sequence conflict2642in Ref. 1; AAC52165
Sequence conflict2729in Ref. 1; AAC52165
Sequence conflict2739in Ref. 1; AAC52165
Sequence conflict2773in Ref. 1; AAC52165
Sequence conflict2802in Ref. 1; AAC52165
Sequence conflict2810in Ref. 1; AAC52165
Sequence conflict2820in Ref. 1; AAC52165
Sequence conflict2829-2831in Ref. 1; AAC52165
Sequence conflict2878in Ref. 1; AAC52165
Sequence conflict2946in Ref. 1; AAC52165
Sequence conflict2953in Ref. 1; AAC52165
Sequence conflict2976in Ref. 1; AAC52165
Sequence conflict3011in Ref. 1; AAC52165
Sequence conflict3022in Ref. 1; AAC52165

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U12147
EMBL· GenBank· DDBJ
AAC52165.1
EMBL· GenBank· DDBJ
mRNA Frameshift
AC101709
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AC152982
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AC153800
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AC155942
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AC167232
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AC171406
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
X69869
EMBL· GenBank· DDBJ
CAA49502.1
EMBL· GenBank· DDBJ
mRNA
S75315
EMBL· GenBank· DDBJ
AAB33573.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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