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

P02469 (LAMB1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Laminin subunit beta-1
Alternative name(s):
Laminin B1 chain
Laminin-1 subunit beta
Laminin-10 subunit beta
Laminin-12 subunit beta
Laminin-2 subunit beta
Laminin-6 subunit beta
Laminin-8 subunit beta
Gene names
Name:Lamb1
Synonyms:Lamb-1, Lamb1-1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1786 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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. Involved in the organization of the laminar architecture of the cerebral cortex By similarity. It is probably required for the integrity of the basement membrane/glia limitans that serves as an anchor point for the endfeet of radial glial cells and as a physical barrier to migrating neurons By similarity. Radial glial cells play a central role in cerebral cortical development, where they act both as the proliferative unit of the cerebral cortex and a scaffold for neurons migrating toward the pial surface By similarity.

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-1 is a subunit of laminin-1 (laminin-111 or EHS laminin), laminin-2 (laminin-211 or merosin), laminin-6 (laminin-311 or K-laminin), laminin-8 (laminin-411), laminin-10 (laminin-511) and laminin-12 (laminin-213).

Subcellular location

Secretedextracellular spaceextracellular matrixbasement membrane. Note: Major component.

Tissue specificity

Widely expressed in the embryo. High levels are detected in the cerebellar basement membrane, at postnatal day 7. Ref.6

Sequence similarities

Contains 13 laminin EGF-like domains.

Contains 1 laminin IV type B domain.

Contains 1 laminin N-terminal domain.

Sequence caution

The sequence AAA39407.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentBasement membrane
Extracellular matrix
Secreted
   DomainCoiled coil
Laminin EGF-like domain
Repeat
Signal
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

cell migration

Inferred from mutant phenotype PubMed 9004048. Source: MGI

embryo implantation

Inferred from mutant phenotype PubMed 15102706. Source: MGI

learning or memory

Non-traceable author statement PubMed 15207330. Source: UniProtKB

negative regulation of cell adhesion

Inferred from direct assay PubMed 7639691. Source: UniProtKB

neuron projection development

Inferred from sequence or structural similarity. Source: HGNC

odontogenesis

Inferred from sequence or structural similarity. Source: HGNC

positive regulation of cell migration

Inferred from sequence or structural similarity. Source: HGNC

   Cellular_componentbasal lamina

Inferred from direct assay PubMed 9396756. Source: MGI

basement membrane

Inferred from direct assay PubMed 12631063PubMed 16041630PubMed 16631359. Source: UniProtKB

extracellular region

Traceable author statement. Source: Reactome

laminin complex

Inferred from direct assay PubMed 8034675. Source: MGI

laminin-1 complex

Inferred from sequence or structural similarity. Source: HGNC

laminin-10 complex

Inferred from sequence or structural similarity. Source: HGNC

laminin-2 complex

Inferred from sequence or structural similarity. Source: HGNC

laminin-8 complex

Inferred from sequence or structural similarity. Source: HGNC

perinuclear region of cytoplasm

Inferred from direct assay PubMed 15207330. Source: UniProtKB

proteinaceous extracellular matrix

Inferred from direct assay PubMed 16554364. Source: MGI

   Molecular_functionenzyme binding

Inferred from physical interaction PubMed 15474030. Source: MGI

extracellular matrix structural constituent

Inferred from sequence or structural similarity. Source: HGNC

glycosphingolipid binding

Inferred from direct assay PubMed 19118221. Source: MGI

integrin binding

Inferred from mutant phenotype PubMed 9004048. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

AGRNP316962EBI-6662997,EBI-457650From a different organism.
Lamc1P024684EBI-6662997,EBI-7059830

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121
Chain22 – 17861765Laminin subunit beta-1
PRO_0000017066

Regions

Domain31 – 270240Laminin N-terminal
Domain271 – 33464Laminin EGF-like 1
Domain335 – 39763Laminin EGF-like 2
Domain398 – 45760Laminin EGF-like 3
Domain458 – 50952Laminin EGF-like 4
Domain510 – 54031Laminin EGF-like 5; truncated
Domain549 – 767219Laminin IV type B
Domain773 – 82048Laminin EGF-like 6
Domain821 – 86646Laminin EGF-like 7
Domain867 – 91650Laminin EGF-like 8
Domain917 – 97559Laminin EGF-like 9
Domain976 – 102752Laminin EGF-like 10
Domain1028 – 108356Laminin EGF-like 11
Domain1084 – 113148Laminin EGF-like 12
Domain1132 – 117847Laminin EGF-like 13
Region1179 – 1397219Domain II
Region1398 – 143033Domain alpha
Region1431 – 1786356Domain I
Coiled coil1216 – 1315100 Potential
Coiled coil1368 – 138821 Potential
Coiled coil1448 – 1778331 Potential

Amino acid modifications

Glycosylation1201N-linked (GlcNAc...) Potential
Glycosylation3561N-linked (GlcNAc...) Potential
Glycosylation5191N-linked (GlcNAc...) Potential
Glycosylation6771N-linked (GlcNAc...) Potential
Glycosylation10411N-linked (GlcNAc...) Potential
Glycosylation11951N-linked (GlcNAc...) Potential
Glycosylation12791N-linked (GlcNAc...) Ref.5
Glycosylation13361N-linked (GlcNAc...) Ref.5
Glycosylation13431N-linked (GlcNAc...) Ref.5
Glycosylation14871N-linked (GlcNAc...) Potential
Glycosylation15421N-linked (GlcNAc...) Potential
Glycosylation16431N-linked (GlcNAc...) Potential
Disulfide bond271 ↔ 280 By similarity
Disulfide bond273 ↔ 298 By similarity
Disulfide bond300 ↔ 309 By similarity
Disulfide bond312 ↔ 332 By similarity
Disulfide bond335 ↔ 344 By similarity
Disulfide bond337 ↔ 362 By similarity
Disulfide bond365 ↔ 374 By similarity
Disulfide bond377 ↔ 395 By similarity
Disulfide bond398 ↔ 411 By similarity
Disulfide bond400 ↔ 426 By similarity
Disulfide bond428 ↔ 437 By similarity
Disulfide bond440 ↔ 455 By similarity
Disulfide bond458 ↔ 472 By similarity
Disulfide bond460 ↔ 479 By similarity
Disulfide bond481 ↔ 490 By similarity
Disulfide bond493 ↔ 507 By similarity
Disulfide bond510 ↔ 522 By similarity
Disulfide bond512 ↔ 529 By similarity
Disulfide bond531 ↔ 540 By similarity
Disulfide bond773 ↔ 785 By similarity
Disulfide bond775 ↔ 792 By similarity
Disulfide bond794 ↔ 803 By similarity
Disulfide bond806 ↔ 818 By similarity
Disulfide bond821 ↔ 833 By similarity
Disulfide bond823 ↔ 840 By similarity
Disulfide bond842 ↔ 851 By similarity
Disulfide bond854 ↔ 864 By similarity
Disulfide bond867 ↔ 876 By similarity
Disulfide bond869 ↔ 883 By similarity
Disulfide bond886 ↔ 895 By similarity
Disulfide bond898 ↔ 914 By similarity
Disulfide bond917 ↔ 933 By similarity
Disulfide bond919 ↔ 944 By similarity
Disulfide bond946 ↔ 955 By similarity
Disulfide bond958 ↔ 973 By similarity
Disulfide bond976 ↔ 990 By similarity
Disulfide bond978 ↔ 997 By similarity
Disulfide bond1000 ↔ 1009 By similarity
Disulfide bond1012 ↔ 1025 By similarity
Disulfide bond1028 ↔ 1040 By similarity
Disulfide bond1030 ↔ 1054 By similarity
Disulfide bond1056 ↔ 1065 By similarity
Disulfide bond1068 ↔ 1081 By similarity
Disulfide bond1084 ↔ 1096 By similarity
Disulfide bond1086 ↔ 1103 By similarity
Disulfide bond1105 ↔ 1114 By similarity
Disulfide bond1117 ↔ 1129 By similarity
Disulfide bond1132 ↔ 1144 By similarity
Disulfide bond1134 ↔ 1151 By similarity
Disulfide bond1153 ↔ 1162 By similarity
Disulfide bond1165 ↔ 1176 By similarity
Disulfide bond1179Interchain Probable
Disulfide bond1182Interchain Probable
Disulfide bond1785Interchain Probable

Experimental info

Sequence conflict1591A → T in AAA39407. Ref.1
Sequence conflict5691I → V in AAA39407. Ref.1
Sequence conflict9931E → D in AAA39407. Ref.1
Sequence conflict13931V → A in AAA39407. Ref.1
Sequence conflict13931V → A in CAA28839. Ref.3
Sequence conflict1531 – 15344MEMP → SGNA in AAA39407. Ref.1
Sequence conflict16921G → C in CAA28839. Ref.3
Sequence conflict17491D → N in CAA28839. Ref.3

Secondary structure

........................................................................ 1786
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02469 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: E7F258170C3626DD

FASTA1,786197,090
        10         20         30         40         50         60 
MGLLQVFAFG VLALWGTRVC AQEPEFSYGC AEGSCYPATG DLLIGRAQKL SVTSTCGLHK 

        70         80         90        100        110        120 
PEPYCIVSHL QEDKKCFICD SRDPYHETLN PDSHLIENVV TTFAPNRLKI WWQSENGVEN 

       130        140        150        160        170        180 
VTIQLDLEAE FHFTHLIMTF KTFRPAAMLI ERSSDFGKAW GVYRYFAYDC ESSFPGISTG 

       190        200        210        220        230        240 
PMKKVDDIIC DSRYSDIEPS TEGEVIFRAL DPAFKIEDPY SPRIQNLLKI TNLRIKFVKL 

       250        260        270        280        290        300 
HTLGDNLLDS RMEIREKYYY AVYDMVVRGN CFCYGHASEC APVDGVNEEV EGMVHGHCMC 

       310        320        330        340        350        360 
RHNTKGLNCE LCMDFYHDLP WRPAEGRNSN ACKKCNCNEH SSSCHFDMAV FLATGNVSGG 

       370        380        390        400        410        420 
VCDNCQHNTM GRNCEQCKPF YFQHPERDIR DPNLCEPCTC DPAGSENGGI CDGYTDFSVG 

       430        440        450        460        470        480 
LIAGQCRCKL HVEGERCDVC KEGFYDLSAE DPYGCKSCAC NPLGTIPGGN PCDSETGYCY 

       490        500        510        520        530        540 
CKRLVTGQRC DQCLPQHWGL SNDLDGCRPC DCDLGGALNN SCSEDSGQCS CLPHMIGRQC 

       550        560        570        580        590        600 
NEVESGYYFT TLDHYIYEAE EANLGPGVIV VERQYIQDRI PSWTGPGFVR VPEGAYLEFF 

       610        620        630        640        650        660 
IDNIPYSMEY EILIRYEPQL PDHWEKAVIT VQRPGKIPAS SRCGNTVPDD DNQVVSLSPG 

       670        680        690        700        710        720 
SRYVVLPRPV CFEKGMNYTV RLELPQYTAS GSDVESPYTF IDSLVLMPYC KSLDIFTVGG 

       730        740        750        760        770        780 
SGDGEVTNSA WETFQRYRCL ENSRSVVKTP MTDVCRNIIF SISALIHQTG LACECDPQGS 

       790        800        810        820        830        840 
LSSVCDPNGG QCQCRPNVVG RTCNRCAPGT FGFGPNGCKP CDCHLQGSAS AFCDAITGQC 

       850        860        870        880        890        900 
HCFQGIYARQ CDRCLPGYWG FPSCQPCQCN GHALDCDTVT GECLSCQDYT TGHNCERCLA 

       910        920        930        940        950        960 
GYYGDPIIGS GDHCRPCPCP DGPDSGRQFA RSCYQDPVTL QLACVCDPGY IGSRCDDCAS 

       970        980        990       1000       1010       1020 
GFFGNPSDFG GSCQPCQCHH NIDTTDPEAC DKETGRCLKC LYHTEGDHCQ LCQYGYYGDA 

      1030       1040       1050       1060       1070       1080 
LRQDCRKCVC NYLGTVKEHC NGSDCHCDKA TGQCSCLPNV IGQNCDRCAP NTWQLASGTG 

      1090       1100       1110       1120       1130       1140 
CGPCNCNAAH SFGPSCNEFT GQCQCMPGFG GRTCSECQEL FWGDPDVECR ACDCDPRGIE 

      1150       1160       1170       1180       1190       1200 
TPQCDQSTGQ CVCVEGVEGP RCDKCTRGYS GVFPDCTPCH QCFALWDAII GELTNRTHKF 

      1210       1220       1230       1240       1250       1260 
LEKAKALKIS GVIGPYRETV DSVEKKVNEI KDILAQSPAA EPLKNIGILF EEAEKLTKDV 

      1270       1280       1290       1300       1310       1320 
TEKMAQVEVK LTDTASQSNS TAGELGALQA EAESLDKTVK ELAEQLEFIK NSDIQGALDS 

      1330       1340       1350       1360       1370       1380 
ITKYFQMSLE AEKRVNASTT DPNSTVEQSA LTRDRVEDLM LERESPFKEQ QEEQARLLDE 

      1390       1400       1410       1420       1430       1440 
LAGKLQSLDL SAVAQMTCGT PPGADCSESE CGGPNCRTDE GEKKCGGPGC GGLVTVAHSA 

      1450       1460       1470       1480       1490       1500 
WQKAMDFDRD VLSALAEVEQ LSKMVSEAKV RADEAKQNAQ DVLLKTNATK EKVDKSNEDL 

      1510       1520       1530       1540       1550       1560 
RNLIKQIRNF LTEDSADLDS IEAVANEVLK MEMPSTPQQL QNLTEDIRER VETLSQVEVI 

      1570       1580       1590       1600       1610       1620 
LQQSAADIAR AELLLEEAKR ASKSATDVKV TADMVKEALE EAEKAQVAAE KAIKQADEDI 

      1630       1640       1650       1660       1670       1680 
QGTQNLLTSI ESETAASEET LTNASQRISK LERNVEELKR KAAQNSGEAE YIEKVVYSVK 

      1690       1700       1710       1720       1730       1740 
QNADDVKKTL DGELDEKYKK VESLIAQKTE ESADARRKAE LLQNEAKTLL AQANSKLQLL 

      1750       1760       1770       1780 
EDLERKYEDN QKYLEDKAQE LVRLEGEVRS LLKDISEKVA VYSTCL 

« Hide

References

« Hide 'large scale' references
[1]"Sequence of the cDNA encoding the laminin B1 chain reveals a multidomain protein containing cysteine-rich repeats."
Sasaki M., Kato S., Kohno K., Martin G.R., Yamada Y.
Proc. Natl. Acad. Sci. U.S.A. 84:935-939(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"Sequencing of laminin B chain cDNAs reveals C-terminal regions of coiled-coil alpha-helix."
Barlow D.P., Green N.M., Kurkinen M., Hogan B.L.M.
EMBO J. 3:2355-2362(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1292-1786.
[4]"Cloning of the mouse laminin alpha 4 cDNA. Expression in a subset of endothelium."
Frieser M., Noeckel H., Pausch F., Roeder C., Hahn A., Deutzmann R., Sorokin L.M.
Eur. J. Biochem. 246:727-735(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 165-172; 539-547 AND 712-719.
Strain: BALB/c.
Tissue: Endothelial cell.
[5]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1279; ASN-1336 AND ASN-1343.
[6]"Mutations in LAMB1 cause cobblestone brain malformation without muscular or ocular abnormalities."
Radmanesh F., Caglayan A.O., Silhavy J.L., Yilmaz C., Cantagrel V., Omar T., Rosti B., Kaymakcalan H., Gabriel S., Li M., Sestan N., Bilguvar K., Dobyns W.B., Zaki M.S., Gunel M., Gleeson J.G.
Am. J. Hum. Genet. 92:468-474(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M15525 mRNA. Translation: AAA39407.1. Different initiation.
CR974423 Genomic DNA. No translation available.
CT571245 Genomic DNA. No translation available.
X05212 mRNA. Translation: CAA28839.1.
PIRMMMSB1. A26413.
RefSeqXP_006515056.1. XM_006514993.1.
UniGeneMm.172674.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4AQSX-ray3.11A21-542[»]
ProteinModelPortalP02469.
SMRP02469. Positions 29-492.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP02469. 6 interactions.
MINTMINT-1206337.

PTM databases

PhosphoSiteP02469.

Proteomic databases

PaxDbP02469.
PRIDEP02469.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000169088; ENSMUSP00000132778; ENSMUSG00000002900.
GeneID16777.

Organism-specific databases

MGIMGI:96743. Lamb1.

Phylogenomic databases

eggNOGNOG241384.
GeneTreeENSGT00720000108616.
HOVERGENHBG052301.
InParanoidP02469.
OrthoDBEOG75XGK0.

Enzyme and pathway databases

ReactomeREACT_188576. Developmental Biology.

Gene expression databases

ArrayExpressP02469.
BgeeP02469.
CleanExMM_LAMB1-1.
GenevestigatorP02469.

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. 9 hits.
PS01186. EGF_2. 2 hits.
PS01248. EGF_LAM_1. 11 hits.
PS50027. EGF_LAM_2. 13 hits.
PS51116. LAMININ_IVB. 1 hit.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLAMB1. mouse.
PROP02469.
SOURCESearch...

Entry information

Entry nameLAMB1_MOUSE
AccessionPrimary (citable) accession number: P02469
Secondary accession number(s): E9PXZ9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 135 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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