Laminin subunit beta-1 precursor - Mus musculus (Mouse)

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P02469 (LAMB1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 133. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1786 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Secreted › extracellular space › extracellular matrix › basement 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 process	Cell adhesion
Cellular component	Basement membrane Extracellular matrix Secreted
Domain	Coiled coil Laminin EGF-like domain Repeat Signal
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell 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_component	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
Molecular_function	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
AGRN	P31696	2	EBI-6662997,EBI-457650	From a different organism.
Lamc1	P02468	4	EBI-6662997,EBI-7059830

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

Chain

22 – 1786

1765

Laminin subunit beta-1

PRO_0000017066

Regions

Domain

31 – 270

240

Laminin N-terminal

Domain

271 – 334

Laminin EGF-like 1

Domain

335 – 397

Laminin EGF-like 2

Domain

398 – 457

Laminin EGF-like 3

Domain

458 – 509

Laminin EGF-like 4

Domain

510 – 540

Laminin EGF-like 5; truncated

Domain

549 – 767

219

Laminin IV type B

Domain

773 – 820

Laminin EGF-like 6

Domain

821 – 866

Laminin EGF-like 7

Domain

867 – 916

Laminin EGF-like 8

Domain

917 – 975

Laminin EGF-like 9

Domain

976 – 1027

Laminin EGF-like 10

Domain

1028 – 1083

Laminin EGF-like 11

Domain

1084 – 1131

Laminin EGF-like 12

Domain

1132 – 1178

Laminin EGF-like 13

Region

1179 – 1397

219

Domain II

Region

1398 – 1430

Domain alpha

Region

1431 – 1786

356

Domain I

Coiled coil

1216 – 1315

100

Potential

Coiled coil

1368 – 1388

Potential

Coiled coil

1448 – 1778

331

Potential

Amino acid modifications

Glycosylation

120

N-linked (GlcNAc...) Potential

Glycosylation

356

N-linked (GlcNAc...) Potential

Glycosylation

519

N-linked (GlcNAc...) Potential

Glycosylation

677

N-linked (GlcNAc...) Potential

Glycosylation

1041

N-linked (GlcNAc...) Potential

Glycosylation

1195

N-linked (GlcNAc...) Potential

Glycosylation

1279

N-linked (GlcNAc...) Ref.5

Glycosylation

1336

N-linked (GlcNAc...) Ref.5

Glycosylation

1343

N-linked (GlcNAc...) Ref.5

Glycosylation

1487

N-linked (GlcNAc...) Potential

Glycosylation

1542

N-linked (GlcNAc...) Potential

Glycosylation

1643

N-linked (GlcNAc...) Potential

Disulfide bond

271 ↔ 280

By similarity

Disulfide bond

273 ↔ 298

By similarity

Disulfide bond

300 ↔ 309

By similarity

Disulfide bond

312 ↔ 332

By similarity

Disulfide bond

335 ↔ 344

By similarity

Disulfide bond

337 ↔ 362

By similarity

Disulfide bond

365 ↔ 374

By similarity

Disulfide bond

377 ↔ 395

By similarity

Disulfide bond

398 ↔ 411

By similarity

Disulfide bond

400 ↔ 426

By similarity

Disulfide bond

428 ↔ 437

By similarity

Disulfide bond

440 ↔ 455

By similarity

Disulfide bond

458 ↔ 472

By similarity

Disulfide bond

460 ↔ 479

By similarity

Disulfide bond

481 ↔ 490

By similarity

Disulfide bond

493 ↔ 507

By similarity

Disulfide bond

510 ↔ 522

By similarity

Disulfide bond

512 ↔ 529

By similarity

Disulfide bond

531 ↔ 540

By similarity

Disulfide bond

773 ↔ 785

By similarity

Disulfide bond

775 ↔ 792

By similarity

Disulfide bond

794 ↔ 803

By similarity

Disulfide bond

806 ↔ 818

By similarity

Disulfide bond

821 ↔ 833

By similarity

Disulfide bond

823 ↔ 840

By similarity

Disulfide bond

842 ↔ 851

By similarity

Disulfide bond

854 ↔ 864

By similarity

Disulfide bond

867 ↔ 876

By similarity

Disulfide bond

869 ↔ 883

By similarity

Disulfide bond

886 ↔ 895

By similarity

Disulfide bond

898 ↔ 914

By similarity

Disulfide bond

917 ↔ 933

By similarity

Disulfide bond

919 ↔ 944

By similarity

Disulfide bond

946 ↔ 955

By similarity

Disulfide bond

958 ↔ 973

By similarity

Disulfide bond

976 ↔ 990

By similarity

Disulfide bond

978 ↔ 997

By similarity

Disulfide bond

1000 ↔ 1009

By similarity

Disulfide bond

1012 ↔ 1025

By similarity

Disulfide bond

1028 ↔ 1040

By similarity

Disulfide bond

1030 ↔ 1054

By similarity

Disulfide bond

1056 ↔ 1065

By similarity

Disulfide bond

1068 ↔ 1081

By similarity

Disulfide bond

1084 ↔ 1096

By similarity

Disulfide bond

1086 ↔ 1103

By similarity

Disulfide bond

1105 ↔ 1114

By similarity

Disulfide bond

1117 ↔ 1129

By similarity

Disulfide bond

1132 ↔ 1144

By similarity

Disulfide bond

1134 ↔ 1151

By similarity

Disulfide bond

1153 ↔ 1162

By similarity

Disulfide bond

1165 ↔ 1176

By similarity

Disulfide bond

1179

Interchain Probable

Disulfide bond

1182

Interchain Probable

Disulfide bond

1785

Interchain Probable

Experimental info

Sequence conflict

159

A → T in AAA39407. Ref.1

Sequence conflict

569

I → V in AAA39407. Ref.1

Sequence conflict

993

E → D in AAA39407. Ref.1

Sequence conflict

1393

V → A in AAA39407. Ref.1

Sequence conflict

1393

V → A in CAA28839. Ref.3

Sequence conflict

1531 – 1534

MEMP → SGNA in AAA39407. Ref.1

Sequence conflict

1692

G → C in CAA28839. Ref.3

Sequence conflict

1749

D → N in CAA28839. Ref.3

Secondary structure

1786

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P02469 [UniParc].

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

FASTA

1,786

197,090

        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' referencesShow '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. 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, MASS SPECTROMETRY.
[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.

PIR

MMMSB1. A26413.

UniGene

Mm.172674.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4AQS	X-ray	3.11	A	21-542	[»]

ProteinModelPortal

P02469.

SMR

P02469. Positions 29-492.

ModBase

Search...

MobiDB

Search...

Protein-protein interaction databases

IntAct

P02469. 6 interactions.

MINT

MINT-1206337.

PTM databases

PhosphoSite

P02469.

Proteomic databases

PaxDb

P02469.

PRIDE

P02469.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000169088; ENSMUSP00000132778; ENSMUSG00000002900.

Organism-specific databases

MGI

MGI:96743. Lamb1.

Phylogenomic databases

eggNOG

NOG241384.

GeneTree

ENSGT00720000108616.

HOVERGEN

HBG052301.

InParanoid

P02469.

OrthoDB

EOG75XGK0.

Enzyme and pathway databases

Reactome

REACT_127416. Developmental Biology.
REACT_131142. Extracellular matrix organization.

Gene expression databases

ArrayExpress

P02469.

Bgee

P02469.

CleanEx

MM_LAMB1-1.

Genevestigator

P02469.

Family and domain databases

InterPro

IPR002049. EGF_laminin.
IPR013015. Laminin_IV.
IPR008211. Laminin_N.
[Graphical view]

Pfam

PF00053. Laminin_EGF. 13 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]

SMART

SM00180. EGF_Lam. 13 hits.
SM00136. LamNT. 1 hit.
[Graphical view]

PROSITE

PS00022. 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]

ProtoNet

Search...

Other

ChiTaRS

LAMB1. mouse.

PRO

P02469.

SOURCE

Search...

Entry information

Entry name

LAMB1_MOUSE

Accession

Primary (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:	January 22, 2014
This is version 133 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata 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

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents