Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q61292 (LAMB2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Laminin subunit beta-2
Alternative name(s):
Laminin-11 subunit beta
Laminin-14 subunit beta
Laminin-15 subunit beta
Laminin-3 subunit beta
Laminin-4 subunit beta
Laminin-7 subunit beta
Laminin-9 subunit beta
S-laminin subunit beta
Short name=S-LAM beta
Gene names
Name:Lamb2
Synonyms:Lams
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length1799 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

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. Ref.5

Laminin-3 (S-laminin) regulates the formation of motor nerve terminals. Ref.5

Subunit structure

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).

Subcellular location

Secreted › extracellular space › extracellular matrix › basement membrane.

Tissue specificity

Neuromuscular synapse and kidney glomerulus.

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.

Sequence similarities

Contains 13 laminin EGF-like domains.

Contains 1 laminin IV type B domain.

Contains 1 laminin N-terminal domain.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentBasement membrane
Extracellular matrix
Secreted
   DomainCoiled coil
Laminin EGF-like domain
Repeat
Signal
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processSchwann cell development

Inferred from direct assay PubMed 9641682. Source: MGI

astrocyte development

Inferred from genetic interaction PubMed 19907020. Source: MGI

axon extension involved in regeneration

Inferred from mutant phenotype PubMed 9396756. Source: MGI

axon guidance

Inferred from genetic interaction PubMed 19295126. Source: MGI

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

cell morphogenesis involved in differentiation

Inferred from genetic interaction PubMed 19907020. Source: MGI

metanephric glomerular basement membrane development

Inferred from mutant phenotype PubMed 16886065PubMed 7670489. Source: MGI

metanephric glomerular visceral epithelial cell development

Inferred from mutant phenotype PubMed 16886065. Source: MGI

neuromuscular junction development

Inferred from mutant phenotype PubMed 17418794Ref.5. Source: MGI

neuron projection development

Inferred from direct assay PubMed 20566382. Source: MGI

retina development in camera-type eye

Inferred from genetic interaction PubMed 19907020. Source: MGI

synapse organization

Inferred from mutant phenotype PubMed 17189701. Source: MGI

visual perception

Inferred from genetic interaction PubMed 19907020. Source: MGI

   Cellular_componentbasal lamina

Inferred from direct assay PubMed 7670489. Source: MGI

basement membrane

Inferred from direct assay PubMed 16041630. Source: UniProtKB

extracellular region

Traceable author statement. Source: Reactome

laminin complex

Inferred from direct assay PubMed 8034675. Source: MGI

laminin-3 complex

Inferred from direct assay PubMed 20566382. Source: MGI

synapse

Inferred from direct assay PubMed 17189701. Source: MGI

   Molecular_functionintegrin binding

Inferred from physical interaction PubMed 20566382. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3535 Potential
Chain36 – 17991764Laminin subunit beta-2
PRO_0000017069

Regions

Domain46 – 285240Laminin N-terminal
Domain286 – 34964Laminin EGF-like 1
Domain350 – 41263Laminin EGF-like 2
Domain413 – 47260Laminin EGF-like 3
Domain473 – 52452Laminin EGF-like 4
Domain525 – 55531Laminin EGF-like 5; truncated
Domain564 – 778215Laminin IV type B
Domain784 – 83148Laminin EGF-like 6
Domain832 – 87746Laminin EGF-like 7
Domain878 – 92750Laminin EGF-like 8
Domain928 – 98659Laminin EGF-like 9
Domain987 – 103852Laminin EGF-like 10
Domain1039 – 109557Laminin EGF-like 11
Domain1096 – 114348Laminin EGF-like 12
Domain1144 – 119047Laminin EGF-like 13
Region1191 – 1410220Domain II
Region1411 – 144333Domain alpha
Region1444 – 1799356Domain I
Coiled coil1257 – 130448 Potential
Coiled coil1473 – 152755 Potential
Coiled coil1577 – 1791215 Potential

