P02469 (LAMB1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

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

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › 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	basal 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_function	enzyme 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
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

21

Chain

22 – 1786

1765

Laminin subunit beta-1

PRO_0000017066

Regions

Domain

31 – 270

240

Laminin N-terminal

Domain

271 – 334

64

Laminin EGF-like 1

Domain

335 – 397

63

Laminin EGF-like 2

Domain

398 – 457

60

Laminin EGF-like 3

Domain

458 – 509

52

Laminin EGF-like 4

Domain

510 – 540

31

Laminin EGF-like 5; truncated

Domain

549 – 767

219

Laminin IV type B

Domain

773 – 820

48

Laminin EGF-like 6

Domain

821 – 866

46

Laminin EGF-like 7

Domain

867 – 916

50

Laminin EGF-like 8

Domain

917 – 975

59

Laminin EGF-like 9

Domain

976 – 1027

52

Laminin EGF-like 10

Domain

1028 – 1083

56

Laminin EGF-like 11

Domain

1084 – 1131

48

Laminin EGF-like 12

Domain

1132 – 1178

47

Laminin EGF-like 13

Region

1179 – 1397

219

Domain II

Region

1398 – 1430

33

Domain alpha

Region

1431 – 1786

356

Domain I

Coiled coil

1216 – 1315

100

Potential

Coiled coil

1368 – 1388

21

Potential

Coiled coil

1448 – 1778

331

Potential

Amino acid modifications

Glycosylation

120

1

N-linked (GlcNAc...) Potential

Glycosylation

356

1

N-linked (GlcNAc...) Potential

Glycosylation

519

1

N-linked (GlcNAc...) Potential

Glycosylation

677

1

N-linked (GlcNAc...) Potential

Glycosylation

1041

1

N-linked (GlcNAc...) Potential

Glycosylation

1195

1

N-linked (GlcNAc...) Potential

Glycosylation

1279

1

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

Glycosylation

1336

1

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

Glycosylation

1343

1

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

Glycosylation

1487

1

N-linked (GlcNAc...) Potential

Glycosylation

1542

1

N-linked (GlcNAc...) Potential

Glycosylation

1643

1

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

1

A → T in AAA39407. Ref.1

Sequence conflict

569

1

I → V in AAA39407. Ref.1

Sequence conflict

993

1

E → D in AAA39407. Ref.1

Sequence conflict

1393

1

V → A in AAA39407. Ref.1

Sequence conflict

1393

1

V → A in CAA28839. Ref.3

Sequence conflict

1531 – 1534

4

MEMP → SGNA in AAA39407. Ref.1

Sequence conflict

1692

1

G → C in CAA28839. Ref.3

Sequence conflict

1749

1

D → N in CAA28839. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1786

Helix Strand Turn

Details...

Helix

30 – 32

3

Beta strand

40 – 43

4

Helix

47 – 49

3

Beta strand

58 – 60

3

Beta strand

62 – 67

6

Beta strand

69 – 72

4

Beta strand

74 – 79

6

Turn

87 – 89

3

Helix

96 – 98

3

Beta strand

122 – 142

21

Beta strand

146 – 155

10

Beta strand

161 – 169

9

Turn

170 – 172

3

Beta strand

173 – 177

5

Turn

200 – 202

3

Beta strand

204 – 210

7

Beta strand

212 – 214

3

Helix

222 – 228

7

Beta strand

229 – 239

11

Helix

252 – 255

4

Beta strand

261 – 270

10

Beta strand

304 – 309

6

Beta strand

342 – 346

5

Helix

348 – 353

6

Beta strand

360 – 364

5

Beta strand

369 – 371

3

Beta strand

381 – 383

3

Beta strand

385 – 387

3

Beta strand

395 – 397

3

Turn

402 – 404

3

Helix

407 – 409

3

Helix

417 – 419

3

Turn

434 – 437

4

Beta strand

454 – 457

4

Turn

462 – 464

3

Turn

474 – 476

3

Turn

488 – 490

3

Sequences

	Sequence		Length	Mass (Da)
	P02469 [UniParc]. Last modified July 27, 2011. Version 3. Checksum: E7F258170C3626DD	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

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. , 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.

PIR

MMMSB1. A26413.

RefSeq

XP_006515056.1. XM_006514993.1.

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.

GeneID

16777.

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_188576. Developmental Biology.

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:	April 16, 2014
This is version 135 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program