Amino acid modifications

Glycosylation2511N-linked (GlcNAc...) Potential
Glycosylation3711N-linked (GlcNAc...) Potential
Glycosylation10861N-linked (GlcNAc...) Potential
Glycosylation12501N-linked (GlcNAc...) Potential
Glycosylation13091N-linked (GlcNAc...) Potential
Glycosylation13491N-linked (GlcNAc...) Potential
Glycosylation15001N-linked (GlcNAc...) Potential
Disulfide bond286 ↔ 295 By similarity
Disulfide bond288 ↔ 313 By similarity
Disulfide bond315 ↔ 324 By similarity
Disulfide bond327 ↔ 347 By similarity
Disulfide bond350 ↔ 359 By similarity
Disulfide bond352 ↔ 377 By similarity
Disulfide bond380 ↔ 389 By similarity
Disulfide bond392 ↔ 410 By similarity
Disulfide bond413 ↔ 426 By similarity
Disulfide bond415 ↔ 441 By similarity
Disulfide bond443 ↔ 452 By similarity
Disulfide bond455 ↔ 470 By similarity
Disulfide bond473 ↔ 487 By similarity
Disulfide bond475 ↔ 494 By similarity
Disulfide bond496 ↔ 505 By similarity
Disulfide bond508 ↔ 522 By similarity
Disulfide bond525 ↔ 537 By similarity
Disulfide bond527 ↔ 544 By similarity
Disulfide bond546 ↔ 555 By similarity
Disulfide bond784 ↔ 796 By similarity
Disulfide bond786 ↔ 803 By similarity
Disulfide bond805 ↔ 814 By similarity
Disulfide bond817 ↔ 829 By similarity
Disulfide bond832 ↔ 844 By similarity
Disulfide bond834 ↔ 851 By similarity
Disulfide bond853 ↔ 862 By similarity
Disulfide bond865 ↔ 875 By similarity
Disulfide bond878 ↔ 887 By similarity
Disulfide bond880 ↔ 894 By similarity
Disulfide bond897 ↔ 906 By similarity
Disulfide bond909 ↔ 925 By similarity
Disulfide bond928 ↔ 944 By similarity
Disulfide bond930 ↔ 955 By similarity
Disulfide bond957 ↔ 966 By similarity
Disulfide bond969 ↔ 984 By similarity
Disulfide bond987 ↔ 1001 By similarity
Disulfide bond989 ↔ 1008 By similarity
Disulfide bond1011 ↔ 1020 By similarity
Disulfide bond1023 ↔ 1036 By similarity
Disulfide bond1039 ↔ 1059 By similarity
Disulfide bond1041 ↔ 1066 By similarity
Disulfide bond1068 ↔ 1077 By similarity
Disulfide bond1080 ↔ 1093 By similarity
Disulfide bond1096 ↔ 1108 By similarity
Disulfide bond1098 ↔ 1115 By similarity
Disulfide bond1117 ↔ 1126 By similarity
Disulfide bond1129 ↔ 1141 By similarity
Disulfide bond1144 ↔ 1156 By similarity
Disulfide bond1146 ↔ 1163 By similarity
Disulfide bond1165 ↔ 1174 By similarity
Disulfide bond1177 ↔ 1188 By similarity
Disulfide bond1191Interchain Probable
Disulfide bond1194Interchain Probable
Disulfide bond1798Interchain Probable

Experimental info

Sequence conflict5451R → P in AAC53535. Ref.1
Sequence conflict5811G → V in AAC53535. Ref.1
Sequence conflict6771F → V in AAC53535. Ref.1
Sequence conflict9561Q → H in AAC53535. Ref.1
Sequence conflict9591E → A in AAC53535. Ref.1
Sequence conflict9731H → P in AAC53535. Ref.1
Sequence conflict13061L → F in AAC53535. Ref.1
Sequence conflict14491T → P in AAC53535. Ref.1
Sequence conflict14601T → S in AAC53535. Ref.1
Sequence conflict14871E → A in AAC53535. Ref.1
Sequence conflict16271W → R in AAC53535. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q61292 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 37CA24B9CDA0791F

FASTA1,799196,579
        10         20         30         40         50         60 
MEWASGEPGR GRQGQPLPWE LRLGLLLSVL AATLAQAPSL DVPGCSRGSC YPATGDLLVG 

        70         80         90        100        110        120 
RADRLTASST CGLHSPQPYC IVSHLQDEKK CFLCDSRRPF SARDNPNSHR IQNVVTSFAP 

       130        140        150        160        170        180 
QRRTAWWQSE NGVPMVTIQL DLEAEFHFTH LIMTFKTFRP AAMLVERSAD FGRTWHVYRY 

       190        200        210        220        230        240 
FSYDCGADFP GIPLAPPRRW DDVVCESRYS EIEPSTEGEV IYRVLDPAIP IPDPYSSRIQ 

       250        260        270        280        290        300 
NLLKITNLRV NLTRLHTLGD NLLDPRREIR EKYYYALYEL VIRGNCFCYG HASQCAPAPG 

       310        320        330        340        350        360 
APAHAEGMVH GACICKHNTR GLNCEQCQDF YQDLPWHPAE DGHTHACRKC ECNGHTHSCH 

       370        380        390        400        410        420 
FDMAVYLASG NVSGGVCDGC QHNTAGRHCE FCRPFFYRDP TKDMRDPAVC RPCDCDPMGS 

       430        440        450        460        470        480 
QDGGRCDSHD DPVLGLVSGQ CRCKEHVVGT RCQQCRDGFF GLSASDPRGC QRCQCNSRGT 

       490        500        510        520        530        540 
VPGSSPCDSS SGTCFCKRLV TGHGCDRCLP GHWGLSHDLL GCRPCDCDVG GALDPQCDEA 

       550        560        570        580        590        600 
TGQCRCRQHM IGRRCEQVQP GYFRPFLDHL TWEAEAAQGQ GLEVVERLVT NRETPSWTGP 

       610        620        630        640        650        660 
GFVRLREGQE VEFLVTSLPR AMDYDLLLRW EPQVPEQWAE LELMVQRPGP VSAHSPCGHV 

       670        680        690        700        710        720 
LPKDDRIQGM LHPNTRFLVF PRPVCLEPGI SYKLKLKLIG TGGRAQPETS YSGLLIDSLV 

       730        740        750        760        770        780 
LQPHVLVLEM FSGGDAAALE RRTTFERYRC HEEGLMPSKA PLSETCAPLL ISVSALIYNG 

       790        800        810        820        830        840 
ALPCQCDPQG SLSSECSPHG GQCRCKPGVV GRRCDVCATG YYGFGPAGCQ ACQCSPDGAL 

       850        860        870        880        890        900 
SALCEGTSGQ CPCRPGAFGL RCDHCQRGQW GFPNCRPCVC NGRADECDTH TGACLGCRDY 

       910        920        930        940        950        960 
TGGEHCERCI AGFHGDPRLP YGGQCRPCPC PEGPGSQRHF ATSCHRDGYS QQIVCQCREG 

       970        980        990       1000       1010       1020 
YTGLRCEACA PGHFGDPSKP GGRCQLCECS GNIDPMDPDA CDPHTGQCLR CLHNTEGPHC 

      1030       1040       1050       1060       1070       1080 
GYCKPGFHGQ AARQSCHRCT CNLLGTDPRR CPSTDLCHCD PSTGQCPCLP HVQGLNCDHC 

      1090       1100       1110       1120       1130       1140 
APNFWNFTSG RGCQPCACHP SRARGPTCNE FTGQCHCHAG FGGRTCSECQ ELYWGDPGLQ 

      1150       1160       1170       1180       1190       1200 
CRACDCDPRG IDKPQCHRST GHCSCRPGVS GVRCDQCARG FSGVFPACHP CHACFGDWDR 

      1210       1220       1230       1240       1250       1260 
VVQDLAARTR RLEQWAQELQ QTGVLGAFES SFLNMQGKLG MVQAIMSARN ASAASTAKLV 

      1270       1280       1290       1300       1310       1320 
EATEGLRHEI GKTTERLTQL EAELTAVQDE NFNANHALSG LERDGLALNL TLRQLDQHLE 

      1330       1340       1350       1360       1370       1380 
ILKHSNFLGA YDSIRHAHSQ STEAERRANA STFAVPSPVS NSADTRRRTE VLMGAQKENF 

      1390       1400       1410       1420       1430       1440 
NRQHLANQQA LGRLSAHAHT LSLTGINELV CGAPGDAPCA TSPCGGAGCR DEDGQPRCGG 

      1450       1460       1470       1480       1490       1500 
LGCSGAAATA DLALGRARHT QAELQRALVE GGGILSRVSE TRRQAEEAQQ RAQAALDKAN 

      1510       1520       1530       1540       1550       1560 
ASRGQVEQAN QELRELIQNV KDFLSQEGAD PDSIEMVATR VLDISIPASP EQIQRLASEI 

      1570       1580       1590       1600       1610       1620 
AERVRSLADV DTILAHTMGD VRRAEQLLQD AHRARSRAEG ERQKAETVQA ALEEAQRAQG 

      1630       1640       1650       1660       1670       1680 
AAQGAIWGAV VDTQNTEQTL QRVQERMAGA EKSLNSAGER ARQLDALLEA LKLKRAGNSL 

      1690       1700       1710       1720       1730       1740 
AASTAEETAG SAQSRAREAE KQLREQVGDQ YQTVRALAER KAEGVLAAQA RAEQLRDEAR 

      1750       1760       1770       1780       1790 
DLLQAAQDKL QRLQELEGTY EENERALEGK AAQLDGLEAR MRSVLQAINL QVQIYNTCQ

« Hide

References

« Hide 'large scale' references
[1]"Structural organization of the human and mouse laminin beta2 chain genes, and alternative splicing at the 5' end of the human transcript."
Durkin M.E., Gautam M., Loechel S., Sanes J.R., Merlie J.P., Albrechtsen R., Wewer U.M.
J. Biol. Chem. 271:13407-13416(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/J.
[2]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary tumor.
[4]"S-laminin gene (Lams) maps to F1 band of mouse chromosome 9."
Aberdam D., Galliano M.-F., Mattei M.-G., Ortonne J.-P., Meneguzzi G.
Mamm. Genome 5:393-394(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 348-428.
Tissue: Lung.
[5]"Aberrant differentiation of neuromuscular junctions in mice lacking s-laminin/laminin beta 2."
Noakes P.G., Gautam M., Mudd J., Sanes J.R., Merlie J.P.
Nature 374:258-262(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
Strain: 129/J.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U43541, U42624 Genomic DNA. Translation: AAC53535.1.
CH466560 Genomic DNA. Translation: EDL21291.1.
CH466560 Genomic DNA. Translation: EDL21292.1.
BC026051 mRNA. Translation: AAH26051.1.
X75928 mRNA. Translation: CAA53532.1.
CCDSCCDS23528.1.
PIRI48749.
RefSeqNP_032509.2. NM_008483.3.
XP_006511711.1. XM_006511648.1.
UniGeneMm.425599.

3D structure databases

ProteinModelPortalQ61292.
SMRQ61292. Positions 44-507.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ61292. 2 interactions.
MINTMINT-4100139.
STRING10090.ENSMUSP00000069087.

PTM databases

PhosphoSiteQ61292.

Proteomic databases

MaxQBQ61292.
PaxDbQ61292.
PRIDEQ61292.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000065014; ENSMUSP00000069087; ENSMUSG00000052911.
GeneID16779.
KEGGmmu:16779.
UCSCuc009rpr.2. mouse.

Organism-specific databases

CTD3913.
MGIMGI:99916. Lamb2.

Phylogenomic databases

eggNOGNOG241384.
GeneTreeENSGT00720000108616.
HOGENOMHOG000007552.
HOVERGENHBG052301.
InParanoidQ8R0Y0.
KOK06243.
OMAQPYCIVS.
OrthoDBEOG75XGK0.
TreeFamTF312903.

Enzyme and pathway databases

ReactomeREACT_206066. Extracellular matrix organization.

Gene expression databases

ArrayExpressQ61292.
BgeeQ61292.
CleanExMM_LAMB2.
GenevestigatorQ61292.

Family and domain databases

InterProIPR002049. EGF_laminin.
IPR013015. Laminin_IV.
IPR008211. Laminin_N.
[Graphical view]
PfamPF00053. Laminin_EGF. 13 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTSM00180. EGF_Lam. 13 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
PROSITEPS00022. EGF_1. 10 hits.
PS01186. EGF_2. 2 hits.
PS01248. EGF_LAM_1. 12 hits.
PS50027. EGF_LAM_2. 13 hits.
PS51116. LAMININ_IVB. 1 hit.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLAMB2. mouse.
NextBio290628.
PROQ61292.
SOURCESearch...

Entry information

Entry nameLAMB2_MOUSE
AccessionPrimary (citable) accession number: Q61292
Secondary accession number(s): Q62182, Q8R0Y0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents